ID A0A1L0GP25_9ASCO Unreviewed; 1007 AA.
AC A0A1L0GP25;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=SAMEA4029010_CIC11G00000004637 {ECO:0000313|EMBL:SGZ57861.1};
OS [Candida] intermedia.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=45354 {ECO:0000313|EMBL:SGZ57861.1, ECO:0000313|Proteomes:UP000182334};
RN [1] {ECO:0000313|EMBL:SGZ57861.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141442 {ECO:0000313|EMBL:SGZ57861.1};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Vacuole membrane
CC {ECO:0000256|ARBA:ARBA00004128}; Multi-pass membrane protein
CC {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; LT635762; SGZ57861.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L0GP25; -.
DR STRING; 45354.A0A1L0GP25; -.
DR OrthoDB; 277019at2759; -.
DR Proteomes; UP000182334; Chromosome vii.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 CDD; cd03875; M28_Fxna_like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR048024; Fxna-like_M28_dom.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147:SF26; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1; 1.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361240};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU361240};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW Reference proteome {ECO:0000313|Proteomes:UP000182334};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Vacuole {ECO:0000256|ARBA:ARBA00022554};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT TRANSMEM 57..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 391..424
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 476..499
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 511..530
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 630..657
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 669..690
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 697..717
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 168..357
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1007 AA; 112711 MW; 1D8920DF3FBCA6AD CRC64;
MAPLSVSSAT PRTPENFDSP RSKPASRAPV SDYSPPLQPN WFIRLIRAVF GYRKTSLTFL
VAIVLFATVI LSSIDNSLSF TVSLPTDALE SSVLDSLWDS LQKIALVEHT YNSEGNDYVH
DLLEEKIAAL VANKKYIEYD NDLNGTNNIM TSVNYLSYAS VSYYESNNLL VRVNGSDASL
PAFLVSAHYD SVPSSYGVTD DGMGVASMLG LLEYFADKST KRPLRTVIFN FNNNEEFGLY
GATAFLHHPW FQQIKYFLNL EGTGAGGKAI LFRGTDYGIV KHFSKVRFPY ATSLFQQGFN
NKLIHSETDY AIYKSMGKLR GLDLAFYKPR DIYHTGADNI KNTNKKSLWH MLSNTIDFTQ
FIAYEKIDLD EEYMGGEAAN SSNDYAAYLS FFNYFVAFSL SQVVIVNIVL LVVSPILSLL
LLVLIFQYKK GWGVNFINVI KFPISFVLSV IILSFITDVL IVPTNLYLVN SSPGTLVSTL
FALFLFLNYA FLNGLNFIFK PFKGHQHDEK LIVIIEASFI TWVILLWSTV KQSHNKIGDD
HTGEFILTVL FVLQSAAALF GLFGWSLKSP RRIALSEGES QPLIGSSSQH RYHSHSDDED
SIAESSSLSL QSGFSEGCSV HEKKSFSYDW LLQFLLIVPL SSLIIYNSGF LVLAGINKSI
QESLEAQDFI YKIIQAFVIV WAIPFLPFIF KLNRVFVLAL LIALIQGGLV ISTKSAFDVE
NPLKLRFLET IDLNANPFTN TVSVSGRLMK LIENILEDIP SFKDNKAELL TSSLGDGMLL
YSYGSQLTPD FIPGNSIQDY LTIEVLRNSS SGSDSPFGLL TGEIEIIAPK NRNCKVSFNV
TDKVIKIFDG VESSSSTHSP VKTVIVYKDE KKGNGSDVEL YNTAGIPEGF SRDHDGNYLF
KDFEGIGQLQ LNKLDWDKKY HIAFQWVPEV VESDFSVDSD VEAQKINVKQ LGVNVECYWS
GLSDVDEFIA ESEQIPAYKE LLHYSPNYVK WANRDRGLVS VTKYAEI
//