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Database: UniProt
Entry: A0A2U9BPB4_SCOMX
LinkDB: A0A2U9BPB4_SCOMX
Original site: A0A2U9BPB4_SCOMX 
ID   A0A2U9BPB4_SCOMX        Unreviewed;      1073 AA.
AC   A0A2U9BPB4;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 9.
DE   SubName: Full=Putative xaa-Pro aminopeptidase 1 isoform 2 {ECO:0000313|EMBL:AWP05977.1};
GN   ORFNames=SMAX5B_007515 {ECO:0000313|EMBL:AWP05977.1};
OS   Scophthalmus maximus (Turbot) (Psetta maxima).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC   Scophthalmus.
OX   NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP05977.1, ECO:0000313|Proteomes:UP000246464};
RN   [1] {ECO:0000313|EMBL:AWP05977.1, ECO:0000313|Proteomes:UP000246464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Martinez P.;
RT   "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT   evaluation of genetic and physical mapping variation across individuals.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP026250; AWP05977.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U9BPB4; -.
DR   Proteomes; UP000246464; Chromosome 8.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2.
DR   Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 3.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR000587; Creatinase_N.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
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; PF00080; Sod_Cu; 1.
DR   SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 3.
PE   4: Predicted;
KW   Aminopeptidase {ECO:0000313|EMBL:AWP05977.1};
KW   Hydrolase {ECO:0000313|EMBL:AWP05977.1};
KW   Protease {ECO:0000313|EMBL:AWP05977.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000246464}.
FT   DOMAIN          349..469
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
FT   DOMAIN          745..862
FT                   /note="Creatinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01321"
SQ   SEQUENCE   1073 AA;  117222 MW;  C9CF81EAAC5A1E3B CRC64;
     MGGVTGQVQF DSTFQTATVT ARFTGPIAGN VYIRLNKGET NPRLLADLVT IGQVNASQTN
     ITLLGSTSTA ASCDVLLGSL DASTLTNLGV VKVGTPLQPE KTRLDKTGLS NSPGFLLFHM
     GSSYKSPPPS QCSNDNVGGH WNPFEINTKD PTYPKVPGST HDNISYPGEV IVARARFQSP
     VIGEIWFTQL ENNPLSDVSI FMDLSYGNPT VTPSRHHMWH VHTYPISSER DDDGRCCSST
     NGHWNPFNIN TGDSSYALHC TPSSPLSCEV ADLSSKHSPI NLSPGVGGVE SKNFFTDVTS
     WLPGSGVIGR SVVIHQAEGG GPRIACANIT KVRIQKASLG NWFGPGMSSG QIRFSQAIPQ
     GPTTINVSLM NLNFFAGGYH VHILPIKPGS VEPCSDANIM GHFNPLAWNV SNSPKPGTGT
     VDQYEDGDIS GKFGMLNGLS QSEAIYMDPD MQLTGPNSIV GRSLVVHYAN GSRMRCADIS
     SERDTEGQWT IAKAVFNSKV TGTVQLRQQM FLDGSSSDII LEVTLQSSTR QETSEASLFI
     TNSRTGSQCN DVGDTYNPFN MTSADSRCSL ANPLSCMVGE ISARQGPVRL TGSQLYTDRI
     IQLSGDHTVV HRSLVLKSRD SIIACTDILP ESPAAEQTFP NVADFSRYDF RRKVANALQL
     EIARVTILPW SPISAAGGRC QQVNFMVSGD VSTELLQSVK TSEKMGIYKE SDSCANTAMS
     PKITGELLRQ LRQAMRNCKY FSDPIQAYIV PSGDAHQSEY IAPCDCRREY ICGFNGSAGT
     AIVTEQYAAM WTDGRYFLQA SQQMDNNWTL MKMGLKETPS QEDWLISILP ENSKVGVDPW
     IFAADQWKNM SKALSSAGHS LVVVQDNLID AVWTDRPKRP STRLRTLGLD YTGLSWQDKI
     TTLRAKMTER KISWFVATAL DEIAWLFNLR GADIEYNPVF FAYTIVGMNT IRLFVDTNRL
     ADPALRDHLQ LDSPSKPELS VQTFPYESVY AELQAVCAAL GPKDKVWICD KASCALTQAI
     PKAHRTPIPY TPLCLSKAVK NATEVQGMKM AHIKDAVALC ELFAWLEKEV LSL
//
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