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Database: UniProt
Entry: A0A0D1C3W4_USTMA
LinkDB: A0A0D1C3W4_USTMA
Original site: A0A0D1C3W4_USTMA 
ID   A0A0D1C3W4_USTMA        Unreviewed;       255 AA.
AC   A0A0D1C3W4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=GrpE protein homolog {ECO:0000256|RuleBase:RU000640};
GN   ORFNames=UMAG_03493 {ECO:0000313|EMBL:KIS68402.1};
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS68402.1, ECO:0000313|Proteomes:UP000000561};
RN   [1] {ECO:0000313|EMBL:KIS68402.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=521 {ECO:0000313|EMBL:KIS68402.1};
RA   Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., Ait-zahra M.,
RA   Allen N., Allen T., An P., Anderson M., Anderson S., Arachchi H.,
RA   Armbruster J., Bachantsang P., Baldwin J., Barry A., Bayul T.,
RA   Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., Borowsky M.,
RA   Boukhgalter B., Brunache A., Butler J., Calixte N., Calvo S., Camarata J.,
RA   Campo K., Chang J., Cheshatsang Y., Citroen M., Collymore A., Considine T.,
RA   Cook A., Cooke P., Corum B., Cuomo C., David R., Dawoe T., Degray S.,
RA   Dodge S., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A.,
RA   Elkins T., Engels R., Erickson J., Farina A., Faro S., Ferreira P.,
RA   Fischer H., Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G.,
RA   Gnerre S., Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K.,
RA   Hafez N., Hagopian D., Hagos B., Hall J., Hatcher B., Heller A.,
RA   Higgins H., Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E.,
RA   Iliev I., Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M.,
RA   Karlsson E., Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E.,
RA   Labutti K., Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T.,
RA   Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., Lui A.,
RA   Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., Manning J.,
RA   Marabella R., Maru K., Matthews C., Mauceli E., Mccarthy M., Mcdonough S.,
RA   Mcghee T., Meldrim J., Meneus L., Mesirov J., Mihalev A., Mihova T.,
RA   Mikkelsen T., Mlenga V., Moru K., Mozes J., Mulrain L., Munson G.,
RA   Naylor J., Newes C., Nguyen C., Nguyen N., Nguyen T., Nicol R., Nielsen C.,
RA   Nizzari M., Norbu C., Norbu N., O'donnell P., Okoawo O., O'leary S.,
RA   Omotosho B., O'neill K., Osman S., Parker S., Perrin D., Phunkhang P.,
RA   Piqani B., Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V.,
RA   Raymond C., Retta R., Richardson S., Rise C., Rodriguez J., Rogers J.,
RA   Rogov P., Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T.,
RA   Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C.,
RA   Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., Stetson K.,
RA   Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., Tenzing P.,
RA   Tesfaye S., Theodore J., Thoulutsang Y., Topham K., Towey S., Tsamla T.,
RA   Tsomo N., Vallee D., Vassiliev H., Venkataraman V., Vinson J., Vo A.,
RA   Wade C., Wang S., Wangchuk T., Wangdi T., Whittaker C., Wilkinson J.,
RA   Wu Y., Wyman D., Yadav S., Yang S., Yang X., Yeager S., Yee E., Young G.,
RA   Zainoun J., Zembeck L., Zimmer A., Zody M., Lander E.;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KIS68402.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 {ECO:0000313|EMBL:KIS68402.1};
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA   de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA   Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA   Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA   Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA   Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA   Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA   Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA   Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA   Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA   Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA   Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA   Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA   Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [3] {ECO:0000313|EMBL:KIS68402.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=521 {ECO:0000313|EMBL:KIS68402.1};
RA   Guldener U., Munsterkotter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003148; KIS68402.1; -; Genomic_DNA.
DR   RefSeq; XP_011389942.1; XM_011391640.1.
DR   AlphaFoldDB; A0A0D1C3W4; -.
DR   STRING; 237631.A0A0D1C3W4; -.
DR   EnsemblFungi; KIS68402; KIS68402; UMAG_03493.
DR   GeneID; 23563929; -.
DR   KEGG; uma:UMAG_03493; -.
DR   VEuPathDB; FungiDB:UMAG_03493; -.
DR   eggNOG; KOG3003; Eukaryota.
DR   InParanoid; A0A0D1C3W4; -.
DR   OMA; YAYEKIA; -.
DR   OrthoDB; 151932at2759; -.
DR   Proteomes; UP000000561; Chromosome 9.
DR   GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IBA:GO_Central.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
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; GRPE PROTEIN; 1.
DR   PANTHER; PTHR21237:SF23; GRPE PROTEIN HOMOLOG, MITOCHONDRIAL; 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   Mitochondrion {ECO:0000256|RuleBase:RU000640};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000561}.
FT   REGION          53..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   255 AA;  27414 MW;  D62A34E981906B5D CRC64;
     MSSSVTRQLG SILRSASRSA LAGSSKQSLA SVAPRTYGLT SASRVMRFST ARTALNSAEK
     KKQDETKASG EAMGATDKDA AAGAGSEALQ AQIKEKDAKI KELQEAILYG KADYQNLQRR
     SKDEKAQAGD FAITKLAKDL TSSIDILGLA LKSVPEELRT APKDLDLKDP RRVVADLYSG
     VDLTSKSLLD MLRTHGIVQF DPTGDKFDPK EHEALYQAPV PGKEPGTVLE CSKVGYKIKD
     RLLRAAEVGV VQSTE
//
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