Protein ID | Agabi119p4|085630 |
Gene name | |
Location | scaffold_05b:180221..181755 |
Strand | + |
Gene length (bp) | 1534 |
Transcript length (bp) | 1002 |
Coding sequence length (bp) | 1002 |
Protein length (aa) | 334 |
PFAM Domain ID | Short name | Long name | E-value | Start | End |
---|---|---|---|---|---|
PF00331 | Glyco_hydro_10 | Glycosyl hydrolase family 10 | 8.9E-113 | 22 | 329 |
Swissprot ID | Swissprot Description | Start | End | E-value |
---|---|---|---|---|
sp|O60206|XLNA_AGABI | Endo-1,4-beta-xylanase OS=Agaricus bisporus GN=xlnA PE=2 SV=1 | 1 | 333 | 0.0E+00 |
sp|Q9HEZ1|XYNA_PHACH | Endo-1,4-beta-xylanase A OS=Phanerochaete chrysosporium GN=xynA PE=1 SV=1 | 18 | 331 | 9.0E-147 |
sp|B7SIW2|XYNC_PHACH | Endo-1,4-beta-xylanase C OS=Phanerochaete chrysosporium GN=xynC PE=1 SV=1 | 10 | 332 | 5.0E-144 |
sp|B4XVN1|XYNA_STRSQ | Endo-1,4-beta-xylanase A OS=Streptomyces sp. GN=xynAS9 PE=1 SV=1 | 19 | 328 | 3.0E-120 |
sp|Q5ZNB1|XYND_TALFU | Endo-1,4-beta-xylanase D OS=Talaromyces funiculosus GN=xynD PE=1 SV=1 | 1 | 330 | 4.0E-119 |
Swissprot ID | Swissprot Description | Start | End | E-value |
---|---|---|---|---|
sp|O60206|XLNA_AGABI | Endo-1,4-beta-xylanase OS=Agaricus bisporus GN=xlnA PE=2 SV=1 | 1 | 333 | 0.0E+00 |
sp|Q9HEZ1|XYNA_PHACH | Endo-1,4-beta-xylanase A OS=Phanerochaete chrysosporium GN=xynA PE=1 SV=1 | 18 | 331 | 9.0E-147 |
sp|B7SIW2|XYNC_PHACH | Endo-1,4-beta-xylanase C OS=Phanerochaete chrysosporium GN=xynC PE=1 SV=1 | 10 | 332 | 5.0E-144 |
sp|B4XVN1|XYNA_STRSQ | Endo-1,4-beta-xylanase A OS=Streptomyces sp. GN=xynAS9 PE=1 SV=1 | 19 | 328 | 3.0E-120 |
sp|Q5ZNB1|XYND_TALFU | Endo-1,4-beta-xylanase D OS=Talaromyces funiculosus GN=xynD PE=1 SV=1 | 1 | 330 | 4.0E-119 |
sp|P07986|GUX_CELFI | Exoglucanase/xylanase OS=Cellulomonas fimi GN=cex PE=1 SV=1 | 11 | 331 | 1.0E-101 |
sp|G4MLU0|XYN5_MAGO7 | Endo-1,4-beta-xylanase 5 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) GN=XYL5 PE=3 SV=1 | 3 | 324 | 1.0E-100 |
sp|Q8J1Y4|XYN5_MAGGR | Endo-1,4-beta-xylanase 5 OS=Magnaporthe grisea GN=XYL5 PE=3 SV=1 | 3 | 324 | 1.0E-100 |
sp|P79046|XYN1_HUMGT | Endo-1,4-beta-xylanase 1 OS=Humicola grisea var. thermoidea GN=xyn1 PE=2 SV=1 | 22 | 327 | 2.0E-95 |
sp|I1RQU5|XYN1_GIBZE | Endo-1,4-beta-xylanase 1 OS=Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) GN=XYL1 PE=1 SV=1 | 26 | 324 | 1.0E-94 |
sp|Q2PGV8|XYN2_AURPU | Endo-1,4-beta-xylanase 2 OS=Aureobasidium pullulans GN=xynII PE=1 SV=1 | 27 | 328 | 3.0E-94 |
sp|B3A0S5|XYNA_FUSO4 | Endo-1,4-beta-xylanase A OS=Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 / NRRL 34936) GN=FOXG_17421 PE=1 SV=1 | 26 | 329 | 8.0E-94 |
