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CAZyme Information: OAG13703.1
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Alternaria alternata | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Ascomycota; Dothideomycetes; ; Pleosporaceae; Alternaria; Alternaria alternata | |||||||||||
| CAZyme ID | OAG13703.1 | |||||||||||
| CAZy Family | AA3 | |||||||||||
| CAZyme Description | glycoside hydrolase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 107101; End:111747 Strand: - | |||||||||||
Full Sequence Download help
| MATTLILSAC LALQAAARTV RSPTPPMGWN SYNTWNCLPS EDKIRTSAQG LIDLGLDKAG | 60 |
| YNFVTVDCGW PSEDRDAEGK LQWNETLFPS GGKALGDFIH GLGLDFGLYS GAGYLQCGSE | 120 |
| ALPASLGFEQ LDAESFAEWG GDSLKYDNCY STSNTTMVDS SSAESQSPAR FQHMAAELEA | 180 |
| VDRDIHYYVC QWGIGTDVGD WAAEIGNTWR ISNDIYNAWR SIWRITNQVV PYFRHTTVGA | 240 |
| FADMDMLIVG LNALSEEEER FHFGMWAINK SPLIIGAALD PERISQSSLA IMENKEVIAI | 300 |
| NQDALAQQAM LVRRDTEEEW DIWMGKLSGS RMVLGVANWK NDSQSVNFDL ASLGIASVDA | 360 |
| RDVWAAKDAG ALSGTQTVDL AGHELRLWIL SNIVEAAPLQ SGSYNSATNA SLSGPAHVFS | 420 |
| CASGTCLPTG SKIEYIDRSS SVIFSNVSAP SAGKNLVGVD FVNYEYAFTT AWEWGDNTRN | 480 |
| MTIAVNGAEA KRWAFPLSGG DWQESLRLHI EVDGFVEGTE NMVEFRGYGD SFAPDLVVCH | 540 |
| SHNNTMFVSL ATALWRADRM TVLTHASTGR KRGDHPARVY PISNCDRGLK VAEPSSQKTI | 600 |
| MTLVPHTSTL LKTGWTFKQG DRSSTHAYLP ARDVPTEIYR DLLKNEKIAD PFNDLNELAV | 660 |
| QWVGDETWTY RTIFAAPSEY GTANTVTRLR FQGLDTFASV YLNGHKVLES DNMFVEHEVD | 720 |
| VSGRLELDEN VLEIVFESAR KKGRELVEQH KEHRFIVHQT EISRGPVRKA QFHWGWDWGP | 780 |
| VLMACGPWKP VSIETWSCQL SSPGVQYELS QNLKSAEVKV KVGWEGVVAA IGFTILKKDS | 840 |
| LEAVAEQKID VSTDDQSGLA EATMAINDIE LWWPRGYGQQ SLYTIKIQAF APDHPSPIHD | 900 |
| ISQQFGFRRA ELITEPDSYG TSFYFRINDI DIFCGGSCWI PGDAFLTRPS PRDSRAWAKL | 960 |
| CADGNQTMLR IWGGGIYEDD ELYNAADEYG VLIWQDFMFA CANYPAYPEY LKSVELEATQ | 1020 |
| NVRRLRNHPS VVIWAGNNED YQIVERYGLQ YDPDDKDPDS WLKTDFPARY IYEYLLPNVV | 1080 |
| KQECSNVLYH PSSPFGNGKS TVLRVDPTIG DIHQWNVWHG TMEPYQRLPD LGGRFVSEFG | 1140 |
| MEAYPHVSTL ESCITRKEDL YPGSMVMDFH NKAIGHERRL ISYLAENFRI RYDLENFAHL | 1200 |
| TQVMQSDALT WAYKSWRRQW NTPGDRKCGG VLVWQLNDCW QTMSWSVTDI HGVPKPAFYA | 1260 |
| IKRTMRPITI GVQRKYQSWT MRPADELWQR DTGHIDMRKL WQDVEHDVWI ANSTLQEVDG | 1320 |
| VVTVRYISIK TGEEIGTRAS ATVQVAANGI TNVLVDHVAQ INHVQHPNEP FDSSKADPFV | 1380 |
| IHATLSINGE YAASDIAWPE PIKYLSFSDP GVQLRYSEDK KTISVSAAKP VKGFVFAENP | 1440 |
| RSHLSDNGFD LVPGETRDVQ VEGFPATALT WRYIEM | 1476 |
Enzyme Prediction help
| EC | 3.2.1.22:1 | 3.2.1.88:1 | 3.2.1.22:1 | 3.2.1.88:1 | 3.2.1.25:3 |
|---|
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH2 | 608 | 1345 | 4.6e-88 | 0.6901595744680851 |
| GH27 | 123 | 369 | 7.3e-65 | 0.982532751091703 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 269893 | GH27 | 1.72e-104 | 25 | 303 | 1 | 271 | glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively. |
| 178295 | PLN02692 | 4.54e-82 | 24 | 393 | 55 | 411 | alpha-galactosidase |
| 166449 | PLN02808 | 8.90e-80 | 24 | 391 | 31 | 384 | alpha-galactosidase |
| 177874 | PLN02229 | 4.67e-74 | 24 | 397 | 62 | 424 | alpha-galactosidase |
| 225789 | LacZ | 6.63e-69 | 614 | 1262 | 18 | 627 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| CBX98985.1|CBM35|GH2|GH27 | 0.0 | 6 | 1476 | 7 | 1497 |
| QRD07513.1|GH2 | 0.0 | 607 | 1476 | 10 | 880 |
