ID A0A0B2WKW6_METAS Unreviewed; 687 AA.
AC A0A0B2WKW6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=RING finger protein {ECO:0000313|EMBL:KHN94132.1};
GN ORFNames=MAM_07972 {ECO:0000313|EMBL:KHN94132.1};
OS Metarhizium album (strain ARSEF 1941).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1081103 {ECO:0000313|EMBL:KHN94132.1, ECO:0000313|Proteomes:UP000030816};
RN [1] {ECO:0000313|EMBL:KHN94132.1, ECO:0000313|Proteomes:UP000030816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 1941 {ECO:0000313|EMBL:KHN94132.1,
RC ECO:0000313|Proteomes:UP000030816};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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:KHN94132.1}.
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DR EMBL; AZHE01000040; KHN94132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2WKW6; -.
DR STRING; 1081103.A0A0B2WKW6; -.
DR HOGENOM; CLU_021364_3_0_1; -.
DR OrthoDB; 4338126at2759; -.
DR Proteomes; UP000030816; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20354; Rcat_RBR_RNF14; 1.
DR CDD; cd23134; RING-HC_ITT1-like; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR047548; Rcat_RBR_RNF14.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR11685:SF457; TRANSLATION TERMINATION INHIBITOR PROTEIN ITT1; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF05773; RWD; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS50908; RWD; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030816};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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 13..167
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 202..481
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 206..251
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 520..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..534
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..580
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 687 AA; 74287 MW; C51EF8A18456E75A CRC64;
MDTAGDDDDP RLMELETLEA IYPEIRHALA HPLGAPGEAP PRFTFELELP VDPAEPVTIL
FPAPSSGLAP DERPGLASAS APAAMAAEPL DSLLVSHLPP LSLRITLPDG YPSRKPPAVT
ISTTPQWLPR ATLRALEDDG ARLWEEAGRD MVAYAYIDHL QRGAENVFGA VGTGSTLEVD
AEHKLAVLDH DINAKKAAFD RETFECGICL DPKKGPRCHK MMDCGHIFCL QCLRDFYADA
IEEGNLSAVR CVTPNCARAR ATSSPSTSAA KGKPKVFISP SELLQIGLPE DLVKRYVTLK
YKTELEADKN TVYCPRRWCN GAARSKRHRK PQGLEFAESS GDETPGTVTE DGAAHHVGEK
TSAKKFDAAD LLAVCEDCGF AFCSRCLHTW HGEFVRCAPK RNNGELAEEE KASLEYLQLH
TSPCPTCNAH AQKTHGCNHM ICSRCDTHFC YLCSAWLDPA NPYKHFNTQS DGKVTSCYMR
LWELEAGDGD DVGLGYAGGR EAGGVPVGGE HLAGIVPEVE EPESDDDSGS DNEADNEAAL
EANPRAVAVA REAPLVLRLM DNQPPQPPPP PPPPPRPAPA ARGRGQAHHR PQGRGRAQHH
HPVPQGAPHR RGPPAPRAAR GHHHGAGRGN AAQQDAREAG VPNAQPGALD PAQEAWVRRF
VQLALLDVED QVEGGDSDSD DGNWQIR
//
