ID A0A1Y2WHA5_9PEZI Unreviewed; 617 AA.
AC A0A1Y2WHA5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Probable Xaa-Pro aminopeptidase P {ECO:0000256|ARBA:ARBA00020658};
DE AltName: Full=Prolidase {ECO:0000256|ARBA:ARBA00032413};
GN ORFNames=M426DRAFT_317103 {ECO:0000313|EMBL:OTB08479.1};
OS Hypoxylon sp. CI-4A.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB08479.1, ECO:0000313|Proteomes:UP000242955};
RN [1] {ECO:0000313|EMBL:OTB08479.1, ECO:0000313|Proteomes:UP000242955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CI-4A {ECO:0000313|EMBL:OTB08479.1,
RC ECO:0000313|Proteomes:UP000242955};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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, ECO:0000256|RuleBase:RU000590}.
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DR EMBL; KZ111526; OTB08479.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2WHA5; -.
DR STRING; 1001833.A0A1Y2WHA5; -.
DR InParanoid; A0A1Y2WHA5; -.
DR OrthoDB; 869at2759; -.
DR Proteomes; UP000242955; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070006; F:metalloaminopeptidase activity; 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 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 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590};
KW Reference proteome {ECO:0000313|Proteomes:UP000242955}.
FT DOMAIN 9..133
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 325..544
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT DOMAIN 555..617
FT /note="Peptidase M24 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16188"
SQ SEQUENCE 617 AA; 68222 MW; 019987699AAD6B5E CRC64;
MEKVDTSERL AELRKLMSEN NVDVYIVPSE DSHASEYIAP SDARRAFISG FTGSAGCAVV
TLDKAALATD GRYFNQASHQ LDNNWELLKQ GLLDVPTWQE WSADQAADGK VVAVDPTLLT
SGAAKKLSDK IKKSGGKELA AVEDNLVDIV WGDSRPPLPN EPIIVLDEKF AGKDAKTKLI
ELRKELDKKK SLGFVVSMLD EIAWLFNLRG NDIPYNPVFF SYAIVTASEA TLYVESSKLS
AECQSYLQEN GVSIKPYKDI FVDASALRQS AQAEKTDESS DGRKFLISNK ASWALKRALG
GDSMVEEIRS PIGDAKAVKN ETELEGMRAC HIRDGAALIE FFAWLEDQLI AKKATIDEVE
AADKLESLRA KQKDFVGLSF PAISSTGPNA AVIHYKPERG SCSVVDPNAV YLCDSGAQYL
DGTTDTTRTL HFGKPTEAEI EAYTLVLKGN IALDRAVFPK GTTGFALDGL ARQYLWQYGL
DYRHGTGHGV GSYLNVHEGP IGIGTRVQYS EVSLSPGNVI SDEPGYYEDG AFGIRIENII
MVKEAKTKYK FGDKPYLGFE HVTMVPYCRK LIDSSRLSPE EKTWLNDYNA DIWNKTKGYF
EKDEVTTAWL KREIQPF
//