ID L2GSI2_VAVCU Unreviewed; 695 AA.
AC L2GSI2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Hsp70-like protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=VCUG_01919 {ECO:0000313|EMBL:ELA46589.1};
OS Vavraia culicis (isolate floridensis) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pleistophoridae;
OC Vavraia.
OX NCBI_TaxID=948595 {ECO:0000313|EMBL:ELA46589.1, ECO:0000313|Proteomes:UP000011081};
RN [1] {ECO:0000313|Proteomes:UP000011081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=floridensis {ECO:0000313|Proteomes:UP000011081};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Becnel J., Sanscrainte N., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The genome sequence of Vavraia culicis strain floridensis.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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; GL877439; ELA46589.1; -; Genomic_DNA.
DR RefSeq; XP_008074935.1; XM_008076744.1.
DR AlphaFoldDB; L2GSI2; -.
DR STRING; 948595.L2GSI2; -.
DR GeneID; 19879788; -.
DR VEuPathDB; MicrosporidiaDB:VCUG_01919; -.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; L2GSI2; -.
DR OMA; YAYHMKS; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000011081; 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 CDD; cd10170; HSP70_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 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; 2.
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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000011081}.
FT REGION 556..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 695 AA; 76117 MW; 10B58161079E0BB0 CRC64;
MSSQNTSKET SKAIGIDLGT TYSCVCAYRN GELEVISNEE GARITPSIVA FDDEGNIVIG
TAAEHRLTSN PDKVVYDVKR LIGRGYDSPV LESSIKKWPF RVVRWDNDRN STTDRPAKSD
AVDNIRIEIM KGGKVMHYDP MEISGYVLGF LKRAAEAVLN SGVTTAVITV PAHFNDNQKE
KTKMAAEIAG FKNVRLLNEP TAAALSYAYD KMRRKEANKE ETVLVFDLGG GTFDVSILKF
EPPSESGAIA EVLNTEGDTF LGGVDFDNVL FEHCLALFLK QNPSVKKEEI KDRAKRRLRM
ACEKAKRNLS AMNSTTIEIE CLHSDLGLCT SITRALFNSL CMKYFRRCMD RVKGCLLGLA
KVKPDYTSEG FLTAASAANT SAINDAIAQV DRVIVVGGSS RIVKIREMLA EIFGEHKLDF
SVHPDEAIAR GAAYQAALIS GGTSLDVECP LLLLDTVPLN ISIETLGGVA TNIIKKNTVI
PTAKTEVFST ASDNQTSVTI NIYEGLGEMV EHNNLIGSFN LCGITPARRG MPQIEVTCDV
DNNGILVVTA REKGSNKSEK LTVSNSNRKT TPEQLEEMHK KHKEFEEADR KKKENVSAKI
EYEAMLYQLN EKVAEVPDQN VKSSLETSLK QHQEWLDAHP NADKDEYVTK KDELMGLLQQ
VAGSAQGAAP GGFDASNFGG APPHSTTEPK VDEVD
//