GenomeNet

Database: UniProt
Entry: V2X3N0_MONRO
LinkDB: V2X3N0_MONRO
Original site: V2X3N0_MONRO 
ID   V2X3N0_MONRO            Unreviewed;       552 AA.
AC   V2X3N0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   03-MAY-2023, entry version 34.
DE   SubName: Full=Ring finger domain protein {ECO:0000313|EMBL:ESK87396.1};
GN   ORFNames=Moror_11666 {ECO:0000313|EMBL:ESK87396.1};
OS   Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS   (Crinipellis roreri).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK87396.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK87396.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK87396.1,
RC   ECO:0000313|Proteomes:UP000017559};
RX   PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA   Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA   Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA   Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA   Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT   "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT   Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT   mechanisms of the biotrophic and necrotrophic phases.";
RL   BMC Genomics 15:164-164(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:ESK87396.1}.
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DR   EMBL; AWSO01000786; ESK87396.1; -; Genomic_DNA.
DR   RefSeq; XP_007853291.1; XM_007855100.1.
DR   AlphaFoldDB; V2X3N0; -.
DR   STRING; 1381753.V2X3N0; -.
DR   KEGG; mrr:Moror_11666; -.
DR   HOGENOM; CLU_030109_0_0_1; -.
DR   OrthoDB; 4593171at2759; -.
DR   Proteomes; UP000017559; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.5.340; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR047126; RNF141-like.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR12109:SF3; RING FINGER PROTEIN 141; 1.
DR   PANTHER; PTHR12109; RING FINGER PROTEIN 141-RELATED; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          211..274
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          297..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          136..201
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        30..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..389
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   552 AA;  62334 MW;  8B6C7BB3155DCCDC CRC64;
     MQIPLRRHKS KSPSRSAASR PVADPFSIAL ALPQSQSFPA PKRNSNPSMS IITMRSSALS
     TEELSDQGQK LKTSRSKAVA AAVPSPSSSG LSKPPTNSKK DKGKERHSHT HTHTHAPQSS
     KDELSEVMGY SGPIAAAEFE RMKKEIEELK GTVQEQKKTI KKQNKKIDEL KGEVASAKSL
     KKEQENQIQA LSSKVAKNDE LLKSIESNLN CQICMEIMNK PFALSPCGHV LCMSCLQDWF
     RKAPPTLDDM DIDPEDADDP EYLKYRQKSC PCCRAIILKR PAPVFVLKSV VNAVTKHKSD
     SHSSTSSSQR SNSPLVGEED PWEGLFPDEH EDDMIDEDDG YLRHYYGHDL YLEDSDSEGL
     ESIMIEVDSD AESVEDNGEG HHHEPEELSD AESLEDPLYV KPSWEPPVGT YTREELRHLP
     AQKAAMLIRG GTLWMIRALH MDYSHRDGFI VYLYGLDDVG QVPYDTMYRR SAEERQKRNL
     HRIFLGWNIR GAREGLIEEG GKEFMNQLLD SYTNEPWRFH VDERRGGKLD VHVLVQADDC
     VDYDTTDTEV YY
//
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