ID A0A401Q0J3_SCYTO Unreviewed; 541 AA.
AC A0A401Q0J3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Stress-70 protein, mitochondrial {ECO:0000256|ARBA:ARBA00019355};
DE AltName: Full=75 kDa glucose-regulated protein {ECO:0000256|ARBA:ARBA00031419};
DE AltName: Full=Heat shock 70 kDa protein 9 {ECO:0000256|ARBA:ARBA00030055};
GN ORFNames=scyTo_0016886 {ECO:0000313|EMBL:GCB78884.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB78884.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB78884.1, ECO:0000313|Proteomes:UP000288216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCB78884.1}.
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DR EMBL; BFAA01010534; GCB78884.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401Q0J3; -.
DR STRING; 75743.A0A401Q0J3; -.
DR OMA; GREQKMT; -.
DR Proteomes; UP000288216; 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 Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 3.
DR InterPro; IPR043129; ATPase_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; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000288216}.
FT REGION 518..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 418..491
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 541 AA; 58514 MW; 279480F19B07C54C CRC64;
MFYLVCSASR RLAAAGRGHW NGLSQDVLRS LARRNYASEA IKGAVIGIDL GTTNSCVAVM
EGKQAKATKD AGQIAGLNVL RVINEPTAAA LAYGLDKSED KVIAVYDLGG GTFDISVLEI
QKGVFEVKST NGDTFLGGED FDQALLKHII KEFKRESGVD LTKDNMALQR VREASEKAKC
ELSSSLQTDI NLPYLTMDAS GPKHLNIKIS RAQFENIVAD LIKRTINPCQ KAMQDAEVSK
SDIGEVILVG GMTRMPKVQA TVQELFGRSP SKSVNPDEAV AVGAAIQGGV LAGDVTDVLL
LDVTPLSLGI ETLGGVFTKL IGRNTTIPTK KGQVFSTAAD GQTQVEIKVF QGEREMAADN
KLLGQFTLVG MPPAPRGVPQ IEVTFDIDAN GIVHVSARDK GTGREQQIVI QSSGGLSKDD
IENMIKNAEK YAEADRRKKE TVEAVNTAEG IIHDTESKME EFKDQLPKEE CDKLREEITK
LKELLARKES ETGETIKAAA SNLQQASLKL FEMAYKKMAS ERESSGSTDN SESGDKKEEK
Q
//
