ID A0A183DN76_9BILA Unreviewed; 811 AA.
AC A0A183DN76;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=HATPase_c domain-containing protein {ECO:0000313|WBParaSite:GPUH_0001018001-mRNA-1};
GN ORFNames=GPUH_LOCUS10167 {ECO:0000313|EMBL:VDN17081.1};
OS Gongylonema pulchrum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Spiruroidea; Gongylonematidae; Gongylonema.
OX NCBI_TaxID=637853 {ECO:0000313|Proteomes:UP000050760, ECO:0000313|WBParaSite:GPUH_0001018001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:GPUH_0001018001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN17081.1, ECO:0000313|Proteomes:UP000271098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; UYRT01077870; VDN17081.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A183DN76; -.
DR WBParaSite; GPUH_0001018001-mRNA-1; GPUH_0001018001-mRNA-1; GPUH_0001018001.
DR Proteomes; UP000050760; Unplaced.
DR Proteomes; UP000271098; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF97; ENDOPLASMIN; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000271098};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 105..281
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 319..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..794
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..811
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 811 AA; 92969 MW; 6008814C81068A1B CRC64;
SPSSAKIGIV SYLIIVHWTF SAFFSNIRLK VSAQKDAGTV KEEIGKSREA SKTDDEVIQR
EEEAIKLDGL SVAEVKELRA KAEKHQFQAE VNRMMKLIIN SLYKNKEIFL RELISNASDA
LDKTRLLSLT DPSVLSATDE LSIRIKADVE NHVLHVIDTG TGMTRMDLIN NLGTIARSGT
SEFLAKLLDS STSVEQQQDM IGQFGVGFYS SYLVADHVVV TSKHNDDDQY IWESDSTSRF
GQSVPRLSFT MSSCRFTVVK DPRGATLKRG TQVTLHLKEE AYDFLEADTL KSLVEKYSQF
INFNIFLWQS KTETVEEPVE EVSKAESHEE KAEDVDGKVE DEKSEPKMKK IEKTTWDWEK
VNNVKPIWMR KNDDVEVEEY NEFYKSITKA AIFLSLIAAI SEQDREKPLA YVHFTAEGEV
TFKSILYVPR HSPYDMFQNY GKGTDNIKLY VRRVFITDDF HDMMPKYLSF IRGIVDSDDL
PLNVSRETLQ QHKLLKKMEP GDFEDFWKEY STNIKLGIME DPSNRTRLAK LLRFYSSHSK
GKMTSLAEYV KRMKDKQDVI FYVAGMSREE VESSPFVERL LKKGYEVLYL VEAVDEYAIQ
AMPEFDGKKF QNVAKEGLKL DDGEKDKEIQ EQLEKDFEPL TNWLKNTALK DQIEKAVVSQ
RLVNSPCALV ASSYGWSGNM ERIMKSQAHA KSYDPTQDFY ANQKKTLEVN ARHPVVKELL
RRVQADKNDK QATDAAKLLF ETATLRSGFT LKDQVGFAER IEQVLRQAME MSLDEPVEEE
PEVEAEESKE EGSEDIDETE RTKVEEEHSE L
//
