ID E6JYK4_PARDN Unreviewed; 734 AA.
AC E6JYK4;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00195, ECO:0000256|HAMAP-Rule:MF_00238};
DE Includes:
DE RecName: Full=Cytidylate kinase {ECO:0000256|HAMAP-Rule:MF_00238};
DE Short=CK {ECO:0000256|HAMAP-Rule:MF_00238};
DE EC=2.7.4.25 {ECO:0000256|HAMAP-Rule:MF_00238};
DE AltName: Full=Cytidine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_00238};
DE Short=CMP kinase {ECO:0000256|HAMAP-Rule:MF_00238};
DE Includes:
DE RecName: Full=GTPase Der {ECO:0000256|HAMAP-Rule:MF_00195};
DE AltName: Full=GTP-binding protein EngA {ECO:0000256|HAMAP-Rule:MF_00195};
GN Name=der {ECO:0000256|HAMAP-Rule:MF_00195,
GN ECO:0000313|EMBL:EFT83831.1};
GN Synonyms=cmk {ECO:0000256|HAMAP-Rule:MF_00238};
GN ORFNames=HMPREF0620_0836 {ECO:0000313|EMBL:EFT83831.1};
OS Parascardovia denticolens DSM 10105 = JCM 12538.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Parascardovia.
OX NCBI_TaxID=864564 {ECO:0000313|EMBL:EFT83831.1, ECO:0000313|Proteomes:UP000004946};
RN [1] {ECO:0000313|EMBL:EFT83831.1, ECO:0000313|Proteomes:UP000004946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10105 {ECO:0000313|EMBL:EFT83831.1,
RC ECO:0000313|Proteomes:UP000004946};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: GTPase that plays an essential role in the late steps of
CC ribosome biogenesis. {ECO:0000256|HAMAP-Rule:MF_00195}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:456216; EC=2.7.4.25;
CC Evidence={ECO:0000256|ARBA:ARBA00001097, ECO:0000256|HAMAP-
CC Rule:MF_00238};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593,
CC ChEBI:CHEBI:456216; EC=2.7.4.25;
CC Evidence={ECO:0000256|ARBA:ARBA00001115, ECO:0000256|HAMAP-
CC Rule:MF_00238};
CC -!- SUBUNIT: Associates with the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00195}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00238}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. EngA (Der) GTPase family.
CC {ECO:0000256|ARBA:ARBA00008279, ECO:0000256|HAMAP-Rule:MF_00195,
CC ECO:0000256|PROSITE-ProRule:PRU01049}.
CC -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009427, ECO:0000256|HAMAP-Rule:MF_00238}.
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:EFT83831.1}.
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DR EMBL; AEON01000001; EFT83831.1; -; Genomic_DNA.
DR RefSeq; WP_006289222.1; NZ_CM001148.1.
DR AlphaFoldDB; E6JYK4; -.
DR KEGG; pdo:PSDT_0797; -.
DR PATRIC; fig|864564.6.peg.877; -.
DR eggNOG; COG0283; Bacteria.
DR eggNOG; COG1160; Bacteria.
DR HOGENOM; CLU_016077_4_0_11; -.
DR Proteomes; UP000004946; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0036430; F:CMP kinase activity; IEA:RHEA.
DR GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR CDD; cd02020; CMPK; 1.
DR CDD; cd01894; EngA1; 1.
DR CDD; cd01895; EngA2; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR HAMAP; MF_00238; Cytidyl_kinase_type1; 1.
DR HAMAP; MF_00195; GTPase_Der; 1.
DR InterPro; IPR003136; Cytidylate_kin.
DR InterPro; IPR011994; Cytidylate_kinase_dom.
DR InterPro; IPR031166; G_ENGA.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR016484; GTPase_Der.
DR InterPro; IPR032859; KH_dom-like.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR NCBIfam; TIGR03594; GTPase_EngA; 1.
DR NCBIfam; TIGR00231; small_GTP; 2.
DR PANTHER; PTHR43834; GTPASE DER; 1.
DR PANTHER; PTHR43834:SF6; GTPASE DER; 1.
DR Pfam; PF02224; Cytidylate_kin; 1.
DR Pfam; PF14714; KH_dom-like; 1.
DR Pfam; PF01926; MMR_HSR1; 2.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR PROSITE; PS51712; G_ENGA; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00238};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00238};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00195}; Kinase {ECO:0000256|HAMAP-Rule:MF_00238};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00195}; Reference proteome {ECO:0000313|Proteomes:UP000004946};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW Rule:MF_00195}; Transferase {ECO:0000256|HAMAP-Rule:MF_00238}.
FT DOMAIN 285..448
FT /note="EngA-type G"
FT /evidence="ECO:0000259|PROSITE:PS51712"
FT DOMAIN 460..633
FT /note="EngA-type G"
FT /evidence="ECO:0000259|PROSITE:PS51712"
FT REGION 173..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 8..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00238"
FT BINDING 291..298
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 338..342
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 400..403
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 466..473
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 513..517
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 578..581
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
SQ SEQUENCE 734 AA; 79567 MW; 9049774551B6EC16 CRC64;
MITVAIDGPS GVGKSSTSRA LAQHFGYAYL DTGAMYRAAA WWVMSQGVDL DQVTEADEER
ITRMVAAFFT EDHCRISLDP SAFDISSDGV SIKEAIRQVR VSTHVSAVSS IIPVRHLLIA
AQRAYIDQEN DPDSFSGGAG IVVEGRDITT VVAPYAQVRV LLTAREEVRQ ARRNAQSAAA
SSAAPAAGAA PRSGDDVAAR DAKDAKVTSF TTAAEGVTTV DNSDLTFDQT LDVLIGLVNE
AIDQDLYDNY LSQLEGYDLD EEDRALLAES EGPVGGQEAT DEKVGVIAVI GRPNVGKSTL
VNRVLGHRAA IVEDTPGVTR DRVSYEAEWA GHDFKLVDTG GWEADVEGID SAIADQASIA
MNMADAIIFV VDGTVGLTQT DDRIASLLRS SGKPVTVAVN KADSQAAEYA AAEFWKLGLG
EPLPISALHG RGVGDLLDAA VNSLSTVEKL TGSLAASDLR RVALIGRPNV GKSSLLNQLA
HENRSVVNDL AGTTRDPVDE VITIGDEKWL FIDTAGIKRR LHKQSGADYY SSLRTQAAIE
RSELALVLFD ASQPISDQDL KIMSSAVEAG RAIVLVFNKW DALDEFDRLR LERLWETEFN
RVAWAQRVNL SAKTGWHTNR LLGAMHIALD SWDKRIPTGK LNSFLGQLQA AHPHPLRGGK
QPRILFATQA ATKPPRFVIF ATGFLEHGYR RYIERSMRER FGFEGSPIQI SVHIREKKKK
GKSGATRRNT PGRT
//
