ID A0A182K886_9DIPT Unreviewed; 660 AA.
AC A0A182K886;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 31.
DE RecName: Full=Heat shock 70 kDa protein cognate 3 {ECO:0008006|Google:ProtNLM};
OS Anopheles christyi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43041 {ECO:0000313|EnsemblMetazoa:ACHR006971-PA, ECO:0000313|Proteomes:UP000075881};
RN [1] {ECO:0000313|Proteomes:UP000075881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACHKN1017 {ECO:0000313|Proteomes:UP000075881};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles christyi ACHKN1017.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACHR006971-PA}
RP IDENTIFICATION.
RC STRAIN=ACHKN1017 {ECO:0000313|EnsemblMetazoa:ACHR006971-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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DR AlphaFoldDB; A0A182K886; -.
DR STRING; 43041.A0A182K886; -.
DR EnsemblMetazoa; ACHR006971-RA; ACHR006971-PA; ACHR006971.
DR VEuPathDB; VectorBase:ACHR006971; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000075881; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR CDD; cd10241; HSPA5-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR042050; BIP_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375:SF144; ENDOPLASMIC RETICULUM CHAPERONE BIP; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 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.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..660
FT /note="Heat shock 70 kDa protein cognate 3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008125271"
FT REGION 637..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 281..308
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 597..629
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 660 AA; 72828 MW; 60DDD53B3A056C56 CRC64;
MKLLKQSALV VVLAVLACSA EEKKEKDKDI GTVVGIDLGT TYSCVGVYKN GRVEIIANDQ
GNRITPSYVA FTADGERLIG DAAKNQLTTN PENTVFDAKR LIGREFTDHT VQHDIKLLPF
KVIEKNSKPH IRVSTGQGDK VFAPEEISAM VLGKMKETAE AYLGHSVKNA VITVPAYFND
SQRQATKDAG AIAGLVVMRI INEPTAAAIA YGLDKNLDGE KNVLVFDLGG GTFDVSLLTI
DNGVFEVVAT NGDTHLGGED FDQRVMDHFI KMYKKKKGKD IRKDNRAVQK LRREVEKAKR
ALSASHQVRI EIESFFEGDD FSETLTRAKF EELNMDLFRS TMKPVHKVLE DADMTKNDVD
EIVLVGGSTR IPKVQQLVKE FFNGKEPSRG INPDEAVAYG AAVQAGVLSG EQDTDAIVLL
DVNPLTMGIE TVGGVMTKLI PRNTVIPTKK SQIFSTASDN QHTVTIQVYE GERPMTKDNH
LLGKFDLTGI PPAPRGIPQI EVSFEIDANG ILQVSAEDKG TGNREKIVIT NDQNRLTPDD
IERMIKDAER FADDDKKLKE RVEARNELES YAYSLKNQLS SKDKLGASVS EDDKAKMEEA
IDEKIKWLDE NQDTEAEEYK KQKKELEDIV QPIIAKLYAS SGGAPPPAGG EEDDELKDEL
//
