YME1_SCHPO
ID YME1_SCHPO Reviewed; 709 AA.
AC O59824;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=ATP-dependent zinc metalloprotease YME1 homolog;
DE EC=3.4.24.-;
GN ORFNames=SPCC965.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX 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., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Putative ATP-dependent protease.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:16823372}; Single-pass membrane protein
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000305}.
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DR EMBL; CU329672; CAA19064.1; -; Genomic_DNA.
DR PIR; T41657; T41657.
DR RefSeq; NP_588514.1; NM_001023503.2.
DR AlphaFoldDB; O59824; -.
DR SMR; O59824; -.
DR STRING; 4896.SPCC965.04c.1; -.
DR MEROPS; M41.026; -.
DR MaxQB; O59824; -.
DR PaxDb; O59824; -.
DR PRIDE; O59824; -.
DR EnsemblFungi; SPCC965.04c.1; SPCC965.04c.1:pep; SPCC965.04c.
DR GeneID; 2538746; -.
DR KEGG; spo:SPCC965.04c; -.
DR PomBase; SPCC965.04c; -.
DR VEuPathDB; FungiDB:SPCC965.04c; -.
DR eggNOG; KOG0734; Eukaryota.
DR HOGENOM; CLU_000688_9_3_1; -.
DR InParanoid; O59824; -.
DR OMA; GFFTYIS; -.
DR PhylomeDB; O59824; -.
DR PRO; PR:O59824; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0031942; C:i-AAA complex; ISO:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; NAS:PomBase.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; ISO:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0035694; P:mitochondrial protein catabolic process; TAS:PomBase.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 1.20.58.760; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01458; FtsH; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR005936; FtsH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; SSF140990; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01241; FtsH_fam; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Mitochondrion; Nucleotide-binding; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..709
FT /note="ATP-dependent zinc metalloprotease YME1 homolog"
FT /id="PRO_0000317333"
FT TRANSMEM 217..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 152..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 531
FT /evidence="ECO:0000250"
FT BINDING 307..314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 530
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 534
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 608
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 709 AA; 78218 MW; 1C1A8DEA54FCAA36 CRC64;
MSRVLHPIFL FGKTSFLYSG CSKFGGRLFN NSIVHGWLRT RSYALASGLH PLRKQKLAHF
EDLANANMSD PYMQAKLYKE LADNFPEAII SRYETQGVAR NSACDRYYQE ALRKKSWSRS
LSNNISLSQS SSSPATSSFS DPKAFSAGVP KFTSDTSSTV SSTPSLNHSL QNSMPPSTPT
PPPVWAPTIV SSALGTSSKT PVYVVVDEPR FTKFFRIFKF IAGLSVASYF VLLGMSIFAE
TSGLNNIMTN TTEQEPMEER AINVRFSDVQ GVDEAKEELE EIVDFLRDPT HFTRLGGKLP
RGVLLTGPPG TGKTMLARAV AGEANVPFFF MSGSQFDEMY VGVGAKRVRE LFAAARKQAP
SIIFIDELDA IGQKRNARDA AHMRQTLNQL LVDLDGFSKN EDLAHPVVFI GATNFPESLD
PALTRPGRFD RHIHVPLPDV RGRLAILLQH TRHVPLGKDV DLSIIARGTS GFAGADLANL
INQAAVYASK NLSTAVSMRD LEWSKDRILM GAERKSAFIT PENKLMTAYH EGGHALVALF
TKNAMRPYKA TIMPRGSSLG MTISLPDMDK DSWTREEYLA MLDVTMGGRA AEELLYGKDK
ITSGAHNDID KATQVARRMV TEFGMSDRIG PVSLEAEMDN LSPATRALVE SEIKSLLEAS
YERSLSLLKS HKKELDALAT ALVDYEFLTA EEMNRVVKGD RDLLRNKLS
