ID W2TB35_NECAM Unreviewed; 2351 AA.
AC W2TB35;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=U5 small nuclear ribonucleoprotein 200 kDa helicase {ECO:0000256|ARBA:ARBA00034541};
GN ORFNames=NECAME_02932 {ECO:0000313|EMBL:ETN78227.1};
OS Necator americanus (Human hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae; Bunostominae;
OC Necator.
OX NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN78227.1, ECO:0000313|Proteomes:UP000053676};
RN [1] {ECO:0000313|Proteomes:UP000053676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24441737; DOI=10.1038/ng.2875;
RA Tang Y.T., Gao X., Rosa B.A., Abubucker S., Hallsworth-Pepin K., Martin J.,
RA Tyagi R., Heizer E., Zhang X., Bhonagiri-Palsikar V., Minx P., Warren W.C.,
RA Wang Q., Zhan B., Hotez P.J., Sternberg P.W., Dougall A., Gaze S.T.,
RA Mulvenna J., Sotillo J., Ranganathan S., Rabelo E.M., Wilson R.K.,
RA Felgner P.L., Bethony J., Hawdon J.M., Gasser R.B., Loukas A., Mitreva M.;
RT "Genome of the human hookworm Necator americanus.";
RL Nat. Genet. 46:261-269(2014).
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000256|RuleBase:RU003750}.
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DR EMBL; KI660008; ETN78227.1; -; Genomic_DNA.
DR RefSeq; XP_013300454.1; XM_013445000.1.
DR STRING; 51031.W2TB35; -.
DR EnsemblMetazoa; NECAME_02932; NECAME_02932; NECAME_02932.
DR GeneID; 25342970; -.
DR KEGG; nai:NECAME_02932; -.
DR CTD; 25342970; -.
DR OMA; QTEIQYY; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000053676; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProt.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd18019; DEXHc_Brr2_1; 1.
DR CDD; cd18021; DEXHc_Brr2_2; 1.
DR CDD; cd18795; SF2_C_Ski2; 2.
DR Gene3D; 1.20.120.1760; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041094; Brr2_helicase_PWI.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR PANTHER; PTHR47961:SF4; U5 SMALL NUCLEAR RIBONUCLEOPROTEIN HELICASE; 1.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF18149; Helicase_PWI; 1.
DR Pfam; PF02889; Sec63; 3.
DR PIRSF; PIRSF039073; BRR2; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023209};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000053676};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003750};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 646..829
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 839..1076
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1493..1668
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 378..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2351 AA; 268873 MW; FE3F9F243EC2D1A0 CRC64;
