ID A0A2N5SJ96_9BASI Unreviewed; 960 AA.
AC A0A2N5SJ96;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=PCANC_16697 {ECO:0000313|EMBL:PLW13315.1};
OS Puccinia coronata f. sp. avenae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW13315.1, ECO:0000313|Proteomes:UP000235388};
RN [1] {ECO:0000313|EMBL:PLW13315.1, ECO:0000313|Proteomes:UP000235388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12NC29 {ECO:0000313|EMBL:PLW13315.1};
RA Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL Submitted (NOV-2017) 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:PLW13315.1}.
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DR EMBL; PGCJ01000953; PLW13315.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5SJ96; -.
DR STRING; 200324.A0A2N5SJ96; -.
DR Proteomes; UP000235388; 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:UP000235388};
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 375..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 419..449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 502..522
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 560..582
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 602..621
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 628..647
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 160..353
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 960 AA; 105907 MW; E34EA3FB0D8B5F6D CRC64;
MKPTQKPKRL PKSVQTNSFT SLLSILLTFL LVSAISTYLR YALPTPKGLP TRTGLLRMRN
QTGAATSRQE VLVDDQEFSE TLANEYIDHL AGTIGYRIVG TEEMAESLEY LNHVLRDLKT
QAEQLGSNKQ FEILTQVDDG AHLFEFIGKK VWKKYFQLSN VIVRLSDPSI PSSRENAVLV
NAHLDSTLPS PGAADDVAGV AVMLEAIRII TQSPDWPMHN GIVFLFNGAE ESLQDASHMF
ITKHPLKDIV RAVINLEACG TAGQEILFQA TSTEMIEAYS KVPRPFGSVI ASEVFRTGLI
ASDTDFRQFV QYGNLTGLDM AIMQNSYLYH SSQDIPSKIE PGAVQHMGEN TMALLKHLTS
SAADLTHIKP ASTTVFFSGL GGLIFIMYSK TTALRVYTSL FVAGMTLITR NVKSKHYSIY
FFGFLAAIGS LLGFVIGSNV VAFIMSIVLG KPLSWYRYES FPILLFGPPA LAGGLSVQHL
FSKLTHKSNR LRSGNDDHVL SHATLSGLIA LNGITSVLGA YFNIGAAYLP AIGLVSMLLS
LMINDFILAP ITGKRGHLHL PMYLAALVLP GFLGVEGLLA FLDLFVPMTG RMGHEVHVDF
MIASLVSAVG FNIVSISLPL AHRFSRRALG QFLVGLLIFS SLVGFWFTRP EWNIFDSDHP
KRLPILHMEN LTSSSPSFDL HIASMDRAPG FENLVQHLMD TLSLSHQSPI LSAINDDIPD
WDIIYPVSQF LKSYQVPLGL IEQQSLAAGH DGDVGTKNKY LSPWTDKFKV TSLESKLDFI
NQQRTIVLAI DHPGIIWTVI AFTADVVHWD LPSRAVRGKR RHHVKEASGF GVDRWTLNVT
IALEEAEFQS AVENEQILKG QRVPIAADDQ QGQAFARLGK LKVEFSGIDQ LGLYPARSKP
KRLTYRPSEP LPNPDQNTHL GWIGKGNGGP GLRLFDKLYP LLPDWVDPFL LSAVSNTGFI
//
