ID D4D865_TRIVH Unreviewed; 1004 AA.
AC D4D865;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=SH3 domain protein {ECO:0000313|EMBL:EFE41962.1};
GN ORFNames=TRV_03301 {ECO:0000313|EMBL:EFE41962.1};
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE41962.1, ECO:0000313|Proteomes:UP000008383};
RN [1] {ECO:0000313|Proteomes:UP000008383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
CC -!- SIMILARITY: Belongs to the SH3RF family.
CC {ECO:0000256|ARBA:ARBA00008649}.
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:EFE41962.1}.
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DR EMBL; ACYE01000169; EFE41962.1; -; Genomic_DNA.
DR RefSeq; XP_003022580.1; XM_003022534.1.
DR AlphaFoldDB; D4D865; -.
DR GeneID; 9581236; -.
DR KEGG; tve:TRV_03301; -.
DR HOGENOM; CLU_005224_1_0_1; -.
DR OrthoDB; 1462937at2759; -.
DR Proteomes; UP000008383; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR16079:SF4; E3 UBIQUITIN-PROTEIN LIGASE CHFR; 1.
DR PANTHER; PTHR16079; UBIQUITIN LIGASE PROTEIN CHFR; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 20..70
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 936..997
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 140..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1004 AA; 110578 MW; 3088E76FB0FC80CB CRC64;
MEKPKEGSSA LVDLGKELTC SICTEILYQP LTLLDCLHTF CGSCLKSWFS WQASNPTDGN
RPRFTCPSCR ASVRDTRHDA KVATLLDLFL QSNPDQVKSA EEKEEIASEY KHGDSVLPEV
GQIVRSASDD EDERLLAEVR DMSLRDVQGA SGSGSGSSGR RHRSPLAPRS RGRSERSPGA
QAREQRVEDA RRRRRAERRM NASPAMRNPR DMSPDSRRVE HQSSLRSLIG STGESAIEDE
ILRQIAEEGL LDGIDLHSLT PTQEDELTER IAQAFRRRHR VPSPTHISRR RESPSPAQPR
PVSQDRQQQQ PHQQERSPSA SASTPRAREP TRRAPPTSRP RLLEPLTAHH AANHRRSASD
QGTGTRRRRT SPTPPTGFSL SSEALAQPAA RTASGGSTAG SGAGSAAGSG PGAHSTGPSR
RRASNSSLPP TSLRNQAILP LQVNRSRRPS SPGERQRRRS PAAINPNGGN TAVEPPPPPP
AVATAPSVVS EITGIHTSNR RQASQSQSQP STPATATAAV NTPVTTSPPP GPIRRVSNPV
ILPSTVPPAQ MLPEPSISCE RCGKNNIQYE LHKVCKLCKS GNYCLCARCY RLGRGCLHWF
GFGHAAQYFF EKKMASLNKP LNEQEPPHKL TWRRYLRPPE ERVEQSSSSS HSPRSAHVPL
SRRVQMGMFC DMCERFTDEC FWKCRECNDG EWGFCNNCVN QDKCCTHPLL PISRVKVKPK
TDAQTSPRTT ASLPSSTEAA EYRPLTFSTQ CNVCTYPIPP STTRFHCIQC NEGDYDMCTN
CYLKLGASGK ISKENGRNGW RRCLQGHRMI IVGFEDHRVG QMRVVVQGLV GGHAWKDEHI
PTPSSGARRD TSNNSNTPTS PVSETNGTPG RIALQRQNSG RWTWTEPTDS SDSNFRQRRR
LNRARQHLSS GPESPSDSSS SSPFPLSTTR FPPSGGIGLR LIAKWSHHPE PDNNDEIMFP
RGAEITEAEN INDDWLWGCY AGQKGFLPGG YVLLIDEVGA DGLR
//
