ID A0A672UMF6_STRHB Unreviewed; 2708 AA.
AC A0A672UMF6;
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};
GN Name=KALRN {ECO:0000313|Ensembl:ENSSHBP00005015246.1};
OS Strigops habroptila (Kakapo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Strigops.
OX NCBI_TaxID=2489341 {ECO:0000313|Ensembl:ENSSHBP00005015246.1, ECO:0000313|Proteomes:UP000472266};
RN [1] {ECO:0000313|Ensembl:ENSSHBP00005015246.1, ECO:0000313|Proteomes:UP000472266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jarvis E.D., Howard J., Rhie A., Phillippy A., Korlach J., Digby A.,
RA Iorns D., Eason D., Robertson B., Raemaekers T., Howe K., Lewin H.,
RA Damas J., Hastie A., Tracey A., Chow W., Fedrigo O.;
RT "Strigops habroptila (kakapo) genome, bStrHab1, primary haplotype, v2.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSHBP00005015246.1}
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; ENSSHBT00005018269.1; ENSSHBP00005015246.1; ENSSHBG00005004163.1.
DR GeneTree; ENSGT00940000155248; -.
DR Proteomes; UP000472266; Chromosome 6.
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; 1.
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 CDD; cd14115; STKc_Kalirin_C; 1.
DR Gene3D; 1.20.58.60; -; 5.
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:SF49; KALIRIN; 1.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000472266};
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 1..122
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1201..1376
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1388..1500
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1566..1631
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1821..1919
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1931..2041
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2165..2230
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2294..2384
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2406..2660
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1514..1562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1651..1738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2058..2125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2252..2271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 848..875
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1537..1562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1651..1701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1702..1724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2058..2084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2100..2120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2435
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2708 AA; 308845 MW; 225BB663F458B4F4 CRC64;
