ID A0A135LTZ7_PENPA Unreviewed; 790 AA.
AC A0A135LTZ7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Peptidase M3A/M3B {ECO:0000313|EMBL:KXG52432.1};
GN ORFNames=PGRI_087160 {ECO:0000313|EMBL:KXG52432.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG52432.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG52432.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG52432.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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:KXG52432.1}.
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DR EMBL; LHQR01000026; KXG52432.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135LTZ7; -.
DR STRING; 5078.A0A135LTZ7; -.
DR OMA; KNFQSAM; -.
DR OrthoDB; 735202at2759; -.
DR Proteomes; UP000070168; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06455; M3A_TOP; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR024080; Neurolysin/TOP_N.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11804:SF84; SACCHAROLYSIN; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000070168};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 296..788
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 790 AA; 89559 MW; ECEBCFCDEB3CE5DA CRC64;
MSFGSPDKFI SPSVPSFPFK RRIPPIITLT SRVHLVAALL AILIVAPFLR IPARLSSALG
HLRTNVSIRS LTTSSMAPAH LRKPPQAPPI FTATPQSVVA DAERLIKSSR AIQDKVVAEI
KPEAATFDNV VRPLAQDDNE MGLESHILGF YQAVSTDSKL RDASSKAEEL MDEFFIEAVM
REDVFTLFDA VLRRNESLDP ESRRLLEKEH KDFVRNGLGL PAGPQRLRFK EIKKRLSQLS
IEFQKNLNEE NGGIWFTPEQ LAGVPKDVLD GLKKGEGENA GKLWLSFKYP DLFPTMKYAI
DPEIRRQVMI ANENKCNQNV PLFRETIILR DEAARLIGYP NHAAFRIEDK MAKTPETVNK
FLGDLRDRLT AGGKKETQKL LDLKNATDPK ADGRYYLWDH RFYDRLMLEK DYSLDQQLIA
EWFPLQTTIE GMLKIFEELF GLEFVEIVGE DRAAIAPTGQ GNDIVWHEDV QVYSVWNDEG
EGSGFVGYLY LDLFPREGKY GHAANFNLQP GFIGKDGNRR FPATALVCNF TKPQPKKPSL
LKHDEVVTLF HELGHGIHDL VSRTIYSRFH GTSTVRDFVE APSQMLENWC WTPSQLRSLS
RHYSTLSPEY LASWQEAQDG EKAKTQPSER IPDDVIENLI RTKHVNDSLF NLRQLHFGIF
DMTVHEPKTH ADIEALPLSA TYNRLRQEIT QMDGPEALGA GSEWGHGEAT FGHLIGGYDA
GYYGYLSSQV YSTDMFYTVF KDDPMNKAAG RRYRYQVLEK GGSQDEMKTL TEFLGREPQT
DAFYKDLGLA
//