sp|Q0CBM8|XYNC_ASPTN | Probable endo-1,4-beta-xylanase C OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) GN=xlnC PE=2 SV=2 | 27 | 328 | 5.0E-81 |
sp|Q4JHP5|XYNC_ASPTE | Probable endo-1,4-beta-xylanase C OS=Aspergillus terreus GN=xlnC PE=2 SV=1 | 27 | 328 | 6.0E-81 |
sp|Q0H904|XYNC_ASPFU | Endo-1,4-beta-xylanase C OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) GN=xlnC PE=2 SV=2 | 17 | 328 | 1.0E-80 |
sp|P23360|XYNA_THEAU | Endo-1,4-beta-xylanase OS=Thermoascus aurantiacus GN=XYNA PE=1 SV=4 | 27 | 333 | 3.0E-80 |
sp|O94163|XYNF1_ASPOR | Endo-1,4-beta-xylanase F1 OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) GN=xynF1 PE=1 SV=1 | 17 | 330 | 8.0E-80 |
sp|Q96VB6|XYNF3_ASPOR | Endo-1,4-beta-xylanase F3 OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) GN=xynF3 PE=1 SV=1 | 3 | 329 | 9.0E-80 |
sp|A1CX14|XYNC_NEOFI | Probable endo-1,4-beta-xylanase C OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) GN=xlnC PE=2 SV=1 | 1 | 328 | 7.0E-78 |
sp|B0Y6E0|XYNC_ASPFC | Probable endo-1,4-beta-xylanase C OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) GN=xlnC PE=2 SV=2 | 17 | 328 | 2.0E-77 |
sp|A1CHQ0|XYNC_ASPCL | Probable endo-1,4-beta-xylanase C OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) GN=xlnC PE=2 SV=1 | 27 | 328 | 2.0E-75 |
sp|Q9P8J1|XYNA_TALPU | Endo-1,4-beta-xylanase A OS=Talaromyces purpurogenus GN=XynA PE=1 SV=1 | 27 | 330 | 6.0E-75 |
sp|B8NXJ2|XYNF3_ASPFN | Probable endo-1,4-beta-xylanase F3 OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167) GN=xynF3 PE=2 SV=1 | 17 | 330 | 2.0E-74 |
sp|Q5S7A8|XYNA_PENCN | Endo-1,4-beta-xylanase A OS=Penicillium canescens GN=xylA PE=1 SV=1 | 27 | 330 | 1.0E-73 |
sp|G4MPQ7|XYN6_MAGO7 | Endo-1,4-beta-xylanase 6 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) GN=XYL6 PE=3 SV=1 | 19 | 329 | 1.0E-73 |
sp|Q8NJ73|XYN6_MAGGR | Endo-1,4-beta-xylanase 6 OS=Magnaporthe grisea GN=XYL6 PE=1 SV=1 | 19 | 329 | 1.0E-73 |
sp|P56588|XYNA_PENSI | Endo-1,4-beta-xylanase OS=Penicillium simplicissimum PE=1 SV=1 | 27 | 330 | 2.0E-73 |
sp|O59859|XYNA_ASPAC | Endo-1,4-beta-xylanase OS=Aspergillus aculeatus GN=xynIA PE=3 SV=1 | 27 | 330 | 2.0E-73 |
sp|C5J411|XYNC_ASPNG | Probable endo-1,4-beta-xylanase C OS=Aspergillus niger GN=xlnC PE=2 SV=2 | 27 | 330 | 2.0E-73 |
sp|A2QFV7|XYNC_ASPNC | Probable endo-1,4-beta-xylanase C OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) GN=xlnC PE=1 SV=1 | 27 | 330 | 5.0E-73 |
sp|Q00177|XYNC_EMENI | Endo-1,4-beta-xylanase C OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) GN=xlnC PE=1 SV=1 | 3 | 332 | 1.0E-72 |
