ID A0A158Q5C9_DRAME Unreviewed; 934 AA.
AC A0A158Q5C9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Hypoxia up-regulated protein 1 {ECO:0000256|ARBA:ARBA00040503};
GN ORFNames=DME_LOCUS1585 {ECO:0000313|EMBL:VDN51612.1};
OS Dracunculus medinensis (Guinea worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000703301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:DME_0000703301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN51612.1, ECO:0000313|Proteomes:UP000274756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has a pivotal role in cytoprotective cellular mechanisms
CC triggered by oxygen deprivation. May play a role as a molecular
CC chaperone and participate in protein folding.
CC {ECO:0000256|ARBA:ARBA00037692}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381}.
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DR EMBL; UYYG01000025; VDN51612.1; -; Genomic_DNA.
DR STRING; 318479.A0A158Q5C9; -.
DR WBParaSite; DME_0000703301-mRNA-1; DME_0000703301-mRNA-1; DME_0000703301.
DR Proteomes; UP000038040; Unplaced.
DR Proteomes; UP000274756; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR CDD; cd10230; HYOU1-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR PANTHER; PTHR45639:SF3; HYPOXIA UP-REGULATED PROTEIN 1; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000274756}.
FT REGION 897..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 934 AA; 106966 MW; 976A84B421B4DEC1 CRC64;
MVSNKTKKFL LNFLFFLLFI EKIILKLLDS LLAAMSVDFG SQFLKIALVK AGVPMEIVLN
KETRRKTPNF IAFKDGERLF GESALAFSVK RPQYSFTHLV DLIGKKIDNP IVKLYQKRFP
FSKLTMNNAG DSLHFEVGDT KYNLETLLAM ILQNAQSFTE EFAGQSVKDI VITVPPFFGQ
AERRALISAV NITGMNLLQL LNHHSAAGLS YGMFRRKQIQ EKAETLLIYD MGASSTVASI
LEYRLEFDKK ENEKNPVVNT LGLGYDRTLG GLELSVRLRD HFITEFKKQI KMKEDISMNA
RSMMKMLHEA ERVKIVLSAN NDHFAQIESA HEEHDFRLKV TREQFEILIS DLEQRLVKPI
IDALQMAEIS INQIDQIVLM GASTRVPFVQ AAVQKFLKEK EIGKFLNTDE AIAMGAVYQA
AHHSKGFKVK KFVVKDLQIF PIQNFQVDFA SNSDKSTESR IVHRSIFSYK SLYPTNNKIL
SFSSFKVDFP FNISYGELKH LSDEQRSEFG SMVVSNIELS GLKDAVDAEL VKDGTIFKGV
KTYFRMDDSG IVHIVAADLV IERGPDEKST LSAIADKITG LFTSGRNVDD KEEKNEAISK
EDQTRYEKMD SNAEDFQPNS KENMTLNATN ITEEKIIKPK VIKIPLKLYE RHQDFIGLSD
SEIHVAKKRL TISLDDFADK ERMKVEREAA YHSIESLVYD LAYKLEQSEY LIFVTEQERK
AINDEVARIR IWLEDEVGVT TSTEEFIKKR RTLDNLLKPI DYRIKQEKDR PRLLSDFVSI
FNHSESFLAL AKNLTEIGVF TEVERSTLEK KINETKMWFI ENNQAQSLLK PTDKPVYTNE
DLLDKMYDLD RELKYLFNKM KITKPKKLFE TVEPGSNNTS SNETVIPTDE LNKQIKLDHE
KSDKLKEPVE VDKSESTKVN TSEADIVRHD ASEL
//