MSSSTSNHDR IRQEDLRKLV TYLASVPSED VCKRGFTVII DMRGSKWDLI KPLLKTLQEA
FPAEIHVALI IKPDNFWQKQ KTNFGSSKFI FETSMVSVEG LAKLVDPSQL TDEFEGSLDY
NHDEWIELRV SLEEFFNSAV HLLSRLEDLQ EMLARKEFPV DVEGSRRLID EHTQLKKKVI
KAPVEELDRE GQRLLQCIRC SDGFSGRNCI PGSADFQSLV PKITSLLDKL HSTRQHLHQM
WHVRKLKLDQ CFQLRLFEQD AEKMFDWISH NKELFLQSHT EIGVSYQHAL DLQTQHNHFA
MNSMNAYVNI NRIMSVASRL SEAGHYASQQ IKQISSQLDQ 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
DLQKELLEDV CADSVDAVQE LIKQFQQQQT ATLDATLNVI KEGEDLIQQL RDSAVSNNKT
PHNSSISHIE SVLQQLDEAQ VQMEELFHER KIKLDIFLQL RIFEQYTIEV TAELDAWNED
LLRQMNDFNT EDLTLAEQRL QRHTERKLAM NNMTFEVIQQ GQDLHQYIME VQASGIELIC
EKDIDLATQV QELLEFLHEK QHELELNADQ THKRLEQCLQ LRHLQAEVKQ VLGWIRNGES
MLNASLVNAS SLSEAEQLQR EHEQFQLAIE KTHQSALQVQ QKAEVLLQAG HYDADAIREC
AEKVALHWQQ LMLKMEDRLK LVNASVAFYK TSEQVCSVLE SLEQEYRRDE DWCGGRDKLG
PASEIDHVIP LISKHLEQKE AFLKACTLAR RNAEVFLKYI HRNNVSMPGV ASHTRGPEQQ
VKAILSELLQ RENRVLHFWT LKKRRLDQCQ QYVVFERSAK QALDWIQETG EYYLSTHNST
GESAEETQEL LKEYGEFRIP AKQTKEKVKL LIQLADSFVE KGHIHATEIR KWVTTVDKRY
RDFSLRMGKY RYSLEKALGI NTEDNKDLEL DIIPASLSDR EVKLRDANHE VNEEKRKSAR
KKEFIMAELL QTEKAYVRDL HECLETYLWE MTSGVEEIPA GILNKEHIIF GNIQEIYDFH
NNIFLKELEK YEQLPEDVGH CFVTWADKFQ MYVTYCKNKP DSNQLILEHA GTFFDEIQQR
HGLANSISSY LIKPVQRITK YQLLLKELLT CCEEGKGELK DGLEVMLSVP KKANDAMHVS
MLEGFDENLD VQGELILQDS FQVWDPKSLI RKGRERHLFL FEISLVFSKE IKDSSGHTKY
VYKNKLLTSE LGVTEHVEGD PCKFALWSGR TPSSDNKTVL KASSIETKQE WIKNIREVIQ
ERIIHLKGAL KEPIQLPKTP AKQRNNSRRD GVDDADSQGD GSSQPDTISI ASRTSQNTVD
SDKLSGGYEL TVVLQDFTAS HSSELSIQVG QTVELLERPS ERPGWCLVRT TERSPPQEGL
VPSSALCISH SRSSVEMDCF FPSGKDAYSV SSNDNGGKSD SVANLQPQPS LNSIQSSPGP
KRSTNTLKKW LTSPVRRLNS GKTESNIKKQ KKVRDGRKSF DLGSPKTGDE TTPQGDSADE
VCIGSSSLLA ARQSSSDVPT AADLVSAIEK LVKSKLVSLC NYAPPSNKRF TNHWSLIIKG
FMKRIEEKGV SEDMKGKDKI VFVFGLERRL HMYVVYCQNK PRSEYIVAEY EAYFEEVQQE
ISQRLTISDF LIKPIQRITK YQLLLKDFLR YSEKAGLECS DIEKAVELMC LVPKRCNDMM
NLGRLQGFEG KLTAQGKLLQ QDTFYVTEQD SGVQSRPKER RVFLFEQIVI FSELLRKGSL
TPGYMFKKSI KMNYLIIEEN VDNDPCKFAL MSRETSDRVI LQAANPEIQQ AWVQDINQVL
DTQRDFLNAL QSPIEYQRKE SSSAVLRPQT GRVPQPNSRP YSSVPVGSEK PLKATSRNPS
LPPLKISTSN GSTGYEHSQP GDKYEQSKVG NEVAGLLLEK AGSSAPPAHW FLLCPFPQTD
LGGCNGTSSM MVIKDYYALK EDEICVNQGE VVQILAINQQ NMFLVYQPAN DHSPAAEGWI
PGNILAPLTK STTDNSDGSI KKSCSWHTLR MRKRAEKESS GKNEANGPRK SKDILGNKVS
VKIINPNFIQ EVAPEFLVPL VDITCLLGDT VILQCKVCGR PKPSITWKGP DQNILDNDNR
LPHIHSDSGE LSLKICNLMP QDSGIYTCVA TNEHGTASTS ATIKVQGNSA ADGATISWKE
NFDLAYAELH EIGRGRFSIV KKCVHKATRK DVAVKFISKK MKKKEQAAHE AALLQHLQHP
QYITVHDTYE SPTSYILVLE LMDDGRLLDY LMNHDELMEE KVAFYIRDTM EALQYLHNCR
VAHLDIKPEN LLIDLRIPVP RVKIIDLEDA VQITGHYHVH HLLGNPEFAA PEVIQGLPVS
LSTDIWSIGV LTYVMLSGVS PFLDESKEET CINVCRVDFS FPPEYFSNVS HAARDFINVI
LQEDFRRRPT AATCLQHPWL QPHNGSYSKI PLDTSRLASF IERRKHQYDV HPVPSVKSFL
MSRLNPGT
//
