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Database: UniProt
Entry: A0A0W8DYH2_PHYNI
LinkDB: A0A0W8DYH2_PHYNI
Original site: A0A0W8DYH2_PHYNI 
ID   A0A0W8DYH2_PHYNI        Unreviewed;      2046 AA.
AC   A0A0W8DYH2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Xaa-Pro aminopeptidase P {ECO:0000313|EMBL:KUG01431.1};
GN   ORFNames=AM587_10015550 {ECO:0000313|EMBL:KUG01431.1};
OS   Phytophthora nicotianae (Buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4790 {ECO:0000313|EMBL:KUG01431.1, ECO:0000313|Proteomes:UP000052943};
RN   [1] {ECO:0000313|EMBL:KUG01431.1, ECO:0000313|Proteomes:UP000052943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA   Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT   "Genomes and virulence difference between two physiological races of
RT   Phytophthora nicotianae.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M24B family.
CC       {ECO:0000256|ARBA:ARBA00008766}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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:KUG01431.1}.
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DR   EMBL; LNFO01000329; KUG01431.1; -; Genomic_DNA.
DR   STRING; 4790.A0A0W8DYH2; -.
DR   EnsemblProtists; KUG01431; KUG01431; AM587_10015550.
DR   OMA; CPATERS; -.
DR   Proteomes; UP000052943; Unassembled WGS sequence.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   CDD; cd01085; APP; 1.
DR   CDD; cd01831; Endoglucanase_E_like; 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   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR040794; CE2_N.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000587; Creatinase_N.
DR   InterPro; IPR037461; CtCE2-like_dom.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR033740; Pept_M24B.
DR   InterPro; IPR032416; Peptidase_M24_C.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR013830; SGNH_hydro.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR   PANTHER; PTHR43763:SF6; XAA-PRO AMINOPEPTIDASE 1; 1.
DR   Pfam; PF17996; CE2_N; 1.
DR   Pfam; PF01321; Creatinase_N; 1.
DR   Pfam; PF16189; Creatinase_N_2; 1.
DR   Pfam; PF13472; Lipase_GDSL_2; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   Pfam; PF16188; Peptidase_M24_C; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR   SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR   SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:KUG01431.1};
KW   Hydrolase {ECO:0000313|EMBL:KUG01431.1};
KW   Protease {ECO:0000313|EMBL:KUG01431.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   DOMAIN          1..125
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REPEAT          400..433
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          543..615
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          667..734
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          139..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          468..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          734..777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          945..983
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        753..773
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        945..973
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2046 AA;  227648 MW;  29F34B8E589D1D59 CRC64;
     MLVDPDMLRR ENLADELEQR FEIFVAPSNE RAFALLGLFQ VNFILLRLDI GNDQTASTSP
     ALAFLREMKR SCFRTPVAAL VDSSFNTDHE AQKLLARALQ QGGICGYFEQ GLAPDIMTQR
     IAKLLRSLTV AQNELTRCRG TATQSTQDEK SPSRKPQADN QAANKTRATP PGSATGSKRL
     PTTEVPNTRP SSVKFDRPGM LLELSLNQRK QCLRQRETLQ ANLASAPHSV LGVDIDVSST
     SPGRPDTPLT TCISPSFGST GRTTQVKKKI PPLPSPKQVS QLIYARPQEL QTRIDRHLYE
     RVHISGPPGP VPQDPLLNHC VVIDPRAQGR DLIVGKAYML YCEQRLDEAL LHCDRALRTP
     NSTLEKLARL LRGALYDARG EHVRAETEFL ACLQLDPSMH EAHFNLSVAR LKLGKDALAL
     EALTQALTLD PQNDKYLQNR GLMYRRMGQF VEAQDEYCKR EVASGTHTAS TGSTLTKRGT
     NSSSVSRSVL PTRGLSKCDL EDGLFAHLFG KPTPDKLALA CPSTERSLEM LSAIVARLQT
     LLFFQDFSHE MLFQVAQALD YDVVACGKSF VLGEAHSQNF YVLLGGRLSI RRRVGTTDFG
     STVTTHHLGT GSVFGCAGFT ISAQASLIAD ECAEIGILWP GDYAATIRAV TSQMNQDIFA
     FLQQLRGFRL LTTSELGHVV GISERKRFRK GDVLLEQNEQ PRHLIVLWKG SCSVFQDFDN
     APLSRRKLRR SANFDGWNED DEDDSDSDSS DSEGPGGSRR DQDEDDKGPP PFHRLIAKPD
     WPLGFQARTR ARKYRRGRRD GLMLSQTPPV VRSLSTAPPL TMSLPMRRLK DKLSSNDKNA
     LVQKCVAPAV FGESRFLDPT HSSSKCSVVA ESLVEVLLFD HMRLQEMDLQ SEVISELFDA
     APKYRSEKEV AQKQADVATW DEYRNLRILE LSKNRWPDAK AIRMHQEQME EEPPASSRGR
     WLARRRTSRL DSGGSRDDNS PPLTALASLL LSSHPPASMT ETRVLAISRG TSVGDDDEPT
     DTSPNVYKFD VAQYKDGSFR FVPACARDLI KYTGRLLHHG AQSARKTKIN TVQFDWPAVA
     FQISVRGTSS VAIRLKGDGN YFNVFVNNEL RCILRASLNA TCCDVAADLD AETEYTIRIC
     KRTEPQMRGA MSTFKVCTFY GFIVEEKAEV LPVDQPEPQP VRKMEFIGDS DTCGFGNEGK
     ASSAKNLFGM KGRMENVYNG YACITARMFD AEEHVLAWSG KGVHSNSADW GPNMPALWKS
     TLASRPGDWD MASWIPDVVV INLGINDLSP PASAETDIIT GYATFLLEVR SYRPDAHIFC
     VVYDDGCMSS EDSETNRKFV SLQLQEIIKV AISKVSKHDN KMHYAFIKVE EGLEKEDYAS
     MMHYAVSGHV KIAKVLAEEI ALRTGIVFEV NWIMLPAEKL RELRVLMSRT NVRLLPLRHL
     LGKTEKGAAS ELTGRPLQAF LVDTADAHQS EYVGDAHKRR EFLTGFTGSN GTALVTPDQA
     FMWTDGRYFL QAEQELSDDW TLMKSEEPGV PSIEQWTKKN LPNDSCLAID PYLTSVLAAR
     NFAKVLKETK IELVALHETE NLVDLVWEDR PAVAPSQVTF LSDEYTGRSV ADKLKSLREA
     VKDKGADAIV LTALDDIAWL FNIRGNDVEF NPVVTSYAVV TPDKATLFLD AANQDDVTQH
     LRPSGVECKP YSSMLKEVSA LTASNKDTKI LVDPAQCNVA VFLAIPAANR KEDTSVVMAQ
     KAIKSAVEIE GMRQAHLRDG AALVKYFSWL EKEMDAGNED QWDEVLVADK QEQFRSQAKD
     YVSLSFDTIS SIGANGSIIH YSPKRGECSK MSTSAMYLND SGAQYLDGTT DVTRTLHFGQ
     PTAYEKSCFT HVLKGHIALA STVFPDKMEG VKLDAITRAP LWKAGLDYRH GTGHGVGAFL
     NVHEKGVLMS FRLNPNGLKI QDGMVLSNEP GYYEDGKFGI RIESVMVVKK AHHIKSPLNR
     DFCEFETLTM APIQQKLIDA SFLTPEEIKW LNAYHKKVHD KLQPLLKDDP DTYAYLVRET
     KPLSLP
//
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