ID A0A498N462_LABRO Unreviewed; 2915 AA.
AC A0A498N462;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=ROHU_036454 {ECO:0000313|EMBL:RXN26494.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN26494.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN26494.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN26494.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN26494.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXN26494.1}.
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DR EMBL; QBIY01012241; RXN26494.1; -; Genomic_DNA.
DR STRING; 84645.A0A498N462; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 5.
DR Gene3D; 1.20.58.60; -; 4.
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; 3.
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; 5.
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; 5.
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 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A498N462};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
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}.
FT DOMAIN 56..202
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1138..1313
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1325..1437
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1501..1566
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1815..1962
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1986..2101
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2367..2432
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2502..2592
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2613..2867
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 282..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1447..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1596..1717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1729..1753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1770..1801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2120..2368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2448..2470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1473..1496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1596..1625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1652..1681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1682..1701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1776..1801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2286..2306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2340..2368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2453..2470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2642
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2915 AA; 328578 MW; 7959C163BD8AFDA1 CRC64;
MYLHCGVVED TDSLSSWWNG NVASLLDNHR WQYAQTGNTL IQLPGFRRNE EMKAMEVLPI
LKEKVAFLSG GRDKRGGPVL TFPSRTNHDR IRHEDLRRLI AYLAGIPSED VCKHGFTVIV
DMRGSKWDSI KPLLKILQES FPCCIHVALI IKPDNFWQKQ RTNFGSSKFE FETTMVSLEG
LSKVVDPSQL TPDFEGSLDY NHEEWIEIRV AFEDFTGNAR HLLARLEEMQ ETVTRKDFPQ
