ID A0A093V5V2_TALMA Unreviewed; 955 AA.
AC A0A093V5V2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Probable Xaa-Pro aminopeptidase PEPP {ECO:0000256|ARBA:ARBA00039424};
DE EC=3.4.11.9 {ECO:0000256|ARBA:ARBA00012574};
DE AltName: Full=Aminoacylproline aminopeptidase {ECO:0000256|ARBA:ARBA00030849};
DE AltName: Full=Probable Xaa-Pro aminopeptidase pepP {ECO:0000256|ARBA:ARBA00039164};
DE AltName: Full=Prolidase {ECO:0000256|ARBA:ARBA00032413};
GN ORFNames=GQ26_0152250 {ECO:0000313|EMBL:KFX47520.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX47520.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX47520.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX47520.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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}.
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:KFX47520.1}.
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DR EMBL; JPOX01000015; KFX47520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093V5V2; -.
DR eggNOG; KOG2737; Eukaryota.
DR HOGENOM; CLU_309266_0_0_1; -.
DR Proteomes; UP000029285; Unassembled WGS sequence.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01087; Prolidase; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR InterPro; IPR007865; Aminopep_P_N.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR PANTHER; PTHR43226; XAA-PRO AMINOPEPTIDASE 3; 1.
DR PANTHER; PTHR43226:SF1; XAA-PRO DIPEPTIDASE; 1.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SMART; SM01011; AMP_N; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:KFX47520.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 502..637
FT /note="Aminopeptidase P N-terminal"
FT /evidence="ECO:0000259|SMART:SM01011"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..323
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 955 AA; 105862 MW; 8D6DABD3796DF295 CRC64;
MPRPPARRAR TVRQAPEKGS IKAVGRKPNT TEDESQANIA TPRRGRDERN NDTQVGADLT
PTRDLNENVI ASSPAENTTT TSIRPPTRAR GYSSTLSLVG RKGDFNSRIG STPGFESSIL
SNFKKRSRQP SLLQMMQADD EDSSDFDDDD FLGGFSPQDE STPLNVARVS NAAERQLAVS
PSRPPLGVAS PSSTESRKRK RQSATVNDEH VEQASPLSRS SSVSTLTPAP ESPIAGMSDE
LPSFTMATPM SSSTASPVRL MTVERQTATT TTDKNETAPP LPKVTTLSLQ TRFLPQRRTR
RRQQADDSDD EEDIDPANED SDEDELAREV RKRPQRSRRK GLSTASSEKT NAKLGKPSRR
GKKNLATGKA VDTQGNKSQR TYSRQAADKE NNYLSDDSSV LSSPPPSEDL NDSELDLPSH
ASKKRVDNRE LQATALKFAE VDQWEMEFED VSYTESTDAT LNLLYFSNVN AFRKLFFFSW
SVIVLEIRVN MTSTDGILAG KYPAKAHARR VVEYLRQNGF QGDGVLYLEA QKTRMIEDND
SEQPFRQRRF FFYLSGCLLP DAHLTYHIST DKLTLFIPPL DPESVIWSGL PLSPAQAKEL
YDVDEVLYTT DVNPTLAHLA SKVGFVFAID GQISDDVSLK SFPDTDKVAL KTAIEECRAV
KDAYEVAMIR KANDVTSQAH VAVLKAAKSA TNERELEAAF IGTCIAQGCR EMAYHPIVAS
GTSSATLHYV NNDEPLIDSS TNKKKLNLLL DAAGEYKAYC ADVTRTFPLS GKFSPESREI
YDIVLEMQTE SLAMLKEGVL WEDVHITAHR VAIKGLLKLG ILRGSEEELL EKRVSVAFFP
HGLGHYLGMD THDTGGHANY ADKDKMFQYL RVRGKLPAGS VITVEPGVYF CRFIIEPYLK
DSELSKYIDA DVLEKYWEVG GVRIEDNIHI TKEGHENLTT APKTADQVEL MINGS
//
