ID A0A665UPP1_ECHNA Unreviewed; 2753 AA.
AC A0A665UPP1;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Echeneis naucrates (Live sharksucker).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Echeneidae; Echeneis.
OX NCBI_TaxID=173247 {ECO:0000313|Ensembl:ENSENLP00000021172.1, ECO:0000313|Proteomes:UP000472264};
RN [1] {ECO:0000313|Ensembl:ENSENLP00000021172.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
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DR Ensembl; ENSENLT00000021913.1; ENSENLP00000021172.1; ENSENLG00000009105.1.
DR OMA; ESYYTEI; -.
DR Proteomes; UP000472264; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd13240; PH1_Kalirin_Trio_like; 1.
DR CDD; cd13241; PH2_Kalirin_Trio_p63RhoGEF; 1.
DR CDD; cd00160; RhoGEF; 2.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd11852; SH3_Kalirin_1; 1.
DR CDD; cd11853; SH3_Kalirin_2; 1.
DR CDD; cd00176; SPEC; 6.
DR Gene3D; 1.20.58.60; -; 5.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR047054; Kalirin_TRIO_PH_1.
DR InterPro; IPR028570; Kalirin_TRIO_SH3_1.
DR InterPro; IPR047053; Kalirin_TRIO_SH3_2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR PANTHER; PTHR22826:SF104; TRIPLE FUNCTIONAL DOMAIN PROTEIN; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00621; RhoGEF; 2.
DR Pfam; PF16609; SH3-RhoG_link; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 2.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00516; SEC14; 1.
DR SMART; SM00326; SH3; 2.
DR SMART; SM00150; SPEC; 6.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 2.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR SUPFAM; SSF46966; Spectrin repeat; 6.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50010; DH_2; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50002; SH3; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000472264};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 1..145
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1232..1407
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1419..1531
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1594..1662
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1834..2011
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2204..2269
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2336..2428
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2456..2711
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1546..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1675..1759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 159..208
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 698..725
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1546..1565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1676..1700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2485
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2753 AA; 313631 MW; 5EB0EA015CFBF6F7 CRC64;
MALFLSFSLC PKGGRDRRGG PILTFPARSN HDRIRPEDLR RLIAYLATIP SEEVARHGFT