DLEGARRMIE EHAALKKRVM KAPVEEVDSE GQRLLQRIQS SESYANRTVP VPPGQREGQG
QPNADTQGLV PRISALLEKL HSTRQNLHQA WHVRKLQLDQ CFQLRLFEQD AEKMFDWIMH
NKGLFLAGYT EIGNNHPHAM ELQTQHNHFA MNCMNVYVNI NRIMSVGNRL LEAGHYASQQ
IKQISGQLEQ EWKAFAAALD ERSALLEMSA TFHQKCDQYM SNVDSWCKAC GEVDLPSELQ
DLEDAIHHHQ GLYEQITAAY SEVSQDGKAL LDKLQRPLTP GSADSLTASA NYSKAVHHVL
DIIHEVLHHQ RQLENIWQHR KVRLHQRLQL CVFQQDVQQN TYTNADKLLE AAEQLAQTGE
CDPEEIYQAA HQLEDRIQDF VRRVEQRKVL LDMSVAFHTH VKEIISDLDS WNEELSQQMN
DFDTEDLTLA EQRLQHHADK ALTMNNLAFH VIHQGQELLQ YVNEVQASGV ELLCDRDVDM
ATRVQDLLEF LHEKQQELDV AAEQHRRHLE QCVQLRHLQA EVKQVLGWIR NGESMLNAGL
ITASSLQEAE QLQREHEQFQ HAIEKTHQSA LQVQQKAEAL LQANHYDMDM IRDCAENVAS
HWQQLMLKME DRLKLVNASV AFYKTSEQVC SVLESLEQEY KREEDWCGGA DKLGPNCETD
HVTPMISKHL EQKEAFLKAC TLARRNADVF LKYMHRNSVS MPGMLSHVKA PEQQVKNILN
ELLQRENRVL HFWTMRKRRL DQCQQYVVFE RSAKQALEWI HDTGEFYLST HTSTGSSIHH
TQELLKEHED FHITAKQTKE RVKLLIQLAD GFCDKGHAHA AEIKKWVTAV DKRYRDFSLR
MDKYRTSLEK ALGISSDSNK ASKDLQLDII PASAPGSEVK LRGDAHELNE EKRKSARRKD
FIMAELIQTE KAYVRDLREC MDTYLWEMTS GVEEIPPGIV NKEHIIFGNM QDLYEFHHNI
FLKELEKYEQ LPEDVGHCFV TWADKFQMYV NYCKNKPDST QLILEHAGGY FDEIQQRHRL
ANSISSYLIK PVQRITKYQL LLKELLTCCE EGKGEIKDGL EVMLSVPKRA NDAMHLSMLE
GFDENIESQG ELILQEAFQV WDPKTLIRKG RERHLFLFEM SLIFSKEVKD SNGRSKYIYK
SKLFTSELGV TEHVEGDPCK FALWVGRTPT SDNKIVLKAS SIENKQDWIK HIREVIQERT
VHLKGALKEP IHIPKPSTAK HKGRRDGEDL DSQGDGSSQP DTISLASRTS QNTLDSDKLS
GGCELTVVIH DFMAGNSNEL TVRRGQTVEV LERLHDKPDW CLVRTTDRSP ALEGLVPCAM
LCIAHSRSSM EMEGIFNHKD ALSVCSNDAI LPGSSATLQP GHVMGSQSSP GPKRTGNTLR
KWLTSPVRRL SSGKADGHVK KLAHKHKKSR DVRKSADAGS QKDSDDSAAT PQDETLEERV
RNEGLSSGTL SKSSSSGMQS CGEEEGEEGA DAVPLPPPMA IQQHSLLQPD AQDDKTSSRL
SVRPSSSETP SAAELVSAIE ELVKSKMALE DRPSSLSVEQ GDSSSPSFNP SDNSLLSSSS
PIDEIEERKT GFLKRRHYIL LELIETERDY VRDLSLVVEG YMNRMREDGV PDDMKGKDKI
VFGNIQQIYD WHRDFFLGEL EKCLEDPDRL GPLFVKHERR LHMYIVYCQN KPKSEHIVSE
YIDTYFEDLK QRLGHRLQIT DLLIKPVQRI MKYQLLLKKA IEVMCIVPKR CNDMMNVGRL
QGFDGKIIAQ GRLLLQDTFM VAEPDGGLLN RMKERRVFLF EQIVIFSEPL DKKRGYSMPG
YLYKYSIKVS CLGLEDSVDG DPCKFALTSR TSNGSKEAFI LHSSHPGVRQ VWMLQISQIL
ESQRNFLNAL TSPIDYQRNH VEGPGVSGSS VQAGGGGGQV MAPGGGGVAP AGSGSRSRPS
RIPQPSRLPQ PLRHHSPALG PGAHEPDGPD KISGMSPRPL SRGPSPSCTT EPDPKVKVPA
SSHPKQTDST ESASKESRDG AGTAQIPRAT VAPLALVKPR PGTVSPMASP LATPAFKDSI
PPCSPGPKTG GSSTSFWSSV PASPASRPGS FTFPGEACDT LGRQNQNQSH RHSTHSKDAD
RMSTCSSASE QSVQSTQSNG SESSSSSNIS TMLVTQDYVA LKEDEINVGQ GEVVQILASN
QQNMFLVFRA ATDQCPAAEG WIPGYVLGHT SAIIPDVPEG TINRKSSSWH TSLRIRKKSE
KREKENKKEA KLENGYRKSR EGLTNKVSVK LLNPNYIYDV PPEILVPLSD VTCDKGECVT
LRCKVCGRPK ATVTWKGPDQ KTLTNNGHFS IAYSETGEAT LRIIGVTSED DGMYTCIATN
DIGSVTSSAS LRVLGTTSDG IRVMWKDNFE SFYTEVAELG RGRFSVVKRC DQRGSKRTVA
VKFVNKKLMK RDQVTHEFSV LQRLQHPHLV RLLDTFETSS SYALVLEMSD QGRLLDYIVS
WGNLTEEKVA FYLRDILEAL QYLHNCRIVH LDLKPENLVV DQSPSQPMVK LTDFGDAVQL
NSTPYVHPLL GSPEFAAPEL VLGDPVSLSS DLWSLGVVTY VMLSGASPFL DESVEETCLN
ICRLDFSFPD DYFQGVSQAA RDFVCLLLRT EPSKRPPAAA CLQDPWLRPG GGRRSAECID
TSRLISFIDR RKHQNDLRPL GGIRAFLQSR LQPRI
//
