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Database: UniProt
Entry: S2JQI7_MUCC1
LinkDB: S2JQI7_MUCC1
Original site: S2JQI7_MUCC1 
ID   S2JQI7_MUCC1            Unreviewed;       836 AA.
AC   S2JQI7;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=HMPREF1544_08365 {ECO:0000313|EMBL:EPB84863.1};
OS   Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS   agent) (Calyptromyces circinelloides).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB84863.1, ECO:0000313|Proteomes:UP000014254};
RN   [1] {ECO:0000313|Proteomes:UP000014254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome sequence of Mucor circinelloides f. circinelloides 1006PhL.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in vacuolar sorting and osmoregulation.
CC       {ECO:0000256|ARBA:ARBA00003273}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000256|ARBA:ARBA00004128};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004128}.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family.
CC       {ECO:0000256|ARBA:ARBA00010918, ECO:0000256|RuleBase:RU361240}.
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DR   EMBL; KE124027; EPB84863.1; -; Genomic_DNA.
DR   AlphaFoldDB; S2JQI7; -.
DR   STRING; 1220926.S2JQI7; -.
DR   VEuPathDB; FungiDB:HMPREF1544_08365; -.
DR   eggNOG; KOG2194; Eukaryota.
DR   InParanoid; S2JQI7; -.
DR   OMA; SPLGNDM; -.
DR   OrthoDB; 277019at2759; -.
DR   Proteomes; UP000014254; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   PANTHER; PTHR12147:SF56; VACUOLAR MEMBRANE PROTEASE; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU361240};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU361240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014254};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Vacuole {ECO:0000256|ARBA:ARBA00022554};
KW   Zinc {ECO:0000256|RuleBase:RU361240}.
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        363..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        409..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        447..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        482..502
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        509..529
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        535..553
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        574..592
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        604..625
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          143..332
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   836 AA;  92901 MW;  0D6FB599F203DDD1 CRC64;
     MSADSDERTP LIRQNPSTSH SSKRLYHVYG MALGFLFLFA AFIHSFRTKL PAPLSDAQAR
     ELDDFSGIHA YNEYLSRFTA PHSANTRENG VMRDWLASVS YDMQKDATAR GLQMDVIGND
     TSEAVVPQDW FTDNEHWFIH SRNVIVRLNG TSGRDEALLI NAHYVDSVPT SNGVTDNGMG
     VVTALEMMRY FIEHPPRNTI IFLFNNFEEG GLLGCKTFIH HPWYASVKLF INLEGAGAGG
     RAMMFRSSNL NAVQKLAGSD AKLVHSSPLG NDMFKAQIIK SDTDYSVFTQ NGVPGLDIAF
     YAPRSHYHTP RDNLAHTTPD ALQYMGQMAL AAAKAIVNSD DMLDTNRDNE LFVYFDILGR
     WMFVYSFTTF QIINLIALLL VPSIGLFLGL KNKPSQQTAF SLVKQKLCLV AQGGIAVFSA
     LVFACLFVVV AVLAMCKINP SMTYGDVYGA GLYTFAAAFL GIQFSQLVLP NKLKQTLATT
     DAAWYGLLSF WSLFLVLAMY AGSKSIASLY FVVYLLAFNA LAALLQAVVP ATQKFRSPLI
     FFTQTIMPFI LLLEMEFLSM DALRHATADG TPEIAVYIFI ALPLVLIALH FVPWVHVACN
     YRKATIAAAV AFFFLFTICS ALQPFNGSWS PNKLVFKQEY NAGDALATVI VTSATGVQAT
     IKSSIPAHEY KTVECSSFNK HLTRCTYQTD LLPKYGGNDT LSEFVLSEVE KTCSETSCIS
     SATYASKNSL MCRVFFDPTQ NDYEAIQHVW VNGREHKASN ISSIITYINN YEQPVNVKVE
     YPKERSPKAT FSCFYDEWTE LEVPAFNAFR DSLPESATVL IRGQGIALVN YKNVTL
//
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