ID M3Y0U0_MUSPF Unreviewed; 2488 AA.
AC M3Y0U0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=POLQ {ECO:0000313|Ensembl:ENSMPUP00000004941.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000004941.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000004941.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
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};
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DR EMBL; AEYP01017745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01017746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01017747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01017748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01017749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01017750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01017751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01017752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01017753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9669.ENSMPUP00000004941; -.
DR Ensembl; ENSMPUT00000005025.1; ENSMPUP00000004941.1; ENSMPUG00000004980.1.
DR eggNOG; KOG0950; Eukaryota.
DR GeneTree; ENSGT00940000158694; -.
DR HOGENOM; CLU_000818_0_1_1; -.
DR InParanoid; M3Y0U0; -.
DR OMA; HNMCQQF; -.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
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:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IEA:Ensembl.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IEA:Ensembl.
DR GO; GO:0006284; P:base-excision repair; IEA:Ensembl.
DR GO; GO:0097681; P:double-strand break repair via alternative nonhomologous end joining; IEA:Ensembl.
DR GO; GO:0042276; P:error-prone translesion synthesis; IEA:Ensembl.
DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
DR GO; GO:0031297; P:replication fork processing; IEA:Ensembl.
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 Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
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 InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
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; SSF53098; Ribonuclease H-like; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 11..195
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 230..463
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 838..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1505..1526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1679..1699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2052..2072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2169..2189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1511..1526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2488 AA; 278603 MW; 637722B5BBA86460 CRC64;
MFEWQAECLL LGQVLEGKNL VYSAPTSAGK TLVAELLMLK RVLEMRKKAL FILPFVSVAK
EKKYYLQSLF QEVGINVDGY MGSASPTRPF SSLDIAVCTI ERANGLINRL IEENKMDLLG
MVVVDELHML GDSHRGYLLE LLLTKICYIT HKSASCQANL ASPLSNAVQI VGMSATLPNL
EIVASWLNAE LYHTNFRPVP LLESIKIGNS IYDSSMKLVR EFQPNLQVKG DEDHVVSLCY
ETICDNHSVL LFCPSKKWCE KLADSIAREF YNLHHQAKGL VRSSELPPVI LEQKGLLEVM
DQLKRSPSGL DSVLQKTVPW GVAFHHAGLT FEERDIIEGA FRQGQIRVLA ATSTLSSGVN
LPARRVIIRT PIFSGQPLDV LTYKQMVGRA GRKGVDTVGE SILVCKNSEK SKGIALLQGS
LKPVRSCLQR QEGEEVTASM IRAILEIIVG GVANTSQEMQ TYASCTFLAA SMKEGKLGIQ
KNQDSVQLGA IEACVMWLLE NEFIQTTEAS DGTEGQVYHP THLGSATLSS SLSPIDTLDI
FADLQRAMKG FVLENDLHIV YLVTPMFEDW TTIDWYRFFC LWEKLPTSMK RVAELVGIEE
GFLARCVKGK VVARTERQHR QMAIHKRFFT SLVLLDLISE VPLKEINQKY GCSRGQIQSL
QQSAAVYAGM ITVFSNRLGW HNMELLLSQF QKRLTFGIQR ELCDLVRVSL LNAQRARFLY
ASGFLTVADL ARANIAEVET VLKNAVPFKS ARKAMDEEEE AVEERRNMRT IWVTGRKGLT
EREAAALIVE EAKMILQQDL VEMGVQWNSY FLLNSDTHSV TSSESEVKEQ KYISQTKRSC
ERLTSQKKNN SMFSDSSAKH SPSTVQDLEK SGEHKNSFYD KLQNGNQERQ VHSISRARKR
ASLNRSKEKL RTSLNEGRAR TKKVVQTLLF EKTKKEAQSF NSKTMSTASG SWKHSKLVKQ
SKHSSPKKDT EICRIDLQEH TMSNPIYYGD EFTLDEKNVE FRSPDPFAEN VSFCAEGKYS
KASFSLEREQ SSKNKTKTNN ILVEHFIRQS QSKKVTCQPT NMVSENGGEF AVVESEKINT
VLVEENNSKN QNVYVKRDTY SVNQCPEKQS DKQTNTYTKQ KKIIERQMPC ETGSSYMNRD
SNVIIKCGIT KFNSEENNSN NFQVSGDNIS RTEILPTREP EGQHENFPNT SRKQEKTEAY
AANKTKNNCV SDLGLVPCEF EDSFYLDTQS EKIIQQMATE NAKPEAKYAK LATGKMQKCL
DNQSSILSFQ NEICITFPGE QHSPGVTNKN HLELKPADNI KQGTDSDGID ILTPESSIFL
SPILLRENGP CFKRNELSVT DSQLNSFLQG YQTQEAMKPV IPLVPQKRTT TGIETECLPV
PETSLNLSDS LLFDSFSEDY LVKEQPPDIQ VKEPLSSALT SNHFSHSVCL QGEGMIRKSN
MNENQDNQQQ YTCFSDESII FSEVDSAQMV EALDNVEICP VQEKQNTAVS FRALELSDPV
TVGNDYPQRE VIGGDKNERS QKPKLTETEE NNAFIWSGAS FDLSPGLQRI LDKVASPLEN
EKQKLTTINL SNLKGKNTEV NDKQKVISNL EPNQGQGISF APNIEVKSKI GTLETNALHA
ETSSHLPCKE NYIVDDNGLI PPTPTPVSAS KLVFPSILGT SSVKLQKTLS ALHLGESYSS
SNIKNPDLSS ESRNGLKEDS PIGDTTFSLQ LSQDGLQLTP TSFSPGSLAI IDVASDQTLF
RTFIKEWQSK KRFSISLACE KISSSTSKSA VIGGRFKPVS SPQETPIRDD GIPVKGCDDI
LVVGLAVCWG GRDAYYFSLQ KEQKHPEISS SLVPPSLDPS LTVKERMWYL LSCFQEESDK
ERSVIIYDFI QSYKILLLSC GISLEQSYED PKVACWLLDP DSKEPTLHSI VSSFLPHELP
LLEEIETGQG IQSLGLNVST EHSGRYRASV ESILTFNAMN QLNSLLKKEN LQGIFCKVEM
PSQYCLALLE LNGIGFSTAE CESQKHVMQA KLDAIESQAY QLAGHSFSFT SSDDIAEVLF
LELKLPPNGE IKNQSSKKTL GSTRRGNDNG RKLKLGKQFS TSKDVLNKLK ELHPLPGLIL
EWRRITNAIT KVVFPLQREK RLNPFLGMER IYPVSQSHTA TGRITFTEPN IQNVPRDFEI
KMPTLVGESP PSQALLPMNR GRDKKSRGLN SRYQAQMEER APDRGMPFSV SMRHAFVPFP
GGLILAADYS QLELRILAHL SHDRRLIQVL NTGADVFRSI AAEWKMIEPE SVGDDLRQQA
KQICYGIIYG MGAKSLAEQM GIKENDAACY IDSFKSRYTG INHFMKETVK NCKRSGFVQT
ILGRRRYLPG INDNNPYHKA HAERQAINTT IQGSAADIVK IATVNIQKKL EIFRSTFKSH
GHRESMLQSD RTGLLPKRKL QGMFSPIRGG FFVLQLHDEL LYEVAEEDVV QVAQIVKNEM
ESAVELSVKL KVKVKIGASW GELKDFDV
//
