ID A0A1V8UI47_9PEZI Unreviewed; 495 AA.
AC A0A1V8UI47;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=B0A51_09848 {ECO:0000313|EMBL:OQO22742.1}, B0A51_09983
GN {ECO:0000313|EMBL:OQO23276.1};
OS Rachicladosporium sp. CCFEE 5018.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO23276.1, ECO:0000313|Proteomes:UP000192386};
RN [1] {ECO:0000313|EMBL:OQO23276.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCFEE 5018 {ECO:0000313|EMBL:OQO23276.1};
RX PubMed=28684563;
RA Coleine C., Masonjones S., Selbmann L., Zucconi L., Onofri S., Pacelli C.,
RA Stajich J.E.;
RT "Draft Genome Sequences of the Antarctic Endolithic Fungi Rachicladosporium
RT antarcticum CCFEE 5527 and Rachicladosporium sp. CCFEE 5018.";
RL Genome Announc. 5:e00397-17(2017).
RN [2] {ECO:0000313|Proteomes:UP000192386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:OQO23276.1}.
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DR EMBL; NAEU01000453; OQO22742.1; -; Genomic_DNA.
DR EMBL; NAEU01000415; OQO23276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8UI47; -.
DR STRING; 1974281.A0A1V8UI47; -.
DR Proteomes; UP000192386; Unassembled WGS sequence.
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 Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR PANTHER; PTHR12147:SF55; PEPTIDE HYDROLASE; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU361240};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW Reference proteome {ECO:0000313|Proteomes:UP000192386};
KW Signal {ECO:0000256|RuleBase:RU361240};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT CHAIN 17..495
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5014484818"
FT DOMAIN 143..356
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 495 AA; 53919 MW; 1E6F0C620DBB786F CRC64;
MKISLAVSGL LATATATSWQ NLPGSNFMPG QPFGYAPEAS WPPTDNNGSQ LIPQAPDRQT
RNMIAQVDQK RLRRTVEKLV SFGTRHTLSQ QNSTTRGIGA ARDWLLREMQ GIAATSDGNV
DVFFNSYIQP VASRILFPVN ITNVVARING TTDPNRVYVV TGHYDSRRLD INDYTGDAPG
ADDDASGVAL VLEMARMCAK LRPAATMIFA AVAGEEQGLY GSNNLAGTLK NQSYNVEGNW
NNDIVGQGSF LPTTPINPHT IRLFGASLFY PNASSANLLQ TTALIGGEND SPARNLGRFI
AEVAAGAVQY LDMQVALIYR PDRFLRGGDH QSFLSKGFPA VRFTEAVEDY KHQHQDPRVQ
DGVVYGDNIE FVNFEYLQRV TRTNLATMWS AANAPAMPKN VTISQSVGVP ATFRNTSLAI
VNNLSKFNWN TGNDTLVASY ELVWRVSGAL QWSHYLNAGN VGTVTADLPK DDLQFGIRAV
GKDGKKSPAV FPLPL
//
