ID A0A2K6RUF6_RHIRO Unreviewed; 2959 AA.
AC A0A2K6RUF6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-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=KALRN {ECO:0000313|Ensembl:ENSRROP00000044662.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000044662.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000044662.1}
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; ENSRROT00000069181.1; ENSRROP00000044662.1; ENSRROG00000045195.1.
DR GeneTree; ENSGT00940000155248; -.
DR Proteomes; UP000233200; Unplaced.
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; cd00063; FN3; 1.
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 CDD; cd14115; STKc_Kalirin_C; 1.
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; 2.
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; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
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:SF49; KALIRIN; 1.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00041; fn3; 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; PF00435; Spectrin; 4.
DR SMART; SM00060; FN3; 1.
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; SSF49265; Fibronectin type III; 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; PS50853; FN3; 1.
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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
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 17..162
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1254..1429
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1441..1553
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1619..1684
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1902..2077
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2089..2199
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2294..2359
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2444..2537
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2544..2638
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2657..2911
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 692..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1567..1615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1723..1830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2217..2273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2385..2427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 901..928
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 703..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1590..1615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1723..1746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1755..1777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1786..1810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2259..2273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2385..2407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2686
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2959 AA; 336873 MW; E9322AB7EF2DEF39 CRC64;
MVLLWSFRND GLKASDVLPI LKEKVAFVSG GRDKRGGPIL TFPARSNHDR IRQEDLRKLV
TYLASVPSED VCKRGFTVII DMRGSKWDLI KPLLKTLQEA FPAEIHVALI IKPDNFWQKQ
