ID A0A2G5VF47_9PELO Unreviewed; 1547 AA.
AC A0A2G5VF47;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN Name=Cnig_chr_I.g129 {ECO:0000313|EMBL:PIC50362.1};
GN ORFNames=B9Z55_000129 {ECO:0000313|EMBL:PIC50362.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC50362.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) 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:PIC50362.1}.
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DR EMBL; PDUG01000001; PIC50362.1; -; Genomic_DNA.
DR Proteomes; UP000230233; Chromosome i.
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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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};
KW Hydrolase {ECO:0000256|RuleBase:RU363044};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU363044};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233}.
FT DOMAIN 574..754
FT /note="Helitron helicase-like"
FT /evidence="ECO:0000259|Pfam:PF14214"
FT DOMAIN 1498..1540
FT /note="DNA helicase Pif1-like 2B"
FT /evidence="ECO:0000259|Pfam:PF21530"
FT REGION 49..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1547 AA; 177824 MW; 223292FBDF737913 CRC64;
MHVGFQLQHP IYQVDPDMND EMDETESGWA HDLHEPGIID GIEDTQLMTQ PTSIPKSQIE
EAGSVPSKNE PSTSGYVKNQ VRLLEDDESK RRRAYQREYQ RKKRALETVH DTQERRQKDA
GQKRKKRDEM SNEEKERRRS DETESKRKRR SLMSEEQREV INSQRAERRQ ISYLLESDSD
TDQRRDGEAE RKRKTRSSMT EEKKLSVRTQ GTDRRREVRL DETEEEQADR QAKDAESKRQ
HRQNETEKER KSRLHILSQK KKEKQAKVRA KVSHETLHYM GPMSEECEHC KALFFKSEVL
GKKMDSINFC CSSGTIKLEE HFANFPPQLQ ELFQGSTDPA KKDRNEQSKN FKAHIRQFNN
SLATASFGPH PERNVNRGHG PFTVKIHGQV YHRAGPLHPV PGQPRKYGQL FFLDSAQAAR
ERMNIPENAQ CDQSIMEELS DLMMRINIFS QSYKLMKEVE EQEEMEAQLA GRPTKQVKML
FDVSKPNLDL RRYNLPTSNE VAVVYVQEDG MVPSRSVSAY SRDQDGWLTI YDTDPIVDPM
TYPLFFPNGE RGWSPGLSRI GSTRKSTRIA QQPYYRYMAM IRKNKFNPIH YGATLTQQFF
VDSWAKTEQN RLKFHRDNQA KIRAEEYQEL KDYVNRGPGE FTPGKQVILP SSFHGSPRHM
IREYQDCMAI VTKTGKPDLF LTFTCNPKWK EIQENLNPGQ IASDRPDLIA RVFYEKVDHL
MDLLLKKNLL GKVSAHIRVF EWQKRGLPHL HMLLTMKDSD KPKSKDDIDR LIRAEIPDPT
QEPRLHDIVT RQMIHRPCGL NNPNSPCTNK DKICMKRFPK PFRDETKWEQ NGYPEYRRRD
DGRSIKSGGC DMTNQHVVPY NSDLLLMFDA HINVEACALI EVVKYLVKYV YKGQDRASIA
IQSVEDGGKE RDEIKEYLDC RYICAPEACH HLFGFSCHVK SHVICRLPIH LPNRQSVTFV
PGKEKEAVAT SERKGSKLME YFKINADFKE MEANGVDISG KEDPRKCSYM NFPTKFVWSD
ELGKWKERLK GGDKVIGRIY AVTPSDPERF ALRLLLLATS GASSFEDLRT VTDDNGDAIV
HPTFVLAARA LGLLKDDAEL QKAMEECGSF QMPTQMRATF ASILLFNEVG DPELLWDKFK
SSMSEDFVFR GCGEEEAEAR AYEDVREKLS RLGKDIKSFI APPTYVLTAP LIDQVDFDDI
RKEGERLIDT LNPQQMDAFR RIMEAVDDPQ LQRLFFLDGP GGSGKTYLYN VIWKVLLGKD
IKIACCAWTG IASTLLPDGR TIASFFKMDI KNDCRASHLK LNSKEAAFLR KLKVLIVDEA
SMIAKNALET MDKVLRDVME NDIPFGGKII ILGGDFRQVL PVIRRGTRKD QVDGCIKMSF
LWQHFQTLHL KSNMRVTGGD TDWIQFLLKV GDGSANDEAD RINLDEELYT TGDLIEEVFG
QKINKFTDLS ESAILTPKNV NVDKMNEDVH NKMEGAEKIF YSRDEIPDDS NRKVITTEFL
NSLNTSSLPP HKLKLKIGSI VMLLRNLDVS SGLCNGTSLL LEVVLGK
//
