ID A0A1S3VJC3_VIGRR Unreviewed; 639 AA.
AC A0A1S3VJC3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 2.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Cold-responsive protein kinase 1-like {ECO:0000313|RefSeq:XP_014518199.2};
GN Name=LOC106775567 {ECO:0000313|RefSeq:XP_014518199.2};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
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; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014518199.2};
RN [1] {ECO:0000313|RefSeq:XP_014518199.2}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014518199.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR RefSeq; XP_014518199.2; XM_014662713.2.
DR KEGG; vra:106775567; -.
DR OrthoDB; 393015at2759; -.
DR Proteomes; UP000087766; Chromosome 10.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.30.430.20; Gnk2 domain, C-X8-C-X2-C motif; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47973; CYSTEINE-RICH RECEPTOR-LIKE PROTEIN KINASE 3; 1.
DR PANTHER; PTHR47973:SF23; CYSTEINE-RICH RLK (RECEPTOR-LIKE KINASE) PROTEIN; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF01657; Stress-antifung; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51473; GNK2; 2.
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_014518199.2};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000087766};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..639
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018324409"
FT TRANSMEM 261..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..130
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 135..239
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 319..607
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 639 AA; 70936 MW; CD53ED1E9D7C7224 CRC64;
MMFEVKLIIL TMMLWIAEHG AKGDPQTYLV NTGCSTYNAS NVESFYANIN ATFSNLRREI
SNNSKHFGTT QQAIGDVLTY AMFQCRNYLS KNDCLSCFNT ASTQIRNCSQ ANGARVIYDG
CFLRYESQMF FDQTNELGKG VLCGKNTSNA TGFGLVGRQV IADIQTATPK TRDFYAATKT
QVANGTAIYA VAQCVETATE DKCLSCMQAG YNNLQSCLPN TEGRAYDAGC FMRYSTTPFF
ADNQTIDIAP YLKKGDSSRK WIIIAASVGA VVALLCVLFA WRWFIKPKRA PRGDILGATE
LKGPVNYKYN DLKAATKKFS AENKLGEGGF GDVYKGTLKN GKVVAVKKLV LGKSSKMEDD
FEGEVKLISN VHHRNLVRLL GCCSKGQERI LVYEYMANSS LDKFLFGNRK GSLSWKQRYD
IILGTXRGLA YLHEEFHVSI IHRDIKTSNI LLDDDLQPKI ADFGLARLLP EDRSHLSTRF
XGTLGYTAPE YAIHGQLSEK ADTYSYGIVV LEIVSGQKST DVKDDEDGRE YLLQRTWKLY
ERGMHLELVD KAIDPNDYDA EDVKKIIEIA LLCTQASAAT RPTMSEVVVL LKSKSLVENL
RPTMPVFVET NMKIRESKSS STSGSSSNAT ASISVLSAR
//
