ID A0A0F2RVM2_9RHOB Unreviewed; 600 AA.
AC A0A0F2RVM2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=X-Pro aminopeptidase {ECO:0000313|EMBL:KJS42704.1};
GN ORFNames=VR71_13180 {ECO:0000313|EMBL:KJS42704.1};
OS Roseovarius sp. BRH_c41.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1629709 {ECO:0000313|EMBL:KJS42704.1, ECO:0000313|Proteomes:UP000033676};
RN [1] {ECO:0000313|EMBL:KJS42704.1, ECO:0000313|Proteomes:UP000033676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c41 {ECO:0000313|EMBL:KJS42704.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KJS42704.1}.
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DR EMBL; LADY01000045; KJS42704.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2RVM2; -.
DR PATRIC; fig|1629709.5.peg.4659; -.
DR Proteomes; UP000033676; 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 Aminopeptidase {ECO:0000313|EMBL:KJS42704.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590}; Protease {ECO:0000313|EMBL:KJS42704.1}.
FT DOMAIN 17..153
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 318..529
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT DOMAIN 542..598
FT /note="Peptidase M24 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16188"
SQ SEQUENCE 600 AA; 64886 MW; 1E00F7CEE9D7B680 CRC64;
MFQSFTETAR PDQGPPRLEA LRRAMADAGL EGWLVPRADA HQGEYVAACD DRLAWLTGFT
GSAGFCAALA DAAGVFTDGR YRVQVRAQVD TGHFTAVDWP ETRLGPWLKQ HLPEGGTVGF
DPWLYTPEQI EALTEALTGS AIHLTSHTNL IDAVWPDRPA PPQGAITPWP DSLAGASHAE
KRAALAETLR KAGQRSAVIT LTDSIAWLFN IRGCDIPRNP VAQGFAIIHD TGHATFFTDP
AKLDATARTH LGDAVTLAPP DAFETALAVL PGPVRLDRAN VPLRVVQVLD AAGVAHQWGA
DPCILPKARK TQAEITATRI AHLRDGAAMC EFLAWFDAQP PGTLTEIDVA RRLEACRAAT
GQLLDISFDT IAGSGPNGAL PHYRVSEASN RTLVDGDLLV LDSGGQYLDG TTDITRTLPV
GIPGADERAA FTRVLQGMIA ISRLRFPRGL AGRDLDAIAR YPLWLADQDY AHGTGHGVGV
YLCVHEGPQR LSRLSEVPLE PGMILSNEPG YYREGAFGIR IENLIVVTAL DPLPGGDRVT
QFGFETLTYT PLDTRLIDAD LLTKPERDWL NTYHTACRDK IGPLLSAPAR LWLDKVTQTS
//
