ID A0A0D9NLW2_METAN Unreviewed; 826 AA.
AC A0A0D9NLW2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=H634G_09677 {ECO:0000313|EMBL:KJK75042.1};
OS Metarhizium anisopliae BRIP 53293.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1291518 {ECO:0000313|EMBL:KJK75042.1, ECO:0000313|Proteomes:UP000054544};
RN [1] {ECO:0000313|Proteomes:UP000054544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRIP 53293 {ECO:0000313|Proteomes:UP000054544};
RX PubMed=25102932; DOI=10.1186/1471-2164-15-660;
RA Pattemore J.A., Hane J.K., Williams A.H., Wilson B.A., Stodart B.J.,
RA Ash G.J.;
RT "The genome sequence of the biocontrol fungus Metarhizium anisopliae and
RT comparative genomics of Metarhizium species.";
RL BMC Genomics 15:660-660(2014).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; KE384752; KJK75042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D9NLW2; -.
DR STRING; 1291518.A0A0D9NLW2; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000054544; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProt.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR024766; Znf_RING_H2.
DR PANTHER; PTHR22763; RING ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR22763:SF165; TRANSMEMBRANE E3 UBIQUITIN-PROTEIN LIGASE 1; 1.
DR Pfam; PF12678; zf-rbx1; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000054544};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..826
FT /note="RING-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002341369"
FT TRANSMEM 448..471
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 477..498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 592..610
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 616..634
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 646..666
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 678..697
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 762..820
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 505..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 826 AA; 91772 MW; 22277F79A0A1EB21 CRC64;
MPSPAQSPAG AVLFILFLVW MLFPEGDYRS QSLALSDLAV DRLARYRDAL HVLNTTRWGD
FAPQNKTTDD GREAKHLNLT GFRETDGFAW DDLETFRQKG LKLSRHAVPP VDGHQLWDVA
QGEAMWTNAS GTVHGDWVRK PGSVSRGYDS YNLSRSVPEV EWMAHKVEWA RNVTGNAGRM
MLRLSGNKTL THYEQLSMDM APLSGGIIRS LRGTATIEDT IGSGLNWEMK LWGVHWPRQG
VILMTTTSEK FEGIFALPHL SPGPDFFQSS QMLLNQTLAR VIRRKEKHVY VDQRMPWNSD
IENPMYTAYP SPHCEYVMYA QVHPPIPPKP TEGQDAAPGA VGDTINAIES ELQYPVGAPI
PRIPKLKMSA VVYSPDCSFF LETKGPPDYP PSEADHLVGM KKEVQTHQIK TWLLLYALVV
FGQVRLLRDQ MKESFTPSTM GRISFGTISA MLIVDGMTFT AAATWVSSAA ATFLPTLALM
FASFLSMTIG GSFLAKIYEV QLPESRGRRD QSSSSTTTAQ DSSANSIGAT PAPGLLPGPV
TASQRVETPI IIPSDQDISA EIAAAASAIP TANRSSPSTP ETPTFQAIIG RFILFSLCVS
FLAISSSTWY PRPRSVFLNT CAFIYLSMWT PQIYRNTLRN CRRALAWPFV LGQSVLRLLP
IAYFWVKEDN FLYATTDVPA FVFLAGWVWI QVVVLAAQQI VGPRFGVPLS WTPDAWDYHP
VLREDNLEGG GLPIGLVVPE ERNSLDRALA GPEKTGVRHI DCAICREVLE VPVVKAGEEE
SSVSGVFARR MYMVTPCRHI FHTACLESWL RFRLQCPICR DELPPI
//
