ID A0A150V6S8_9PEZI Unreviewed; 833 AA.
AC A0A150V6S8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Glycoside hydrolase family 55 protein {ECO:0000313|EMBL:KYG46222.1};
GN ORFNames=M433DRAFT_65583 {ECO:0000313|EMBL:KYG46222.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG46222.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG46222.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG46222.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYG46222.1}.
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DR EMBL; JPDO01000125; KYG46222.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150V6S8; -.
DR STRING; 766039.A0A150V6S8; -.
DR Proteomes; UP000075602; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR PANTHER; PTHR31339; PECTIN LYASE-RELATED; 1.
DR PANTHER; PTHR31339:SF9; PLASMIN AND FIBRONECTIN-BINDING PROTEIN A; 1.
DR Pfam; PF12708; Pectate_lyase_3; 2.
DR SUPFAM; SSF51126; Pectin lyase-like; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KYG46222.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..833
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007571480"
FT DOMAIN 98..323
FT /note="Pectate lyase superfamily protein"
FT /evidence="ECO:0000259|Pfam:PF12708"
FT DOMAIN 452..639
FT /note="Pectate lyase superfamily protein"
FT /evidence="ECO:0000259|Pfam:PF12708"
SQ SEQUENCE 833 AA; 90863 MW; AE82F2086B15FF7D CRC64;
MQFYSFLVPS LVAIGGVSAQ HVHWQPAEVL QDVESQLQEF HHWTSYQGPS PTYWHHPSPQ
PTYTQPPSPS GTCAYWLDDI KHQGIAAFNP DPETYQVFRN VQDFGAKGDG VTDDTDAINL
AISSGNRCGP GTCASSTTTP AVVYFPPGVY MINDSIIDYY FTQIIGNPNC LPTIRAFPTF
HGALGLIDGD EYVAGGNLGF GSTNVFWRQI RNFIIDTTLV PATSAVTGIH WPTAQATSIQ
NVIFHLSEAN GTLHQGIFIE SGSGGFMNDL VFYGGRYGSV FGNQQFTMRN LTFYNAVTAI
SQIWDWGWTY KSISINNCSV GLDMSSGGPT AQSVGSVTFI DSEINDTPIG IITAHGPTSQ
PPSGGSLILE NVYLNNVPIA VQGEDNATAL PGTPANSHIA AWGEGHSYTP NGPQNFEGFI
NPVSRPSSLL QSDGKYYERS KPQYEQYPVS DFISARSMGA TGNGHTDDTA ALQAAIMAAK
FQNKILYVDQ GDYLISRTIY IPGGSRIVGE SYPVILSSGP FFNNMNRPQP VVMIGRPGEQ
GSIEWSDMIV STQGQQEGAI LFEYNLNSPS SAPSGIWDVH SRIGGFAGSD LQVAQCPTTP
NIVVTEENLN RSCIAAFMDI TFTQWSSGLY LENNWFWTAD HDVDNPDLTQ ISVFAGRGLL
DESQEGTFWL VGTAVEHHTK YQYQFADTKT VFAGQIQTET PYYQPNPSAP IPFPYVASLH
DPVFPEKTVV DGNVTIPNAD AWGLRIVDSS DILIYGAGLY SFFDNYSTTC SNEGNGEVCQ
NRIFEVIGSD SVNVYNLNTV GTHYMIELDG MNKAYYADNL NGFIDTVALF RTS
//
