ID E3N466_CAERE Unreviewed; 260 AA.
AC E3N466;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Glycine cleavage system H protein, mitochondrial {ECO:0000256|ARBA:ARBA00018130};
GN ORFNames=CRE_24143 {ECO:0000313|EMBL:EFO85348.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GcvH family.
CC {ECO:0000256|ARBA:ARBA00009249}.
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DR EMBL; DS268523; EFO85348.1; -; Genomic_DNA.
DR RefSeq; XP_003096825.1; XM_003096777.1.
DR AlphaFoldDB; E3N466; -.
DR STRING; 31234.E3N466; -.
DR EnsemblMetazoa; CRE24143.1; CRE24143.1; WBGene00067669.
DR eggNOG; KOG3373; Eukaryota.
DR HOGENOM; CLU_1070552_0_0_1; -.
DR InParanoid; E3N466; -.
DR OrthoDB; 52189at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:InterPro.
DR CDD; cd06848; GCS_H; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR002930; GCV_H.
DR InterPro; IPR033753; GCV_H/Fam206.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR11715; GLYCINE CLEAVAGE SYSTEM H PROTEIN; 1.
DR PANTHER; PTHR11715:SF3; GLYCINE CLEAVAGE SYSTEM H PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF01597; GCV_H; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000008281}.
FT DOMAIN 155..233
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 260 AA; 29403 MW; 3AF393D413844592 CRC64;
MRFFSIFSLF RGKISGLTGF LIVIKLKNAS LTHFFPEKDY LNHNRVVRPA SAAIVDTDHL
NRPLFFERNE EKASFRSVRS DSIKPQAKSR RMGRAMRVIV VGGKKVGKTA ILRQVACVED
ITNKAADAVV LFYSSADYES FNRVDSLKKW LDRQFGKDKK EEQLGDVVFI ELPDEGTEIS
KGDSTGAVES VKAASDIYAP ISGTVTQKNV KLEEEAGLIN KSPFEKGWLY KLKVKSEDEL
KKLLTEQQYE QFKKDEEAAH
//
