ID D8U190_VOLCA Unreviewed; 147 AA.
AC D8U190;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=GrpE protein homolog {ECO:0000256|RuleBase:RU000640};
GN ORFNames=VOLCADRAFT_62474 {ECO:0000313|EMBL:EFJ46593.1};
OS Volvox carteri f. nagariensis.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN [1] {ECO:0000313|EMBL:EFJ46593.1, ECO:0000313|Proteomes:UP000001058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX PubMed=20616280; DOI=10.1126/science.1188800;
RA Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT "Genomic analysis of organismal complexity in the multicellular green alga
RT Volvox carteri.";
RL Science 329:223-226(2010).
CC -!- FUNCTION: Essential component of the PAM complex, a complex required
CC for the translocation of transit peptide-containing proteins from the
CC inner membrane into the mitochondrial matrix in an ATP-dependent
CC manner. {ECO:0000256|RuleBase:RU000640}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|RuleBase:RU000640}.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000256|ARBA:ARBA00009054,
CC ECO:0000256|RuleBase:RU004478}.
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DR EMBL; GL378350; EFJ46593.1; -; Genomic_DNA.
DR RefSeq; XP_002952450.1; XM_002952404.1.
DR AlphaFoldDB; D8U190; -.
DR STRING; 3068.D8U190; -.
DR GeneID; 9628700; -.
DR KEGG; vcn:VOLCADRAFT_62474; -.
DR eggNOG; KOG3003; Eukaryota.
DR InParanoid; D8U190; -.
DR OrthoDB; 36313at2759; -.
DR Proteomes; UP000001058; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd00446; GrpE; 1.
DR Gene3D; 3.90.20.20; -; 1.
DR Gene3D; 2.30.22.10; Head domain of nucleotide exchange factor GrpE; 1.
DR HAMAP; MF_01151; GrpE; 1.
DR InterPro; IPR000740; GrpE.
DR InterPro; IPR013805; GrpE_coiled_coil.
DR InterPro; IPR009012; GrpE_head.
DR PANTHER; PTHR21237:SF40; CELL CYCLE AND APOPTOSIS REGULATOR PROTEIN 2; 1.
DR PANTHER; PTHR21237; GRPE PROTEIN; 1.
DR Pfam; PF01025; GrpE; 1.
DR PRINTS; PR00773; GRPEPROTEIN.
DR SUPFAM; SSF58014; Coiled-coil domain of nucleotide exchange factor GrpE; 1.
DR SUPFAM; SSF51064; Head domain of nucleotide exchange factor GrpE; 1.
DR PROSITE; PS01071; GRPE; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU000640};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Mitochondrion {ECO:0000256|RuleBase:RU000640};
KW Reference proteome {ECO:0000313|Proteomes:UP000001058}.
FT COILED 7..34
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 147 AA; 16619 MW; B51DDA775B2ED9E0 CRC64;
MVATGGVREA QERLQRLQAD FDNFKRRASA EREQLVVRVK ADALRPILAV ADNFERAAIQ
IKPKTDGERA VQDAYQTVYN ELKEFLKKEG LQEVGVEGEA FDPNQHEAVM REDRNDVDDG
TVTGVFQRGY RLGEVLVRPA LVKVAYN
//