| QBZ66458.1|GH2 | 1.88e-317 | 611 | 1473 | 8 | 894 |
| AEO64472.1|GH2 | 2.27e-313 | 601 | 1474 | 1 | 879 |
| AEO59187.1|GH2 | 8.95e-309 | 603 | 1474 | 1 | 895 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5N6U_A | 2.89e-128 | 634 | 1273 | 48 | 661 | Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12],5N6U_B Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12],5N6U_C Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12],5N6U_D Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12] |
| 2VJX_A | 6.38e-105 | 610 | 1270 | 10 | 656 | Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VJX_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VL4_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VL4_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VMF_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VMF_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VO5_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VO5_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VOT_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VOT_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VQT_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VQT_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VR4_A Transition-state mimicry in mannoside hydrolysis: characterisation of twenty six inhibitors and insight into binding from linear free energy relationships and 3-D structure [Bacteroides thetaiotaomicron VPI-5482],2VR4_B Transition-state mimicry in mannoside hydrolysis: characterisation of twenty six inhibitors and insight into binding from linear free energy relationships and 3-D structure [Bacteroides thetaiotaomicron VPI-5482] |
| 2JE8_A | 6.68e-105 | 610 | 1270 | 12 | 658 | Structure of a beta-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],2JE8_B Structure of a beta-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482] |
| 7OP6_A | 6.83e-105 | 610 | 1270 | 12 | 658 | Chain A, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP6_B Chain B, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP7_A Chain A, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP7_B Chain B, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482] |
| 2WBK_A | 1.68e-104 | 610 | 1270 | 10 | 656 | Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis [Bacteroides thetaiotaomicron VPI-5482],2WBK_B Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis [Bacteroides thetaiotaomicron VPI-5482] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| sp|Q5B7W2|MANBB_EMENI | 4.85e-270 | 607 | 1473 | 5 | 838 | Beta-mannosidase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=mndB PE=1 SV=2 |
| sp|A1D911|MANBB_NEOFI | 9.05e-268 | 611 | 1463 | 9 | 830 | Beta-mannosidase B OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=mndB PE=3 SV=1 |
| sp|Q4WAH4|MANBB_ASPFU | 1.28e-267 | 611 | 1463 | 9 | 830 | Beta-mannosidase B OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=mndB PE=3 SV=1 |
| sp|B0YBU9|MANBB_ASPFC | 5.06e-267 | 611 | 1463 | 9 | 830 | Beta-mannosidase B OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=mndB PE=3 SV=1 |
| sp|Q0CCA0|MANBB_ASPTN | 2.64e-266 | 611 | 1473 | 9 | 838 | Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 0.000249 | 0.999738 | CS pos: 17-18. Pr: 0.9751 |