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Database: UniProt
Entry: M1XK33_9METZ
LinkDB: M1XK33_9METZ
Original site: M1XK33_9METZ 
ID   M1XK33_9METZ            Unreviewed;       632 AA.
AC   M1XK33;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Molecular chaperones GRP78/BiP/KAR2, HSP70 superfamily {ECO:0000313|EMBL:CCQ18651.1};
GN   Name=hsp70C {ECO:0000313|EMBL:CCQ18651.1};
OS   Sycon ciliatum.
OC   Eukaryota; Metazoa; Porifera; Calcarea; Calcaronea; Leucosolenida;
OC   Sycettidae; Sycon.
OX   NCBI_TaxID=27933 {ECO:0000313|EMBL:CCQ18651.1};
RN   [1] {ECO:0000313|EMBL:CCQ18651.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23511216; DOI=10.1016/j.ympev.2013.03.005;
RA   Minaya M., Pimentel M., Mason-Gamer R., Catalan P.;
RT   "Distribution and evolutionary dynamics of Stowaway Miniature Inverted
RT   repeat Transposable Elements (MITEs) in grasses.";
RL   Mol. Phylogenet. Evol. 68:106-118(2013).
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; HF570334; CCQ18651.1; -; mRNA.
DR   AlphaFoldDB; M1XK33; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd10233; HSPA1-2_6-8-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; 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:SF395; HEAT SHOCK 70 KDA PROTEIN COGNATE 1-RELATED; 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.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003322}.
FT   REGION          608..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   632 AA;  69125 MW;  172A27C8DC633797 CRC64;
     MKANSKTAIG IDLGTTYSCV GVYQHGKVEI LANSQGNRTT PSYVAFSDTE RLIGDAAKDQ
     VARNPKNTIF DAKRLIGRQF TDTAVQKDMK HWPFQVINVN GQPKLQVEYQ GENKVLSPEE
     VSSMVLSKMK ETAEAYLGTG VTDAVVTVPA YFNDSQRQAT KDAGRIAGLN VLRIINEPTA
     AALAYGLDKR MSSEQNVLVY DLGGGTFDVS ILSIDNGLFA VKSTAGDTHL GGEDFDNRLV
     EHFVAEFKRK HKQDLSGDAR ALRRLRTACE RAKRTLSSST DASVEIDSLY RGIDFYSKIT
     RARFEELCSD LFRSTLEPVE RALNDAKMGK SEIHEVVLVG GSTRIPKIQK LLQDYFNGKE
     LNKGINPDEA VAYGAAVQAA ILSGVKDERV DSVVLLDVAP LSLGIETAGG VMTTLIKRNT
     TIPTRAGETF TTYSDNQPGV TVQVYEGERA MTKDNHLLGR FELSGMPPAP RGVPKIDVSF
     DIDANGILHV TAKDQSSGRS SDICITNEKG RLSKADIERM VAEAEQFQQA DDAQRERVAA
     RNQLESYAFN VRSAMSDSAS KLSADEVKKV TSATQDALDW LEKNQLAEKE EIEHRMSDLQ
     QLCSPIMAKL HGGADNNGKE PSTQGPNVEE VD
//
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