ID V2XNZ7_MONRO Unreviewed; 403 AA.
AC V2XNZ7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=CCHC-type domain-containing protein {ECO:0000259|PROSITE:PS50158};
GN ORFNames=Moror_12742 {ECO:0000313|EMBL:ESK95472.1};
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:ESK95472.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK95472.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK95472.1,
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:ESK95472.1}.
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DR EMBL; AWSO01000077; ESK95472.1; -; Genomic_DNA.
DR RefSeq; XP_007845217.1; XM_007847026.1.
DR AlphaFoldDB; V2XNZ7; -.
DR KEGG; mrr:Moror_12742; -.
DR HOGENOM; CLU_000384_30_12_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 InterPro; IPR032567; LDOC1-rel.
DR InterPro; IPR005162; Retrotrans_gag_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR PANTHER; PTHR15503:SF22; CCHC-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR15503; LDOC1 RELATED; 1.
DR Pfam; PF03732; Retrotrans_gag; 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 340..355
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 403 AA; 46503 MW; D6F3B4C5BDC5A78C CRC64;
MSQPLTETPE EDPGTRRTLT PSSISTGSRP TEFEERFSPS TPKPPESDTL NTSTNSPEEL
DLFQRLLQGL KNSPRSPKTQ LEVMAKDKKP SGSRLKREEL VVEEAVIGSA MPVQVVSAVK
EVKAALLRAF TGTWKDAKKF LREVLIYVAL NPKVFPDDRS KKLFLLLYMT HGPGEFWKND
KTDLLLAFNP DAEKVTWSEF LDDFRTSFEP LDPALKAQLE LKDLRMKDRA NEYMYQFTYL
AKQTGYNDAA QIVAFKRGLP RSLALKIMTR PEGAPTTIKD WMNTAILFDE SYKEALEYGK
TWDDEHGGRK PQRNFRKKED VAIKQIVDVD WKEYMAKGLC FRCGRNRHCI KDCPDMPKKE
EKKQEEPKKL SREERFTKIR ALVNEQLKED KDFLLDLMEQ EGF
//