sp|P33559|XYNA_ASPKW | Endo-1,4-beta-xylanase A OS=Aspergillus kawachii (strain NBRC 4308) GN=xynA PE=1 SV=2 | 27 | 330 | 2.0E-72 |
sp|Q4P902|XIN1_USTMA | Endo-1,4-beta-xylanase UM03411 OS=Ustilago maydis (strain 521 / FGSC 9021) GN=UMAG_03411 PE=1 SV=1 | 19 | 328 | 4.0E-72 |
sp|I1S3T9|XYNC_GIBZE | Endo-1,4-beta-xylanase C OS=Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) GN=XYLC PE=1 SV=1 | 19 | 330 | 6.0E-72 |
sp|Q60041|XYNB_THENE | Endo-1,4-beta-xylanase B OS=Thermotoga neapolitana GN=xynB PE=3 SV=1 | 54 | 327 | 4.0E-71 |
sp|G4MTF8|XYN2_MAGO7 | Endo-1,4-beta-xylanase 2 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) GN=XYL2 PE=3 SV=1 | 19 | 328 | 1.0E-70 |
sp|P10478|XYNZ_CLOTH | Endo-1,4-beta-xylanase Z OS=Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) GN=xynZ PE=1 SV=3 | 54 | 327 | 1.0E-69 |
sp|B8NER4|XYNF1_ASPFN | Probable endo-1,4-beta-xylanase F1 OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167) GN=xynF1 PE=3 SV=1 | 26 | 328 | 8.0E-69 |
sp|W0HFK8|XYN1_RHIOR | Endo-1,4-beta-xylanase 1 OS=Rhizopus oryzae GN=xyn1 PE=1 SV=1 | 27 | 327 | 8.0E-68 |
sp|P29417|XYNA_PENCH | Endo-1,4-beta-xylanase OS=Penicillium chrysogenum GN=XYLP PE=1 SV=2 | 27 | 300 | 5.0E-66 |
sp|Q6PRW6|XYN_PENCH | Endo-1,4-beta-xylanase OS=Penicillium chrysogenum GN=Xyn PE=1 SV=1 | 27 | 300 | 6.0E-66 |
sp|P26514|XYNA_STRLI | Endo-1,4-beta-xylanase A OS=Streptomyces lividans GN=xlnA PE=1 SV=2 | 13 | 329 | 1.0E-65 |
sp|P46239|GUNF_FUSOX | Putative endoglucanase type F OS=Fusarium oxysporum PE=2 SV=1 | 27 | 303 | 1.0E-64 |
sp|I1S3C6|XYND_GIBZE | Endo-1,4-beta-xylanase D OS=Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) GN=XYLD PE=1 SV=1 | 24 | 327 | 3.0E-64 |
sp|Q01176|XYN2_MAGGR | Endo-1,4-beta-xylanase 2 OS=Magnaporthe grisea GN=XYL2 PE=1 SV=1 | 19 | 328 | 2.0E-63 |
sp|O74717|XYN2_CLAPU | Endo-1,4-beta-xylanase 2 OS=Claviceps purpurea GN=xyl2 PE=2 SV=1 | 19 | 307 | 5.0E-63 |
sp|P36917|XYNA_THESA | Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum GN=xynA PE=1 SV=1 | 28 | 329 | 3.0E-54 |
sp|P38535|XYNX_CLOTM | Exoglucanase XynX OS=Clostridium thermocellum GN=xynX PE=3 SV=1 | 28 | 329 | 3.0E-53 |
sp|P14768|XYNA_CELJU | Endo-1,4-beta-xylanase A OS=Cellvibrio japonicus (strain Ueda107) GN=xynA PE=1 SV=2 | 53 | 332 | 3.0E-47 |
sp|Q59675|XY10C_CELJA | Endo-beta-1,4-xylanase Xyn10C OS=Cellvibrio japonicus GN=xyn10C PE=1 SV=2 | 55 | 330 | 1.0E-46 |
sp|P40943|XYN1_GEOSE | Endo-1,4-beta-xylanase OS=Geobacillus stearothermophilus PE=1 SV=1 | 4 | 329 | 7.0E-46 |
sp|Q12603|XYNA_DICTH | Beta-1,4-xylanase OS=Dictyoglomus thermophilum GN=xynA PE=3 SV=1 | 55 | 328 | 1.0E-45 |
