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CCM1_YEAST
ID   CCM1_YEAST              Reviewed;         864 AA.
AC   P48237; D6VUT1;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Mitochondrial group I intron splicing factor CCM1;
DE   AltName: Full=COB and COX1 mRNA maturation protein 1;
DE   AltName: Full=Required for respiratory growth protein 2;
DE   Flags: Precursor;
GN   Name=CCM1; Synonyms=DMR1, RRG2; OrderedLocusNames=YGR150C; ORFNames=G6642;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8585325; DOI=10.1002/yea.320111410;
RA   Skala J., Nawrocki A., Goffeau A.;
RT   "The sequence of a 27 kb segment on the right arm of chromosome VII from
RT   Saccharomyces cerevisiae reveals MOL1, NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2,
RT   NSR1 genes and ten new open reading frames.";
RL   Yeast 11:1421-1427(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=16823961; DOI=10.1021/pr050477f;
RA   Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT   "Toward the complete yeast mitochondrial proteome: multidimensional
RT   separation techniques for mitochondrial proteomics.";
RL   J. Proteome Res. 5:1543-1554(2006).
RN   [7]
RP   FUNCTION.
RX   PubMed=19562342; DOI=10.1007/s00294-009-0260-z;
RA   Moreno J.I., Buie K.S., Price R.E., Piva M.A.;
RT   "Ccm1p/Ygr150cp, a pentatricopeptide repeat protein, is essential to remove
RT   the fourth intron of both COB and COX1 pre-mRNAs in Saccharomyces
RT   cerevisiae.";
RL   Curr. Genet. 55:475-484(2009).
RN   [8]
RP   FUNCTION.
RX   PubMed=19751518; DOI=10.1186/gb-2009-10-9-r95;
RA   Merz S., Westermann B.;
RT   "Genome-wide deletion mutant analysis reveals genes required for
RT   respiratory growth, mitochondrial genome maintenance and mitochondrial
RT   protein synthesis in Saccharomyces cerevisiae.";
RL   Genome Biol. 10:R95.1-R95.18(2009).
RN   [9]
RP   SUBCELLULAR LOCATION, RNA-BINDING, AND FUNCTION.
RX   PubMed=20124025; DOI=10.1534/genetics.110.113969;
RA   Puchta O., Lubas M., Lipinski K.A., Piatkowski J., Malecki M., Golik P.;
RT   "DMR1 (CCM1/YGR150C) of Saccharomyces cerevisiae encodes an RNA-binding
RT   protein from the pentatricopeptide repeat family required for the
RT   maintenance of the mitochondrial 15S ribosomal RNA.";
RL   Genetics 184:959-973(2010).
CC   -!- FUNCTION: RNA-binding protein involved in the specific removal of group
CC       I introns in mitochondrial encoded transcripts. Maintains the stability
CC       of the small subunit mitochondrial 15S rRNA and thus the expression of
CC       the mitochondrial genome. {ECO:0000269|PubMed:19562342,
CC       ECO:0000269|PubMed:19751518, ECO:0000269|PubMed:20124025}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:20124025}.
CC   -!- MISCELLANEOUS: Present with 876 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the CCM1 family. {ECO:0000305}.
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DR   EMBL; X85807; CAA59808.1; -; Genomic_DNA.
DR   EMBL; Z72935; CAA97164.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08242.1; -; Genomic_DNA.
DR   PIR; S60441; S60441.
DR   RefSeq; NP_011666.1; NM_001181279.1.
DR   AlphaFoldDB; P48237; -.
DR   BioGRID; 33398; 47.
DR   DIP; DIP-6575N; -.
DR   IntAct; P48237; 2.
DR   STRING; 4932.YGR150C; -.
DR   MaxQB; P48237; -.
DR   PaxDb; P48237; -.
DR   PRIDE; P48237; -.
DR   EnsemblFungi; YGR150C_mRNA; YGR150C; YGR150C.