VIVDMRGSKW DSIKPLLKIL QESFPSCIHV ALIIKPDNFW QKQRTNFGSS KFEFETVMVS
LEGLTKIVDP SQLTADFEGS LEYNHDDWIE VRLSFETFAS DATRALARLE ELQETLSQRD
LPRDLEGARR LMEEHAALKK RATKASVEEL DTQGRRLLQR LQSQIAGDSN DHHHGLHTHA
DAHNLGAKVT GLLDKLHGTR QNLQQLWHMR KLKLDQCFQL RLFEQDAEKM FDWIMHNKGL
FLTSYTEIGG NHQHAVELQT QHNHFAMNCM NVYVNINRIM SVGNRLLESG HYASQQIQQI
SGQLEQEWKA FAAALDERST LLEMSASFHQ KADQYMSKVE PWCKACGEGE LPSELQDLED
TIHHHQGLYE HITTAYSEVS QDGKSLLDKL QRPLTPGSAD SLMASANYSK AVHHVLDIIH
EVLHHQRQLE NIWQHRKVRL HQRLQLCVFQ QDVQQVLDWI ENHGEAFLSK HTGVGKSLHR
ARALQKRHED FEEVAQNTYT NADKLLEAAE QLAQTGECDP EEIYQAAHQL EDRIQDFVRR
VEQRKVLLDM SVAFHTHVKE LWTWLEELQK ELLDDVYAES VEAVQDLIKR FGQQQQTTLQ
ATVNVIKEGE DLIQQLRLSL DSAISSNKTP HNSSMAHIES VLQQLDEAQG QMEELFQERK
IKLELFLQLR IFERDAIDII SDLESWNEEL SQQMSDFDTE DLTLAEQRLQ HHADKALTMN
NLTFDVIHQG QELLQYVTEV QASGVELLCD RDVDMATRVQ DLLEFLHEKQ QELDLAAEQH
RRHLEQCVQL RHLQAEVKQV LGWIRNGESM LNAGLITASS LQEAEQLQKE HEQFQHAIEK
THQSALQVQQ KAEALLQANH YDMDMIRDCA EKVADHWQQL MLKMEDRLKL VNASVAFYKT
SEQVCSVLES LEQEYKREED WCGGADKLGP NSESDHVTPM ISKHLEQKEA FLKACTLARR
NADVFLKYLH RNSVNMPGML SHVKAPETQV KNILNELLQR ENRVLHFWTM RKRRLDQCQQ
YVVFERSAKQ ALEWIHDTGE FYLSTHTSTG SSIHHTQELL KEHEDFQITA KQTKERVKLL
IQLADGFCDK GHAHALEIKK WVSSVDKRYR DFSLRMDKYR TCLETALGIS SDSNKSKDLQ
LDIIPATAPG SEVKLRDAAH ELNEEKRKSA RRKEFIMAEL IQTEKAYVRD LRECMDTYLW
EMTSGVEEIP PGIVNKEHII FGNMQDLYEF HHNIFLKELE KYEQLPEDVG HCFVTWADKF
QMYVNYCKNK PDSTQLILEH AGPYFDEIQQ RHRLANSISS YLIKPVQRIT KYQLLLKELL
TCCEEGKGEI KDGLEVMLSV PKKANDAMHL SMLDGFDGNI DSQGELILQE SFQVWDPKTL
IRKGRDRHLF LFEMSLVFSK EVKDSNGHSK YLYKSKLFTS ELGVTEHVEG DPCKFALWVG
RTPTSDNKIV LKASSIENKQ DWIKHIREVI QERTVHLRGA LKEPIHIPKA TTAKHKGRDG
EELDSQGDAS SQPDTISIAS RTSQNTLDSD KLSGGCELTV VIHDFVASNG GSSGELTVRR
GQTVEVLERL HDKPDWCLVR TTDRSPAQEG IVPCSMLCIA HSRSSMEMEG VLLSYSSGKR
GNNDNDALQP GSSQTLGPHS SPGPKRPGNT LRKWLTSPVR RLSSGKADGH VKKLAHKHKK
NRDGTRKNMD TISGSQKDSD DSAVLCLNQK FSYFNSTPPP PPPLSLCQSA SRLSARPNSS
ETPSAAELVS AIEELVKSKM VRWKSYNKVT KYLHKSNTIF NLCLVFTAYF KINQLSSPQG
YMSRMKEEGV PDDMRGKDKI VFGNIHQIYD WHKDFFLGEL EKCLEDPDRL APLFVKQERR
LHMYIVYCQN KPKSEHIVSE YIDTYFEDLK QRLGHRLQVT DLLIKPVQRI MKYQLLLKDL
LKVSKKAGVE TTELEKAVEV MCVVPKRCND MMNVGRLQGF DGKIVAQGRL LLQDTFMVSD
QDGGLLSRMK ERRVFLFEQI VIFSEPLDKK KGFSTPGYLF KNSIKVSWLG LEENADDPCK
FTLTSRSSSG NLERYTLHSM SPGVSQVWIH QVGQILENQR NFLNGITSLL SSPHKIDTKI
TSDSCLLSFV IPSIVLKVSC SFFELISSFH EGHSRLISFC TNLIFVSTML VTQDYVAVKE
DEISVVQGEV VQMLASNQQN MFLVYRAANE HCPAAEGWIP GFVLGHTSSS TTPEVPEGTI
KYVEETFSQF LRQKKRLDKE GRKTENGYRK SQDSLANKVS VKVDKDLHLS VSSASPEFLI
PVSDVACENG DSVTLWCKVC GRPRATVTWR GPENTTLSSN GHYSITFSET GEAALHILGV
SVEDSGVYTC VATNVAGSVT SSASLRVSGE TCVIIQILKS FINCEVLWKG SFESHYTEIT
ELGRGRFSVT KRCDQRGSKR TVAAKHVNKK LLRREQVVQE IRLLQTLDHP NLVKLLDTYE
TANSYVLVLE MADQGRFMDY IVSWGNLTEE KVALYLRDIL EALHYLHGWG IAHLDLKPEN
IVVEHASCQP VIKLTDFGDA AQLSPPSPYI HPLLGSPEFS APEIVLGQPA SLMSDLWSLG
VVTYVILSGA SPFLDESLEE TCLNICRLDF SFPEDYFQGV SPAARDFVRL LLQGEPERRP
SAAACLQEPW LLPRAHLDTS RLISFIERRK HQNDVRPIGT IKAFLQSRLA NHI
//
