ID A0A1L7X208_9HELO Unreviewed; 994 AA.
AC A0A1L7X208;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Related to vesicular transport-associated repeat protein Tb-291 {ECO:0000313|EMBL:CZR59061.1};
GN ORFNames=PAC_08953 {ECO:0000313|EMBL:CZR59061.1};
OS Phialocephala subalpina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Mollisiaceae; Phialocephala;
OC Phialocephala fortinii species complex.
OX NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR59061.1, ECO:0000313|Proteomes:UP000184330};
RN [1] {ECO:0000313|EMBL:CZR59061.1, ECO:0000313|Proteomes:UP000184330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR59061.1,
RC ECO:0000313|Proteomes:UP000184330};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SH3RF family.
CC {ECO:0000256|ARBA:ARBA00008649}.
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DR EMBL; FJOG01000013; CZR59061.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L7X208; -.
DR STRING; 576137.A0A1L7X208; -.
DR OrthoDB; 1462937at2759; -.
DR Proteomes; UP000184330; 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; 3.30.60.90; -; 1.
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 InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR16079:SF4; E3 UBIQUITIN-PROTEIN LIGASE CHFR; 1.
DR PANTHER; PTHR16079; UBIQUITIN LIGASE PROTEIN CHFR; 1.
DR Pfam; PF00018; SH3_1; 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 Reference proteome {ECO:0000313|Proteomes:UP000184330};
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 9..65
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 932..993
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 88..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 994 AA; 110366 MW; 0E96F1927038B5E7 CRC64;
MDLEKELTCS ICTEVLYQPL TLLDCLHTFC GSCLKEWFSW QLTSARNNPN SLPAGSTPYT
CPSCRAPVRD TKHNATVTTL VDMIVAASPE KGKSDEEKEE LKSKYAPGEN VLPKVEEREK
TLRERRVEDA DRRLMNEVRD LSLREVGVES PEARRERRRR EESRSQGTRA PRSRDPSRDS
RSTDERDRER RRRREAERQG SGSNGALQPE PESTDDRRRR RSAERRSRND EPTRTAARQI
EHQSSLRSLI SASDVDSREM EEEILRQIRE EGLLDGIDLE NIDVSEQDQI SERIAEAFRR
RQSERARQEP ARRSNTSATS AISTVSAVST AGAVGGEQRR RRTHSSAPDS REHSGDDSVR
PSSRRQRAHS RSPSSASQDQ PSRPPQSMSA VQAAHLEVQS GDEGRHRRRR TGSSSRSATT
PTPVAETLAR PAARSQTDLS NRPQSAILTS TRPSVSASAR STTDPIVAQA AELPAPQSRS
RASSNSSPRL RSAARMEDST ISTAMTERRT RAPPENIFVP VAGPSVISSP TTDQSLMPAP
LSPRNPPHSG SLSDRAHALS SGSRPTSSGS IASRNRLQLY PEPSITCNRC AKPHIEYELH
YNCGICHNGN WNICLSCYRS GAGCLHWFGF GQAAWAKWEK LSQGGEPIER PHMLTGSRYL
PPKIIPGGAE GRRTLTTDDP QKRLQSGTFC ASCLAWTNEC YWRCDLCNEG DWGFCNVCVN
QGNSCSHPLL PLTYKPAETN TPPLSPTHDH RTPASASILT GPGVMDIGPF KPLTFSTKCD
NCHHPIQPSQ SRYHCFSCVS KVPDTLPGDY DVCTTCYSNL IKARRISAEN GQNGWRRCLQ
GHRMIIIGFE DNRGGQRRVI VQDLVGGRGL SEQPSTHTDH SGTELQKWSW GDGVHIRGDD
THMKLVTKDV MKTAPSSSPE LVLDAAFPPD GGVGMLAVAL WPWWPTPDAD DELMFPKGAE
VKECKNVNDD WWHGTYMGKR GLFPAPYVKT LDKI
//
