ID A0A850V5V1_9CORV Unreviewed; 1050 AA.
AC A0A850V5V1;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE RecName: Full=Helicase POLQ-like {ECO:0000256|ARBA:ARBA00069099};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
DE AltName: Full=Mus308-like helicase {ECO:0000256|ARBA:ARBA00076391};
DE AltName: Full=POLQ-like helicase {ECO:0000256|ARBA:ARBA00074990};
DE Flags: Fragment;
GN Name=Helq {ECO:0000313|EMBL:NWH37574.1};
GN ORFNames=CHLHAR_R03348 {ECO:0000313|EMBL:NWH37574.1};
OS Chloropsis hardwickii.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Corvoidea; Irenidae; Chloropsis.
OX NCBI_TaxID=667144 {ECO:0000313|EMBL:NWH37574.1, ECO:0000313|Proteomes:UP000640999};
RN [1] {ECO:0000313|EMBL:NWH37574.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B10K-IZ-033-78 {ECO:0000313|EMBL:NWH37574.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NWH37574.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Single-stranded 3'-5' DNA helicase that plays a key role in
CC homology-driven double-strand break (DSB) repair. Involved in different
CC DSB repair mechanisms that are guided by annealing of extensive
CC stretches of complementary bases at break ends, such as microhomology-
CC mediated end-joining (MMEJ), single-strand annealing (SSA) or
CC synthesis-dependent strand annealing (SDSA). Possesses both DNA
CC unwinding and annealing activities. Forms a complex with RAD51,
CC stimulating HELQ DNA helicase activity and ability to unwing DNA.
CC Efficiently unwinds substrates containing 3' overhangs or a D-loop. In
CC contrast, interaction with the replication protein A (RPA/RP-A) complex
CC inhibits DNA unwinding by HELQ but strongly stimulates DNA strand
CC annealing. Triggers displacement of RPA from single-stranded DNA to
CC facilitate annealing of complementary sequences.
CC {ECO:0000256|ARBA:ARBA00053573}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00048988};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034617};
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
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:NWH37574.1}.
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DR EMBL; WEIW01001284; NWH37574.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A850V5V1; -.
DR OrthoDB; 2320933at2759; -.
DR Proteomes; UP000640999; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd18026; DEXHc_POLQ-like; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR FunFam; 1.10.3380.20:FF:000002; helicase POLQ-like isoform X1; 1.
DR FunFam; 3.40.50.300:FF:000813; helicase POLQ-like isoform X1; 1.
DR FunFam; 3.40.50.300:FF:001293; helicase POLQ-like isoform X5; 1.
DR FunFam; 1.10.150.20:FF:000058; Helicase, POLQ like; 1.
DR Gene3D; 1.10.3380.20; -; 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; IPR050474; Hel308_SKI2-like.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C-like.
DR InterPro; IPR046931; HTH_61.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR048960; POLQ-like_helical.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR PANTHER; PTHR47961:SF12; HELICASE POLQ-LIKE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF14520; HHH_5; 1.
DR Pfam; PF20470; HTH_61; 1.
DR Pfam; PF21099; POLQ_helical; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:NWH37574.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000640999}.
FT DOMAIN 304..478
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 530..718
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWH37574.1"
FT NON_TER 1050
FT /evidence="ECO:0000313|EMBL:NWH37574.1"
SQ SEQUENCE 1050 AA; 117061 MW; 36FCB97F4066FE3A CRC64;
MAEPRLAVRR KSRPGSERKR SRAPAPPIAA SSPVARKRPS CGGEGPLAEA PCSNDSEEDM
FGDYDSFYGN DSLIAQVDDI EHKYLQDKST DVKAAGEVGN LHSGVHQKEQ DNFSASENVV
VLKSDKEGAC QMHDGDPADG NQELTESILD DLPSSQLLYF EKMDELSSAS RTSPVSKGRD
EHVNSSSGKI RDSLSFYAGA EHRNRPTDSS SHSKCVLNKT ESLKDHLKSA MTGNARAQTL
QVSKTKQLKE AIISEEIFVA RKAIESSSVD RGPFYGLPSK VKDLFRQLRG IEALYEWQHD
CLTLESLQQR KNLIYSLPTS GGKTLVAEII ILQELLCRQK DVLMILPYVA IVQEKVWTQG
LSSFGIELGF LVEEYAGSKG RFPPIKRRVK KSLYIATIEK GHTLVNSLIE TERINDLGLV
VVDELHMLGE GSRGAVLEIT LAKILYTSKK TQIIGMSATL NNVGDLQKFL QAEYYTNNFR
PVELKEYIKI RDTIYAVDSK TENGFAFSRL LNFKYSSNLE KADPDHIIAL VTEVIPKYSC
LIFCPTKKNC ENVASMVCKY LKKEFRAHRE EEKQDLIKNL KSIGNGTVCP VLKQTIPFGI
AYHHSGLTND ERKSIEEAYS SGVLCLLACT ATLAAGVNLP ARRVILRAPY VGNDFLKKNQ
YKQMIGRAGR AGIDSAGESI LIVQEKDKHL VQDLVHSPLE NCYSNLLLEL TKGMQSLLLS
LVGLKIAVTH EEVDNFMCCT LLGVQQQLLS KEKSISEIIK DGLENLIEKG LLRGRISEKD
HNSKSTLTIT PLGKATYKGS IDLAYCNLLY RDLKKGLEGL ILESNLHLLY LSTPYDLTST
CSPDWMIYLR QFNQLSAAEQ KVADIVGVPE SFITKKASGQ AIRKNVNNAV VNRFYLTFVL
YTLLKETDVW SVSEKFNMSR GYVQNLLSSA ASFASCLLHF CEELEEFWVY KALLTELTKQ
LTYCVKTELI PLMEVAGVLE ARAKQLYSAG YKTLAHLANA NPETLVRMIE HLSRRQAKQI
ISSAKMLLSE KAEALQEEVE ELLKVPTDIP
//
