ID A0A2P2E580_9LEPT Unreviewed; 1883 AA.
AC A0A2P2E580;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Kinase domain protein {ECO:0000313|EMBL:GBF52036.1};
GN ORFNames=LPTSP4_35740 {ECO:0000313|EMBL:GBF52036.1};
OS Leptospira ryugenii.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1917863 {ECO:0000313|EMBL:GBF52036.1, ECO:0000313|Proteomes:UP000245133};
RN [1] {ECO:0000313|EMBL:GBF52036.1, ECO:0000313|Proteomes:UP000245133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YH101 {ECO:0000313|EMBL:GBF52036.1,
RC ECO:0000313|Proteomes:UP000245133};
RA Nakao R., Masuzawa T.;
RT "Novel Leptospira species isolated from soil and water in Japan.";
RL Submitted (FEB-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 -!- 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:GBF52036.1}.
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DR EMBL; BFBB01000009; GBF52036.1; -; Genomic_DNA.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000245133; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR43642; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR PANTHER; PTHR43642:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:GBF52036.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245133};
KW Transferase {ECO:0000313|EMBL:GBF52036.1}.
FT DOMAIN 7..269
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 1883 AA; 214671 MW; 9F2EC806FF7C5CEE CRC64;
MLSLGGCEHL ELIHRSDRHT IYRGIKNSLP VILKILNKEY PSQKELNDFA SEYHILQSLA
SHRIVKAISL EKIENTLGII FADIGGKALY KTSVLQYSLS QKIELFIKAV EGLQTIHDAE
LMHRDIKIHN IILNEETGDL QIIDFGSASR LTKQNTFISL HQSVEGTLAY ISPEQTGRMN
RTVDYRTDFY SLGITFYQIF TGKVPFFFPD PLELIHAHIA KTPIPPVDIS NIPSSISNII
LKLMEKDPND RYQSAQGILK DLIKCRVYFE KYGLDGLNKF QLKVAEEDFS SRFQIPQKLY
GREKEIQSIQ SMFKSITKGA SGLLFVSGVS GIGKTSLVSE IRKSVTESRG YYLTGKFDLL
KRSIPYRAIS QAFQSLVQQI LTEGEASIQR WKLSLQNALG HNAKLLVDMV PDLASLLGEI
PEMVSLSAEE AENRFHEAFQ NFLDCLCKNE HPLVIFLDDL QWADLPSLQL IETIFLHSDR
QHLFLILAYR SSEVVQGDAF SQTLERLKRI QKNHQEIFLF PIEKPDVYNL VKETLSCDPN
TAGQLAEDLF HKTKGNPFFI NAVFQGYYDK DLIKFRQNVW QLDLNKIKAE QIAENVIDFM
VDKVKELPEN LSQVLKFAAC VGNWFRTEVF IHIYNQPRDI VTETLIQLSN EGFLNQTDFE
VNFIHDKIRE ATYSLIPEKT RSLYHYQIAN GYISLLHQYK LDDYIFTIVN QLNQGIAYLR
TEEEFQRHID YNLLAGKKAL SSLAAEAAAD FLKMAIRSLS PNSWQSDYER TLNIYSYLAR
AEYLSKNFEE AERIFNLILE NSKTAEDQSV VYELKSSIYV SQNKMDEALS ILKKAVGRLG
IRLPAKPSEI SPLPEIIKFK VKFGKRKIES LYDAPLLEEK KSNLILHLLN SAIAPSFIGQ
PALFPVIVLK MVNLSIRKGN SPLSAFAYSL FGIIQGSGLG DFNAGFAFGQ LALRLLNRFK
EEAKAVECKI RFIYANMISP WKRHAKEGES EFLKSISSGR ESGDLQYTSY AINNLHFQKI
LMRQNLLEIK ESFQKYDKLF QNLKQYNAYQ LYQLNQQFIE NLSGTIEDKV SLIGTYFDER
VVLPEWIESK NANALFDFYL TKSRLEFLFG DARKALEYSW LADPYESAML GMMFVPEHVF
FQTLIIAECH EQSSIKDKKA LLKRVAKNIK RLAKWSESCS ENYAHKYFIS LALQSWLLGK
KEEAIARFKK AISLARLHGY LFEEAIANEW LAKYWLWKGE EPYAKYHLQE AKYAYETWGA
VNKASQLVSE HSFLKQSSYL PKDLSQKIDP KHSISPIHST SSHQFDLISV IKASQAISSE
IQLDKLLETM MRILLENAGA ESGLFILNRA EGFRIEAIGN FNRDEILTSQ GIPLTDADKY
PIHLINYVIR SKSVLLLNNA LAEGVFVNDP YILSHQSKSI LCYPIINHGI LTGIIYLENN
LLTSAFTEDQ IEVLKVLSAQ IGMSVENSLL FSNLEEKVEE RTKNLNDALI AVSSLKEQQD
MDYFLNTLLV EPLGVNHAHS KLVEVEFFLR QKKTFQFRGK DYELGGDINI SDNLKLAGKS
YTVFLNGDAM GKSVQGAGGV LVIGTIFKSI IQRTNSTDYG ADLYPERWIK NAYYEMQKAF
ESFDGTMLMS TIFGLLDEEM GTLYFMNVSH PDLVLFRSGA AHYVRRSNEL PKLGHDDPTL
SVSLNVISLQ NDDIILIGSD GKDDLIIGTD DAGYDIFNDD ETLFLNHVEA SKADLEQIYE
LVGKSGMIID DLSLLKIKWL GKKDTIPESI HLETLQEIQA LKVRKDFTSA LELARGTHEL
YPDRNEYLLE ISQIYAEEGE YKLAIDFGEK LRLREPKDTT NILNLVKCYL QIGKKNRAKE
ILHLALQALG QDPKLKEASE LLT
//
