GenomeNet

Database: UniProt
Entry: D4YMX5_9MICO
LinkDB: D4YMX5_9MICO
Original site: D4YMX5_9MICO 
ID   D4YMX5_9MICO            Unreviewed;       824 AA.
AC   D4YMX5;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   18-SEP-2019, entry version 49.
DE   RecName: Full=Thymidylate kinase {ECO:0000256|HAMAP-Rule:MF_00165};
DE            EC=2.7.4.9 {ECO:0000256|HAMAP-Rule:MF_00165};
DE   AltName: Full=dTMP kinase {ECO:0000256|HAMAP-Rule:MF_00165};
GN   Name=tmk {ECO:0000256|HAMAP-Rule:MF_00165,
GN   ECO:0000313|EMBL:EFG47440.1};
GN   ORFNames=HMPREF0183_1232 {ECO:0000313|EMBL:EFG47440.1};
OS   Brevibacterium mcbrellneri ATCC 49030.
OC   Bacteria; Actinobacteria; Micrococcales; Brevibacteriaceae;
OC   Brevibacterium.
OX   NCBI_TaxID=585530 {ECO:0000313|EMBL:EFG47440.1, ECO:0000313|Proteomes:UP000005714};
RN   [1] {ECO:0000313|EMBL:EFG47440.1, ECO:0000313|Proteomes:UP000005714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49030 {ECO:0000313|EMBL:EFG47440.1,
RC   ECO:0000313|Proteomes:UP000005714};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C.,
RA   Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L.,
RA   Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y.,
RA   Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L.,
RA   Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F.,
RA   Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M.,
RA   Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S.,
RA   Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J.,
RA   Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J.,
RA   Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D.,
RA   Worley K., Gibbs R.;
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC       salvage pathways of dTTP synthesis. {ECO:0000256|HAMAP-
CC       Rule:MF_00165}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528,
CC         ChEBI:CHEBI:456216; EC=2.7.4.9; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00165, ECO:0000256|SAAS:SAAS01114966};
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000256|SAAS:SAAS01070220}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EFG47440.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; ADNU01000037; EFG47440.1; -; Genomic_DNA.
DR   RefSeq; WP_005883937.1; NZ_ADNU01000037.1.
DR   STRING; 585530.HMPREF0183_1232; -.
DR   EnsemblBacteria; EFG47440; EFG47440; HMPREF0183_1232.
DR   eggNOG; ENOG4108ZMD; Bacteria.
DR   eggNOG; COG0125; LUCA.
DR   OrthoDB; 257682at2; -.
DR   BioCyc; GCF_000178455-HMP:HMPREF0183_RS12095-MONOMER; -.
DR   Proteomes; UP000005714; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00165; Thymidylate_kinase; 1.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039430; Thymidylate_kin-like_dom.
DR   InterPro; IPR018095; Thymidylate_kin_CS.
DR   InterPro; IPR018094; Thymidylate_kinase.
DR   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00041; DTMP_kinase; 1.
DR   PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070209};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005714};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:EFG47440.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070211};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070205};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005714};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204, ECO:0000313|EMBL:EFG47440.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     24     45       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     65     87       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     99    118       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    124    145       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    152    170       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    182    204       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    234    254       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    266    285       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    297    315       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    347    366       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    378    403       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      479    667       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND     481    488       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
FT   REGION      701    824       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    707    721       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    780    800       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   824 AA;  87222 MW;  ABB652D20A6B222D CRC64;
     MDTQTVLSKP HAGTIGHAAL EVGAWLVALS SAAISFAIVG IHGFGGAMDI SRYGELTQIQ
     RDGGFNSSFA VPGLLAFFAL AVAGVLIPPK KLTQLKESVR SQLLTLFAAA TACVSVVVVF
     IPTFWLTLIV AALLGMLVGV LAAHAPELHT KPWRTGGLAV GIFLLVTYYF ELEHGVPAGA
     HALRWLLFVG AILLIVAALM VLVFPLSSDR DIDDLHTFPH TLAIKRSRGH MSIAFPWACY
     ALFAVLGALF LLPLPATVDG GYGQGAIGLM TAAVLLGWAA GYESGPTFAP GMTRPRLTAF
     ALVAAGLLMI CAGLIDELSG KAVLMALTAF CVGVGVRAQK YEFSRRVGLA VGALLATLLC
     GLDLTFDIHL SAVTTWVLSA SGVAFSAIGL LAFATGILAI FFFSPMGVRG MGVDLMNAFQ
     VSGDSSPRAT APAFAVAEDQ ETRVLPAATT SADEPQDAGA NYLAVPEPVT PSTGLFIAIE
     GGDGAGKTTQ IRKLVEHLES RGFDPVIATR EPGGTPVGKS IRSVLLDGEA VSKKSEALLY
     AADRAHHVAT LVAPSLEQDG AVVTDRYIDS SLAYQAGGRE LSEDDVLALS RWATSGLVPN
     LTLVLDIDPR VAAERMGNRE DANHLDKQSL EFKDRVRAGF LRLAEAEPDR YAVIPAGRSV
     NEVAEHIQRV VDAIIDGEES ADVADTFEPI APRGVFVGVP TERMSPEDAQ KAVDEHRYAE
     SPQFLTEPIK ADGAEDADSA ASAESTEDTE NAATTVLPQR PKAEGAPKPG GPTRAQAEPE
     TPETQEKPTD TAEPDPETYR AKLQRQSMIE QQARQRLRDA RRNS
//
DBGET integrated database retrieval system