ID V2Y9A4_MONRO Unreviewed; 319 AA.
AC V2Y9A4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=CCHC-type domain-containing protein {ECO:0000259|PROSITE:PS50158};
GN ORFNames=Moror_5466 {ECO:0000313|EMBL:ESK88259.1};
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:ESK88259.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK88259.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK88259.1,
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:ESK88259.1}.
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DR EMBL; AWSO01000673; ESK88259.1; -; Genomic_DNA.
DR RefSeq; XP_007852434.1; XM_007854243.1.
DR AlphaFoldDB; V2Y9A4; -.
DR KEGG; mrr:Moror_5466; -.
DR HOGENOM; CLU_000384_30_3_1; -.
DR OrthoDB; 1275937at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR032567; LDOC1-rel.
DR InterPro; IPR005162; Retrotrans_gag_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR15503:SF22; CCHC-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR15503; LDOC1 RELATED; 1.
DR Pfam; PF03732; Retrotrans_gag; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 256..271
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 319 AA; 36711 MW; 27913F89100FF9D2 CRC64;
MAEDKKPSGS RPRREEPAAE EAVIGSAMPV QVVSAVKEVK AALPRAFTGS RGEAKRFLRE
VLIYVALNPK AFPDDRSKKL FLLSYMTDGA GEFWKNDKAD LLLAFDPEAE KVTWSEFLDD
FRTSFEPLDP ALKAQLELKD LKMKERADEY TYQFIYLAKQ TGYNDAAQIV AFKRGLPKSL
VFKIMTRPEG APTTIKDWIN AAIIFDESYK QALEYGKTWD EEHGGKKQRS FRKKEDVAIK
QIGEIDRKEY MSKGLCFRCG RAGHRIRDCP DMPKKDEQKK EEPRKMTKEE RFAKIRALVN
DQPKEDKDFL IDLMEQEGF
//
