ID A0A3G6JAK0_9CORY Unreviewed; 778 AA.
AC A0A3G6JAK0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:AZA13500.1};
GN Synonyms=cmk {ECO:0000256|HAMAP-Rule:MF_00238};
GN ORFNames=CCHOA_05495 {ECO:0000313|EMBL:AZA13500.1};
OS Corynebacterium choanae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1862358 {ECO:0000313|EMBL:AZA13500.1, ECO:0000313|Proteomes:UP000269019};
RN [1] {ECO:0000313|EMBL:AZA13500.1, ECO:0000313|Proteomes:UP000269019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=200CH {ECO:0000313|EMBL:AZA13500.1,
RC ECO:0000313|Proteomes:UP000269019};
RA Kleinhagauer T., Glaeser S.P., Spergser J., Ruckert C., Kaempfer P.,
RA Busse H.-J.;
RL Submitted (NOV-2018) 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}.
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DR EMBL; CP033896; AZA13500.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G6JAK0; -.
DR KEGG; ccho:CCHOA_05495; -.
DR OrthoDB; 9805918at2; -.
DR Proteomes; UP000269019; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
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; TIGR00017; cmk; 1.
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 SMART; SM00382; AAA; 3.
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:UP000269019};
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 345..508
FT /note="EngA-type G"
FT /evidence="ECO:0000259|PROSITE:PS51712"
FT DOMAIN 518..691
FT /note="EngA-type G"
FT /evidence="ECO:0000259|PROSITE:PS51712"
FT REGION 257..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00238"
FT BINDING 351..358
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 398..402
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 460..463
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 524..531
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 571..575
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 636..639
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
SQ SEQUENCE 778 AA; 85499 MW; 7AC582A3C8B6EE4F CRC64;
MTHSTNPGYS PQDYAGYDQI NNQPNNGLLL AIDGPSGTGK STVARALAQI LGAQYLDTGA
MYRVATLYCQ QQGIDLADEA AVVAATADLP LVISDDPQST AVLLGGKDVQ TAIREADVTN
NVSQVAAYQG VRSNLVALQQ QLAHDAGRCV VEGRDIGTVV LPEAPAKVFL TASAEQRANR
RYQQDKAAGR NVTLDEVLQA VIARDEYDST RAVSPLQPAD DADIIDTSDY DQQTVIDIVL
DVVLDSAVQQ GYLDPSLIED DDEQDLDDDT TAVDAQPQSD DELSVTYVTA EDYLATDGSF
DDTDFAIDLD NPDFTKELDD EQWAAIEANF GLENAAQQHT EEALPTVAIV GRPNVGKSTL
VNRFLGRREA VVEDFPGVTR DRVSYVAEWN GRRYFVQDTG GWDPDAKGIH ASIARQAEIA
MAEADVIVMV VDTKVGITET DAVMAKKLQR SQVPVLLVAN KFDSDNQYGD VAEFWGLGLG
YPWPVSAQHG RGGADVLDEV INLFPEVPRN TTITEGPRRV ALVGKPNVGK SSLLNKITGD
DRSVVDNVAG TTVDPVDSLV QLDQHLWRFV DTAGLRKKVK TASGHEYYAY LRTKAAIDAA
EVCVFLIDAS SPISEQDQKI LNLVVESGRA LVIAYNKWDL VDEDRRYELE REIERQLAYI
PWARRVNISA KTGRALQKIE PFLLEALESW DQRISTGRLN NWLRTVIAAN PPAMRGGRLP
RVLFATQAAS RPPVIVLFTT GFLDHGYRRF LERRLREEFG FPGSPIRIAV RVREKRSR
//
