ID V7BC98_PHAVU Unreviewed; 1072 AA.
AC V7BC98;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESW15175.1};
GN ORFNames=PHAVU_007G050300g {ECO:0000313|EMBL:ESW15175.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW15175.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; CM002294; ESW15175.1; -; Genomic_DNA.
DR RefSeq; XP_007143181.1; XM_007143119.1.
DR AlphaFoldDB; V7BC98; -.
DR EnsemblPlants; ESW15175; ESW15175; PHAVU_007G050300g.
DR GeneID; 18624921; -.
DR Gramene; ESW15175; ESW15175; PHAVU_007G050300g.
DR KEGG; pvu:PHAVU_007G050300g; -.
DR eggNOG; ENOG502QWDY; Eukaryota.
DR OMA; IRYEQYL; -.
DR OrthoDB; 899613at2759; -.
DR Proteomes; UP000000226; Chromosome 7.
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; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.430.20; Gnk2 domain, C-X8-C-X2-C motif; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR002902; GNK2.
DR InterPro; IPR038408; GNK2_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; PTHR27002:SF589; CYSTEINE-RICH RECEPTOR-KINASE-LIKE PROTEIN; 1.
DR PANTHER; PTHR27002; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD1-8; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF01657; Stress-antifung; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS51473; GNK2; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000226};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1072
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004754757"
FT TRANSMEM 278..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..135
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 140..249
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 338..592
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 570..673
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 679..787
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 848..1072
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1072 AA; 119671 MW; 13120A2049E5D7C2 CRC64;
MIIFNSNCFI SFLLLSLLGS LTPLTSATPK YNDIYCPKNA SYQSNTTTFQ TNLNVLFASL
TSNATQGVVS YTTTMGFGST NAVNGLFLCR ADLFSATSND CVATAVTEIR RRCPNQTESI
IWYDECMVRY TDRYFSPTSV VPRANLWDDK NISTSDWGSF NQTLSSLLSG LATKAAGSQS
ASKFAIGEMN FTATSRVYGL AQCASGMTNA QCEACLVNAS ITLGTCCQGK QGARALLAWC
DIRYDLYQFY NTSIASSPVP SPPPPPSEKK KSGSQRTIII VVVAVAATIL VFSGGYFLVR
RSRRNYKTLL KENFGDDSAT LESLQFSLAT IEVATKKFSY ENKIGRGGFG EVYKGILLDG
RHIAVKKLSH TSRQGVLEFK NEILLIAKLQ HRNLVTLIGF CLENQEKILI YEYFFDYIFT
DSHKTRLLSW IERYKIIQGI AQGILYLHDH SRLKVIHRDL KSSNVLLDNN MNPKISDFGI
ARIIALEQDQ GSTNRIVGTY GYMSPEYAMH GQFSEKSDVY SYGVIVLEII SSKKNSCSLL
SDDVDDLLSD AWRYWRDETP LKILDQNIEE SSNHNEVLKC IQIGLLTYHN NLNALLSNLS
SNTDIDYGFY NFSYGQDSST VNAIGLCRGD VKPDACRRCL NDSKVLLTQL CPNQKEAIGW
YDQCMLRYSN RSLFNTMETS HSFALWNPGN ASDIDQFNLV LGNLLDSLIG QATTLGDSQR
KFAAANVSES VFQTIYGLVQ CTPDLSEQDC SECLTGAISE IPQCCDGKRG GRILRPSCNF
RYEIYRFYDL TDVKIPPAPA PAPKVSVLPP LSTDTLSTEV QVENDDEIRS SETLQLDFST
IMTATNNFSD ANRLGQGGFG PVYKGKLSNG QDVAVKRLCK NSLQGDIEFK NEVMLVAKLQ
HRNLVKLIGF CLERRERLLV YEFVPNKSLD FFIFEYVFRG QFSVKSDVYS FGVLVLEIVT
DQKNSWACRG ENEGDLLTYT WQNWREGTVS NIIDPTIIDS SRNEIMRFIH IALLCVQEKV
TDRPTMASVV LMLSSYSVSL PLPSKPAFSV RSRNVSVIQS EEYDPVSGNS IN
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