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Database: UniProt
Entry: A0A226DA19_FOLCA
LinkDB: A0A226DA19_FOLCA
Original site: A0A226DA19_FOLCA 
ID   A0A226DA19_FOLCA        Unreviewed;      1552 AA.
AC   A0A226DA19;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN   ORFNames=Fcan01_23945 {ECO:0000313|EMBL:OXA41096.1};
OS   Folsomia candida (Springtail).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC   Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX   NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA41096.1, ECO:0000313|Proteomes:UP000198287};
RN   [1] {ECO:0000313|EMBL:OXA41096.1, ECO:0000313|Proteomes:UP000198287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VU population {ECO:0000313|EMBL:OXA41096.1,
RC   ECO:0000313|Proteomes:UP000198287};
RC   TISSUE=Whole body {ECO:0000313|EMBL:OXA41096.1};
RA   Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT   "The genome of Folsomia candida.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU363044};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU363044};
CC   -!- SIMILARITY: Belongs to the helicase family.
CC       {ECO:0000256|RuleBase:RU363044}.
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:OXA41096.1}.
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DR   EMBL; LNIX01000030; OXA41096.1; -; Genomic_DNA.
DR   OMA; QSMDTQR; -.
DR   Proteomes; UP000198287; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR   CDD; cd18809; SF1_C_RecD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR010285; DNA_helicase_pif1-like.
DR   InterPro; IPR025476; Helitron_helicase-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR049163; Pif1-like_2B_dom.
DR   PANTHER; PTHR45786:SF82; ATP-DEPENDENT DNA HELICASE; 1.
DR   PANTHER; PTHR45786; DNA BINDING PROTEIN-LIKE; 1.
DR   Pfam; PF14214; Helitron_like_N; 1.
DR   Pfam; PF05970; PIF1; 1.
DR   Pfam; PF21530; Pif1_2B_dom; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU363044};
KW   DNA damage {ECO:0000256|RuleBase:RU363044};
KW   DNA recombination {ECO:0000256|RuleBase:RU363044};
KW   DNA repair {ECO:0000256|RuleBase:RU363044};
KW   Helicase {ECO:0000256|RuleBase:RU363044, ECO:0000313|EMBL:OXA41096.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU363044};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU363044};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198287}.
FT   DOMAIN          450..630
FT                   /note="Helitron helicase-like"
FT                   /evidence="ECO:0000259|Pfam:PF14214"
FT   DOMAIN          1371..1417
FT                   /note="DNA helicase Pif1-like 2B"
FT                   /evidence="ECO:0000259|Pfam:PF21530"
FT   REGION          1..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1552 AA;  176860 MW;  F152D4329D976F3D CRC64;
     MGPKRQQTDE ERNLQQVEAK RRRAEAQRLR RANLTDEQRN QHREQNSQTK RNRIANMSDE
     ERNLHRKQNA QSERNRVANM SDEQRRQRRE NDAQNTRNTR QNMTAEQTSL YQNVHNMRLS
     TSRTRVRQRS LAATIATALT DNFDETTIPL HSCGQLNSVC QFCQAKHFAS ERPTDGYFNI
     CCNKGKVFLT QIRQSEFLKD LLTNNHEHSK NFMENIRSFN SSLAFASMGA NIAPPPGYGP
     YAFRIHGQIY HRAGALNPCN GGQRKFAQLY ILDPYEASEQ RLRMSENSKC NPDLMNELSQ
     FMTQQNPFAD ACKMLHEVEQ ESIADAQLHG VEPSTVSMAI IQDRNSDLRR YNAPRTNEVA
     VIFQNGNGDP PLERDLIIHC RVTADNPDQR ACQRINILDP NLEPMTYPLL FPYGDQSWGL
     NIRLQDRPGV LRNRPQSANP RQNVTQMQFY AYRFAIRDAF NPFLSAGKLT QQYIVDAYVK
     TEANRLNYLR QNQKALMAES YQGLIDHIGS VAEQQGLNPG KPVILPSSCQ GSPRNMTQNY
     LDAMAIVREY GTPDLFITMT CNPKWNEITE NLGPGQSAEF RPDLVARVFK IKLKELLSDI
     CDKHVLGIPI AHVHVIEFQK RGLPHAHMLI ILKKEFKPSD CDKIDKLVCA EIPNIETNPR
     LHEIVTKHMI HGPCGVHNLN SPCMDSLTNE CTKKFPKAFQ NATVIEGNKG YPLYRRRNNG
     ISVMIKNKRI DNRWIVPYNP SLSLKYNCHL NVEVCASIKS VKYLFKYVYK GHDCANVTIR
     EETTLHHYEI QTYMDSRYVS APEGAWRLFG FEMHKQSHTI IRLAVHLPGN QSIVFNPNDV
     AQAVANNEHR HTTFTAWFAL NSTLPSDEHC LYADTPKKYW FPPNLRVWQK RKQEKRGEKV
     IGRMYTVSLQ DHPESYYLRL MLLHVKGATS FENLRTFNGV RCDTFLEASK RMGLLSNDET
     WDNTMADAVI SSMPRQLREL FATICVFACP PNILQLWDKY KEYLIEDYSR HPNHDADCIQ
     CENLALRDIQ DIFIIHGKSC NEFGLRTPPT NIPRNIDDYF DVEAERERGA EMYETLNDEQ
     KAAFNTIIES INCNIPQSRC FFLDGPGGSG KTYLYKTLLS TVRGMGEVAL PVASTGIAAN
     LLKGGRTYHS QFKLKVPLDE TCTSSIRQTS SEAELIRRAK LIIWDEATMA PSIALDAVDR
     CLKHLMENNL PFGGKVLLLG GDFRQTLPVV PHASRAAIVE SSVKFNKYWE HFKILKLHNN
     VRSEDPEFSK WLIDLGNGSL PTTEVLPDDV IEIPENMIRT DSIVEEIFGK KLTVQDVHKF
     SKMAILCPKN VDVDKINEDV LDILEGEKVT YLSSDSIVDE TDVDRQNYPI EFLHDQTSSG
     MAPHKLNLKI GAIVMLLRNL NTKHGLCNGT RLIVKELKPN LIIAEVLTGP AQGNIVFIPR
     IDLTPSNPDL PFTLKRRQFP IKLAFAMTIN KSQGQTLDKV GVYLPDPVFS HGQLYVALSR
     AKRSCDVKMK IVDGPLQACG GSDKCTVSTF KNEKVRGQHT EGGPRPLPWV DK
//
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