GenomeNet

Database: UniProt
Entry: A0A0A2I5Q6_PENEN
LinkDB: A0A0A2I5Q6_PENEN
Original site: A0A0A2I5Q6_PENEN 
ID   A0A0A2I5Q6_PENEN        Unreviewed;      1106 AA.
AC   A0A0A2I5Q6;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Peptidase M16, core {ECO:0000313|EMBL:KGO54565.1};
GN   ORFNames=PEX2_070980 {ECO:0000313|EMBL:KGO54565.1};
OS   Penicillium expansum (Blue mold rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO54565.1, ECO:0000313|Proteomes:UP000030143};
RN   [1] {ECO:0000313|EMBL:KGO54565.1, ECO:0000313|Proteomes:UP000030143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8 {ECO:0000313|EMBL:KGO54565.1,
RC   ECO:0000313|Proteomes:UP000030143};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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:KGO54565.1}.
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DR   EMBL; JQFZ01000221; KGO54565.1; -; Genomic_DNA.
DR   RefSeq; XP_016596936.1; XM_016744369.1.
DR   AlphaFoldDB; A0A0A2I5Q6; -.
DR   STRING; 27334.A0A0A2I5Q6; -.
DR   MEROPS; M16.008; -.
DR   GeneID; 27679789; -.
DR   HOGENOM; CLU_004639_1_2_1; -.
DR   OrthoDB; 129328at2759; -.
DR   PhylomeDB; A0A0A2I5Q6; -.
DR   Proteomes; UP000030143; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR032632; Peptidase_M16_M.
DR   PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   Pfam; PF16187; Peptidase_M16_M; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          33..203
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          230..408
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          414..702
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          709..886
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          113..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1106 AA;  125940 MW;  18566402D17BBEA0 CRC64;
     MAQIERITEN LEKPELDDRS YRVIRLPNKL EALLVHDPDT DKASAAVNVN VGNFSDEDDM
     PGMAHAVEHL LFMGTKKYPK ENAYNQYLAS HSGSSNAYTA ATETNYFFEV SATGDSSAPK
     SSGDSTPAET NDNNGVATNG NGSDGKSPLY GALDRFAQFF VAPLFLESTL ERELQAVDSE
     NKKNLQSDLW RLMQLNKSLS NPKHPYSHFS TGNLQTLKED PQKRGLEVRS EFIRFYEKHY
     SANRAKLVVL GRESLDTLEQ WVSELFSDVE NKNLAQNRWD DVQPFTEKDM CTQVFVKPVM
     DTRSMDMYFP FLDEEDLHDT QPSRYISHLI GHEGPGSVLS YLKAKGWANG LSAGAMPVCA
     GSAFFTISVR LTPEGLKQYQ EVANVVFEYI AMIKQRDPEQ WIFDEMKNLA EVDFRFKQKT
     PASRFTSRLS SVMQKSLPSE WLLSGSLLRR FDSDLIKKAL SYLRADNFRL VVVSQEFPGT
     WDQKEKWYGT EYKVEKIPQE FLGGLQKALE STEATRTSNV HMPHKNEFVP TRLSVEKKEV
     AEPTNTPKLI RHDDRVRLWF KKDDRFWVPK ATVEVTLRNP LVWATPANLI KTKLYSELVR
     DSLDEYSYDA ELAGLDYHLS ANILGLDISV SGYNDKMSAL LDKVLNTMRG LVVNQDRFHI
     IKERLTRAFR NAEYQQPYYQ VGDYTRYLLA ERSWVNEQYL EELEHVECDD VVNFFPQLLE
     QTHIEVLAHG NLYKEDALRM TDSIEKILGG RPLPPSQWYL RRNMTLPPGA NYVYPRSLKD
     PANVNHCIEY YLYIGLFSDD VLRSKLQLFA QLTDEPAFDQ LRSKEQLGYV VWSGARYNAT
     TLGYRVIIQS ERTAQYLESR IETFLRQFGP ILEKMPEEEF EGHKRSVVNK RLEKLKNLSS
     ETGRYWSHVG SEYFDFLQHE TDAANVRALT KADLIAFYQQ YIDPSSATRA KLAIHMNAQS
     GAQVEAPKPA EQRTRLVEVV TKHLEAAEFT VDSARFAKAL DEVDTTAADK SQVIFAMKNF
     LETETGLSQK KIEPVLETLD EKLSSQLKEL GLDSSSDTQG AANGNGEAQK AVVITDVPTF
     KARLPVSTGP VPVTDLSEYE DFDAKL
//
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