ID A0A1X2I8X6_9FUNG Unreviewed; 918 AA.
AC A0A1X2I8X6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=BCR42DRAFT_468958 {ECO:0000313|EMBL:ORZ11795.1};
OS Absidia repens.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ11795.1, ECO:0000313|Proteomes:UP000193560};
RN [1] {ECO:0000313|EMBL:ORZ11795.1, ECO:0000313|Proteomes:UP000193560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ11795.1,
RC ECO:0000313|Proteomes:UP000193560};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family.
CC {ECO:0000256|RuleBase:RU361240}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORZ11795.1}.
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DR EMBL; MCGE01000020; ORZ11795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2I8X6; -.
DR STRING; 90262.A0A1X2I8X6; -.
DR OrthoDB; 277019at2759; -.
DR Proteomes; UP000193560; Unassembled WGS sequence.
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:SF54; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1-RELATED; 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|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:UP000193560};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|RuleBase:RU361240}.
FT TRANSMEM 394..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 432..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 474..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 571..596
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 608..629
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 636..657
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 173..354
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 918 AA; 102628 MW; 0AA9F79CD0F9A015 CRC64;
MTFQGKDNTD FEPAYFSKLD NNLDRRSGAG WSWLRLIGYC ILAVMLSTHL HYKLPAPKTH
RGIDPKTGLV EFSERNAIDT ISYLSDTLGY RIVGTVEEAQ SADYLKNMIR EYKQTSATIP
GAPKFDVWIQ QETGSHRFDI MDHMVLKAYT NITNIIVRLS CPETNDMSAG RTCEDSAVLV
NSHFDTTLGS PGATDDGSGT AVMLDIIRVL SQRDWTGYKN SIVFLFNGAE ETLQDASHAF
ITMHDLKDSI KSVVNIDACG TTGREILFQA NSREMIEAYK QAPYPHGTVM ANDVFRTGLI
LSDTDFRQFV QYGNLTGIDM AIYKNSYLYH THLDITRHLE PGAMQHLGEN TLAIIDHLAK
NTSLDGMVRT SEIVFFDVHG IFFMVYSWAT AYKIQMSTVL IAYAFIGYII YKTSQSTPYR
PINVLALSYV RSTVSLWLSA IASLVLPTTV ALFLTSSMIH RHMAWFAHEW YGTLIFSPMG
LFGAYGVQYL FYSLPGPRHV DMEYGVFNSS VSAFAGVTFL TTLTGVASSY IFWVFTVVLL
SAAMINEFFL KSTLPDVKYR LPEPKVHLWT YAISTLPLTF IFSDNIYALI DIFVPLTGRM
GVDTPVDVII SVIFGAVAFF GCLPSMAHIH RFGKNYLAKV LTCVAIGQVA ILMSVIVSGG
TPGGWAFPYD EMHPKRLFIQ HLKNLTSGEA YIAVAEADKG PYINTVLDSL KTELNVDVEQ
RPGSEGMKDW DSVYPFSHFL GGYRLNTEPY IRAHSNNPKV SQAVSLANEF PGPFPTLTVH
NDTYNPVTGV RSFSIYSMAP SYTWTVISFH GLVVDWSIQN EEPLTYPSRY VVRHVTGFGN
DGWKLDLAVK VPESDRALAE VGQWKMQFEF TALEKEGFAG RGEERLIGGV GMLGVIQRIL
PVWTTTTWLS SAVQEWEL
//
