ID A0A2G5VMM0_9PELO Unreviewed; 1257 AA.
AC A0A2G5VMM0;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
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.g2885 {ECO:0000313|EMBL:PIC53014.1};
GN ORFNames=B9Z55_002885 {ECO:0000313|EMBL:PIC53014.1};
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:PIC53014.1, 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:PIC53014.1}.
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DR EMBL; PDUG01000001; PIC53014.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5VMM0; -.
DR STRING; 1611254.A0A2G5VMM0; -.
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 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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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 550..728
FT /note="Helitron helicase-like"
FT /evidence="ECO:0000259|Pfam:PF14214"
FT REGION 1..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1257 AA; 145250 MW; 218C53324B8BD4B9 CRC64;
MAKRTKKPKA KQPPARVRRP RTRDVKDEAR EVGATSSTPS TSTTKPSQKR RLAMKKAEAA
VKKFHQREEE SEEVRSKRRR LDALNKKKAR EEETEEKHEN RTSSNKERTS RARSEETVDQ
YQSRKSSNAA RTSKARSEET DDKYHCRTSF NRDRTSRARS EETEEQYHHR KSSDRARKSR
ARSEETDEKR DRRKSADAER ASKARSKESG AETLRRRVQD KEHKAVTRAA ESAEVSKYRK
EADRKRHYSH VTEDRGIARK DVRVEENYLG TMSEQCSSCG ALHFKGKQPQ SKQFNTCCRH
GLIQLPLFYN FPKELRDLFT SSISESVEFL KNIRTYNNSL AMGSIVAHVV TPKGGGPYTY
RLHGQVFHVT GALHPDPGQE HLCAQLFIID TEEAAAELAN RKVKVSCSKD LYKKLINLLH
MYNPFVNSYK MMREKEEEEE ILATAENRDV REVKMVFRSN KSLNPNRYQL PTAEEIAVVF
VGDEDENPGK RAITVYQRST GTFQYLLDTD KETDPLCYPL LFVDGKYGWH VNQQRQDGHG
GMTKMSAREF YSYYLHTRPN FSPLHHAKKL FQQFCVDVWT KIEQDRLNFI RQHQDQLRVE
SVQGLMDHIS SEDDGPCGKR IFLPNTFTGS PRHFVSLYQD ALAVVSRFGK PDLFLTMTCN
PRWKEIQEAL LPGQEPVDRP DIVSRVFKLK LEELKKDLFV KNIFGEVAAW IYVIEFQKRG
LPHMHLLMIL KNEWKPRTAS EIDDIVCAEL PDPAEDQELF EIISTTQMHR PCGIYNPDSS
CMVGDACSKH FPKDFRERTS VENDGFPMYR RRDDGRSVAF KTKNFGVIQL DNRSVVPYNK
YLSKKFRSHA NLEICGNVGA VKYLYKYLYK GTSRAAIHIY TDKNGVEHMT ENEVNSYLDT
RYVCAPESIW HIFDFRMSDR STPVMQLKVH LKNAQGVVYK EGEEKDAAQR GQLRDTTLTA
WFAANQRCYD ELESTGMIPE DVVDCRGIYY VEMPEHFQFT KGKWALRKNA TRSIGRMHFV
SPRDQERFAL RVMLLNVTDA KSYEDLQTVG GVFYEKFVDA AKAAGYLTED IFYEKSLEEA
ASFHSAPQLR GFFVTLLMFG EIHNAEELWY RFLDDFAEDF VYKHFPKEKA EALAYNDLIV
RMNAMGEKLE KWMSLGYERI MPDDVIDFDY CTKEGDRMRS TLVAEQEEVV KAVLDAVKSG
GGLIYVDGPG GSGKTYVYLC LINILQGMHL KVIPIAWIGI AASLYCLMEE RWLHSSI
//
