ID A0A0F7ZNN3_9HYPO Unreviewed; 943 AA.
AC A0A0F7ZNN3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HIM_06499 {ECO:0000313|EMBL:KJZ74050.1};
OS Hirsutella minnesotensis 3608.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Hirsutella.
OX NCBI_TaxID=1043627 {ECO:0000313|EMBL:KJZ74050.1, ECO:0000313|Proteomes:UP000054481};
RN [1] {ECO:0000313|EMBL:KJZ74050.1, ECO:0000313|Proteomes:UP000054481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3608 {ECO:0000313|EMBL:KJZ74050.1,
RC ECO:0000313|Proteomes:UP000054481};
RX PubMed=25359922; DOI=10.1093/gbe/evu241;
RA Lai Y., Liu K., Zhang X., Zhang X., Li K., Wang N., Shu C., Wu Y., Wang C.,
RA Bushley K.E., Xiang M., Liu X.;
RT "Comparative genomics and transcriptomics analyses reveal divergent
RT lifestyle features of nematode endoparasitic fungus Hirsutella
RT minnesotensis.";
RL Genome Biol. Evol. 6:3077-3093(2014).
CC -!- SIMILARITY: Belongs to the SH3RF family.
CC {ECO:0000256|ARBA:ARBA00008649}.
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DR EMBL; KQ030529; KJZ74050.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7ZNN3; -.
DR OrthoDB; 1462937at2759; -.
DR Proteomes; UP000054481; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054481};
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 16..71
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 880..941
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 96..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 237..264
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 122..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 943 AA; 105181 MW; DC83B7CC9B9EBDA9 CRC64;
MDPRKPSLDL EKELTCSICT ELLYQPLTLL DCLHTFCGAC LKEWFGFQAS SAEKSPSPPI
GTSIFTCPSC RSTVRDTRHN ATVVTLLDMF VAAQPGKART AAEREEMARK YQPGEQVLPK
IDARELTADE RRADEEDRRL LNEVRERSLQ EATAGPLHPP RSRRRTGSRS ADDRARHRRN
QSSDGHSRTD RDGRRRSPTE DSGRHSADVV TDERRQREWS DSWPRQVEHQ SSLRSLIEST
QLDQRDIEKE IEELARQIQE EGLLDGLDLD NIDLERDNEL SRRVTEAYRR RQRERSRQES
ARRANSGARL LDTADSGSRR RASSNGRADS RTRTGSRPAS GHGQPEDRSR PPPSNSSALD
VRDPARRARR RTSSGGRRAT TPVFSASEPR PAARSQTDLS SRPQQSSDPS TPRQIFDERR
SSSTPTVTAT SVPPSEAAAT GTSNASFADR APQWNPASGE PPANPVEAPD QQRETPVNQR
ESHSTQDMTP APLTRAARPS ELAIVHSAVG NPLSSPKPPG HQRTRSHLYP EPSIACARCN
KPHMEYDWHY NCAICLGGQW NICLDCYRAG KGCLYWFGFG HGAWNKWEKA RQSDESLARP
HQLTASRYLP PPSTPGGADG RKTLTTNDPR TRLETGTFCA RCFAWTNHCF WRCDVCNEGD
WGYCNNCVNQ GKSCSHMLLP LTHEPPQPSQ SASGRPRSPI SPDRPATAAI FSGPQASSMG
PFKPLTFKTR CDVCQDPISP SQVRYHCFNC TSVLVPDAPP GDYDICASCY CNLVDRGQIS
IENGHSGWRR CLNGHRMVVI GFVEGKVGQW RYVESDLVGG RVLRSEAFDG PEHQDQGLQI
WSWRQGKDTL RRLVTADVSA TAPTMTTSTS YTQAFPPDGG AGKRAYARWS WYPNAKADDE
LLFPKGAEVR EVEDVNGDWF FGTYMGSKGL FPAPYVRLAE QSQ
//
