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Database: UniProt
Entry: A0A0N4ZRZ9_PARTI
LinkDB: A0A0N4ZRZ9_PARTI
Original site: A0A0N4ZRZ9_PARTI 
ID   A0A0N4ZRZ9_PARTI        Unreviewed;      1777 AA.
AC   A0A0N4ZRZ9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:PTRK_0001128100.1};
OS   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001128100.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0001128100.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   STRING; 131310.A0A0N4ZRZ9; -.
DR   WBParaSite; PTRK_0001128100.1; PTRK_0001128100.1; PTRK_0001128100.
DR   Proteomes; UP000038045; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd18667; CD1_tandem_CHD3-4_like; 1.
DR   CDD; cd18662; CD2_tandem_CHD3-4_like; 1.
DR   CDD; cd15532; PHD2_CHD_II; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 2.40.50.40; -; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR012957; CHD_C2.
DR   InterPro; IPR009462; CHD_II_SANT-like.
DR   InterPro; IPR012958; CHD_N.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR009463; DUF1087.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45623:SF17; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED; 1.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   Pfam; PF08074; CHDCT2; 1.
DR   Pfam; PF06461; CHDII_SANT-like; 1.
DR   Pfam; PF08073; CHDNT; 1.
DR   Pfam; PF00385; Chromo; 1.
DR   Pfam; PF06465; DUF1087; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00628; PHD; 2.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01146; DUF1086; 1.
DR   SMART; SM01147; DUF1087; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00249; PHD; 2.
DR   SUPFAM; SSF54160; Chromo domain-like; 2.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50013; CHROMO_2; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          216..263
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          274..321
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          465..518
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          587..771
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          902..1067
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1138..1160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1200..1241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1387..1413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1574..1597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1737..1777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1200..1215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1216..1233
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1762..1777
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1777 AA;  205417 MW;  DF8EBC2A342B0207 CRC64;
     MSSYDNEVTK EEYQDGSQLE MKEDSTVPSE EEEEYGTRKS KSSKSKKSKK GSKPESIEDI
     CEQLGVSNPD IEYTNEDFDT ISSYRQYQAK FRDAIESVNT GAKPQKISTF ISAKYKEFQE
     IQLSYVGNKG GKRSTRDTVS REKSVKSGKS KSRNNENGDS DDEFEELLKA HDRQLDEEEK
     EKEERKADRL RKIAERKAAI EASKIKKPKL ENIEHNDFCE ACHGDGEVLL CDFCPKAYHL
     SCSDPNLDEP PEGDWMCPCC REEIELKEKI AKHKQFCNIC KEGEYLLYCS NCPYSYHAYC
     MNPPLEQLPD DDYLCPRCTV PDPPNKPDKI LSWKFEEYLY PEPWKKSDLP PATNSENLKK
     IKEITYLRPA RKMEPQKERF FFVKWKYQSY WHCEWISELA MEVHHVMTWR TYWKRNDPDH
     PPNYDDDDDN DNGDGEERVH RKNKAHDPLE LYDRFYKYGV KPCWLVIQRI INHVSYGKNQ
     YDYLVKWSEL AYDKSTWERD DFDIPGYEQA IINYWQHRHD MAGESIPKPI RKKIEAKKAE
     DGIVEDDSKK KKVVYDIRKK HETQPDYISE CGGTLHPYQL EGINWLRHCY SQGTHAILAD
     EMGLGKTVQA MSFLYSLYKE NACPGPFLVA APLSTLLNWE REAHIWCKDF YCVTYSGDKD
     ARAIIREHEF SFQEGAVKAG SKATKMKDPQ NVKFHVLLTS YELVNIDKAI LSSIHWGALV
     VDEAHRLKNN QSLFFRNLRE YKIGYRLLLT GTPLQNNLEE LFHLLNFLCP NSFNDLEEFT
     QAFSDVSKED QIQKLHSMLG PHMLRRLKAD VLTGMPSKTE LIVPVDLSPM QRKWYRNILT
     KNFEALSIKG GTSMSLINVL MELKKCCNHP FLFSKASIEA PKTANGMYEL NALVKASGKL
     IVMQKMLRKL YEQGNRVLIF SQMTRMLDVL EDFCEAEGYK FERIDGSITG QIRQEAIDRF
     NAPGAKQFIF LLSTRAGGLG INLATADTVI IYDSDWNPHN DTQAFSRAHR LGQKNTVLVY
     RFVTRNSVEE KVTSVAKKKM LLNHLVVRAN SSGKGPSLSK TELDDVLRWG TEELFKEDDN
     NDENNDGKPS ENAIVWDDEA IDKLLERKLF DPNEKVEEKK DWSDEYLSTF KVATYATKEV
     EEEEEEEEVE REVIKQDGKE TDPDYWEKLL RHHYEQDQES ELQKLGKGKR VRKQVNYATN
     TVTQEWQNNT QDNDDDYSES FSDDSGDSDE GDSDSAANDL KRRKNYSDDI LPPLVSKVNG
     QIEILGFNPR QRKAFYQSIM RWGMPPNDAY QSQWLVPDLK SKSERAYKVY AALFLRHLCE
     DASTKSEFFS DGVPREGMNK HHVLSRIGMM GLIRRKINEY ESLNSEWSIP EIKEAIDKAA
     KLGVDVSSQS QSRDMTPNEL SVASKSDETE VNETSINETI TDDLMDVTIT EESEIKEEVE
     IKKEIEDCIF NINDGGFTEL HTLWVKEEEA ANQGKKYEVW HRRHDYWLLL GCCVHGYAYY
     REIYDDPRFA ILKKPFEYFE ETKNVTISLQ DKIKFMQRRH RLLEQAMVME EQLRRVAFVS
     NQISSSIAKK AEIAKNKEHE SSEQSNVELS ENSPPEFKLD KESELKNRML MTKVIGQLED
     LVSDLKDCSA RTPTTLEHVS NTLNKIILPE KDLLRRLSVK DETAIAGVSC VAPPAPFLSG
     DIKEKLCGLQ PKYATFMMSD YALKKNTEEK NKSNDDIEAT METDEITNDK IVTTSDENKQ
     IDDVSNKMEV ESAPVLIQEG TSEKQIKEDE KETPTVS
//
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