ID A0A0V0ZVX5_9BILA Unreviewed; 930 AA.
AC A0A0V0ZVX5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Heat shock cognate 71 kDa protein {ECO:0000313|EMBL:KRY16428.1};
DE Flags: Fragment;
GN Name=MDH2 {ECO:0000313|EMBL:KRY16428.1};
GN ORFNames=T12_11552 {ECO:0000313|EMBL:KRY16428.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY16428.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY16428.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY16428.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381}.
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:KRY16428.1}.
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DR EMBL; JYDQ01000078; KRY16428.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0ZVX5; -.
DR Proteomes; UP000054783; 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 GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd10233; HSPA1-2_6-8-like_NBD; 1.
DR CDD; cd01337; MDH_glyoxysomal_mitochondrial; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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 InterPro; IPR022383; Lactate/malate_DH_C.
DR InterPro; IPR001236; Lactate/malate_DH_N.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR001252; Malate_DH_AS.
DR InterPro; IPR010097; Malate_DH_type1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01772; MDH_euk_gproteo; 1.
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 Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 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 SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
DR PROSITE; PS00068; MDH; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Stress response {ECO:0000313|EMBL:KRY16428.1}.
FT DOMAIN 619..762
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 764..928
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY16428.1"
SQ SEQUENCE 930 AA; 102007 MW; 9309EC0786F02E92 CRC64;
LLRCTMSKNA IGIDLGTTYS CVGVFQHGKV EIIANDQGNR TTPSYVAFTD TERLIGDAAK
NQVALNPHNT VFDAKRLIGR RFDDAAVQSD MKHWPFKIIN DGSKPKIQVE YKGESKSFTP
EEISAMVLVK MKETAEAYLG KTVKDAVITV PAYFNDSQRQ ATKDAGTISG LNVLRIINEP
TAAAIAYGLD RKGGGERNVL IFDLGGGTFD VSILTIEDGI FEVKSTAGDT HLGGEDFDNR
MVNHFVAEFK RKNKKDMSSN PRALRRLRTA CERAKRTLSS STQASIEIDS LYEGIDFYTT
ITRARFEELN ADLFRSTLEP VEKALRDAKL DKAVIHEVVL VGGSTRIPKV QKLLQDFFNG
KELNKSINPD EAVAYGAAVQ AAILSGEKHE AVQDLLLLDV TPLSLGIETA GGVMTALIKR
NTTIPTKVSQ VFTTYSDNQP GVLIQVYEGE RAMTKDNNLL GKFELTGIPP APRGVPQIEV
TFDIDANGIL NVSAVDKSTG RQNKITITND KGRLSKEDID RMVREADQYK QEDEKQRDRI
QAKNGLESYA FNVKSTIEDE KLKDKIPESD RKAVLNKCEE VLRWLETNQL AEKDEFEHKQ
KDLESLCNPI MAKLYQGGMK VAVLGASGGI GQPMSLLLKM CPQINHLALY DLVKTIGVGA
DLSHLSTNTK ISAHNGKEQL KDALDGCDVV LIPAGVPRKP GMTRDDLFNT NASIVKELTE
AVAKYSPKAM LCIISNPVNS TVPIAAEVLK KYGVYDYRRL FGVTTLDIIR SNTFIAEAKS
LDVKMVNCPV IGGHSGVTII PVLSQCKPSV IFDEEEAKQL TVRIQEAGTE VVKAKEGTGS
ATLSMAYAGM LFTHSLLDAM CGKSGIIECT FVQSDIIPGI PYFSTPVLLG RNGVERNLGL
PAMNNFEKKL LDTALPELKK NIEKGIKFIN
//