KTNFGSSKFI FETSMVSVEG LTKLVDPSQL TEEFDGSLDY NHEEWIELRL SLEEFFNSAV
HLLSRLEDLQ EMLARKEFPV DVEGSRRLID EHTQLKKKVL KAPVEELDRE GQRLLQCIRC
SDGFSGRNCI PGSADFQSLV PKITSLLDKL HSTRQHLHQM WHVRKLKLDQ CFQLRLFEQD
AEKMFDWISH NKELFLQSHT EIGVSYQYAL DLQTQHNHFA MNSMNAYVNI NRIMSVASRL
SEAGHYASQQ IKQISTQLDQ EWKSFAAALD ERSTILAMSA VFHQKAEQFL SGVDAWCKMC
SEGGLPSEMQ DLELAIHHHQ TLYEQVTQAY TEVSQDGKAL LDVLQRPLSP GNSESLTATA
NYSKAVHQVL DVVHEVLHHQ RRLESIWQHR KVRLHQRLQL CVFQQDVQQV LDWIENHGEA
FLSKHTGVGK SLHRARALQK RHDDFEEVAQ NTYTNADKLL EAAEQLAQTG ECDPEEIYKA
ARHLEVRIQD FVRRVEQRKL LLDMSVSFHT HTKELWTWME DLQKEMLEDV CADSVDAVQE
LIKQFQQQQT ATLDATLNVI KEGEDLIQQL RSAPPSLGEP SEARDSAVSN NKTPHSSSIS
HIESVLQQLD DAQVQMEELF HERKIKLDIF LQLRIFEQYT IEVTAELDAW NEDLLRQMND
FNTEDLTLAE QRLQRHTERK LAMNNMTFEV IQQGQDLHQY IMEVQASGIE LICEKDIDLA
AQVQELLEFL HEKQHELELN AEQTHKRLEQ CLQLRHLQAE VKQVLGWIRN GESMLNASLV
NASSLSEAEQ LQREHEQFQL AIEKTHQSAL QVQQKAEVLL QAGHYDADAI RECAEKVALH
WQQLMLKMED RLKLVNASVA FYKTSEQVCS VLESLEQEYR RDEDWCGGRD KLGPAAEIDH
VIPLISKHLE QKEAFLKACT LARRNAEVFL KYIHRNNVSM PSVASHTRGP EQQVKAILSE
LLQRENRVLH FWTLKKRRLD QCQQYVVFER SAKQALDWIQ ETGEFYLSTH TSTGETTEET
QELLKEYGEF RVPAKQTKEK VKLLIQLADS FVEKGHIHAT EIRKWVTTVD KHYRDFSLRM
GKYRYSLEKA LGVNTEDNKD LELDIIPASL SDREVKLRDA NHEVNEEKRK SARKKEFIMA
ELLQTEKAYV RDLHECLETY LWEMTSGVEE IPPGILNKEH IIFGNIQEIY DFHNNIFLKE
LEKYEQLPED VGHCFVTWAD KFQMYVTYCK NKPDSNQLIL EHAGTFFDEI QQRHGLANSI
SSYLIKPVQR ITKYQLLLKE LLTCCEEGKG ELKDGLEVML SVPKKANDAM HVSMLEGFDE
NLDVQGELIL QDAFQVWDPK SLIRKGRERH LFLFEISLVF SKEIKDSSGH TKYVYKNKLL
TSELGVTEHV EGDPCKFALW SGRTPSSDNK TVLKASNIET KQEWIKNIRE VIQERIIHLK
GALKEPLQLP KTPAKQRNNS KRDGVEDIDS QGDGSSQPDT ISIASRTSQN TVDSDKLSGG
CELTVVLQDF SAGHSSELTI QVGQTVELLE RPSERPGWCL VRTTERSPPL EGLVPSSALC
ISHSRSSVEM DCFFPLVKDA YSHSSSENGG KSESVANLQA QPSLNSIHSS PGPKRSTNTL
KKWLTSPVRR LNSGKADGNI KKQKKVRDGR KSFDLGSPKP GDETTPQGDS ADEKSKKGWG
EDEPDEESHT PLPPPMKIFD NDPTQDEMSS SLLAARQAST EVPTAADLVS AIEKLVKNKL
SLEGGSYRGS LKDPAGCLNE GMAPPTPPRN PEEEQKAKAL RGRMFVLNEL VQTEKDYVKD
LGIVVEGFMK RIEEKGVPED MRGKDKIVFG NIHQIYDWHK DFFLAELEKC IQEQDRLAQL
FIKHERKLHI YVWYCQNKPR SEYIVAEYDT YFEEVKQEIN QRLTLSDFLI KPIQRITKYQ
LLLKDFLRYS EKAGLECSDI EKAVELMCLV PKRCNDMMNL GRLQGFEGTL TAQGKLLQQD
TFYVIELDAG MQSRTKERRV FLFEQIVIFS ELLRKGSLTP GYMFKRSIKM NYLVLEENVD
NDPCKFALMN RETSERVILQ AANADIQQAW VQDINQVLET QRDFLNALQS PIEYQRKERS
TAVMRSQPAR LPQASPRPYS SVPVGSEKPP KGSSYNPPLP PLKISTSNGS PGFEYHQSGD
KFEASKQNDL GGCNGTSSMA VIKDYYALKE NEICVSQGEV VQVLAINQQN MCLVYQPASD
HSPAAEGWVP GSILAPLTKA TAAESSDGSI KKSCSWHTLR MRKRAEVENT GKNEATGSRK
PKDILGNKVS VKETNSSEES ECDDLDPNTS MEILNPNFIQ EVAPEFLVPL VDVTCLLGDT
VVLQCKVCGR PKPTITWKGP DQNILDTDNS SATYTVSSCD SGEITLKICN LMPQDSGIYT
CIATNDHGTT STSATVKVQG VPAAPNRPIA QERSCTSVIL RWLPPSSTGN CTISGYTVEY
REEGSQIWQQ SVASTLDTYL VIEDLSPGCP YQFRVSASNP WGISLPSEPS EFVRLPEYDA
AADGATISWK ENFDSAYTEL NEIGRGRFSI VKKCIHKATR KDVAVKFVSK KMKKKEQAAH
EAALLQHLQH PQYITLHDTY ESPTSYILIL ELMDDGRLLD YLMNHDELME EKVAFYIRDI
MEALQYLHNC RVAHLDIKPE NLLIDLRIPV PRVKLIDLED AVQISGHFHI HHLLGNPEFA
APEVIQGIPV SLGTDIWSIG VLTYVMLSGV SPFLDESKEE TCINVCRVDF SFPHEYFCGV
SNAARDFINV ILQEDFRRRP TAATCLQHPW LQPHNGSYSK IPLDTSRLAC FIERRKHQND
VRPIPNVKSY IVNRVNQGT
//
