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Database: UniProt
Entry: Q9AYP5_BRACM
LinkDB: Q9AYP5_BRACM
Original site: Q9AYP5_BRACM 
ID   Q9AYP5_BRACM            Unreviewed;       827 AA.
AC   Q9AYP5;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE   Flags: Fragment;
GN   Name=SRK22 {ECO:0000313|EMBL:BAB21001.1};
OS   Brassica campestris (Field mustard).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3711 {ECO:0000313|EMBL:BAB21001.1};
RN   [1] {ECO:0000313|EMBL:BAB21001.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=9649545;
RA   Hatakeyama K., Takasaki T., Watanabe M., Hinata K.;
RT   "Molecular characterization of S locus genes, SLG and SRK, in a pollen-
RT   recessive self-incompatibility haplotype of Brassica rapa L.";
RL   Genetics 149:1587-1597(1998).
RN   [2] {ECO:0000313|EMBL:BAB21001.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Hatakeyama K., Takasaki T., Watanabe M., Hinata K.;
RT   "Molecular characterization of SLG and SRK in an S22 haplotype of self-
RT   incompatible Brassica rapa L.";
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
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; AB054061; BAB21001.1; -; mRNA.
DR   AlphaFoldDB; Q9AYP5; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0060320; P:rejection of self pollen; IEA:UniProtKB-KW.
DR   CDD; cd00028; B_lectin; 1.
DR   CDD; cd01098; PAN_AP_plant; 1.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.90.10.10; Bulb-type lectin domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001480; Bulb-type_lectin_dom.
DR   InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR003609; Pan_app.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR022126; S-locus_recpt_kinase.
DR   InterPro; IPR021820; S-locus_recpt_kinase_C.
DR   InterPro; IPR000858; S_locus_glycoprot_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR024171; SRK-like_kinase.
DR   PANTHER; PTHR32444; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR32444:SF231; S GLYCOPROTEIN; 1.
DR   Pfam; PF01453; B_lectin; 1.
DR   Pfam; PF11883; DUF3403; 1.
DR   Pfam; PF12398; DUF3660; 1.
DR   Pfam; PF08276; PAN_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00954; S_locus_glycop; 1.
DR   PIRSF; PIRSF000641; SRK; 1.
DR   SMART; SM00108; B_lectin; 1.
DR   SMART; SM00473; PAN_AP; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50927; BULB_LECTIN; 1.
DR   PROSITE; PS50948; PAN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000313|EMBL:BAB21001.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000313|EMBL:BAB21001.1};
KW   Self-incompatibility {ECO:0000256|ARBA:ARBA00022471};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000313|EMBL:BAB21001.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        417..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          5..127
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          323..403
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          499..781
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAB21001.1"
SQ   SEQUENCE   827 AA;  94486 MW;  70E5C1A62089195E CRC64;
     IYFNTLSSTE TLTISSNRTL VSPGDVFELG FFRTNSSSGW YLGIWYKKVS YRTSVWVANR
     DSPLFNAIGT LKISSNNLVL RGQSNKSVWS TNLTRGNERF PVVAELLANG NFVIRYSNKN
     DASGFLWQSF DYPTDTLLPE MKLGYDLKTE QNRFLTSWRN SDDPSSGEIS YFLDTESGMP
     EFYLLKSGLR AYRSGPWNGV RFSGIPGDQY LSYMVYNYTE NSEEVAYTFR MTTHSIYSRL
     KISSKGFLER LTWTPTSIAW NLIWYLPVEN QCDVYMVCGV YSYCDENTSP MCNCIQGFMP
     LNEQRWDLRD WSSGCTRRTR LSCSGDGFTR MRKMKLPETK MANVYRSIGV KECEKRCLSD
     CNCTAFANAD IRNGGTGCVI WTGRLDDIRN YYADGQDLYV RLAAADLVKK RDANWKIISL
     IVGVSVVLLL MIMFCLWKKK QNRAKAMASS IVNHQRNQNV LMNTMTQSNK RQLSRENKIE
     EFELPLIELE AVVKATENFS NCNELGRSGF GIVYKGMLDG QEVAVKRLSK TSLQGIDEFM
     NEVRLIARLQ HINLVRILGC CIEADEKILI YEYLENSSLD YFLFGKKRSS NLNWKDRFAI
     TNGVARGLLY LHQDSRFRII HRDLKPGNIL LDKYMIPKIS DFGMARIFAR DETQARTDNA
     VGTYGYMSPE YAMDGVISEK TDVFSFGVIV LEIVSGKRNR GFYQVNPENN LPSYAWTHWA
     EGRALEIVDP VIVDSLSSLP STFKPKEVLK CIQIGLLCIQ ERAEHRPTMS SVVWMLGSEA
     TEIPQPKPPV YCLIASYYAN NPSSSRQFDD DESWTVNKYT CSVIDAR
//
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