ID W9XDZ5_9EURO Unreviewed; 617 AA.
AC W9XDZ5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Probable Xaa-Pro aminopeptidase P {ECO:0000256|ARBA:ARBA00020658};
DE EC=3.4.11.9 {ECO:0000256|ARBA:ARBA00012574};
DE AltName: Full=Aminoacylproline aminopeptidase {ECO:0000256|ARBA:ARBA00030849};
DE AltName: Full=Prolidase {ECO:0000256|ARBA:ARBA00032413};
GN ORFNames=A1O5_00061 {ECO:0000313|EMBL:EXJ75555.1};
OS Cladophialophora psammophila CBS 110553.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ75555.1, ECO:0000313|Proteomes:UP000019471};
RN [1] {ECO:0000313|EMBL:EXJ75555.1, ECO:0000313|Proteomes:UP000019471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ75555.1,
RC ECO:0000313|Proteomes:UP000019471};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the removal of a penultimate prolyl residue from
CC the N-termini of peptides. {ECO:0000256|ARBA:ARBA00002443}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of any N-terminal amino acid, including proline, that
CC is linked to proline, even from a dipeptide or tripeptide.;
CC EC=3.4.11.9; Evidence={ECO:0000256|ARBA:ARBA00001424};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|ARBA:ARBA00008766, ECO:0000256|RuleBase:RU000590}.
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:EXJ75555.1}.
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DR EMBL; AMGX01000001; EXJ75555.1; -; Genomic_DNA.
DR RefSeq; XP_007738872.1; XM_007740682.1.
DR AlphaFoldDB; W9XDZ5; -.
DR STRING; 1182543.W9XDZ5; -.
DR GeneID; 19184799; -.
DR eggNOG; KOG2413; Eukaryota.
DR HOGENOM; CLU_011781_2_3_1; -.
DR OrthoDB; 869at2759; -.
DR Proteomes; UP000019471; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01085; APP; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR033740; Pept_M24B.
DR InterPro; IPR032416; Peptidase_M24_C.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR PANTHER; PTHR43763:SF6; XAA-PRO AMINOPEPTIDASE 1; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF16189; Creatinase_N_2; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF16188; Peptidase_M24_C; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:EXJ75555.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000019471}.
FT DOMAIN 9..144
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 326..541
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT DOMAIN 555..617
FT /note="Peptidase M24 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16188"
SQ SEQUENCE 617 AA; 68761 MW; BD0929D182933C00 CRC64;
MEKVDTTKRL SQLRDRMREH KLDVYIVPSE DSHQSEYIAP CDARRAYISG FTGSAGTAVI
TLEKAALSTD GRYFNQASKQ LDENWLLLKQ GMEDVPTWQE WTTEQAEGGK TVGVDPTVIT
ASDARKLSET LKKKSHATLV GVSENLVDNI WNDRPPRPAE RVIVLSEKYA GKPYQQKLDD
LRKELKKKKA VGMVVSMLDE VAWLFNLRGS DIPYNPVFFS YAAVTPNSAT LYIDSAKIGS
EVREHLEGAV EIKSYDDLFS DLTSIAETAA IEFQTNGVTK SHPNRLLLSN KSSWALYLGL
GGEDKVEESR SPIADAKAIK NPTELEGMRQ CHIRDGAALS EYFAWLEGEL HNGSWVDEVQ
AADKLEAIRS KGEHFVGLSF DTISATGPNA AVIHYSPERG NCSTIDVRAV YLCDSGAQYL
DGTTDTTRTL HFGTPSDMEI KAYTLVLKGV IALDRAVFPK GTTGFAIDAF ARQHLWREGL
DYRHGTGHGV GSYLNVHEGP IGIGTRAAYS EVSLSIGNVI SDEPGYYEDG NFGIRIENMI
MACEAKTNHK FGDKPWIGFE HVTMVPMCRK LIDPSLLDPE ERAWLNAYHE EVWEKTSGFF
DKDERTTKWL RRETAPI
//
