ID A0A2D0S3A6_ICTPU Unreviewed; 1279 AA.
AC A0A2D0S3A6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=myo3a {ECO:0000313|RefSeq:XP_017337239.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017337239.1};
RN [1] {ECO:0000313|RefSeq:XP_017337239.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017337239.1};
RG RefSeq;
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR RefSeq; XP_017337239.1; XM_017481750.3.
DR AlphaFoldDB; A0A2D0S3A6; -.
DR GeneID; 108272896; -.
DR KEGG; ipu:108272896; -.
DR CTD; 53904; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000221080; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; 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 GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd01379; MYSc_Myo3; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 3.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036083; MYSc_Myo3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR46256; AGAP011099-PA; 1.
DR PANTHER; PTHR46256:SF4; MYOSIN-IIIA; 1.
DR Pfam; PF00612; IQ; 4.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 5.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Vision {ECO:0000256|ARBA:ARBA00023305}.
FT DOMAIN 103..823
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 642..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..726
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 915..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..930
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1054
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1090
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 196..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1279 AA; 145620 MW; 4A2706FE2E4CCA2F CRC64;
MRALFKIPRN PPPSLQQPEI WSDQFNDFIC KCLIKDFELR PNVQDLLQHA FIKQITGQEE
TLQKQLTELI ELNHQIGVIE KIRHERIHTK KDDNMKSQSD EPDDMEDLAT LEVLDENTVT
EHLQKRYSNE QIYTYVGDIL IAINPFHKID LYTPEHSKMY IGTKRTVNPP HIFAVADVAY
QSMVSYNTDQ CIVISGESGA GKTESAHLLV QQLTLLGKAN NRTLQEKILL VNNLVEAFGN
ACTAINDNSS RFGKYLEMKF TCEGTVVGAQ IYEYLLEKSR VIHQAAGERN FHIFYYIYAG
LAERKKLAHY KLSDSKTPKY FQNENVKLVP DIVGNASYKE HFEAVEQCFK VIGFTLEELG
SVYSIVAAIL ITGDIEFASV ATEHQTDKST IANVAVLESA ASLLCIRSDE LKEALTSHCV
VARGETIVRP NTVEKATEVR DAMSKALYGR LFSWIVNRIN SLLRHDNQNG EEDKEQNIGI
LDIFGFENFK RNSFEQLCIN IANEQIQFYF NQHIFAWEQD EYLNEDVDVR VIEYEDNRPL
LDLFLQKPMG MLSLLDEESR FPQATDQTLV EKFEDNLKSK NFWRPMRVDL GFGINHYAGK
VIYTASGFLA KNRDALPADI ILLLRSSENE LISKLVTNPL TKTGNLAHTK GKGTGSGRLS
SRQRSPQRSV NIVKGENGAE SIHHPRETTN MRTQTVASYF RYSLMDLLSK MVAGQPHFVR
CIKPNNDRQA HKFDREKVLI QLRYTGILET AKIRRQGYSH RIVFANFIQR YYMLGFRVNE
EPAVTPEACA AILEKTKMEN WALGKTKVFL KYYHVEQLNL MIKRTTDRIV LVQACVRCWL
AVQNYRKTLG KRTQSAVVLQ SAYRGHKVRR QMVDDKAKPK EDTTIVEFQA LCRGYLARKK
YKELVDEKNK AATKIQAHFK GHKQRKSFQR RKEAMQKENG QNTEEVKDDA PVEEDKLAAD
SAQEDGAKEP ENGEEKTAPS EDEPEAASPG SGEEQETKAA TVIQSNFRGF KERKKLQEEG
KLPTKGKKDT DSQTQENDSL PDPSEEEKPA EAGQEQEPTE ATPDVPDVPD GEEERTEAVQ
DAESKQNDEE QAQTDVNSLE SLTKHISSVS EDFLMLQQKL NQIIMAHQIN PSSNGMFTRG
QVMNSSLGTD QQPSAGTQQT RMSRRSTKPK TLSTPEDSTY YSLIHRSVQE RARKQSTKKL
LDADDQYYQS LNSNTSTGET SGDTEIPESQ TPTSNTPKSS NQDRNSLLRM LSMENEDNPH
DYRKLLRKTS QRGRLIEQS
//
