ID V2Z160_MONRO Unreviewed; 692 AA.
AC V2Z160;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Protein kinase regulator {ECO:0000313|EMBL:ESK97684.1};
GN ORFNames=Moror_17391 {ECO:0000313|EMBL:ESK97684.1};
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:ESK97684.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK97684.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK97684.1,
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm,
CC cytoskeleton, actin patch {ECO:0000256|ARBA:ARBA00004134}. Endosome
CC membrane {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004125}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
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:ESK97684.1}.
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DR EMBL; AWSO01000019; ESK97684.1; -; Genomic_DNA.
DR RefSeq; XP_007842964.1; XM_007844773.1.
DR AlphaFoldDB; V2Z160; -.
DR STRING; 1381753.V2Z160; -.
DR KEGG; mrr:Moror_17391; -.
DR HOGENOM; CLU_016105_0_0_1; -.
DR OrthoDB; 1423392at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd01786; RA_STE50; 1.
DR CDD; cd00174; SH3; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR PANTHER; PTHR15735:SF20; PROTEIN NERVOUS WRECK; 1.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00536; SAM_1; 1.
DR Pfam; PF00018; SH3_1; 2.
DR SMART; SM00314; RA; 1.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ESK97684.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000313|EMBL:ESK97684.1}.
FT DOMAIN 10..73
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 251..328
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 477..557
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 596..656
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 136..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 98..132
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 136..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..216
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 692 AA; 75253 MW; 064C0EEC08153D56 CRC64;
MAMDRNLMDW DEADVHKWLT SIGYAQYETN IKEHRISGDI LCMLDQETLK GVGVSTVGQR
LAILKAVYNL KIQYNIPIDS DSYVPPSEAQ EKAQELTVER LHSMLSDQAQ RLRVLEEENK
ILNSTLQSFL DDYNSLRSSL SSPPQDASSP PLRRQHSFKW AQYVKPNKSP TKPISDSNDS
PHPSPQQLEH DIPPYTRQTP RQPPQAPPPL PPPPASSSST NTATDSSPTP TAITPTPKPT
ATRQDSSDNL KSFKVSLEDP TYKVLPAALK KYRINNDNWE NYAMFICYGS PGNRIERCLS
YDEKPLLLFQ KLKDAKKNPV FMLKHIKDIR SPIVVAQQKH AARKASSTIS AGDQAPSNTA
TTTTTSATTT TQKSTHTPSR SITRPPKLEV HDLSNNVPSG LHSAAPISGS GNGAWPDVGV
GSPVNEQQPG LATPNPNTSA PTQTPNSAAT ATPTSNPNPN SNTSTRDPLP TTSPSPGTIS
YAVAIYPYMA EQADEFDVVV GDTFIILSRA RGWWVVQRDP EGTGVLSDST TAAASEGEEN
AGKQGWVPAG CLLETMKPVA VAIREAREAR GGSVSEEVDS GGGDGKNPIL PLSIISTSFP
GIALMDYKKK GEEELDLVKD DTLRVFKRYN HWSYAVKEDG GDRGWVPSWF IGKVANTYNQ
GSMSNSGLST HLDSSETAPP QVSPMSSAFP VR
//
