GenomeNet

Database: UniProt
Entry: G1XUQ2_ARTOA
LinkDB: G1XUQ2_ARTOA
Original site: G1XUQ2_ARTOA 
ID   G1XUQ2_ARTOA            Unreviewed;       609 AA.
AC   G1XUQ2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase P {ECO:0000256|ARBA:ARBA00020658};
DE   AltName: Full=Prolidase {ECO:0000256|ARBA:ARBA00032413};
GN   ORFNames=AOL_s00215g710 {ECO:0000313|EMBL:EGX43101.1};
OS   Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS   (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX   NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX43101.1, ECO:0000313|Proteomes:UP000008784};
RN   [1] {ECO:0000313|EMBL:EGX43101.1, ECO:0000313|Proteomes:UP000008784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC   {ECO:0000313|Proteomes:UP000008784};
RX   PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA   Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA   Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA   Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT   "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT   provide insights into nematode-trap formation.";
RL   PLoS Pathog. 7:E1002179-E1002179(2011).
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}.
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:EGX43101.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ADOT01000321; EGX43101.1; -; Genomic_DNA.
DR   RefSeq; XP_011128214.1; XM_011129912.1.
DR   AlphaFoldDB; G1XUQ2; -.
DR   STRING; 756982.G1XUQ2; -.
DR   MEROPS; M24.009; -.
DR   GeneID; 22899169; -.
DR   eggNOG; KOG2413; Eukaryota.
DR   HOGENOM; CLU_011781_2_3_1; -.
DR   InParanoid; G1XUQ2; -.
DR   OMA; EPGMILS; -.
DR   OrthoDB; 869at2759; -.
DR   Proteomes; UP000008784; 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:UP000008784}.
FT   DOMAIN          7..132
FT                   /note="Creatinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01321"
FT   DOMAIN          318..534
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
FT   DOMAIN          548..608
FT                   /note="Peptidase M24 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16188"
SQ   SEQUENCE   609 AA;  67677 MW;  E97215EF40BD81B9 CRC64;
     MVNTTERLAA LRALMKENGI DVYIVPSEDA HQSEYTSPCD GRREYISGFT GSAGWALITH
     DKAALSTDGR YFNQAEQQLD ENWTLLKQGM ADVPTWSEWV AAEATGGKNV GVDASLLTYA
     FSKSLKTKIQ KKGGGDLVGM TENLVDKVWG SERPARPAEP VIILDKKFAG KDFVEKIEDL
     RKELAKQKSH GLVLTGLDEI MWLFNIRGSD IPFNPVFFCY ATVTPTATTL FINPQQRSSE
     LEAHLGEHVQ LVAYDNVLTT LTALSEKTVD ENAAEPQKFL FPANASWALA QALGEGRLEE
     VRSPVTVAKA IKNETELEGM RQCHIRDGVA LIEYFAWLEE QLQSGVELDE VDAADKLEEY
     RKTKENFVGL SFGTISSTGA NAAVIHYHPE RPTAAKIDPN AIYLCDSGAQ FYDGTTDTTR
     TLHFGTPTPM EIKAYTLVLK GNIALGQAVF PKGISGYQLD PLARQFLWSE GLDYRHGTGH
     GVGSFLNVHE GPQGIGTRIQ YSEVPLELGN VISNEPGYYE DGKFGIRIEN IILVVPIKTN
     HQFGEKPYWG FETVTMVPMC RSLTDVSLLT EDEKKYLNEY HKEVFEKTSP LLSGDQRALK
     WLQRETAPY
//
DBGET integrated database retrieval system