ID S4RAZ6_PETMA Unreviewed; 511 AA.
AC S4RAZ6;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000002377.1, ECO:0000313|Proteomes:UP000245300};
RN [1] {ECO:0000313|Ensembl:ENSPMAP00000002377.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; S4RAZ6; -.
DR Ensembl; ENSPMAT00000002389.1; ENSPMAP00000002377.1; ENSPMAG00000002170.1.
DR GeneTree; ENSGT00940000159792; -.
DR Proteomes; UP000245300; Unplaced.
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 CDD; cd01093; CRIB_PAK_like; 1.
DR Gene3D; 3.90.810.10; CRIB domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033923; PAK_BD.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR45832:SF8; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45832; SERINE/THREONINE-PROTEIN KINASE SAMKA-RELATED-RELATED; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00285; PBD; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000245300}.
FT DOMAIN 12..25
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 377..511
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 89..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 406
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 511 AA; 56874 MW; 094AC60D4F368210 CRC64;
MFTKKKKQRP QISAPCNFEH RVHTGFDLAE GRFTGLPPQW QSLLADTANR PKPVVDASYI
TPVDLAPMKI IVRGSKKLPI NDSIVTEMSS LSVSRSNSLR VREDRDCERE TDGTHTDGRF
GRSDRISQPK VVNGRQGSLE QGYNRKGQGR PPPGYPVAIT KERPPQIPVN NHQPASPCKK
CPLLESQLWH MTEPSAGVMH RNKERERFHD GDGDRAVVSV RDDSGRPKSS YEVHPVATGP
KRKDRQSQSA SDSSGSGPPR AHSQQSITES QSQRVFDSSA KRGSGKNEQH PAAVDHSEPS
LDTGDIGSSN SAQQQSRHHP DDNHNQQPSS LNHSHVIQSN GPSAPTKKQH QPPRISHEQF
RAALQQVVDP GDPSQFLGSF IKIGEGSTGV VCLAEDKRTG KQVAVKRMHL RKQQRRELLF
NEVVIMREYH HENVVNMYNS YLVDDELWVV MEFLEGGALT DIVTHTRMNE EQISAVCVSV
LRALAYLHGQ GVIHRDIKSD SILLTADGRV R
//
