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Database: UniProt
Entry: R5AGG6_9CLOT
LinkDB: R5AGG6_9CLOT
Original site: R5AGG6_9CLOT 
ID   R5AGG6_9CLOT            Unreviewed;       632 AA.
AC   R5AGG6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Protein kinase {ECO:0000313|EMBL:CCX42395.1};
GN   ORFNames=BN454_01655 {ECO:0000313|EMBL:CCX42395.1};
OS   Clostridium sp. CAG:1024.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262770 {ECO:0000313|EMBL:CCX42395.1, ECO:0000313|Proteomes:UP000017946};
RN   [1] {ECO:0000313|EMBL:CCX42395.1, ECO:0000313|Proteomes:UP000017946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:1024 {ECO:0000313|Proteomes:UP000017946};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCX42395.1}.
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DR   EMBL; CAWJ010000237; CCX42395.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5AGG6; -.
DR   STRING; 1262770.BN454_01655; -.
DR   Proteomes; UP000017946; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06577; PASTA_pknB; 3.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.10.20; -; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR005543; PASTA_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR   PANTHER; PTHR45832:SF24; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45832; SERINE/THREONINE-PROTEIN KINASE SAMKA-RELATED-RELATED; 1.
DR   Pfam; PF03793; PASTA; 3.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 3.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51178; PASTA; 3.
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   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:CCX42395.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000017946};
KW   Transferase {ECO:0000313|EMBL:CCX42395.1}.
FT   DOMAIN          10..280
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          339..408
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          409..475
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          477..545
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   BINDING         39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   632 AA;  67356 MW;  1E4B3C6E422D8851 CRC64;
     MIGVILNHRY RIAALIGTGG MAQVYRAVNL TTRKNVAIKM LKPEYRENPE FLRRFEREAR
     AVLHLSHENI VRAYGVGQYD GMPYIVLEYV EGRTLKEIIQ ERGAMPAKSA VSLCTQVLDA
     LSAAHEAGII HRDVKPQNVI ITPSGRAKLT DFGIARDVQA TTVTFAGSTV LGSAHYLSPE
     QAKGKPVTAE SDLYSVGVML YEMLTGDVPF SSDSTVSIAL KHINETPLSP IELNPRIPPA
     LNEAVLIALR KEPLERFDSA RRMAWAINRA LRDPNWHPIT GREQQPDADM AFSAGSGAMG
     QPDGSIARLH GAWKIAIVVG VFISILIGTF LATRSSFTGK SGSLAVVPSL TGKTLQEAQS
     KAADYGLALE IEGYVASTAV DYGRIVSQSP DAGFSVKSGS SVKVSVSAGP EVPVVPNLAG
     KTYDETVAAI QAAGLQLGTV SYQVSDVAIG YVCAQSPLAG TEIIPGSTVD IIISATAANM
     IPMPAITSLS LSDALAALDA VGFERIYLRY DEAGMAENTG EIISQQPNAG ETVPSNMTVT
     LTVSGAAPSD CVSDIAYNLT IEKSGTPVMV TIEETVSGVH VERILFEGLL QKGEKVPVSF
     TATAQASGRY ELILYVNGTE VRRQDTGFSV KE
//
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