ID   MAS5_SCHPO              Reviewed;         407 AA.
AC   O74752;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   18-APR-2012, entry version 75.
DE   RecName: Full=Mitochondrial protein import protein mas5;
DE   Flags: Precursor;
GN   ORFNames=SPBC1734.11;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Probably involved in mitochondrial protein import (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- SIMILARITY: Contains 1 CR-type zinc finger.
CC   -!- SIMILARITY: Contains 1 J domain.
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DR   EMBL; CU329671; CAA21305.1; -; Genomic_DNA.
DR   PIR; T39658; T39658.
DR   RefSeq; NP_595428.1; NM_001021336.1.
DR   HSSP; Q80TN4; 2CUG.
DR   ProteinModelPortal; O74752; -.
DR   SMR; O74752; 3-68, 104-331.
DR   IntAct; O74752; 1.
DR   STRING; O74752; -.
DR   EnsemblFungi; SPBC1734.11.1; SPBC1734.11.1:pep; SPBC1734.11.
DR   GeneID; 2539671; -.
DR   KEGG; spo:SPBC1734.11; -.
DR   PomBase; SPBC1734.11; -.
DR   eggNOG; COG0484; -.
DR   HOGENOM; HBG635315; -.
DR   KO; K09503; -.
DR   OMA; ETIRDED; -.
DR   OrthoDB; EOG473T10; -.
DR   NextBio; 20800825; -.
DR   ArrayExpress; O74752; -.
DR   GO; GO:0005829; C:cytosol; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:PomBase.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0009408; P:response to heat; IEA:InterPro.
DR   Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1.
DR   Gene3D; G3DSA:2.10.230.10; HSP_DnaJ_cys-rich; 1.
DR   InterPro; IPR012724; DnaJ.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_N.
DR   InterPro; IPR018253; Heat_shock_DnaJ_CS.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR003095; Hsp_DnaJ.
DR   InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; DnaJ_N; 1.
DR   SUPFAM; SSF49493; HSP40_DnaJ_pep; 2.
DR   SUPFAM; SSF57938; HSP_DnaJ_cys-rich; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51188; ZF_CR; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Complete proteome; Cytoplasm; Lipoprotein; Metal-binding;
KW   Methylation; Nucleus; Prenylation; Protein transport;
KW   Reference proteome; Repeat; Transport; Zinc; Zinc-finger.
FT   CHAIN         1    404       Mitochondrial protein import protein
FT                                mas5.
FT                                /FTId=PRO_0000314107.
FT   PROPEP      405    407       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000396683.
FT   DOMAIN        6     68       J.
FT   REPEAT      137    144       CXXCXGXG motif.
FT   REPEAT      153    160       CXXCXGXG motif.
FT   REPEAT      179    186       CXXCXGXG motif.
FT   REPEAT      195    202       CXXCXGXG motif.
FT   ZN_FING     124    207       CR-type.
FT   REGION      129    131       Substrate binding (By similarity).
FT   REGION      209    210       Substrate binding (By similarity).
FT   REGION      241    243       Substrate binding (By similarity).
FT   COMPBIAS     68    107       Gly-rich.
FT   METAL       137    137       Zinc 1 (By similarity).
FT   METAL       140    140       Zinc 1 (By similarity).
FT   METAL       153    153       Zinc 2 (By similarity).
FT   METAL       156    156       Zinc 2 (By similarity).
FT   METAL       179    179       Zinc 2 (By similarity).
FT   METAL       182    182       Zinc 2 (By similarity).
FT   METAL       195    195       Zinc 1 (By similarity).
FT   METAL       198    198       Zinc 1 (By similarity).
FT   BINDING     110    110       Substrate; via amide nitrogen (By
FT                                similarity).
FT   SITE        329    329       Involved in dimerization (By similarity).
FT   MOD_RES     404    404       Cysteine methyl ester (By similarity).
FT   LIPID       404    404       S-farnesyl cysteine (By similarity).
SQ   SEQUENCE   407 AA;  44821 MW;  3A76A614B7369426 CRC64;
     MVKETKLYEV LNVDVTASQA ELKKAYRKLA LKYHPDKNPN AGDKFKEISR AYEILADEEK
     RATYDRFGEE GLQGGGADGG MSADDLFASF FGGGMFGGGM PRGPRKGKDL VHTIKVTLED
     LYRGKTTKLA LQKKVICPKC SGRGGKEGSV KSCASCNGSG VKFITRAMGP MIQRMQMTCP
     DCNGAGETIR DEDRCKECDG AKVISQRKIL TVHVEKGMHN GQKIVFKEEG EQAPGIIPGD
     VIFVIDQKEH PRFKRSGDHL FYEAHVDLLT ALAGGQIVVE HLDDRWLTIP IIPGECIRPN
     ELKVLPGQGM LSQRHHQPGN LYIRFHVDFP EPNFATPEQL ALLEKALPPR KIESAPKNAH
     TEECVLATVD PTEKVRIDNN VDPTTATSMD EDEDEEGGHP GVQCAQQ
//