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Database: UniProt
Entry: U3K8X3_FICAL
LinkDB: U3K8X3_FICAL
Original site: U3K8X3_FICAL 
ID   U3K8X3_FICAL            Unreviewed;      1095 AA.
AC   U3K8X3;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000011477.2, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000011477.2, ECO:0000313|Proteomes:UP000016665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23103876; DOI=10.1038/nature11584;
RA   Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA   Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA   Wolf J.B.;
RT   "The genomic landscape of species divergence in Ficedula flycatchers.";
RL   Nature 491:756-760(2012).
RN   [2] {ECO:0000313|Ensembl:ENSFALP00000011477.2}
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC       {ECO:0000256|ARBA:ARBA00005446}.
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DR   STRING; 59894.ENSFALP00000011477; -.
DR   Ensembl; ENSFALT00000011523.2; ENSFALP00000011477.2; ENSFALG00000010981.2.
DR   Ensembl; ENSFALT00000035875.1; ENSFALP00000025308.1; ENSFALG00000010981.2.
DR   eggNOG; KOG0351; Eukaryota.
DR   GeneTree; ENSGT00940000156800; -.
DR   HOGENOM; CLU_001103_1_0_1; -.
DR   Proteomes; UP000016665; Chromosome 10.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd18016; DEXHc_RecQ2_BLM; 1.
DR   CDD; cd18794; SF2_C_RecQ; 1.
DR   Gene3D; 1.10.150.80; HRDC domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR012532; BDHCT.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR010997; HRDC-like_sf.
DR   InterPro; IPR002121; HRDC_dom.
DR   InterPro; IPR044876; HRDC_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032284; RecQ_Zn-bd.
DR   InterPro; IPR018982; RQC_domain.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   NCBIfam; TIGR00614; recQ_fam; 1.
DR   PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR   PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR   Pfam; PF08072; BDHCT; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00570; HRDC; 1.
DR   Pfam; PF16124; RecQ_Zn_bind; 1.
DR   Pfam; PF09382; RQC; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00341; HRDC; 1.
DR   SMART; SM00956; RQC; 1.
DR   SUPFAM; SSF47819; HRDC-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50967; HRDC; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016665}.
FT   DOMAIN          354..529
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          555..702
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          888..968
FT                   /note="HRDC"
FT                   /evidence="ECO:0000259|PROSITE:PS50967"
FT   REGION          25..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          112..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          977..1070
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..141
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        977..1003
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1048..1066
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1095 AA;  119849 MW;  9322D03820AA6855 CRC64;
     MPQFADTCTS VPFPCAVSSV FRDTPTGGRC SAGSSEARQE KDPTTHPAAD PGAEDSGEAV
     PVAQQLLRVT EAICELVDAI PLQELQALGC ARALLQHRDR RRKLLANYNS VSVNQNGTTP
     PFPRSWKPPV EQSPPVCPGA GPGSGPSWSF SSDRNSPKPT NLPSVLSLHS SGSSAKTNQT
     LAAPCASRQG AEELPCARGG GREGAAPRLS LQSCSSSWEQ AAGAPRAQST AASASPAGSS
     LGTRHPDLDL HLFDIDDLDE DWESPGAAAA TEGPPAKSLC SKLLSRAKGS VGSGPAAPKP
     GLLMATKSPP DPVVHNPALE RFRGMKFPHS AEMMNIFHKK FGLHCFRTNQ LEAINAALLG
     EDCFVLMPTG GGKSLCYQLP ACVSAGVSVV ISPLRSLIID QVQKLKTLDI AATYLTGDRT
     DADASKIYMQ LSKKDPVIKL LYVTPEKVCA SSRLMSALEN LYDRKLLARF VIDEAHCVSQ
     WGHDFRQDYK RLNVLRRRFH RVPMMALTAT ATPRVQKDIL NQLEMLRPQV FTMSFNRHNL
     KYDVLPKKPK KVAMDCLEWI KKYHPHDSGI IYCLSRHECD TTAAILQKEG LAALAYHAGL
     TDSSRDLVQQ KWVNQEGCQV ICATIAFGMG IDKPDVRYVI HASLPKSIEG YYQESGRAGR
     DGEMSHCLLF YSYSDVTRLR RLILMEKDGN SHTRQTHFNN LYSMVHYCEN VVECRRVQLL
     AYFGETNFNP TFCKDHPEVI CDNCSRKKDY RCRDVTEDVR SIVRFVRQHC GQAGHGRGSP
     ASGRYTLNMM VDIFLGSTSA KIQSGIFGKG AAYSRHNAER LFRKLVLDKI LDEDLYITAN
     DQAVAYVILG ERAQAVLDGS LQVEFHETES ASAIRRQRAS MAKMSQREEV VKQCLSELTD
     TCKTLGKVFD VHYFNIFSTS TLKKIAESLS SDMEVLLQID GVTEDKLEKY GAEIIKVMDK
     YSECSFPEDA ACSGVDTATG STGSLGSDAE DAGTTSSYFG NNTNQRRKRK RPPNSRDCKR
     KKTSGGGSQQ FQPRGGYSRY RRTKKLPSSK AAASSSASSV SYSAGGTQGA AGKLAMMALP
     KPKSRSFLQP SFSVF
//
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