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Database: UniProt
Entry: F6H2Q8_VITVI
LinkDB: F6H2Q8_VITVI
Original site: F6H2Q8_VITVI 
ID   F6H2Q8_VITVI            Unreviewed;       597 AA.
AC   F6H2Q8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=VIT_00s0125g00210 {ECO:0000313|EMBL:CCB46500.1};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   EMBL; FN595230; CCB46500.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6H2Q8; -.
DR   PaxDb; 29760-VIT_00s0125g00210-t01; -.
DR   eggNOG; ENOG502QUW9; Eukaryota.
DR   HOGENOM; CLU_000288_114_5_1; -.
DR   InParanoid; F6H2Q8; -.
DR   Proteomes; UP000009183; Unassembled WGS sequence, unordered.
DR   ExpressionAtlas; F6H2Q8; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR021720; Malectin_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR48006; LEUCINE-RICH REPEAT-CONTAINING PROTEIN DDB_G0281931-RELATED; 1.
DR   PANTHER; PTHR48006:SF34; OS08G0203400 PROTEIN; 1.
DR   Pfam; PF11721; Malectin; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        212..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          269..543
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          573..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   597 AA;  65090 MW;  DC97935FD40BBADF CRC64;
     MLSCTHVTDT SFAIKCGGSE VTTSDGTVYE ADNSISGTAP TSFYVSRTEK WGVSNVGLFV
     DKIANTSLVT GTNTPELFKT SRISPGSLRY YGMGLENGPY IVSLQFAEMI LKDPSTKTWE
     STGRRVFDIY IQGILQLGDF DISKEAGGVQ KAIEKKFNAT VSENYLEIHL FWAGKGTCCI
     PYDGYYGPSI SALSVVSASE RTIPPEKGKT GLIAGIAIAA GILSLIVISA VFYIKRKGSD
     MNEDIELPEI GPRPSTFSYA ELRTATENFN AINKLGEGGF GAVYKGTLSD GRVVAVKQLS
     LASQHGKSQF IAEIATISAV QHRNLVKLYG FCIKGNKRLL VYEYLENKSL DHSLFGKNDL
     HLDWPTRFSI GLATARGLAY LHEESRPRII HRDVKASNIL LDAELCPKIS DFGLAKLYDD
     KKTHISTRVA GTIGYLAPEY AMRGHLTEKA DVFGFGVVAL EIVSGRPNYD NSLEAEKMYL
     LEWAWTLHEN NRSLDLVDPK LTTFDENEAA RVIGVALLCI QASPALRPTM SRVVAMLAGD
     IEVSTVASKP GYLTDWDFKD ITTSFLSDDT QTSVASTSTS YPAPTPVNLS EPMLSAP
//
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