ID W5MME3_LEPOC Unreviewed; 1370 AA.
AC W5MME3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=MAST1 {ECO:0000313|Ensembl:ENSLOCP00000009552.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000009552.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000009552.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AHAT01007633; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01007634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01007635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01007636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01007637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01007638; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01007639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01007640; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01007641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSLOCT00000009563.1; ENSLOCP00000009552.1; ENSLOCG00000007853.1.
DR GeneTree; ENSGT00940000157700; -.
DR HOGENOM; CLU_000288_9_0_1; -.
DR Proteomes; UP000018468; Linkage group LG6.
DR Bgee; ENSLOCG00000007853; Expressed in camera-type eye and 6 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion 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 CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd05609; STKc_MAST; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.20.1480.20; MAST3 pre-PK domain-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037711; MAST.
DR InterPro; IPR015022; MAST_pre-PK_dom.
DR InterPro; IPR023142; MAST_pre-PK_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356:SF150; MICROTUBULE-ASSOCIATED SERINE_THREONINE-PROTEIN KINASE 1; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF08926; DUF1908; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF140482; MAST3 pre-PK domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 374..647
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 648..716
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 963..1051
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1300..1370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..902
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1090
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1370 AA; 151382 MW; D1C05AFE5246AE33 CRC64;
MDDSGIIRRR RLQKDLPLPR KSSGCRTSNR KSLILTSTSP TLPRPHSPLP GHIGSSPLDS
PRNFSPSTPA HFSFASSRSH GHRTDRADGR RWSLASLPSS GYGTNTPSST SSSSSQERLH
QLPFQPTMDE LHFLSKHFGS TESITDDDGG RRSPAVRPRS RSLSPGRSPS CYDNEIVMMN
HVYKERFPKA TAQMEERLSE FITAFSPENV LPLADGVLSF IHHQIVELSR DCLTKSQEGV
ITTVYFLELQ ENLDKLLQDA FERSESSEVA FVTQLVKKLL IIISRPARLL ECLEFNPEEF
YHLLEAAEDH AKEGHLVKTD IPRYIISQLG LTRDPLEEMV NLDSYDSEGP HTPETDDSVE
GKVKAKKPPN ETDFQTIKLI SNGAYGAVYL VRHRETRQRF AMKKINKQNL ILRNQIQQAF
VERDILTFAE NPFVVSMFCS FETRRHLCMV MEYVEGGDCA TLLKNIGALP VEMARMYFAE
TVLALEYLHN YGIVHRDLKP DNLLITSMGH IKLTDFGLSK MGLMSMTTNL YEGHIEKDAR
EFLDKQVCGT PEYIAPEVIL RQGYGKPVDW WAMGIILYEF LVGCVPFFGD TPEELFGQVI
SDEIVWPEGD EALPGDAQSL ISALLQTNPL MRLGTGAAFE VKQHSFFKDL DWNSLLRQKA
EFIPHLESEE DTSYFDTRSE RYHHINSYEE DDTNDDEPVE IRQFSSCSPR FSKVYSSMEH
LSQLEQKPPA VTKRDPKTQK EDKVTKRESL GSFGMRDKSW RTSSPDMKRF SCSESSYTES
DSSPPLGARR RFSALMDTQR FASPQEGDSE TQQLKQAQSR PAQEGGASTP TSQSEPKLIR
EGNGVSAAAT NDKAPKAGDM ATAGKDTTDP SSPRATSDLV LRRARHQQLS GDAAEKRSSR
PGNKVIKSAS ATALSVIIPA VEQHAGSPLA SPMSPRSLSS NPSSRDSSPS RDYCPAVTSL
RSPITIHRSG KKYGFTLRAI RVYMGDSDVY SVHHIVWHVE EGGPAQEAGL CAGDLITHVN
GESVHGLVHT EVVELILKSG NKVIVTTTPF ENTSIKIGPA RKSSYKSKMA RRNKKTVPKE
GQESTKKRSS LFRKITKQSN LLHTSRSLSS LNRSLSSSDS LPGSPTHSLS ARSPTQSYRS
TPDSSYLGAS SQSSSPASST PNSPAASHHM RPSSLHGLSP KLHRQYRSAR CKSAGNIPLS
PLAHTPSPTQ SSPPPLPGHT VGSSNTTQTF PAKLHSSPPV VRPRPKSAEP PRSPLLKRVQ
SAEKLGSPLS SDKKAALRKH SLEVSHADYR KESFHSELGL QSLLETEGEN AAPAPTPALR
NGLSQARQEA GPPGVSAQQG RSAGRERQGR DVPRREERRA GNVAHPGGDL
//