DR   GeneID; 853053; -.
DR   KEGG; sce:YGR150C; -.
DR   SGD; S000003382; CCM1.
DR   VEuPathDB; FungiDB:YGR150C; -.
DR   eggNOG; ENOG502QUX2; Eukaryota.
DR   HOGENOM; CLU_334653_0_0_1; -.
DR   InParanoid; P48237; -.
DR   OMA; RALYYKY; -.
DR   BioCyc; YEAST:G3O-30853-MON; -.
DR   PRO; PR:P48237; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P48237; protein.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0019843; F:rRNA binding; IDA:SGD.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IMP:SGD.
DR   GO; GO:0000963; P:mitochondrial RNA processing; IMP:SGD.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:2000234; P:positive regulation of rRNA processing; IMP:SGD.
DR   GO; GO:0008380; P:RNA splicing; IMP:SGD.
DR   GO; GO:0016072; P:rRNA metabolic process; IMP:SGD.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR002885; Pentatricopeptide_repeat.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   Pfam; PF13041; PPR_2; 1.
DR   TIGRFAMs; TIGR00756; PPR; 1.
DR   PROSITE; PS51375; PPR; 2.
PE   1: Evidence at protein level;
KW   Mitochondrion; mRNA processing; mRNA splicing; Reference proteome; Repeat;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..864
FT                   /note="Mitochondrial group I intron splicing factor CCM1"
FT                   /id="PRO_0000202830"
FT   REPEAT          319..355
FT                   /note="PPR 1"
FT   REPEAT          356..390
FT                   /note="PPR 2"
FT   REGION          80..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   864 AA;  101423 MW;  5A773DEAA33D84FE CRC64;
     MYMARCGPKN NVLCFPFQLS FLFSKRLINK RFKYTLQTED EKNMMGSLSK NKIITPEDVE
     FKLAQLREFS NTLKERIHNT KSVNSDGHQS NSIAPISEDS RNVNVTKTSS VPNEEKSKNL
     SDLIHSSFLE KMDHLVPKVI RERVADDDIL AKNLFDRSHS NWAPVIDRLY VSEKRFMDID
     SREFSVWLNG TVKYLPFHSI LHLDEMLLEQ INGDVVKFNT HMYECIFNNL GNLKPTNFNQ
     DGTNDKVILK MKELLERYDK ALKITEERIN KKEGFPSKVP KMTQAILNNC LKYSTKCSSF
     HDMDYFITKF RDDYGITPNK QNLTTVIQFY SRKEMTKQAW NTFDTMKFLS TKHFPDICTY
     NTMLRICEKE RNFPKALDLF QEIQDHNIKP TTNTYIMMAR VLASSSSNAV VSEGKSDSLR
     LLGWKYLHEL EDKNLYRHKK DDLNLFLAMM ALAAFDGDIE LSRALYYLFI AKKYKTLCAN
     WKGNILVDQD TIWKSTLMPE MLNYLMLAYA RFDPRNLPVL SGYEKGIELR RKFLREFDSS
     MRLDDTDKLV KFKLPFLPIS DLNSEAQVLA ESNAIWSFNM ENGGTRNTLT SSNEAALEDI
     KKYRQLLDSF AQEAEDFNEF KFKVMYEVTK MQRESINVNV FNKISLHTYL SIPINLKQQK
     EFLRRLTFFT FQQHEFEAVI KRLYEGYRNI PSSHTRDQNS ISTEAISVSK PETTEDLNLI
     MHDIWYITCL RHKIMMDTTL YELVMKAAIE FQNEDLAKKV WNDRGKFRTT VPFLKMDQRI
     RIAKDQKFAH LMVEFFTKQG KYSDAIAIIL SSKNRFNWTY SMVRNLHKAL EEIEDRNSVE
     ILLDVVNKKS HAKALKWEEQ ELNM
 
 
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