ID G3Y7B3_ASPNA Unreviewed; 1756 AA.
AC G3Y7B3;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 65.
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=ASPNIDRAFT_213466 {ECO:0000313|EMBL:EHA21208.1};
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA21208.1, ECO:0000313|Proteomes:UP000009038};
RN [1] {ECO:0000313|EMBL:EHA21208.1, ECO:0000313|Proteomes:UP000009038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
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:EHA21208.1}.
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DR EMBL; ACJE01000015; EHA21208.1; -; Genomic_DNA.
DR STRING; 380704.G3Y7B3; -.
DR MEROPS; M24.A10; -.
DR HOGENOM; CLU_002492_0_0_1; -.
DR Proteomes; UP000009038; Unassembled WGS sequence.
DR GO; GO:0000145; C:exocyst; IEA:InterPro.
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 GO; GO:0006904; P:vesicle docking involved in exocytosis; IEA:InterPro.
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 InterPro; IPR007191; Sec8_exocyst_N.
DR InterPro; IPR048630; Sec8_M.
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 Pfam; PF20652; Sec8_C; 1.
DR Pfam; PF04048; Sec8_N; 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 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 9..142
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 321..537
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT DOMAIN 550..587
FT /note="Peptidase M24 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16188"
FT DOMAIN 724..863
FT /note="Exocyst complex component Sec8 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04048"
FT DOMAIN 979..1228
FT /note="Exocyst complex component Sec8 middle helical
FT bundle"
FT /evidence="ECO:0000259|Pfam:PF20652"
FT REGION 613..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1756 AA; 194862 MW; D860F6B40254AD76 CRC64;
METVDTSERL TRLRQLMQER KVDVYIVPSE DSHQSEYIAP CDGRREFISG FSGSAGTAII
SMTKAALSTD GRYFNQASKQ LDSNWALLKR GVEGFPTWQE WTTEQAEGGK VVGVDPALVT
PAGARSLSET LKKNGSSLVG VEQNLVDLVW GKDRPAPPRE AVRVHPAQYA GKSFQEKISD
LRKELENKKA AGIVISMLDE IAWLFNLRGT DIPYNPVFFS YALITPTTVD LYVDEDKLTP
EVKAHLGQDV VIKPYDSIFA DAKALSEARK QDATGAAPKF LLSNKASWAL SLSLGGEEQV
EEVRSPIADA KAIKNDVELA GMRSCHVRDG AALIEYFAWL ENELINKKTT LDEVDAADKL
EQIRSKHDLY AGLSFDTISS TGPNGAVIHY KPEKGSCSII DPTAIYLCDS GAQYLDGTTD
VTRTFHFGNP TDLEKKAFTL VLKGLISIDT AVFPKGTSGF ALDALARQFL WKEGLDYLHG
TGHGIGSYLN VHEGPMGIGT RVQYTEVPIA AGNVISDEPG FYEDGKFGIR IENVIMAREV
QTTHKFGEKP WLGFEHVTTA PLGRNLINAT LLSEDELKWV NEYHAEVQFF GMSGRNPYAN
GYGYSDTSRY DRGDGGYGGS SNSLGMNGYG GGSAERERRP GGYGGFYPEP SSSSLSPGQS
PERRRERQER DGDHSSSRSR TRDGEADRRA LGSRDGRPRG DNSWLGSNSS GENVTGHAAG
PQAIEDVLQM VQREWDFVAS ENCVPVQVAL QLMDTSTLGK ADREPDFIRI NDKIQRTLKS
VVNEHHQGFN SSIGTYHKIQ SSIQSSQSRV RTLKISLEEA KSGLLSTKPE LKGLATSSQK
YDDIIQLFSQ IQEIQSLPER LESRISDKRF LAAVEVLHNA LRLLRRSELE NIGALADIRA
YFGNQEASLT DILIEELHDH LYLKSPYCSS RWKPPAADGE GNGAHPSSWT GTSSWERPVY
AFLGKLDAST PMVEDASRNP EADTFYYIQL LIEALNKMGH LDIAVDRIEQ RLPVELFAVV
DKTNAEIDAR YPNNTRGFAS QDSKSNLPTD IIEKRGHVLS EFLWTLYAKF EAIAEGHRVV
HDVIAAIVER EGIPKGSALA GGFKELWKLY QSEIRSLMHD YLATDGESSF RPRLEETETK
RQLYTGQRDK NKKMFKLSET DHTSEIQAEQ NELDEILRSS VPGLVTKSSQ KTAIIDASDA
RQGNSGTGHK ILIEPSVFNM SLLLPPSLSF IQRLKEIVPV DSDIAMSTLT SFLDDFLVNV
FLPQLDETVT DLCTLSFISP DAFTEDPHWS GVSPRPVFRG TVKFMSIIRE FSKMLSSIPH
DQAFTQLLLS QIVTYYDKCC GWYKAIVTKT SPRDNGEVRL KAAARHAESG DVHDIITELW
NGVTENKREL VDKETDILIS STNEVPLEPY DIISDPKTVV SLSLLFNSMQ WFASHLAQLR
QITQPASDTR QAESRPANRR WTLIGAMKPK CEGINQPVYL PLNQETATVF DTTLQSLRDF
ACTALFALHV DIRCGIIHML KRTMEGPKPR NTRSSEPTTP SPSSLASWWH ILSNQPTAAS
PTVLELNNDL IAFDTNISSY LGPSERWFIT SGLARFIDRT FVANTCHIGA MNENGALRLQ
LDVLVLQQNL KNIIIDPTDG VRKDDSSSPQ QNSEQIEVVA LPRSAKFLDW FLEGAEKALD
YAKDEKESFA AHGDQALAAG NGEPFTYDEL KVLIDLCFSD ILLGPRGAEN REEFMAAKKA
SADALLRLNE VMWDSK
//
