ID A0A016TX28_9BILA Unreviewed; 1849 AA.
AC A0A016TX28;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Helicase protein {ECO:0008006|Google:ProtNLM};
GN Name=Acey_s0071.g621 {ECO:0000313|EMBL:EYC07370.1};
GN Synonyms=Acey-F52B5.3 {ECO:0000313|EMBL:EYC07370.1};
GN ORFNames=Y032_0071g621 {ECO:0000313|EMBL:EYC07370.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC07370.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
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:EYC07370.1}.
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DR EMBL; JARK01001407; EYC07370.1; -; Genomic_DNA.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0022414; P:reproductive process; IEA:UniProt.
DR CDD; cd17917; DEXHc_RHA-like; 1.
DR CDD; cd02325; R3H; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.30.1370.50; R3H-like domain; 1.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF145; ATP-DEPENDENT RNA HELICASE DHX29; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF01424; R3H; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00393; R3H; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF82708; R3H 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; PS51061; R3H; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635}.
FT DOMAIN 41..103
FT /note="R3H"
FT /evidence="ECO:0000259|PROSITE:PS51061"
FT DOMAIN 196..361
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 834..1003
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1425..1849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1425..1495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1506..1525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1526..1608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1609..1624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1625..1645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1656..1701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1711..1727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1752..1796
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1797..1811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1812..1842
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1849 AA; 211760 MW; 40D28F3A522D92E6 CRC64;
MAYYGNHGKG RTKNHHNNFD RDEPNGFKNP QYGPHVQLID ANWERQVTAK LDEFMNGTAT
ELCFPPMERP ERRRLHELAR RKGLQTSSEG REPNRRCVVH RRPTPKLAAV GANETQPIRL
TADIRKALSN FICQYPISAQ AIDRHLAAPK SRDRSQRDMS NRERPEMLVP QRSNISMEMQ
KQRNMLPAYQ QRADVLRAIN DHKVVLITGG TGCGKTTQVP QFLLEDAYEH QQPLRIVCTQ
PRRLPAIAVA SRVARERGES LGSTVGYHIR LEQRTSPQTV LTYCTSGVLL RMLTQDDAAR
DISHIILDEI HEREQNTDYL LIALKQALKK RNDLKVILMS ATMEGNLKLF TKYFGEKVEV
KHVDIPSRLF TVERYFLGDV IAMTGFVPEE SMFSSMFMSA GFPEVCSFPT VGDWSMKTEW
EAEPAHPRLP EAMTAPNLQS LAGNNCATPS SSNPMAGGHM MTSSSVASFT QHGKQQHTAN
FMNVAQQLVN SQQSSSNHQQ QPPQPMSAPP QGVVHHPQQQ QQPPMQPGYV QQPGAVYVQH
SAYQQGYPQQ PHGYQQGQVR QVYTQQPAGV ALQHSTWGGG MDQSFTGVVH AHPDVVELPN
EALDPETLEQ FRQMGYTNNE EVGPTVAYGA EWRVAEGDVQ PHWQHTQSYS TMPNSAYQQG
HLQSWDTQVV YPTPPGPYHK NSQQQPMFYV PESFDNSPST KSVSYFGQSM DGYPMPMHSH
HTMPQGSGGS PAAYTVPPPQ HGPPPLPGYQ HMQNSGPQLP MDSYASAVQR SEKELEMMRH
QLGTALPDRP ESFDPHIRQL IAARRLDQSA LVNMYLKCGG QQWAEAVDLD LAMAVVKYCM
DSRVDGAILV FLPGFDDIVQ MRDKINNETW PLRRPVIFTL HSQMNSFDQQ KVFDAVGQNE
RKVILSTNIA EASLTIDDVV FVVDCGKVKE KTYDHTSRIS QLKVTWIAKS NAEQRAGRAG
RCREGYCFRL YSVDDYDEML ETQMAEMQRT AIHDVCLHAK MFAPENMTVK QFLQMAPEPP
VADAVDKSMD FLEQLGALYS EASTSDTDLT TQSSPNIEPQ LTDLGRLVAQ LPLDPQLARL
LLFGVVLRCL NPVVTLVAAL SHRDPFILAL SEEREQSNRQ RDSFGKRDFS DHITLIRAFN
EFNEKGPKEV TAFCRANYLS LPAMRMIAGI RRQLLIELRR VRIISYDGDP MSALRDATYN
KYSSCWPMVQ AAIVAGCYPG IGFVRAGNKL KKIRTSTEAA ATLHPSSVIK RQVLAASKRS
DVINQYVTED SEDPVIEYLA FHELAKIDEG LTLRTVTVIP PCAVVLFAGS MRLKKSTIQN
FNITDPDSED EGDVDEDAPS RDVVHPIEHW IGVRATYSDM KRLIQLRFKV MSYFLSAIHK
PQILANPMKE DNDLLATLAQ VLQTDHQEMK FNQCVLPQPP LFYPQHQVPT SSTSNSSYSS
HNGQQAPANR FPHRENSASQ PNMNAAAEPS TKQAPPSSHN ENLPASNSVS NFQSGGFEKR
FDEEQAPPPQ QQQQQQQQQQ QQQDREQPDR YQDQRERRHG QDDYGYQKGR RDNYDQRQQR
YNRNRDDWQR NRPYQPREGG YRDNREKVER QQSFRERERE RERSGRDDTA PGPSQQQQQH
RQRVQGYNNR DRDYRQNDRD WNRGDSSGPD QLTWQQREME RNDNYRERQG RREYNNYRQR
QYNKYDDDRE EPVPEDPRVD RNDDDGWDDE DYQAAGYHHD QQDYQHKHNR HYHRPYNNRG
GFRGRGRGGF YHNRHYNRDD NRRDMPDDDR GDRDGRDARD GGDNRDRDHV EGNSRNNDRG
FYRQGGKNYE NNRSMDNDRE KHSERSRVFY NSNKHYSDRR RRGSNSNYN
//
