AMPP2_PYRTT
ID AMPP2_PYRTT Reviewed; 926 AA.
AC E3RNJ5;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Probable Xaa-Pro aminopeptidase PTT_10145;
DE EC=3.4.11.9;
DE AltName: Full=Aminoacylproline aminopeptidase;
DE AltName: Full=Prolidase;
GN ORFNames=PTT_10145;
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1;
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
CC -!- FUNCTION: Catalyzes the removal of a penultimate prolyl residue from
CC the N-termini of peptides. {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR EMBL; GL534210; EFQ92700.1; -; Genomic_DNA.
DR RefSeq; XP_003299200.1; XM_003299152.1.
DR AlphaFoldDB; E3RNJ5; -.
DR SMR; E3RNJ5; -.
DR STRING; 861557.E3RNJ5; -.
DR EnsemblFungi; EFQ92700; EFQ92700; PTT_10145.
DR KEGG; pte:PTT_10145; -.
DR eggNOG; KOG2737; Eukaryota.
DR HOGENOM; CLU_017266_1_2_1; -.
DR OrthoDB; 352329at2759; -.
DR Proteomes; UP000001067; 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 Gene3D; 3.40.350.10; -; 1.
DR Gene3D; 3.90.230.10; -; 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 InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SMART; SM01011; AMP_N; 1.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW Protease; Reference proteome.
FT CHAIN 1..926
FT /note="Probable Xaa-Pro aminopeptidase PTT_10145"
FT /id="PRO_0000411850"
FT REGION 505..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..741
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 274
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 435
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 476
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 476
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 926 AA; 104628 MW; F4B46BD92342492C CRC64;
MEVLDATGLA ERLRWEDNDY WLHLEAETPF DKYPAKQHAR RVQAKLGIED GLIYLPGQPA
RNNEDSDMPA PFRQRRYFYY MSGCDEPDCH LMYDIRRDVL TLFIPRIKPE RVIWNGRGST
PAEALAKYDI DQVHHSQDLT YIIQNWAFKH QHTSIYILHP SSRIPGCDNL MPRIDSHSLQ
PAISLCRMIK DDHEIKRIRK ANDISSQAHR EVLANIHKYK NEAQVEGLFM DVCISQQAKQ
QAYDPIAASG PNAGTLHYDA NNEDLAGRQL MCLDAGCEYE LYASDITRTF PLSASWPSKE
AENIYNLVQR MQETCIERLE PGVRYLDLHI MAHQIAIDGL LRLGILCNGT REEIYKAGTS
RAFFPHGLGH HIGLEVHDVG QAELMSVRRG KPVYQQAPSL YPENFHDPVY DSETCHAPTD
PQSSHLEEGM VVTVEPGIYF SVYALQHFYL PSPIHSKFIN LEVLERYLPV GGVRIEDDLL
ITANGHENLT TAPKGEAMLD IIRQGNPGTT EILNPSPTPP RRMRSENRTP RLRAPGISKK
TLQPLLTPLA RAATLPTELR QQDDIDFEPI VGPSLFSGFS RAMTTEEKIQ QWKQKRDSVP
TAPSRPTKAK NLSPVCGENT ANVQHVYMST VSDLSSLSQS SVGSGSTSMC KNCGILVQTL
DRLRQNLSSS TQTSPKPMTV PTFESRQKSH TVEEKHREMV CTDSLLDKVS IGQSNRAIGP
EERRRKAQSD HHHHSRLKAA TGEVKSRFST RYTPAGVPPL MPSHDQYSIT RRPNPERMQP
VADTPIVPPR HLTYMTSTPQ QSTENPALAD LGLPRASAEI AAIRATKQAG QEKLDTQRTT
LDAFQDEGQR LVIRSRHRLI PQTSMPVLMS QNPYHHHSNR SHGREGNNAT NKRSMIDSQP
AERRTRPERP ERPARDYVPG DEFLTR
