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TIM14_EMENI
ID   TIM14_EMENI             Reviewed;         105 AA.
AC   Q5B4H1; C8V868;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit tim14;
DE   AltName: Full=Presequence translocated-associated motor subunit pam18;
GN   Name=pam18; Synonyms=tim14; ORFNames=AN4559;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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. In the complex, it is required to stimulate activity of mtHSP70
CC       (SSC1/sscA) (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with PAM16/pamP. Component of the PAM complex, at
CC       least composed of mtHsp70, MGE1/mgeA, tim44, PAM16/pamP, PAM17/pamQ and
CC       PAM18/pamR (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The J domain is essential for co-chaperone activity and
CC       mediates the heterodimerization with the J-like domain of PAM16.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TIM14 family. {ECO:0000305}.
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DR   EMBL; AACD01000078; EAA60902.1; -; Genomic_DNA.
DR   EMBL; BN001303; CBF77258.1; -; Genomic_DNA.
DR   RefSeq; XP_662163.1; XM_657071.1.
DR   AlphaFoldDB; Q5B4H1; -.
DR   SMR; Q5B4H1; -.
DR   STRING; 162425.CADANIAP00005879; -.
DR   EnsemblFungi; CBF77258; CBF77258; ANIA_04559.
DR   EnsemblFungi; EAA60902; EAA60902; AN4559.2.
DR   GeneID; 2872360; -.
DR   KEGG; ani:AN4559.2; -.
DR   VEuPathDB; FungiDB:AN4559; -.
DR   eggNOG; KOG0723; Eukaryota.
DR   HOGENOM; CLU_017633_13_3_1; -.
DR   InParanoid; Q5B4H1; -.
DR   OMA; GFQQTMT; -.
DR   OrthoDB; 1600166at2759; -.
DR   Proteomes; UP000000560; Chromosome III.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IBA:GO_Central.
DR   GO; GO:0001671; F:ATPase activator activity; IBA:GO_Central.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR036869; J_dom_sf.
DR   SUPFAM; SSF46565; SSF46565; 1.
PE   3: Inferred from homology;
KW   Chaperone; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Protein transport; Reference proteome; Translocation; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..105
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit tim14"
FT                   /id="PRO_0000071112"
FT   TOPO_DOM        1..3
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        24..105
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          52..105
FT                   /note="J"
SQ   SEQUENCE   105 AA;  11605 MW;  196B2B2444D6A27D CRC64;
     MASALTLGLG VATAAFLGRA GLVAYRRSKG GVNALGKAFY KGGFEPRMNR REAALILELP
     ERTLNKEKVR KKHRQLMLLN HPDRGGSPYL ATKINEAKEF LDKHT
 
 
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