ID A0A0V0TIR5_9BILA Unreviewed; 377 AA.
AC A0A0V0TIR5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=dTMP kinase {ECO:0000256|ARBA:ARBA00012980};
DE EC=2.7.4.9 {ECO:0000256|ARBA:ARBA00012980};
GN Name=dtymk {ECO:0000313|EMBL:KRX38868.1};
GN ORFNames=T05_14228 {ECO:0000313|EMBL:KRX38868.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX38868.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX38868.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX38868.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core and F(0)
CC - containing the membrane proton channel, linked together by a central
CC stalk and a peripheral stalk. During catalysis, ATP synthesis in the
CC catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation. Part of the complex
CC F(0) domain. Minor subunit located with subunit a in the membrane.
CC {ECO:0000256|ARBA:ARBA00024864}.
CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004992}.
CC -!- SIMILARITY: Belongs to the ATPase F chain family.
CC {ECO:0000256|ARBA:ARBA00005895}.
CC -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC {ECO:0000256|ARBA:ARBA00009776}.
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:KRX38868.1}.
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DR EMBL; JYDJ01000252; KRX38868.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0TIR5; -.
DR STRING; 144512.A0A0V0TIR5; -.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:UniProtKB-KW.
DR CDD; cd01672; TMPK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00165; Thymidylate_kinase; 1.
DR InterPro; IPR019344; F1F0-ATPsyn_F_prd.
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 NCBIfam; TIGR00041; DTMP_kinase; 1.
DR PANTHER; PTHR10344; THYMIDYLATE KINASE; 1.
DR PANTHER; PTHR10344:SF1; THYMIDYLATE KINASE; 1.
DR Pfam; PF02223; Thymidylate_kin; 1.
DR Pfam; PF10206; WRW; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE 3: Inferred from homology;
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Kinase {ECO:0000313|EMBL:KRX38868.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW Transferase {ECO:0000313|EMBL:KRX38868.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 178..354
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
SQ SEQUENCE 377 AA; 44037 MW; F70983B6367B0B03 CRC64;
MINSIIEWQN RYIQRLDPTI VKRVDRYIDA VKKSRSSRQI LTLLPQRMVL NASEKIWKNY
LRKADFGLLP KEYNKKIHGP YCPWRYYGKK DTNIFDVKLA DFSAWMSRRD TSARGIMAAM
SRGYYSWIYH WFSPRVANAA PLCHLLAFMA FARMILNHNN FKRDQFLMEN CRGALIVFEG
LDRSGKTTQV RLLSNFLQCH AFPVVTMRFP TRAGVIGEML DQYLNKKVEM ENHVAHLLFS
ADRWAVHSEI ENNIKCGTTV IVDRYLFSGI AFSAAKGLDF DWCMNADRGL PQPDVVFFVD
VKPETLKNRG EFGVERFDDE EFQRSVRHNY QRLTDKYWQV IDGEKSQKEI ADQIERTVCD
LLKSPAMASP LKMFGYT
//
