ID A0A091GRW1_9AVES Unreviewed; 363 AA.
AC A0A091GRW1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Outer mitochondrial transmembrane helix translocase {ECO:0000256|ARBA:ARBA00040718};
DE Flags: Fragment;
GN ORFNames=N303_09608 {ECO:0000313|EMBL:KFO76817.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO76817.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO76817.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO76817.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-with a C-terminal TM segment(out) + ATP + H2O =
CC [protein]-with a C-terminal TM segment(in) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:66168, Rhea:RHEA-COMP:16963, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:90782, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00036758};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC outer membrane {ECO:0000256|ARBA:ARBA00004572}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004572}. Postsynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00037805}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00037805}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. MSP1 subfamily.
CC {ECO:0000256|ARBA:ARBA00038383}.
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DR EMBL; KL447758; KFO76817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091GRW1; -.
DR STRING; 55661.A0A091GRW1; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd19520; RecA-like_ATAD1; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45644; AAA ATPASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G12920)-RELATED-RELATED; 1.
DR PANTHER; PTHR45644:SF2; OUTER MITOCHONDRIAL TRANSMEMBRANE HELIX TRANSLOCASE; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Membrane {ECO:0000256|ARBA:ARBA00022787};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00022787};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Reference proteome {ECO:0000313|Proteomes:UP000053760}.
FT DOMAIN 126..262
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO76817.1"
FT NON_TER 363
FT /evidence="ECO:0000313|EMBL:KFO76817.1"
SQ SEQUENCE 363 AA; 41050 MW; B17505D7A0AD7B1C CRC64;
KMVHAEAFSR PLSSHEVVGL IFRLTIFGAV TYFTIKWMVD AIDPTRKQKV EAQKQAEKLM
KQIGVKNVKL TEYEMSIAAH LVDPLSMHVT WSDIAGLDDV ITDLKDTVIL PIKKKYLFEN
SRLLQPPKGV LLYGPPGCGK TLIAKATAKE AGCRFINLQP STLTDKWYGE SQKLAAAVFS
LAIKLQPSII FIDEIDSFLR SRSSSDHEAT AMMKAQFMSL WDGLDTDYNC QVIVMGATNR
PQDLDSAIMR RMPTRFHINQ PALKQREAIL KLILKNENVD RRVDLLEVAK ETDGFSGSDL
KEMCRDAALL CVREYVNSAC EEEAHDEDEI RPVQQQDLHR AIEKMRRSKD ATLQNVLMHV
SLD
//