ID V2XUV6_MONRO Unreviewed; 1226 AA.
AC V2XUV6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=Moror_7121 {ECO:0000313|EMBL:ESK96335.1};
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:ESK96335.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK96335.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK96335.1,
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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:ESK96335.1}.
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DR EMBL; AWSO01000050; ESK96335.1; -; Genomic_DNA.
DR RefSeq; XP_007844375.1; XM_007846184.1.
DR AlphaFoldDB; V2XUV6; -.
DR STRING; 1381753.V2XUV6; -.
DR KEGG; mrr:Moror_7121; -.
DR HOGENOM; CLU_007379_0_0_1; -.
DR OrthoDB; 1423507at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR46006:SF7; DH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46006; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR AT 64C, ISOFORM A; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT DOMAIN 134..483
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 959..1222
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 27..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1226 AA; 135755 MW; DC1310A1FEBDB967 CRC64;
MKTLFRLGGT KEKDKDLSSL SRQWMEIPAW PPPSTSVPHR DPSIKPLPDI PDAIGPEESE
STPGPSTSSS KPPTPPGLGS ARIDVGNSKA SSTRTASPYS QMSNTRGGEF LSATGWSEVA
DEDLVFNVGS QERTRQEALF EIVYNEERYV QELAKMKETF INPLLHPSSS SGAVSPISPS
SNFNYRDDLY HSESSSESTD QLPPIAARFL APAPSQTSRH KHPRSPYRRL IGNGTTTVPF
PSRSHHSLPP PPRSNQLNSS TESLGKQSTL VEHSSQSDHQ QDRNYNQGRS TVGKEKGMLH
EPKKSDTKNA VLGDTVAMHQ LPEDLRICLE AIDNGVFDGH KRLSEALRER YDEQFPLVRS
LADVFVANSD IFQGYTTYFR HLERALEQVD AALSNVLTKK PHNQGMAEWQ KVCSLLQRLE
ETACEKGESG LTVALCKPFQ RLFKYPLLIQ NVLFHTNPST SEYDSMLQVV AKVESIARSI
EDEKIEKEER DKTRDVLARI EGLHRVRQLA APKPSRILIE ERQYPSTTES STKGGLPQQG
TRGKSSFKRL SDVLSAENMR LGAKKDLWLV AFNDVVLLCQ RVGTTSLPLV AAMDSRTPEV
QGRTLYATTG RRYSHTKPRN LYKFIKIETW VIGGVARLRE GVVLMEDVVR SRTQVGEAQP
RILPTPDDDE DDDSGADSDF STKARISSSY WGADKVTIQK PPIKPRATNA RGGGGPNYSR
ESSANAKFGT RLVSGGHSGT TPRPASRRTA ATPTSSNTVN PTGPRPDWNS NTSAATSRRA
IALPMPKRPR NTSQTSAATR TIGTAANISL SIPSEDHGVG LYRAILNEED HIGNTTMQSG
RNPPKHDILG HTSNPVEMSK TLSAPSSTNP SRSTTPDNGG MIDTVQDLQA LLVLRDPMKA
LLSLDFTVPD SLTHIQRLTQ EASSRINSRY RKLCLRCLLV LVKKHHILPE SLFLKHITRE
GTHPLRGGGF SDIWRGIFKK QSVCLKVMRT HLEANERKRN KVVAAFCKEA LVWTQLNHPN
VLPLLGVDTE LFQPALCLVS PWMWNGDIIT YLEEHPDHDR LRSVYEIASG LAYLHSLEPM
VIHGDIKGAN ILVDDLCSCR LSDFGLAAIK ESQRIASTTS GGPKGTMRWM APELFQPEAN
GKTDNSPKDV YAYACTVLEI MTGKPPFPDL LDAAIILKVI TGERPSRPSD VWCPDKVWDL
VERCWSHNPS ERPRAAEIER YLVSKG
//