MDEDVPNVFL FYPNLIGYGR IVLAVVSFYT MAESPFIALF CYALSAALDA FDGWAARTYN
QSSRFGAMLD QLTDRCGTMA LCMALCRFYP SWMFWIQMST VIDVASHWLH LHATDLTRAD
SHKKSDNPIL HLYYTNRLFL GFISDNVGKA REFVLLTTLL MDMADELARV QQYEYRQNSN
LVLQVDYNLT DRRGREEPTG EVLPLSDRVL KGMKMGDKYM RTKAPIHEQK KKRFFHLTSF
SDHCLRKLAH LIPERRRQMR RISESCRSRS LVITQNLWEA INHEHKKLSR LMRLSWLSYK
KLLAISLETF CVVELLLGPL TDERTAVLIN LARKITDFSM EDEHKMEMDE LDENEGVNVH
FDESDEEQDA VIDEIKNVDE SSSDDEGGEE AEHNETLKGG GFDEEDQGTK KDALHPRDID
AHWIQRSLAK FFNDPIVAQQ KVTEVLGILK DSVDDRECEN KLVLLLGFDH FDFIRILRQH
RHMVLYCTLL KQAQDEEKAK ANIEEEMKSR PELHHILAQL LETDEADIVE TERAKREKTA
QRRAAAAAGE EAVAAGQWLA GRKVLDLDDL AFSQGSHLMS NKRCELPDGS YRKQKKSYEE
IHVPALKPRP FAEGEKLIDI SELPKWAQPA FDGFKSLNRI QSRLCESALN SDEHLLLCAP
TGAGKTNVAL LTILHEIGKH LNDDGSVKVD EFKCIYIAPM KSLVQEMVGN FTKRLAPFGI
TVGEMTGDAQ MSKEQFMATQ VIVCTPEKYD IVSRKGGERA YSQLVRLVII DEIHLLHDDR
GPVLEAIVVR TLRQVEQTHD DCRLVGLSAT LPNYQDVGTF LRVKPEHLYY FDNSYRPVPL
EQQYIGVTEK KALKRFQAMN EVVYDKIMEH AGKSQVLIFV HSRKETAKTA KAIRDACLEK
DTLSAFMREG SASTEILRTE AEQVKNHDLK DLLPYGFAIH HAGMNRLDRT LVEDLFADKH
IQVLFSTATL AWGVNLPAHT VIIKGTQIYN PEKGRWTELG ALDVMQMLGR AGRPQYDSKG
KGILITNHSE LQFYLSLMNQ QLPVESQMIA RLPDMLNAEV VLGTISSVSD AMSWLGYTYL
YIRMLKSPTL YGIPADQAQS DPLLEQRRAD LIHTACLQLD KGNLVKYDKK SGLVQATELG
RIASHYYCTF ESMQTYNQLL KPTATEIDLF RIFSLSNEFK NIAVREEEKL ELQKLAEHVP
IPIKESLDES SAKTNVLLQA YISQLKLDGF ALQSDMVFIA QSAGRLFRAL YEIVLWRGWA
ALALKVLSLC KMVTARQWQS LNPLHQFKKI PTEIVRSIDK RNYSFERLYD LDQHQLGELI
RMPKMGKPLY KFIRQFPKLE MTTLIQPITR TTLRIELTIT PDFQWDEKVH GSAEGFWIFV
EDVDGELILH HEYFLLKQKF CTEEHVVKMF VPVFDPLPPL YFVRVVSDRW LGSETVLPIS
FRHLVLPEKY PPPTELLDLQ PLPISALNNK HFEAVFQAKE IKIFNPIQTQ VFRTVYESND
NVLIAAPNGS GKTACAELAI LRHFDNNPDA KCVYVTPMED MAAKVYNDWQ DRLGIALDRT
VVLLTGEPST DLKLLQRGKL IIATPERWDN VSRRWKQRKN VQAVKLFIVD DLHMIGGTIG
PVLEVICSRM RYMSAQLDTT VRIVGFSSSL TNARDVGAWL GCSAAATFNF LPNTRPVPLE
LYIQGFNLSH TASRLAAMVR PVYQSISRHA GKLNPKPALV FVPGRRQSRS TAIDMLTMAH
ADGAPQRFLH INEKDEIFVK LLNSLQDPTL RETLLCGVGF LHEGTHTKDF QIVERLFNSG
AIQVCIAPRT MCYQINMAAY LVVIMDTQFY NGKYHVYEDY PIGDVLHMVG LANRPGRDPD
AKCVLMCQSS KKDFFKKFLY EPLPVESHLD HCLHDHFNAE IVTKTIENKQ DAIDYLTWTF
LYRRMTQNPN YYNLQEISHR HLSDALSELV ENTLKDLENS KCIAIKDDMD TMPLNLGMIA
AYYYISYTTI GDYFVIFLTK FFISHLLIEL FSMSLQAKTK LRALIEIIAN ASEFASIPMR
HREDVVLKQL AARLPGQLKN QKFSDPHVKD YVFPFEVMFR KDLIMAVTSR QRDLFGLWVN
LLIHAHLSRI QLSAELSKDT DMAVLKAIRL VQACVDVLSS NGWLSPAIHA MELSQMLTQA
MYSNESYLKQ LPHCNSGLLE RAKQKKVESV FELLELDDDV RRDILRMEDV QLADVAKFCN
NYPSIEVEHE LESDSVNIGD TLLVNVTMER ENHINGLAPP VVAPLFPQKR KEEGWWLVVG
DPAANALYSI KRLTINEKAK MQLDFVAQSA GRFEYKLYFI CDSYLGADQE FDFSVKVEDH
SRSRKRRRDD D
//
