ID A0A0C9T4L9_PLICR Unreviewed; 873 AA.
AC A0A0C9T4L9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=PLICRDRAFT_180757 {ECO:0000313|EMBL:KII83063.1};
OS Plicaturopsis crispa FD-325 SS-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Amylocorticiales; Amylocorticiaceae; Plicaturopsis.
OX NCBI_TaxID=944288 {ECO:0000313|EMBL:KII83063.1, ECO:0000313|Proteomes:UP000053263};
RN [1] {ECO:0000313|EMBL:KII83063.1, ECO:0000313|Proteomes:UP000053263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-325 SS-3 {ECO:0000313|EMBL:KII83063.1,
RC ECO:0000313|Proteomes:UP000053263};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JUN-2014) 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}.
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DR EMBL; KN832585; KII83063.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9T4L9; -.
DR HOGENOM; CLU_015120_0_0_1; -.
DR OrthoDB; 277019at2759; -.
DR Proteomes; UP000053263; 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:UP000053263};
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 384..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 463..481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 488..507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 513..532
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 539..562
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 614..634
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 149..342
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 873 AA; 94483 MW; DADA805AEE12C4F6 CRC64;
MAVKRKQTSK LPSKGVWGPL RSLLALSPVL IGAPLLALKL HYALPVPFTE LYNPATNTPQ
ISETRILQHA QHLSETIGFR TVGTSEHAQA DAWMVQQAEE IKRQCEEAVA RSGGTRKLEC
EVWRQEGSGS HRFDMMSKRL YKTYVNLSNI VIRISAGTPE SKAHAVLVNA HLDSTLPSPG
AADDALSVGV MLECARVLVA REEWEPEYAI ILLFNHAEES LQDASHLYST QHPTRDTVRA
VINLEAAGTT GRELLFQATS EQMIQAYSHV PRPFGTVFAN DVFSSGVLLS DTDFRQFEQY
LNVTGLDMAV VGNSYLYHMR KDLVENIQPG VAQHMGENTL ALLEHLSSAA SPLPELTAGY
SRPTTVFFSH LGWFFVYSFA TARILYSALL AATLVFVYLS YADPAPALKK GVGRGVWSAQ
VRGAGAIVLG VLGAIVLPNV QAAVMQRVLG KGMSWFSSEV STIVLYGPTA LAGALASQLL
VSRLPEHVLL TSLLLLQAGA SAAIQLVGYG SAAMFFLTAA PLLASLVLDT LIRRKGQTVT
LWAYALGSLT PLLTGAQLMS TTLDVFVPLT GRIGADAPAD NVIATIVAIL CAHMFPLVLP
FAHRFPRAAL RRSVGVLGVA IVIVTAVFAA RSPFDAMHQK RLFVLHTENV TTHERHLHIS
TADGAPGYDA LVQDIARTFG RSDAPVHPIV MDDYNSDWDS LYPFSAFLTP YKIELPAIDG
AASPWSAGDK FTVTAENDVV DEAAGTRSLT LRIDHPGIIW TVIAFDAHVL KWTLDDNPPA
EYARHHIKEA SFYGIDTWSV DLVLQLPASG SPALAVNYVG VQEQGMWPAK KAEKEGGGQA
MALFEDFDAW LEEKTGGTVE PLLLGSIGGI AVV
//
