ID A0A665THJ3_ECHNA Unreviewed; 3028 AA.
AC A0A665THJ3;
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:ENSENLP00000009349.1, ECO:0000313|Proteomes:UP000472264};
RN [1] {ECO:0000313|Ensembl:ENSENLP00000009349.1}
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; ENSENLT00000009795.1; ENSENLP00000009349.1; ENSENLG00000004245.1.
DR InParanoid; A0A665THJ3; -.
DR OMA; IRYLHNC; -.
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:SF206; TRIPLE FUNCTIONAL DOMAIN PROTEIN-RELATED; 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; 7.
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; 2.
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 43..189
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1283..1458
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1470..1582
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1621..1686
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1937..2080
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2116..2231
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2475..2540
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2609..2699
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2722..2977
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 266..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1713..1875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1892..1926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2255..2315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2348..2477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2555..2580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 745..775
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1789..1803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1804..1823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1844..1875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1898..1923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2255..2286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2352..2388
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2390..2404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2417..2438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2448..2477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2560..2580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2751
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 3028 AA; 341327 MW; CA4EA52C8108F076 CRC64;
SYHYCPTTAC ASSLSSYVGV FSSLSIVSLH PGFRRNEEMR AMEVLPILKE KVAFLSGGRD
RRGGPVLTFP SRSNHDRIRT DDLRRLIAYL AGIPSEEVCK HGFTVIVDMR GSKWDSIKPL
LKILQESFPS CIHIALIIKP DNFWQKQRTN FGSSKFEFET TMVSLEGLTK VVDPSQLTAD
FDGSLDYNHE EWIEVRVAFE EFSGHATQML ARLEEMQETV SRKDFPQDLE GARRMIEEHA
TLKKKVIKAP IEELDTEGQR LLQRIQSSES FSNRNGSSGS GGSSSSGSGV CNADTQGLVP
RITQLLDKLH STRQHLHQAW HVRKLQLDQC FQLRLFEQDA EKMFDWIMHN KGLFLAGYTE
IGNNHPHAVE LQTQHNHFAM NCMNVYVNIN RIMSVGNRLL ESGHYASQQI KQISGQLEQE
