TIM16_EMENI
ID TIM16_EMENI Reviewed; 135 AA.
AC Q5B187; C8VFQ0;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit tim16;
DE AltName: Full=Presequence translocated-associated motor subunit pam16;
GN Name=pam16; Synonyms=tim16; ORFNames=AN5693;
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 regulate activity of mtHSP70
CC (SSC1/sscA) via its interaction with PAM18/TIM14. May act by
CC positioning PAM18/pamR in juxtaposition to mtHSP70 at the translocon to
CC maximize ATPase stimulation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with PAM18/pamR. 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 Peripheral membrane protein {ECO:0000250}.
CC -!- DOMAIN: The J-like region, although related to the J domain does not
CC stimulate ATPase activity of mtHSP70. It nevertheless mediates the
CC heterodimerization with the J domain of PAM18 and is therefore
CC essential for PAM complex function (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TIM16/PAM16 family. {ECO:0000305}.
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DR EMBL; AACD01000098; EAA62786.1; -; Genomic_DNA.
DR EMBL; BN001305; CBF81393.1; -; Genomic_DNA.
DR RefSeq; XP_663297.1; XM_658205.1.
DR AlphaFoldDB; Q5B187; -.
DR SMR; Q5B187; -.
DR STRING; 162425.CADANIAP00003372; -.
DR EnsemblFungi; CBF81393; CBF81393; ANIA_05693.
DR EnsemblFungi; EAA62786; EAA62786; AN5693.2.
DR GeneID; 2871982; -.
DR KEGG; ani:AN5693.2; -.
DR VEuPathDB; FungiDB:AN5693; -.
DR eggNOG; KOG3442; Eukaryota.
DR HOGENOM; CLU_101461_0_1_1; -.
DR InParanoid; Q5B187; -.
DR OMA; AKYLIQI; -.
DR OrthoDB; 1640138at2759; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IEA:EnsemblFungi.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IEA:EnsemblFungi.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR005341; Tim16.
DR PANTHER; PTHR12388; PTHR12388; 1.
PE 3: Inferred from homology;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Protein transport;
KW Reference proteome; Translocation; Transport.
FT CHAIN 1..135
FT /note="Mitochondrial import inner membrane translocase
FT subunit tim16"
FT /id="PRO_0000214092"
FT REGION 30..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..111
FT /note="J-like"
FT REGION 114..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 135 AA; 15100 MW; 6FC62DE04D4F44EC CRC64;
MAHRIVTQVV VTGARVFGRA FAEAYKQASA ASKYQQKTGK SAGGSSSSGI TLDEACKILN
VKPPQAGETN LEQVMERFKK LFDLNDPQKG GSFYLQSKIL RARERIEAEV REAERKAAHE
KELKEGWKPK VYKDR
