ID A0A1I8CKC9_9BILA Unreviewed; 1850 AA.
AC A0A1I8CKC9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Heat shock protein 70 {ECO:0000313|WBParaSite:RSKR_0000573500.1};
OS Rhabditophanes sp. KR3021.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Alloionematidae;
OC Rhabditophanes.
OX NCBI_TaxID=114890 {ECO:0000313|Proteomes:UP000095286, ECO:0000313|WBParaSite:RSKR_0000573500.1};
RN [1] {ECO:0000313|WBParaSite:RSKR_0000573500.1}
RP IDENTIFICATION.
RC STRAIN=KR3021 {ECO:0000313|WBParaSite:RSKR_0000573500.1};
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR WBParaSite; RSKR_0000573500.1; RSKR_0000573500.1; RSKR_0000573500.
DR Proteomes; UP000095286; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd10170; HSP70_NBD; 1.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.120.1000; -; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 3.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR InterPro; IPR001791; Laminin_G.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00301; HEATSHOCK70.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 4.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 2.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1779..1805
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 791..958
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1113..1150
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1381..1547
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1543..1580
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT COILED 225..252
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 1140..1149
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1850 AA; 208150 MW; EF9BE8C773C9252D CRC64;
MSDCAKYVER YPIGIDLGTT YSCAAVYMGD HIEIIKNNND IKRLIGRGFN DKTVQEDIKL
HPFNISGSSD NCIEMDVKYG GQTIKLNPEM ISALILNKIK HDAEVYLKYE VTEAVITVPA
YFTDSQRNST KIAGEMVGLE VLQIINEPTS AAIAYGFGHR GEASKTVLIF DFGGGTFDVS
IVKVKNFEID VLTTDGNSHL GGSDFDASIS TFLMIELQKK HNLDVKHDKK RYAELKVKAE
IAKKELSDKN ETIVEFYFDE SISIKITRQK FEMMCMYLME DAIKTVEKAL KDTNLTTKQI
DDVVLIGGTS RIPKIQKMLE NMFGDTVLRR SVNPDEAVAH GAALKATHIV ERTRRSLADF
RISDICPMSL GIQLINDGMS VLIPKNSKLP IENEKTYFTT ADNQXIDDVV LIGGTSRIPK
IQKMLENMFG DTVLRRSVNP DEAVAHGAAL KATHIVERTR RSLADFRISD ICPMSLGIQL
INDGMSVLIP KNSKLPIENE KTYFTTADNQ TSVAIIIKEG ECDIASKNNT LDKFTLDGIP
PLPMGQARIQ AKMTIDVSGI LNVTATVEAN GNTKNIIIKR DTNNFAQQNV TSMKQKIASL
IKQQLERETF KDDQNRLIDK ITKILEKIDD DEKLWTGNIN QKSKYIKDSN ATISMIEELE
FKNRINLNSI HDKLMASLLP FPHDCSEKTF TKLELSFDEV QSIQKVAIIA PLGTYYILTS
LTEGEDDDLV GVFMQNGQKM VVHSSLTANY IEWHTIDILV KRIKIVPIFD NGNSMKYHSP
QLIINSCTYN TKLLYVDDQS YTVDSYNAGL VSMYENELVV TFRTFESGLF FFSLADQGDM
LIAQIVNGHI EVLFDFGSLS KSVISGGIAL NDGNWHEMKW IHQFDSVKLV IDGVLLNSTT
PAGLYRKLDF NFEVEIGGRP YDQYSKDIQS SYHGCLAKVN LNNIDLLSYA PKDKFSECHM
AKPQILTIND SDSSVYIPYS FMPFTFEFRM LRQTSNLITV LDGKNESLLS LAVQKNNSLY
LIAEKNEIKQ EFVPSFLISD GSWHSISIKM RNGRLNVEMN GLIVLWLEGS FVRTLGLSLT
AFNLTGVGCF RSASVDFKNA VVFGKVHRDK CSYKEMCLPC PCQNKGVCSQ TALDNFECSC
PNGFSGKFCH TAMYPYSCED HLQRLLLQTK KFQGIFGGFK SKLKLEPNVT IDIDGSGPNT
PFQVECRFSN KTHPDQSESI ETVLFHDLLQ GMYVTGTTEP GSIRKVLNYG MSESTIEKFI
DGFSSCKQFQ RYQCRGGSKL MTYGNERRPS SWYATRNGQQ GLQWADAPPY SRVCECAMNA
SCSFNRMCNC DSGRDGIDEG YNSHLQLLPV IQLYAGGTHK TSSVNISIGP LICSQKIAFD
VVTFNDRNQR LVGSHTFNGP IFDLYLQVRF SHSLMTIFTW ESKNSERWFQ LFVREGYLVA
QIVNGGRSQE VQSGLKINDD SWHTVYWEAD LNTMKLVVDK EETSVSMYNI LPWTYNYIIG
SRNERGFSGF AGQMRNFYLC GKAINLSGLA RKLHSNNGIK VGLEGFCKPH YCKNGGKCVE
MYDNFKCNCS MTAFDGDRCN QERSAWIPLR SELSIPWQHP SQMSNCYRMG VQTHSTNVSL
IKAKALFADS SFNLSITVEG NLNVSMYDGF FFLHQKIVKE SNFSDNTMKD IHFCATKKAF
ELKVDDKVVL TFDGNFTFFS TFNVWNFVDH KFMGCVARLQ IGASFPLKNP VETRLTYTSH
VKFDVCPHEK LLYKETEQPD TSKKSDISIS VVSESHQKML ILTPIIGVSI GSVLCILLCC
FVCYVKNKPD GVYKTNEAMS GYCSGSPSKS AEYLMTNRSL PVPQNKEYFC
//
