ID G1X517_ARTOA Unreviewed; 805 AA.
AC G1X517;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=SH3 domain-containing protein {ECO:0000259|PROSITE:PS50002};
GN ORFNames=AOL_s00043g791 {ECO:0000313|EMBL:EGX51772.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX51772.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX51772.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
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:EGX51772.1}.
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DR EMBL; ADOT01000061; EGX51772.1; -; Genomic_DNA.
DR RefSeq; XP_011119579.1; XM_011121277.1.
DR AlphaFoldDB; G1X517; -.
DR STRING; 756982.G1X517; -.
DR GeneID; 22890542; -.
DR eggNOG; ENOG502QUK9; Eukaryota.
DR HOGENOM; CLU_349819_0_0_1; -.
DR InParanoid; G1X517; -.
DR OMA; YWNRNIC; -.
DR OrthoDB; 2600928at2759; -.
DR Proteomes; UP000008784; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd11856; SH3_p47phox_like; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR13847:SF129; FAD DEPENDENT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 458..535
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
SQ SEQUENCE 805 AA; 90050 MW; 78810DA9A1EDD8F8 CRC64;
MVSEHFPDPQ LPSEESTSSF WLKQPDEFLL GHRTTVELPT EADIIIIGSG IAGAQTARYL
SEQDGGAWVK GRKIVMLEAR EACWGATGRN GGHCKPSLYA YPRLQHLFDD LGISETLTAI
NFELRNLSLL TSYIQENGVD CDFHRLPSCD AYFDQESFSL AVHSIQTLRQ HAPELADKLT
IVTDKPTLAS LRIPSAVGAI TIKDAAKLWP YKLVAHILKD LIKSQYLNLQ TSTPVLAIST
LNDGAPVPLH RVHTPRGALT APVVIHATNA FASHLVPAMR DAIYPVRAQM SALTPPKSLI
SNPLKHTYGL VDGERSKAEY LVQEDVHANG TGGAFLLGGG RKYAKNQGVG ITDDNHIDTD
VGDYLRSSVG KYFDDECGYP VADKDTMCDA QYMWSGIMGF SADERPWVGK VPGTEGQYIL
AGFEGHGMAY TTGSAKALAE ILRHRYPVLP DEVYSKYWNR NICMALYDYE AQDTAEMENV
LVRGREVSIR AGDVVEIIEK GHNGWWFGCI IKSSDQSNVN TFGWFPSNFV EELPYGHARG
GFEPSMYASL QEYPKDIFQW FPRSFTVTEE RLKNARGILE SGDLETVRRR ARGPAIYSGN
EEKEEKLYKE MLYERYKLQF AVKLAECGKD EDNIFPTLES SALTNIEQKY LDAPAHIIRK
AKLAKPLKQL SKLSGTETHK IDQARVLSIL SKLSHSKDEE AGSTKEKERK ERNSAHKAEL
RAIIREKIKE MKKGSQDSQE KIMTACNKCQ RGEVIARDFA TETSSPLVKD LRASQTLERH
PLLRGLKTED NKEGEEWVMI VNEKR
//
