ID A0A077ZJU2_TRITR Unreviewed; 1470 AA.
AC A0A077ZJU2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=dTMP kinase {ECO:0000256|ARBA:ARBA00012980};
DE EC=2.7.4.9 {ECO:0000256|ARBA:ARBA00012980};
GN ORFNames=TTRE_0000719601 {ECO:0000313|EMBL:CDW58870.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW58870.1};
RN [1] {ECO:0000313|EMBL:CDW58870.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW58870.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; HG806438; CDW58870.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077ZJU2; -.
DR STRING; 36087.A0A077ZJU2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR CDD; cd11648; RsmI; 1.
DR CDD; cd01672; TMPK; 1.
DR CDD; cd01025; TOPRIM_recR; 1.
DR Gene3D; 3.30.60.80; -; 1.
DR Gene3D; 3.40.1360.10; -; 1.
DR Gene3D; 6.10.250.240; -; 1.
DR Gene3D; 3.30.1310.10; Nucleoid-associated protein YbaB-like domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.8.420; RecR Domain 1; 1.
DR HAMAP; MF_01877; 16SrRNA_methyltr_I; 1.
DR HAMAP; MF_00274; DNA_YbaB_EbfC; 1.
DR HAMAP; MF_00017; RecR; 1.
DR HAMAP; MF_00165; Thymidylate_kinase; 1.
DR InterPro; IPR000878; 4pyrrol_Mease.
DR InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR InterPro; IPR004622; DNA_pol_HolB.
DR InterPro; IPR000093; DNA_Rcmb_RecR.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007557; PSP1_C.
DR InterPro; IPR023627; Rcmb_RecR.
DR InterPro; IPR015967; Rcmb_RecR_CS.
DR InterPro; IPR008189; rRNA_ssu_MeTfrase_I.
DR InterPro; IPR018063; SAM_MeTrfase_RsmI_CS.
DR InterPro; IPR039430; Thymidylate_kin-like_dom.
DR InterPro; IPR018095; Thymidylate_kin_CS.
DR InterPro; IPR018094; Thymidylate_kinase.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034137; TOPRIM_RecR.
DR InterPro; IPR010377; YabA.
DR InterPro; IPR036894; YbaB-like_sf.
DR InterPro; IPR004401; YbaB/EbfC.
DR NCBIfam; TIGR00096; 16S rRNA (cytidine(1402)-2'-O)-methyltransferase; 1.
DR NCBIfam; TIGR00103; DNA_YbaB_EbfC; 1.
DR NCBIfam; TIGR00041; DTMP_kinase; 1.
DR NCBIfam; TIGR00678; holB; 1.
DR NCBIfam; TIGR00615; recR; 1.
DR NCBIfam; NF041131; RicT_YaaT_fam; 1.
DR PANTHER; PTHR46111; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE I; 1.
DR PANTHER; PTHR46111:SF1; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE I; 1.
DR Pfam; PF13177; DNA_pol3_delta2; 1.
DR Pfam; PF04468; PSP1; 1.
DR Pfam; PF21176; RecR_HhH; 1.
DR Pfam; PF02132; RecR_ZnF; 1.
DR Pfam; PF02223; Thymidylate_kin; 1.
DR Pfam; PF13662; Toprim_4; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR Pfam; PF06156; YabA; 1.
DR Pfam; PF02575; YbaB_DNA_bd; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF111304; Recombination protein RecR; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
DR SUPFAM; SSF82607; YbaB-like; 1.
DR PROSITE; PS51411; PSP1_C; 1.
DR PROSITE; PS01300; RECR; 1.
DR PROSITE; PS01296; RSMI; 1.
DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:CDW58870.1};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 211..306
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 924..1009
FT /note="PSP1 C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51411"
FT COILED 8..35
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 935..962
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1140..1174
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1470 AA; 167282 MW; 55E07AA1C9E4C85B CRC64;
MMRGMGNMQG MMKQMQKMQK EMVKAQDELN VKEFTGSSTN DLVTVTFTGD KNMKAMTINP
ELIDPEDPDM LQDMIVLAVN DAITKITKET DQTMGKYTKG LPGIADVEQV PTWSSKAERV
REAFLEERKD RMQYPEPIAK LIESYMKLPG IGQKTATRLA FFTIDMKDES VNEFARSLIS
VKRDLRFCSV CGNITEEDPC EICSDTTRDR GTILVVEEPK DVMSMEKVRE YHGLYHVLHG
VLSPMEGTGP EDINIAPLIK RLHDDEVKEV IIATNATTEG EATAMYLSRL IKPAGIKVTR
LAYGLSVGSD IEYADEITLL KAREKIKIIL GDKNVNGLFI TIEGPDGAGK TSVLNELYPR
LQLTAKRSIV KTREPGGIPI AEKIRHVILD PSNDRMDDRT EALLYAAARR QHLIEKVWPA
LDEDKIVLCD RFVDSSLAYQ GAGRGIGIEE VAKINEFAIE GTTPDITLYL DVDSDTGLQR
IMKNRTNQID RLDSEGLQFH QRVRHAYLKL AEENPDRIIK IDARKRLDEV TFRWMDKSLI
LLKLKSAVRQ YLSCQSKAST SIKMEEAKKL QTIQPIVFRQ LQNSFEHGRL AHAYLFEGDQ
GTGKAELALW FAKHQFCLNL QEEMPCETCN NCLRITSKDH PDVVEIEPDG QSIKVDQIRA
LQSELTKSGF ESAKKVVIIH QAEKMNMNSA NSLLKFLEEP PANFMIILET QSLGKILPTI
RSRCQIIHFQ ALSTERLQSR LEAEQIPEKT AKLLANLTNS YTKAVEISKD EWFNEARDVV
IQWFNYLEKN DPQAFIYVQK KMVRTFKDKA QQQLAFEMLA YFVKEKRDQV MRQNQIGVEK
YNYLLEDVLS ASQKLEANRV GRTMVEVVGV RFRDAGHIYY YAPGKNEYFY NDKVLVESQQ
AHQIATVAIP KIEIEKKDLS DDLKTILHKA SDKELKKVAQ NEADAEAAFK TAKEKIRAHE
LEMKLIRVEY TFDRSKMIFY FTADGRIDFR ELVKDLAGVF RTRIELRQIG VRDEAKILGG
IGPCGRPLCC STFLGDFIPV SIKMAKDQGL SLNPTKISGL CGRLMCCLKY ENGEYEAAKK
EMPDYGKEIN TPEGRGKVIG LNLLSKVVKV RLFGRDATID FDYQELVEAE LDMQKNLEDL
VSMKETLLEL VEKNAKLEME NERLRERIRE IDEKKSPVLD ERQELSESRL NLEKIYEDGF
HVLPTPIGNL EDMTFRAVKT LQTVDLIASE DTRNTQKLLN HFDVKVPQKS LHEHNYNERI
PELLDFLKKG RSIAQVSDAG MPSISDPGHE LVVACIEEDI PVVALPGATA GMTALIASGL
LPQPFYFYGF LQRKKSAQKK ELEELKNQTA TLIFYESPHR VKETLKNISE ILGNRDVVIS
RELTKLYEEY LRGTVTELMD YLSEHSLKGE CCLLVSGTTE VLEEEVFQGT LKEQVEALVE
EGQLTKEAIK SVAKRHGLKK QDVYREYHEL
//
