ID A0A1V9X7U1_9ACAR Unreviewed; 2025 AA.
AC A0A1V9X7U1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=DNA polymerase theta-like {ECO:0000313|EMBL:OQR69619.1};
GN ORFNames=BIW11_12152 {ECO:0000313|EMBL:OQR69619.1};
OS Tropilaelaps mercedesae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC Tropilaelaps.
OX NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR69619.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR69619.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR69619.1};
RX PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT is shaped by the parasitic life history.";
RL Gigascience 6:1-17(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000256|ARBA:ARBA00024632};
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:OQR69619.1}.
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DR EMBL; MNPL01020321; OQR69619.1; -; Genomic_DNA.
DR STRING; 418985.A0A1V9X7U1; -.
DR InParanoid; A0A1V9X7U1; -.
DR OrthoDB; 208079at2759; -.
DR Proteomes; UP000192247; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; IEA:UniProt.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR CDD; cd18026; DEXHc_POLQ-like; 1.
DR CDD; cd08638; DNA_pol_A_theta; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.3380.20; -; 1.
DR Gene3D; 3.30.70.370; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR002298; DNA_polymerase_A.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR046931; HTH_61.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR048960; POLQ-like_helical.
DR PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF20470; HTH_61; 1.
DR Pfam; PF21099; POLQ_helical; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000192247}.
FT DOMAIN 52..226
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 318..478
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 850..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1050
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1065
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1087
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2025 AA; 224665 MW; 04DEFC70AEE735F6 CRC64;
MADVKRLSQL GSQELHQLED ISQWGLPSAI VDNYQEKGVT RMFPWQVQCL MSSGVLQGKN
LVYSAPTSAG KTLVAELLML KRVLETRKKA IMILPFVSVT REKMFYFQNL FSSGGLRVGG
YMGSHFPVGG FQTVDIAVCT IEKANALVNK LLQENELDLL CCVVVDELHM LGEPQRGYLL
ELLLTKLLYD QRHSCSSSIQ LIGMSATLPN LDLVAHWLDA SIYRTEYRPV PLTECVKVGS
APPLNVITGQ VAEVPVLRCA LPRSVDDPDG CLGLVIRTVS QGFGVLMFLP TKTWCEKMSQ
QIARAFLAVG KPSSEPENVD PELLQLGADL RAINKRNELQ EVLEKLRQTP AGLDENLKKT
IPYGVAFHHA GLTYDERDII ENAFKAGVLN VLTATSTLSS GVNLPARRVL IRTPIFARQL
LDVLTYKQMI GRAGRKGIDD RGESILICKD HEREQAMRLA TMKLAPVQSC LASRGSVSSA
FKRAILEVVA SGMATTLSEV ESYTKCTFLN ECEQAALSQR VADEGRHENG YMACLAADAC
IEFLVKNDFI QVLPEESGVR AVTPTKLAQA VLASSLSPDQ ALLVLRELRK CRENFVLEND
LHIIYEVTPY FISEQASIDY SVLSEFFDAL SEDRRRVANL IGFDLGYVYK CIRGAASKRD
KEMQEPLHRR FYVALALNEL VQEVSLADVS AKFGLQKGML QNLQQSAATF AGMMAIFCKR
LGWHNLELLI AQFQKRLHFG VQQELCELLQ LVPMTAQAAR ILFNAGFIAL PELARAELHE
VEAAFRSARV YQGKYVDFQE GESSADVRWI YLNGFDGVTE REAARLLIDQ ARKTLHDWLG
VKVDFERKEQ ALSQQPLAKD HQQETNDGAD NDTDQNAPLD TSTKQALVDG ATEKANTLQR
HQEAEPSQTA CHRQSGTVQA IAELKLTETT TPSRSCTSHG SDLSATLKQS KTLTERSTNP
VHHENDVRTG GQASTKTQLD GSATTSEKNN EKSRVSLNSS RIMGENSFHE GVEHCSTPTR
NPTKDKREEV KQSTNLQTTS VASNTAHSAF HDYESLKRSK RYPSTEGVED TSAAGQPSVQ
RSSIENAEED SIFGEVKTQQ RDQPQVPEKN GSMDMRDSSL FDDIDTQPDD TPTIQEHQPA
NIRSRRPSMA KRLTNANPAA SVRVTPTKIR MLEEEGQKIQ VALRASKKRC LEEECTNGEK
KSKPNSSPSF DGDMKLERRS ASEDSMAFFN SSQLKDITQN AKNALADRLP RVASENDSDL
IFDCVLTCQR GLSNEAANGD DVLPQEVEAS ADAVDMVSTL TGPSKMQTNS VQDSDSDLFS
DGENALPIAA AKEPIGDNFS EDESSLDLHL TSSSSSLTFI PSKDSSSLLE TGGELRCVRE
LTEAELFRQI EAAGRRFSLS LETEPAESSV RIEPAILGSR TPSTANAGLS VGSRRLVGFC
VAVKSDEGIF YTLRERDERN AMLLKKILEP SCVYTIAVLD CLNQLKTVMV TLGLVPDSEN
VRFEVEKIGI DLHMDAGIAH WLLDSSACSC PSLENLCQQY CPMLTDKVGK SRSTSVPRSC
IESCLHLSIL KAARHHLSTM SISQEVFRRE MRICVVLARI DLNGFGYDDK TCEAQVNAMR
DLQLQLESKM ACRAQRAFKI SSPTEVSRVI YTLFKDELVK LKIITGREPP GKLKLSSKAI
LVKLAEQDEF PQWIVDARKI ASILAKDMFP VLRAKQFHSG LNQHRIYSTS SPYTATGRMA
SNEPNLQSMA RNFRSAGEEI LIRRGFVPMS GSVILSADFS QLEMRLLAHL SGDMRLCQMF
SDPEGDVFAH VASQWRQRRL EDVSSRERQQ AKELCYGIIY GKSVKSLAED LAVTQEEGEI
FLQSFHATFP GIQKYTSKVI ANCRQLGYVE TLLGRRRYLP NITSSNIHLK ARAERQAINS
TIQGSAADLL KSCLIGIDAE LAKRFPESFK PHRSYGASTH VPIRGAFIVM QLHDEIILEV
HESILSTVSQ LVRFRMERAI SLRVPLVVKL KTGPHWSSVT PFEAL
//