sp|O69230|XYNC_PAEBA | Endo-1,4-beta-xylanase C OS=Paenibacillus barcinonensis GN=xynC PE=1 SV=1 | 22 | 329 | 2.0E-44 |
sp|P07528|XYNA_BACHD | Endo-1,4-beta-xylanase A OS=Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) GN=xynA PE=1 SV=1 | 55 | 329 | 2.0E-42 |
sp|O69231|XYNB_PAEBA | Endo-1,4-beta-xylanase B OS=Paenibacillus barcinonensis GN=xynB PE=1 SV=1 | 55 | 301 | 2.0E-41 |
sp|Q02290|XYNB_NEOPA | Endo-1,4-beta-xylanase B OS=Neocallimastix patriciarum GN=xynB PE=2 SV=1 | 55 | 301 | 8.0E-41 |
sp|C6CRV0|XYNA1_PAESJ | Endo-1,4-beta-xylanase A OS=Paenibacillus sp. (strain JDR-2) GN=xynA1 PE=1 SV=1 | 58 | 329 | 2.0E-40 |
sp|P40942|CEXY_CLOSR | Thermostable celloxylanase OS=Clostridium stercorarium GN=xynB PE=1 SV=1 | 7 | 329 | 3.0E-40 |
sp|P10474|GUNB_CALSA | Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus GN=celB PE=3 SV=1 | 55 | 330 | 3.0E-39 |
sp|P45703|XYN2_GEOSE | Endo-1,4-beta-xylanase OS=Geobacillus stearothermophilus GN=xynA PE=1 SV=1 | 56 | 329 | 2.0E-38 |
sp|P40944|XYNA_CALSR | Endo-1,4-beta-xylanase A OS=Caldicellulosiruptor sp. (strain Rt8B.4) GN=xynA PE=3 SV=1 | 43 | 303 | 8.0E-38 |
sp|Q60037|XYNA_THEMA | Endo-1,4-beta-xylanase A OS=Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) GN=xynA PE=1 SV=1 | 52 | 300 | 1.0E-34 |
sp|P49942|XYNA_BACOV | Endo-1,4-beta-xylanase A OS=Bacteroides ovatus GN=xylI PE=2 SV=1 | 54 | 255 | 1.0E-34 |
sp|D5EY13|XYFA_PRER2 | Endo-1,4-beta-xylanase/feruloyl esterase OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) GN=xyn10D-fae1A PE=1 SV=1 | 26 | 329 | 3.0E-34 |
sp|Q60042|XYNA_THENE | Endo-1,4-beta-xylanase A OS=Thermotoga neapolitana GN=xynA PE=1 SV=1 | 56 | 300 | 6.0E-34 |
sp|P23556|XYNA_CALSA | Endo-1,4-beta-xylanase A OS=Caldicellulosiruptor saccharolyticus GN=xynA PE=1 SV=1 | 55 | 300 | 2.0E-32 |
sp|P48789|XYNA_PRERU | Endo-1,4-beta-xylanase A OS=Prevotella ruminicola GN=xynA PE=3 SV=1 | 9 | 328 | 2.0E-32 |
sp|P07529|XYNA_CRYAL | Endo-1,4-beta-xylanase OS=Cryptococcus albidus PE=1 SV=2 | 19 | 308 | 3.0E-28 |
sp|P26223|XYNB_BUTFI | Endo-1,4-beta-xylanase B OS=Butyrivibrio fibrisolvens GN=xynB PE=3 SV=1 | 55 | 303 | 1.0E-22 |
sp|P51584|XYNY_CLOTM | Endo-1,4-beta-xylanase Y OS=Clostridium thermocellum GN=xynY PE=1 SV=1 | 54 | 327 | 1.0E-20 |
sp|P29126|XYNA_RUMFL | Bifunctional endo-1,4-beta-xylanase XylA OS=Ruminococcus flavefaciens GN=xynA PE=3 SV=1 | 92 | 300 | 8.0E-20 |
sp|P23557|XYN4_CALSA | Putative endo-1,4-beta-xylanase OS=Caldicellulosiruptor saccharolyticus PE=3 SV=1 | 64 | 328 | 2.0E-18 |
