ID V2YST5_MONRO Unreviewed; 399 AA.
AC V2YST5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 13-SEP-2023, entry version 38.
DE SubName: Full=Pa2g4 protein {ECO:0000313|EMBL:ESK94714.1};
GN ORFNames=Moror_14273 {ECO:0000313|EMBL:ESK94714.1};
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:ESK94714.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK94714.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK94714.1,
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 -!- SIMILARITY: Belongs to the peptidase M24 family.
CC {ECO:0000256|ARBA:ARBA00007319}.
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:ESK94714.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AWSO01000123; ESK94714.1; -; Genomic_DNA.
DR RefSeq; XP_007845989.1; XM_007847798.1.
DR AlphaFoldDB; V2YST5; -.
DR STRING; 1381753.V2YST5; -.
DR KEGG; mrr:Moror_14273; -.
DR HOGENOM; CLU_041451_2_1_1; -.
DR OrthoDB; 1054240at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR CDD; cd01089; PA2G4-like; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR004545; PA2G4.
DR InterPro; IPR047113; PA2G4/ARX1.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR00495; crvDNA_42K; 1.
DR PANTHER; PTHR10804:SF11; PROLIFERATION-ASSOCIATED PROTEIN 2G4; 1.
DR PANTHER; PTHR10804; PROTEASE FAMILY M24 METHIONYL AMINOPEPTIDASE, AMINOPEPTIDASE P; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT DOMAIN 27..188
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT REGION 375..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 399 AA; 43626 MW; C93F42B740039CCF CRC64;
MSDSEKPAAA AADAKKPPVF AEADLTKYKT VADIVHNVMK KLIELAVDGA RILDLCIEGD
KLIEQGTGAV YNKAVKGNKV PKGLAFPTSI SVNNTVSHFS PLESDPQSSQ TLAKDDVVKI
HVGAHIDGFA AVSAETIVIG ASTENPVTGR RADVLKAAWH AAELAMRTVK VGNKNWAVTE
VVQKAAAAWD CKPVEGMLSC QQTQNVIDGK KRIILNPNEA QKRDFEAATF AEGEVYGIDI
LVSSDEDGKA RVEESRTTIY QRDSNVTYQL KMKTSRAVFS EVQKRAGAFP FNIRCLEDEK
RARMGLQEAV QHSLVKPYEV VYTPANTFVA AFHFTIALLP NGPSLITHPP IWYKPELVKT
EKELADEELK SLLSKPLREN KKSKKKKAKA EGGEDANED
//
