ID A0A0N5CES7_STREA Unreviewed; 1036 AA.
AC A0A0N5CES7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Helicase ATP-binding domain-containing protein {ECO:0000313|WBParaSite:SPAL_0001636400.1};
OS Strongyloides papillosus (Intestinal threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001636400.1};
RN [1] {ECO:0000313|WBParaSite:SPAL_0001636400.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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|ARBA:ARBA00000600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000256|ARBA:ARBA00000600};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC {ECO:0000256|ARBA:ARBA00007913}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01341}.
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DR AlphaFoldDB; A0A0N5CES7; -.
DR STRING; 174720.A0A0N5CES7; -.
DR WBParaSite; SPAL_0001636400.1; SPAL_0001636400.1; SPAL_0001636400.
DR Proteomes; UP000046392; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:InterPro.
DR CDD; cd21407; 1B_UPF1-like; 1.
DR CDD; cd18039; DEXXQc_UPF1; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR CDD; cd21400; ZBD_UPF1-like; 1.
DR Gene3D; 2.40.30.230; -; 1.
DR Gene3D; 6.10.140.1240; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047187; SF1_C_Upf1.
DR InterPro; IPR040812; UPF1_1B_dom.
DR InterPro; IPR018999; UPF1_CH/ZBD.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR PANTHER; PTHR10887:SF364; REGULATOR OF NONSENSE TRANSCRIPTS 1; 1.
DR Pfam; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF18141; UPF1_1B_dom; 1.
DR Pfam; PF09416; UPF1_Zn_bind; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51997; UPF1_CH_RICH; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01341}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01341};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU01341}.
FT DOMAIN 66..221
FT /note="Upf1"
FT /evidence="ECO:0000259|PROSITE:PS51997"
FT DOMAIN 430..560
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 19..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..106
FT /note="C3H"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 88..116
FT /note="CC/SHH/C"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 948..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1036 AA; 116372 MW; A49EE0A1C2195752 CRC64;
MAAKEDGLCL SENDDYEHMA AASQDSEYEE NLDLDDIDSV IDNTNNKTDE GSDDEGEYDG
LLGPDFSKLP PHACRYCGIH NVNQVLQCST CEKWFCNGKG ITTGAHILQH MIRAQHREIN
FHKEAELGDS VLECYQCGVK NIFLLGFVPA KNDNVIVVLC RNCSSMATKS ANWCADEWHC
LIEERSLLPW IAKVPTVKER IKSFRITTAQ IKALEELWRI NPSADISDLH KPGLDEAVEP
VQRTYKDAYN YRRILAPLIR LEADYDKAAK EALKPTVSNV KWDYAKNKKI LATFQIQELL
TSGIKLMIGD ELKLKHNQTL LGTTWECHGH LIKVPDHHSE DFVLEFDESF QLPSAKRIIY
TVEFIWNATS YTRMYNALDT LAQKPNCVSS YIYEKLMGHP TSEALLNVKL PKSFNVPGLP
DLNHSQVNAV RQALRKPLTL IQGPPGTGKT VCSANLIYHL VHQRKGKILV CAPSNIAVDQ
LAEKLHQTKL KVIRLCAKGR EDVQSPVAFL SLHNQLKTLT QDTDLQTLLR MKEEGGGLSA
TDESRLKIII KAKEKVLLSK ADVICCTCVC AADSRISFLK FKSVLIDECS QATEPEIMVS
VVKARSQLIL VGDHCQLGPV VMCEKANAAG FSQTLFERLM LNGNVPIRLQ VQYRMHPAMS
AFPSNVFYEG SLQNGVTSSD RILSNLTFQW PVPNKPIIFW HTDGTEELSP TGTSYLNRAE
AINVELLATM FLNSGVRPEQ IGIITPYGGQ RAYIVQHMHA CGTLHYKLYN EIEVANVDAF
QGREKDLIIV SCVRSNENNG IGFLSDPRRL NVALTRSKYG LVIIGNAKVL SKNILWNHLL
LNYREQGCFM DGHINNLRPS QIPLPKERSL IEFFKKHTRF VSPALSMTEP VKLQTVDLTK
SYPTGMQNPN SFIFQNTHPS ATYQPFVFRQ PTLGQVNGFQ NAIQSQCENT RQGVNKRTKN
NHSNSRSGSS YSQRGNDMLS QEMEYGTLQS QEMSQTSISF SRMSESQMSA PFDIEPNMSQ
IARDLNGLML SEDSKI
//
