ID K5VEH3_PHACS Unreviewed; 678 AA.
AC K5VEH3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Peptidase M3A/M3B catalytic domain-containing protein {ECO:0000259|Pfam:PF01432};
GN ORFNames=PHACADRAFT_265095 {ECO:0000313|EMBL:EKM49553.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM49553.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM49553.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM49553.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
CC -!- FUNCTION: Cleaves proteins, imported into the mitochondrion, to their
CC mature size. While most mitochondrial precursor proteins are processed
CC to the mature form in one step by mitochondrial processing peptidase
CC (MPP), the sequential cleavage by MIP of an octapeptide after initial
CC processing by MPP is a required step for a subgroup of nuclear-encoded
CC precursor proteins destined for the matrix or the inner membrane.
CC {ECO:0000256|ARBA:ARBA00025208}.
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}.
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DR EMBL; JH930480; EKM49553.1; -; Genomic_DNA.
DR RefSeq; XP_007401620.1; XM_007401558.1.
DR AlphaFoldDB; K5VEH3; -.
DR STRING; 650164.K5VEH3; -.
DR GeneID; 18919012; -.
DR KEGG; pco:PHACADRAFT_265095; -.
DR HOGENOM; CLU_001805_1_2_1; -.
DR InParanoid; K5VEH3; -.
DR OrthoDB; 735202at2759; -.
DR Proteomes; UP000008370; 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:UP000008370};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 222..669
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 678 AA; 77514 MW; 7462EC35D28BB01B CRC64;
MASLTPPQPA PSWTHSPEDV RRIAKELIDN DRKLMDKISS LPPEECTFDS VRDLLALARS
EADFEHVMEP LAFYQNVSPS KDLRDASNEA EAMARDYGVE MSMRLDLFQA KQAAQENIKK
SGQKLTPEEE RLVEKMILDG TRAGLALPEE KRTELTTLKK ELSATSLEFS KNFNEEKGTI
AFTLEDLKGV PADVVSGYSK RTEDGKDLYD VTFKTPDIFP VLKFAENPTI RQRAFEAYES
RLSINVPVLD KILGLRRKIA DLLNYSTWAD YVTEVKMAKN AKTVKEFLAD LEQKLRPVAL
KEREILLALK QEEHKKKGLE FDGEFNIWDY RYYDRKYVEK SLDLDDMLVK EYFPVTVVVP
AILEIYQNLL GVKFVEVKGE TWHPEVQQFA VWEKDAKDES GFVGWCYLDL FPRESKYSHA
AVWGLLSGYK REDGSRSYPL TAMVANLAKP TPSKPALMRH DDVTTFFHEM GHVFHGLLSK
TRFARFHGTS VARDFVEAPS QMLENWCWEP RVLERMSSHF DTKKPLPADL IEKIVKSRYV
NVGLFYLRQL FFANFDLKVH IDKEADDYTE LWNTMREKIS LVSAGKPTPG QGSFGHIAGG
YDAGYYGYTY SLVFAADMYA TVFKGDPLDP ARGQRYREHI LRPGGSQDDL VSLKNFLGRE
PNSEAFIKEL FGDNKSSL
//
