ID A0A3B4VKB9_SERDU Unreviewed; 2105 AA.
AC A0A3B4VKB9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:ENSSDUP00000031019.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000031019.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000031019.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 STRING; 41447.ENSSDUP00000031019; -.
DR Ensembl; ENSSDUT00000031555.1; ENSSDUP00000031019.1; ENSSDUG00000022307.1.
DR GeneTree; ENSGT00940000158694; -.
DR OMA; HNMCQQF; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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 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 164..343
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 382..568
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 15..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1057
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2105 AA; 231930 MW; 398FB1621DD7ACB7 CRC64;
CHGLLQQFHT IRGRVTEHLF KPQAEEPTEP PAPRRDRQKR SSGTKGSPLG KEESGSSKNA
DPPLDARRDY ILFSPTRLAA AMKRAKLQQS FQNQSTSVLT VPTGLELSSL SDTLPQPGIA
LCAPLEQAEK LLLSSWGLPK PVLERYQKHG VTHMFEWQAQ CLTVGQVLQG CNLVYSAPTS
AGKTLVSELL MLKRVLETKR KALFILPFVS VAKEKMHYLQ SVFEEAGVRV EGYMGSTSAA
GGFTALDVAV CTIEKANSLI NRLIEEDSMG LLGMVVVDEL HMVGDSGRGY LLELLLTKIR
YIAQKQSTTG SLSNGVQIIG MSATLPNLSL LASWLGAELY QTDYRPVPLQ EHLKVGCNIY
DKSLSVVRPF TPVLHIKGDD DHIVSLCYET VRDGHSVLLF CPSKNWCEKL ADSIYHQHIL
HLIPVCLNQE ALVDVIAQLR RTPAGLDPIL QRTVPWGVAF HHAGLTFDER DVLEGAFRQG
MVRVLAATST LSSGVNLPAR RVIIRTPTFN GHLLDPLTYK QMAGRAGRKG VDTTGESVLV
CKEAERQKGI SLLNGALQPI NSCLVRREGE GVTTSMLRAI LEIIVGGVAS TPQDVRLYAS
CSLLAASMKC DSKHKSNEPN NKGAIEACVE WLMENEFISI QKDGQGTERY CPTQLGAATL
SSSLSPPEAL GIFADLQRAM KGFVLENDLH ILYLITPLYA EWTTIDWYQF FCLWEQLSSS
MKRVAEMVGV QEGFLARSVS GKLVAKTEKQ RRQMAIHKRF FTTLVLQDLV NEVPLGTVAS
KYNCNRGQLQ SLQQSASTYA GMVTVFCKRL GWHNMELLLS QYQTRLSFGV QRELVDLVRV
SLLNATRARA LYAQGLCTVA ELARATVADV EKALRNAVPF KSSKRAVDES EMEAAERRSL
RCVWVTGGRA LTEQEAATEI VSEARLLLQE DLARLGVQWD PTTLPPGAPA VNSCDNRHSS
DTETSSVSYL SSPEVSPGPG GGDNVDEDKN EGGGGDDNEA LDANQVASES PNRSSSFLFD
SLYDSSLLAG LSPQQILDQS DEEESECHLP STQERRRSEL LANQDAEKQE AIQWGESSFN
LSEWGDSLFV GEHFLERQSL LRHSERTRHE QEARHCQAQQ PDADHQFTNG QNKNKPGGRQ
GRINKEGESG NQVEEEKEAK MNVLLPDNVP QSTVHCSPGL QEIFDRWPSM SDQSWHNTTT
GHTATQTHTT HTAAANTVDA PDLPQTLMQV SRKRGKVNVQ SAAAESDSQP EQPPTHDTEN
VRERPGSAGD LIPPTPETPP VTPRIKLTTS SVQSPLTTRN HLSEAADTEQ PDSMPDWSRK
HQLRHPKTLP ESEPKSVPCS SSKTKPPRHC ASPSSPRPKP PSDTESPVTD EGFTLQLSQD
SSLCSSNSGT FSIVDVASER RLFDTFIKEW KTKERYSLAL ACERREHRQQ PEGEIGGKHT
RAHQKLNRTD GFPVRDSDGL VLIGLSVCWG ARDAYYISLQ QEQSKGLSAS LAPPPLDGDL
PVSERLGQVK ACLSRPLAGL KGDVIVTYDI IQVYKTLVLS CGISLEGSCE DPKVACWLVD
PGSEERTLPN MVTVYCPEEL PLLDGLGNAH AHCPRVRAAT KSVLVHAVMN HLTSLLEKDD
LFRSVEMPSQ VCLALLELNG LGFSVRECER QKHVMQAKLT ALESQAYNLA GHSFSLTSID
DIAQVLFLEL HLPPNGDVGG SKSKKTLGYT RRGGGRVRLG KQFSTTKDVL EKLCPMHPLP
GVILEWRRIT NALTKVVFPL QREKQHHPTL AMDRIYPIAQ THTATGRVSF TEPNIQNVPK
DFEIYMPTVV GESPPSQNGQ MTTKKRRSVV PSVTAGAAEQ GPAFSVSMRH AFVPFSGGMI
LAADYSQLEL RVLAHLSKDQ RLLQVLNGGA DVFRCIAAEW KSVDPETVKD NLRQQAKQIC
YGIIYGMGAK SLGEQMGVEE NDAACYIESF KARYKGINAF LKETVKNCIK SGYVQTLMGR
RRYLPGITNT NTHIKAHAER QAVNTTVQGS AADIVKLATV NIQKQLRKTF PAAPLSHQAG
TSQLRGAYFV LQLHDELIYE TTEEDLIQVA QIVKREMESA VKLYVKLKAK VKVGPSWGNL
QDLDL
//