WKAFAAALDE RSTLLEMSAS FHQKCDQYMS NVDSWCKACG EVDLPSELQD LEDAIHHHQG
LYEHITAAYS EVSQDGKALL DKLQRPLTPG SADSLTASAN YSKAVHHVLD IIHEVLHHQR
QLENIWQHRK VRLHQRLQLC VFQQDVQQVL DWIENHGEAF LSKHTGVGKS LHRARALQKR
HEDFEEVAQN TYTNADKLLE AAEQLAQTGE CDPEEIYQAA HQLEDRIQDF VRRVEQRKVL
LDMSVAFHTH VKELWTWLEE LQKELLDDVY AESVEAVQDL IKRFGQQQQT TLQVTVNVIK
EGEDLIQQLR DSAISSNKTP HNSSINHIES VLQQLDEAQA QMEELFQERK IKLELFLQLR
IFERDAIDII SDLESWNEEL TGQMNDFDTE DLTLAEQRLQ HHADKALTMN NLTFDVIHQG
QELLQYVNEV QASGVELLCD RDVDMATRVQ DLLEFLHEKQ QELDLAAEQH RRHLEQCVQL
RHLQAEVKQV LGWIRNGESM LNAGLITASS LQEAEQLQRE HEQFQHAIEK THQSALQVQQ
KAEALLQANH YDMDLIRDCA ESVASHWQQL MLKMEDRLKL VNASVAFYKT SEQVCSVLES
LEQEYKREED WCGGADKLGP NCETDHVTPM ISKHLEQKEA FLKACTLARR NADVFLKYMH
RNSVNMPGML SHVKAPEQQV KNILNELLQR ENRVLHFWTM RKRRLDQCQQ YVVFERSAKQ
ALEWIHDTGE FYLSTHTSTG SSIHHTQELL KEHEDFHITA KQTKERVKLL IQLADGFCEK
GHSHAGEIKK WVTAVDKRYR DFSLRMDKYR CSLEKALGIS SDSNKASKDL QLDIIPPTAP
GSEVKLRDAA HELNEEKRKS ARRKEFIMAE LIQTEKAYVR DLRECMDTYL WEMTSGVEEI
PPGIINKEHI IFGNMQDLYE FHHNIFLKEL EKYEQLPEDV GHCFVTWADK FQMYVNYCKN
KPDSTQLILE HAGNYFDEIQ QRHRLANSIS SYLIKPVQRI TKYQLLLKEL LTCCEEGKGE
IKDGLEVMLS VPKKANDAMH LSMLEGFDEN IESQGELILQ ESFQVWDPKT LIRKGRERHL
FLFEMSLVFS KEVKDSNGRS KYIYKSKLFT SELGVTEHVE GDPCKFALWV GRTPTSDNKI
VLKASSIENK QDWIKHIREV IQERTIHLRG ALKEPIHIPK ATTAKHPKGR RLISHASHLS
GGCELTVVIH DFMASNSNEL TVRRGQTVEV LERCHDKPDW CLVRTTDRSP AQEGLVPCSM
LCIAHSRSSM EMEGIFNHKD TLSVCSNDSI MPGSSATLQP GHGIGSHTSP GPKRPGNTLR
KWLTSPVRRL SSGKADGHVK KLAHKHKKSR EMRKSGEMTI GSQKDSDDSA ATPQDETVEE
RVRNEGLSSG TLSKSSSSGM QSCGEEEGEE GADSVPLPPP MAIQQHSLLQ SDSQDDKTSS
RLSVRPSSSE TPSAAELVSA IEELVKSKMA LEDRPSSLSV EQGDSSSPSL NPSDNSLLSS
SSPIEEMDER RTSILKKRHY ILLELMETER DYVRDLGLVV EGYMSRMKEE GVPDDMKGKD
KIVFGNIHQI YDWHKDFFLG ELEKCLEDPD RLGPLFLKQE RRLNMYVVYC QNKPKSEHIV
SEYIDTYFED LKQRLGHRLQ ITDLLIKPVQ RIMKYQLLLK VGLLQSSRGS VEVMCIVPKR
CNDMMNVGRL QGFDGKIVAQ GRLLLQDTFM VSDPEGSLLG RMKERRVFLF EQLVIFSEPL
DKKKGFSLPG FLYKNSIKVS SLGLEENVEG DPCKFILTSR STNGAAESFV LHSSHPGVRE
VWTLQISQIL ESQRNFLNAL TSPIEYQRNH VGASGGSCVS SMAAPSGGSS GSSIPSGPQG
GSRRPSRIPQ PSRLPQPLRH HPGADPEGPN KISGMKPHSV YEKFVLYAQN NPTAASIVAP
IPRATVGPLP STPTSKPRPG AVPPIASPLP TPSFGKDILP PPPPSPGHKS GSGFWSSMPG
SPASRPGSFT FPGEAGESPV RQNSNQIQTG SGTGNQTHRH STHSKEADRM STCSSASEQS
IQSTQSNGSE SSSSSSVSTM LVTHDYMAVK EDEISVSQGE VVQILASNQQ NMFLVFRAAT
EQGPAAEGWI PGFVLGHTSA IVPDCPEGSI KKSSSWHTSL RIRKKSEKKE KEAKKETKLE
NGYRKSRDGL ANKVSVKLLN PNYIYDVPPE FLVPLSDVTC DSGESVTLRC KICGRPRATV
TWKGPNQSNL TNNGHFSIAY SDTGEATLRI LGVASEDDGI YTCVATNDLG SITSSASLRV
LGKTVSTDGI RVSWKDNFES HYTEVVELGR GRFSVVKRCD HQGTKRTVAV KHVNKKLMRR
DRVTQELNLL QRLQHPHIVS LIDTYETSSS YVLVLEMADQ GRLLDYVVSW GNLTEEKVAC
YLRDVLEALH YLHNCRIVHL DVKPENLLVA HTSSGQPAVK ITDFGDAVQL NSAHYVHPLL
GSPEFASPEL VLGEPVSITS DLWSLGVVTY VLLSGASPFL DESAEETCLN ICQLDFSFPR
DYFQGVSQAA RDFVCLLLRA DPSRRPPAEL CLQEPWLQAG LADGRARAEG CLDTSRLISF
IDRRKHQTDA RPIGGIRSFI QSRLQPRV
//
