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Database: UniProt
Entry: V2XWD2_MONRO
LinkDB: V2XWD2_MONRO
Original site: V2XWD2_MONRO 
ID   V2XWD2_MONRO            Unreviewed;       193 AA.
AC   V2XWD2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Myosin regulatory light polypeptide 9 {ECO:0000313|EMBL:ESK98082.1};
GN   ORFNames=Moror_408 {ECO:0000313|EMBL:ESK98082.1};
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:ESK98082.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK98082.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK98082.1,
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:ESK98082.1}.
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DR   EMBL; AWSO01000011; ESK98082.1; -; Genomic_DNA.
DR   RefSeq; XP_007842593.1; XM_007844402.1.
DR   AlphaFoldDB; V2XWD2; -.
DR   STRING; 1381753.V2XWD2; -.
DR   KEGG; mrr:Moror_408; -.
DR   HOGENOM; CLU_061288_9_2_1; -.
DR   OrthoDB; 312751at2759; -.
DR   Proteomes; UP000017559; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   PANTHER; PTHR23049; MYOSIN REGULATORY LIGHT CHAIN 2; 1.
DR   PANTHER; PTHR23049:SF34; MYOSIN REGULATORY LIGHT CHAIN SQH; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          38..73
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          115..150
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   193 AA;  22364 MW;  A23A18B98E49BAEC CRC64;
     MSRYPSHLSP SLPSTLTKSQ KSRARREPSG VFSLFQAPQI QQFKEAFQLI DHDKDGWVNE
     SDLREIFTSL GITPTKTQLD QLLSARPGDS TTSDARGINF TMFLTMMSER LFEFDTEPEL
     IEAFESFDEN DSGYVKVEDM RKWLSEVGDR MDDREIDRFL KGPFTDRQGN FNYREWVKVL
     RVNEDGEDGQ ITQ
//
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