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
//