sp|P23551|XYNA_BUTFI | Endo-1,4-beta-xylanase A OS=Butyrivibrio fibrisolvens GN=xynA PE=3 SV=1 | 78 | 333 | 1.0E-16 |
sp|P23030|XYNB_CELJU | Endo-1,4-beta-xylanase B OS=Cellvibrio japonicus (strain Ueda107) GN=xynB PE=1 SV=2 | 55 | 303 | 6.0E-13 |
GO Term | Description | Terminal node |
---|---|---|
GO:0005975 | carbohydrate metabolic process | Yes |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds | Yes |
GO:0016787 | hydrolase activity | No |
GO:0003824 | catalytic activity | No |
GO:0044238 | primary metabolic process | No |
GO:0071704 | organic substance metabolic process | No |
GO:0008150 | biological_process | No |
GO:0008152 | metabolic process | No |
GO:0016798 | hydrolase activity, acting on glycosyl bonds | No |
GO:0003674 | molecular_function | No |
SignalP signal predicted | Location (based on Ymax) |
D score (significance: > 0.45) |
---|---|---|
Yes | 1 - 18 | 0.45 |
Type of sequence | Sequence |
---|---|
Locus | Download genbank file of locus
The gene with 5 kb flanks (if sufficient flanking sequence is available). For use in cloning design programs. NOTE: features (genes or exons) that are only partially contained within the sequence are completely excluded. |
Protein | >Agabi119p4|085630 MYLVTLILLGMLPIGYCQLNTLAVRAGKKYFGTATDNPELGDAPYVAQLGNTADFNQITAGNSMKWDATEPSRGT FTFANGDTVANMARNRGQLLRGHTCVWHSQLPNWVTSGNFDNSTLLSIVQNHCSTLVSHYRGQMCYWDVVNEPFN EDGSFRQSVFFQKTGTAYIATALRAARNADPNTKLYINDFNIEGTGAKSTGMINLVRSLQQQNVPIDGIGVQAHL IVGQIPSSIQQNLQNFANLGVEVAITELDIRMTLPVTQQKLEQQQEDYRTVIRACKAVSRCVGVTVWDWTDRYSW VPGVFTGEGAACPWDENLAKKPAYQGIVDGWSQ* |
Coding | >Agabi119p4|085630 ATGTATCTCGTCACGTTGATACTTCTCGGTATGCTGCCGATAGGCTATTGCCAACTCAATACGCTTGCCGTACGA GCTGGAAAGAAATATTTTGGTACGGCAACCGATAACCCTGAATTGGGAGATGCTCCGTATGTTGCCCAACTCGGT AACACGGCAGATTTCAATCAAATCACCGCGGGAAACAGTATGAAATGGGACGCCACGGAGCCCTCCCGAGGGACT TTCACCTTTGCAAATGGCGACACGGTTGCCAACATGGCCCGAAACCGTGGGCAGCTTCTCAGAGGGCACACCTGT GTTTGGCACTCGCAGCTTCCAAACTGGGTCACATCTGGCAATTTTGACAATTCAACCCTTCTAAGCATTGTCCAA AACCACTGCTCGACTTTAGTCTCCCATTACAGGGGTCAAATGTGTTATTGGGATGTAGTCAATGAGCCGTTCAAC GAGGATGGCAGCTTTAGGCAATCAGTCTTCTTCCAGAAGACTGGGACCGCTTATATCGCCACAGCACTCCGAGCC GCTCGTAATGCAGACCCAAACACGAAGCTCTATATCAACGATTTCAACATTGAAGGTACCGGGGCCAAGTCCACT GGCATGATTAATCTCGTCCGGAGCCTTCAACAGCAGAACGTCCCCATTGACGGCATCGGCGTACAAGCTCACTTG ATTGTTGGCCAAATTCCTTCCAGTATACAGCAAAATCTACAGAACTTTGCGAACCTCGGAGTAGAAGTCGCAATT ACTGAGCTTGATATCAGAATGACACTTCCTGTCACACAGCAAAAGCTTGAGCAACAGCAAGAAGATTATCGGACC GTCATTCGGGCATGCAAGGCTGTTTCCCGCTGCGTCGGTGTTACAGTTTGGGATTGGACTGATAGGTACTCTTGG GTTCCAGGAGTTTTCACTGGTGAAGGAGCCGCTTGCCCATGGGATGAAAATTTGGCGAAGAAACCCGCATATCAA GGCATCGTGGATGGCTGGAGTCAATGA |
