ID A0A226F6E9_FOLCA Unreviewed; 1584 AA.
AC A0A226F6E9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN ORFNames=Fcan01_01002 {ECO:0000313|EMBL:OXA64910.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA64910.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA64910.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA64910.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA64910.1};
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:OXA64910.1}.
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DR EMBL; LNIX01000001; OXA64910.1; -; Genomic_DNA.
DR OMA; VICARII; -.
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:OXA64910.1};
KW Hydrolase {ECO:0000256|RuleBase:RU363044};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU363044};
KW Reference proteome {ECO:0000313|Proteomes:UP000198287}.
FT DOMAIN 491..672
FT /note="Helitron helicase-like"
FT /evidence="ECO:0000259|Pfam:PF14214"
FT DOMAIN 1408..1453
FT /note="DNA helicase Pif1-like 2B"
FT /evidence="ECO:0000259|Pfam:PF21530"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1584 AA; 180468 MW; CF996F6527185FF8 CRC64;
MPPKRQRTAE GDAERKRQHA ENMRMRRANR SEEQRLEERE RNAENKRNRI ANLSAEERSI
ERERRAEIER NRVASRSEEQ CSIERERHAE IERNRVASLS EEQRSLERVR HAEIERNRVA
SLSEEQRSVE LQRNSKNKRH RAANMATTQR IEQRRANVAA ASTSRAATRL RNLNQTIHAA
SINRFNEADI QQHTCGELNV PCSFCGAKHF LKERPQDKKF TQCCQKGKVV LPPIKLAPNI
EKLMKKEHEY SNNFFENIRS INSALAFASM GANIAPPPGY GPYCFRINGQ IYHRTGSLHP
TNGDQRKFAQ LYILDPDEAC DQRMMIRENA HCNAEIMREL SSFMAQNNPF AKAFKMLYEV
EKECLAEATL NGVEPATVAM AIVQDRNSDQ RRYNAPRVNE VAVIFQNADG EPQLERDILI
HCRPNENDLN PKRTERINIL DPNLEPMVYP LLFPYGDQSW GIDLKLNRPP SLANMRQPSA
NPRTRITQMQ YYGYRLSIRD ELNPFLCAGK LTQQYFVDAY VKTEANRLNF CRQNQGTLRA
EQYAGLIDYI QTAANDQGLI PGRAVILPSS FIGSPRNMAQ NYQDAMAIVR KFGKPDFFVT
MTCNPKWPEI TDNLQYGQKA EFRPDLVTRV FNLKLKELLD DISKKQILGI LTAKVHVIEF
QKRGLPHAHI LLMVKNDGPV DAEKLNQLIS AEIPDINECP RLHAVVTKHM VHGPCGSANL
NSPCMVNNKC SKEFPKPFQN ETLVNCDGYP KYRRRNTGQT DVNGRQIDNS WIVPYNPYMS
LKYNCHINVE SCASVKSVKY LFKYVYKGHD CANIAISEQD VLNHDEIKTF MDSRYISAPE
AAWRLFGNSM HEQSHTIYRL PVHLPSEQTV YFNADNVEAA AERAGSKETM LTAWFKLNDT
DEDARLYLYA DIPEHYVFNK VSGVWKPRQR ETNNTIGRMY PVNLSTDTEK YCLRLLLLHK
RGVTSFEDLR TVEDVIYPTF KEAAQKSGIF SDDATWDFAL TDAAIWKMPR QMRDLFAYIC
VFAVPPNALE LFEKYKSDLY EDFARDARHN HTDNCQHCTN LALVEIQAIL ILSYKKCVDF
GLPSPPANMR AAADEYFDVL AEKQKGDALQ DTLNDEQRNA FDTVLNAAEN ENLPHRIFFM
DGVGGSEKTH VYKTILSTVR GEGNIALPMA STGIAANLLD GGRTYHSQFK FRIPIDDTTT
SPIRSNSADA ELFRQAKLLI WDEATMAPSL ALAAVDKFLK EVMNNQKPLG GKVLLLGGDF
RQTLPVVPHA SRSAIVEASL KFNSLWRKVK ILHLLSNVRS VDKSYSDWLL KLGDGTLETP
LGLPKDTIEI PEQLICRESI IYEIYGERLT VANVANFSKM AILCPKNTDV DNINEEILNI
LEGNSVTYFS TDSVDDESAE DRQHYPVEFL NGLTPSGMPV HKLNLKKGSN IMLLRNLNTK
RGLCNGTRLI VEDLKPNLII AKVLTGFAQQ QIVFIPRIDL STANADFPFV LRRRQFPIKL
AFAMTINKSQ GQTLDKVGVY LPEPVFSHGQ LYVALSRVRR FADAKIKIID GPEQGKLIEG
SDRVFTKNVV YEEIFAKQLD PDCQ
//
