ID A0A0D1ZSC6_9EURO Unreviewed; 963 AA.
AC A0A0D1ZSC6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV08_05777 {ECO:0000313|EMBL:KIW15727.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW15727.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW15727.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW15727.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SH3RF family.
CC {ECO:0000256|ARBA:ARBA00008649}.
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DR EMBL; KN847495; KIW15727.1; -; Genomic_DNA.
DR RefSeq; XP_016235943.1; XM_016380116.1.
DR AlphaFoldDB; A0A0D1ZSC6; -.
DR STRING; 91928.A0A0D1ZSC6; -.
DR GeneID; 27332860; -.
DR VEuPathDB; FungiDB:PV08_05777; -.
DR HOGENOM; CLU_005224_1_0_1; -.
DR OrthoDB; 1462937at2759; -.
DR Proteomes; UP000053328; 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; 1.
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:UP000053328};
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 21..75
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 899..962
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 101..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 963 AA; 105678 MW; 1C77649F13528E86 CRC64;
MAAAAVPSST GLLNLEKELV CFICTEILYQ PLTLLDCLHT FCGSCLKEWF SHQHRKALHS
HSSSSAAAYT CPTCRAVVKD VQHNAMINTL LEMFLAANPE KDRSQEEKAE MAQAYKPGDD
ILPKIDGHRR RERRRREEEN VSHDRRGQDD RSRREQQLHP SSADTRRGPR SSSGSTTTRE
RRPRSDSSRN SDRTGRHQRQ SSVDAVGSRA RSGDNTSTED VPSSSPALGS PRHPDAVEAR
QRGARTVAHQ ASLISIVSAS ESGTGTGESL NEAQVMQEIL AAGLLDGINI DDLTEAEQDE
LSEMIAERYR QLHPERLRRA PSNGVASNGQ GPTSGRSEEQ REEVGRRPRA VSSSSQRQQT
HPSPRTSRSV VISSPAIRPP TSFPQSTTDP VLPTFQDRAH RRRASNESGR SEQSATRTGR
RSATDLAERP QSSSTALERP RQLANTNRAN TEPRTHPRAS EMWQATGRQV ASPPQTGSPA
SQSPRIVMSS VNTGPVPTTI PSSEPSIPAI PATATSTGHT EPSVTCARCS RRRIQYEVHK
HCSSCNLDLC MSCYRIGRGC NHWFGFGHAA MFKFDSSHPA RPGQAIELPH LLIGRQYQRP
SVFQELSLRN STQTSLDTSS PNSRLLEGNF CDRCGAFANE CFWSCDYCND GEWGFCNDCV
NTNHCCSHPL LPVAHKSTVP NVAPRLNPST QPGAPTLSPF SAVGGAPSPA HSAPSSATST
TGFGADVRLD FVPLVITTNC DICLRPIPPD DLRYHCPEHV TPSPENSDQK GDYDLCQSCY
LSFVKSGRIK HEDGPDGWRL CPEGHRMIAV VFEMDADGGQ RRIIRSDVVG GTKMTGADMA
AWKLARANLH ETPSADLAVN SSTTRGKWTW REDTTSTRRA TRARTARLSA PADFPPNGGI
GKICRALWSY YPEEGEEGKG ELMFPRHAEV SEIEEVNEDW WFGVYAGDMG YCPAAYLRDI
ASG
//