Transcript | >Agabi119p4|085630 ATGTATCTCGTCACGTTGATACTTCTCGGTATGCTGCCGATAGGCTATTGCCAACTCAATACGCTTGCCGTACGA GCTGGAAAGAAATATTTTGGTACGGCAACCGATAACCCTGAATTGGGAGATGCTCCGTATGTTGCCCAACTCGGT AACACGGCAGATTTCAATCAAATCACCGCGGGAAACAGTATGAAATGGGACGCCACGGAGCCCTCCCGAGGGACT TTCACCTTTGCAAATGGCGACACGGTTGCCAACATGGCCCGAAACCGTGGGCAGCTTCTCAGAGGGCACACCTGT GTTTGGCACTCGCAGCTTCCAAACTGGGTCACATCTGGCAATTTTGACAATTCAACCCTTCTAAGCATTGTCCAA AACCACTGCTCGACTTTAGTCTCCCATTACAGGGGTCAAATGTGTTATTGGGATGTAGTCAATGAGCCGTTCAAC GAGGATGGCAGCTTTAGGCAATCAGTCTTCTTCCAGAAGACTGGGACCGCTTATATCGCCACAGCACTCCGAGCC GCTCGTAATGCAGACCCAAACACGAAGCTCTATATCAACGATTTCAACATTGAAGGTACCGGGGCCAAGTCCACT GGCATGATTAATCTCGTCCGGAGCCTTCAACAGCAGAACGTCCCCATTGACGGCATCGGCGTACAAGCTCACTTG ATTGTTGGCCAAATTCCTTCCAGTATACAGCAAAATCTACAGAACTTTGCGAACCTCGGAGTAGAAGTCGCAATT ACTGAGCTTGATATCAGAATGACACTTCCTGTCACACAGCAAAAGCTTGAGCAACAGCAAGAAGATTATCGGACC GTCATTCGGGCATGCAAGGCTGTTTCCCGCTGCGTCGGTGTTACAGTTTGGGATTGGACTGATAGGTACTCTTGG GTTCCAGGAGTTTTCACTGGTGAAGGAGCCGCTTGCCCATGGGATGAAAATTTGGCGAAGAAACCCGCATATCAA GGCATCGTGGATGGCTGGAGTCAATGA |
Gene | >Agabi119p4|085630 ATGTATCTCGTCACGTTGATACTTCTCGGTATGCTGCCGATAGGCTATTGCCAACTCAATACGCTTGCCGTACGA GCTGGAAAGAAATATTTTGGTACGGCAACCGATAACCCTGAATTGGGAGATGCTCCGTATGTTGCCCAACTCGGT AACACGGCAGATTTCAATCAAATCACCGCGGTGAGTATATATCGTGGATCAATGGAGCTCGCTATCTAATAAGTC ATGTAGGGAAACAGTATGAAATGGGTGCGACCGTTTCTATGGTCTAAAAAACACTCTTGAGTTATAACTTCATCT CAGGACGCCACGGAGCCCTCCCGAGGGACTTTCACCTTTGCAAATGGCGACACGGTTGCCAACATGGCCCGAAAC CGTGGGCAGCTTCTCAGAGGTTCTTGAATATTATAATCTACCGTTGCCGGATCTCGTCATTGACTACCGTCTAGG GCACACCTGTGTTTGGCACTCGCAGCTTCCAAACTGGGTCACATCTGGCAATTTTGACAATTCAACCCTTCTAAG GTGTCCGACACTTGAACCCATATCAACGTTCAAAATTTGATTCACTCCACCTAGCATTGTCCAAAACCACTGCTC GACTTTAGTCTCCCATTACAGGGGTCAAATGTACGTTCGAACCTCTTTCAGTAACGTCAAGGACTGACGAATTAT CTCTAATAGGTGTTAGTACAATCTGTCAAACTAGCCTCATTCGCTACTCATCAACTTGCGCCCTATAGACAGTTG GGATGTAGTCAATGGTTCGACTCAGGTTTAATATTTCTACTTGATCCGACATGACTCAATTTTTAGAGCCGTTCA ACGAGGATGGCAGCTTTAGGCAATCAGTCTTCTTCCAGAAGACTGGGACCGCTTATATCGCCACAGCACTCCGAG CCGCTCGTAATGCAGACCCAAACACGAAGCTCTATGTAAGCACCTTCAATCGTCGAGCCTGAATAAGTTTGCTCA ACTACGCGCAGATCAACGATTTCAACATTGAAGGTACCGGGGCCAAGTCCACTGGCATGATTAATCTCGTCCGGA GCCTTCAACAGCAGAACGTCCCCATTGACGGCATCGGCGTACAAGCTCACTTGATTGTTGGCCAAATTCCTTCCA GTATACAGCAAAATCTACAGAACTTTGCGAACCTCGGAGTAGAAGTCGCAATTACTGAGCTTGATATCAGAATGA CACTTCCTGTCACACAGCAAAAGCTTGAGCAACAGCAAGAAGATTATCGGACCGTCATTCGGGCATGCAAGGCTG TTTCCCGCTGCGTCGGTGTTACAGTTTGGGATTGGACTGATAGGGTGGGTTGTTTTGATTTGATGTCGCGACCGC ATGTATTTACACCCCTTAGTACTCTTGGGTTCCAGGAGTTTTCACTGGTGAAGGAGCCGCTTGCCCATGGGATGA AGTGAGCTTTTTCGATATAAACCCCCCTTTTAGAAGCGTACTGACAATTGAAAAGAATTTGGCGAAGAAACCCGC ATATCAAGGCATCGTGGATGGCTGGAGTCAATGA |