ID A0A1Z4LZ91_9CYAN Unreviewed; 710 AA.
AC A0A1Z4LZ91;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:BAY86527.1};
GN ORFNames=NIES267_60370 {ECO:0000313|EMBL:BAY86527.1};
OS Calothrix parasitica NIES-267.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1973488 {ECO:0000313|EMBL:BAY86527.1, ECO:0000313|Proteomes:UP000218418};
RN [1] {ECO:0000313|EMBL:BAY86527.1, ECO:0000313|Proteomes:UP000218418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-267 {ECO:0000313|EMBL:BAY86527.1,
RC ECO:0000313|Proteomes:UP000218418};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) 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};
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DR EMBL; AP018227; BAY86527.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4LZ91; -.
DR OrthoDB; 5518868at2; -.
DR Proteomes; UP000218418; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24193:SF121; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24193; ANKYRIN REPEAT PROTEIN; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 9.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50297; ANK_REP_REGION; 6.
DR PROSITE; PS50088; ANK_REPEAT; 7.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:BAY86527.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:BAY86527.1};
KW Transferase {ECO:0000313|EMBL:BAY86527.1}.
FT DOMAIN 15..281
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 403..435
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 498..530
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 532..565
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 566..600
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 601..632
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 633..674
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 675..710
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 710 AA; 79869 MW; 39E00D1C2FB0296C CRC64;
MEPLHQPNNI IAQKYKIIST LGEGGSGITY LAQDLQNNQN VALKALSLHR MTDWKAMELF
EREAKILAQL NHPAIPDYLE YFDAEIDGEK YFYIAQQLAP GKSLAKLVEE NFRTNEQQIK
DIAKQILEIL IYLHSQTPAV VHRDIKPQNI IYDKDGKVFL VDFGAVQDTY YSTFMRGSTV
VGTYGYMSPE QFRGQSVPAT DLYGLGATLL FLLTHRSPAD FPTDGLKIDF RSRVKVSDDF
ADWLDKMLEP DLEDRFSSAR EALEVLQGKR KVITATKKPM LWKAVVGMGF SVLVTVGVFH
HYKWAILNRL AFVPTESICD NVNDIKNYVT YGGNPSLNLK SSDSSKRKKT LLRCAIEANS
QPLAEFLIAK GANINEELHY VKSVDWAKFL IDKGADVNRK INYAQTPLHY AVINQRKDIV
ELLLSHQAGV NAEDKFGYTP LLLLFEIHRK NSNDLNIQLL NDYRVDVRYI NAKSKRLRLP
LMKLLVEKGA NINIQNYQGY APLHLAVKQN DREIVKYLIR KKAKVDIRTK NNAETPLMLA
AKETAEIPIV KILTDNGADV NAKESDGNTP LHIASMNTQK SKDIIRLLVK SGANINAKAN
NGKTPLHNAI KVGKNRVKVL VDLGANVNAK DYKGETPIHT AIRHWINNRN EQDSIMNSIR
YLVKSGANIN AKNNNGLTLL HIVAKEGHLK DLDIVEFVSQ LGASFGVKNN
//
