ID A0A4U0WVP0_9PEZI Unreviewed; 1031 AA.
AC A0A4U0WVP0;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Xaa-Pro aminopeptidase {ECO:0000256|ARBA:ARBA00012574};
DE EC=3.4.11.9 {ECO:0000256|ARBA:ARBA00012574};
DE AltName: Full=Aminoacylproline aminopeptidase {ECO:0000256|ARBA:ARBA00030849};
DE Flags: Fragment;
GN ORFNames=B0A49_04911 {ECO:0000313|EMBL:TKA67147.1};
OS Cryomyces minteri.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Cryomyces.
OX NCBI_TaxID=331657 {ECO:0000313|EMBL:TKA67147.1, ECO:0000313|Proteomes:UP000308768};
RN [1] {ECO:0000313|EMBL:TKA67147.1, ECO:0000313|Proteomes:UP000308768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5187 {ECO:0000313|EMBL:TKA67147.1,
RC ECO:0000313|Proteomes:UP000308768};
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 -!- 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:TKA67147.1}.
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DR EMBL; NAJN01000943; TKA67147.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U0WVP0; -.
DR STRING; 331657.A0A4U0WVP0; -.
DR Proteomes; UP000308768; 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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01087; Prolidase; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 2.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR Gene3D; 6.10.250.3410; DBF zinc finger; 1.
DR InterPro; IPR007865; Aminopep_P_N.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR013939; Regulatory_Dfp1/Him1.
DR InterPro; IPR006572; Znf_DBF.
DR InterPro; IPR038545; Znf_DBF_sf.
DR PANTHER; PTHR43226; XAA-PRO AMINOPEPTIDASE 3; 1.
DR PANTHER; PTHR43226:SF4; XAA-PRO AMINOPEPTIDASE 3; 1.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF08630; Dfp1_Him1_M; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF07535; zf-DBF; 1.
DR SMART; SM01011; AMP_N; 1.
DR SMART; SM00586; ZnF_DBF; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS51265; ZF_DBF4; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000308768};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00600}.
FT DOMAIN 979..1028
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 552..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:TKA67147.1"
SQ SEQUENCE 1031 AA; 115388 MW; 8EBBCDA08E3312C6 CRC64;
TPGISALEYH RRRSKLAQAL PKNSIAVIAA SDTKYRSGAV FYEFHQDPNF LYLTGFNEPE
ALAVIEKAGS DVEYKFHLFV RPKDPQAELW DGARSGLQAA QDVFNADEAR FVYDINRVHA
HLPDIVGSAR AVYTDLPGSL KSKSAFTRYF YGGSDAKPEG FAKILKDSRH FDTEKKMWNY
LEYGFRTQGC DSSAYVPVVA GGRHALSIHY VRNDDKLKDG DLVLVDAGGE YGGYITDITR
TWPVNGKFSD PQRDLYETIL KVQRSCVALC REDADVTLDK LHTIAENGLR QGLAQIGFDM
SGKALETLFP HHLGHYIGLD VHDSPGYPRT GRLRAGQCIT IEPGIYVPDD DRWPAHFRGT
GIRIEDSVCI QEESPLVLTT EAVKEVVDIE ALLAAAAGKR SRSYASDQRE HAYGQAPPAK
KHIIEIKDDE NSEPRPFARP NNTQDFERVF MKKTSNAPPT AFERKLAAVR DGNQARPMLP
EKEHRTIIAN SSETIRQWQR YYQKVFPQFV FYFESIPEEV RVKASRQIAM LGAKEEKFFS
KAVTHVVTTR TIPPEIHTAS PADGQTTSSS ANASRGDNVG PKTINPSLLD RIADSRSQAA
EKKSSSLLDT TLQRRTHAVG QPHDFEVRRV QAGSGDILHK AREMGMKIWA LEKLQRMMTT
MFTDTGDQPH GHNTRSNSTA TLVPSREREA DLQQLLKNEK LNGPADRDMA VLTSDMVQFR
GYYVYVHDMD EQTRPVMGRD YPKPANKENG KWPQLRLTPA GRCPFVEDQA HTRKLQNQLR
EQDAKKAKEG SSAAAAPRTR TRAAAAVAAT KTENPVLGEI QSNARRGLRD VAYERDAKPS
KPLDPPLVIP AKRGNPSDSN SVPSLFGSAQ ANLRTMPRMI GVSSTAISST APGARVGTSK
DIQQLKRKVL EKNSVPSNNS IPSSYMNDMR AAINGDRAPP PRAAKRKAQE TLGFIREEED
GQRPSKRSVI TRKKKVDEKE LKPGYCENCR DKFEDFSEHI MSRKHRKFAL TPDNWKELDE
LLVQLDRPRK D
//
