ID F2AXZ1_RHOBT Unreviewed; 762 AA.
AC F2AXZ1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:EGF25443.1};
GN ORFNames=RBWH47_04860 {ECO:0000313|EMBL:EGF25443.1};
OS Rhodopirellula baltica WH47.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=991778 {ECO:0000313|EMBL:EGF25443.1, ECO:0000313|Proteomes:UP000006222};
RN [1] {ECO:0000313|EMBL:EGF25443.1, ECO:0000313|Proteomes:UP000006222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH47 {ECO:0000313|EMBL:EGF25443.1,
RC ECO:0000313|Proteomes:UP000006222};
RX PubMed=23273849;
RA Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., Richter M.,
RA Achstetter T., Glockner F.O., Harder J.;
RT "Expression of sulfatases in Rhodopirellula baltica and the diversity of
RT sulfatases in the genus Rhodopirellula.";
RL Mar. Genomics 0:0-0(2012).
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:EGF25443.1}.
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DR EMBL; AFAR01000229; EGF25443.1; -; Genomic_DNA.
DR AlphaFoldDB; F2AXZ1; -.
DR PATRIC; fig|991778.3.peg.4863; -.
DR Proteomes; UP000006222; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05663; M28_like_PA_PDZ_associated; 1.
DR CDD; cd00989; PDZ_metalloprotease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147:SF26; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1; 1.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 4: Predicted;
KW Aminopeptidase {ECO:0000313|EMBL:EGF25443.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:EGF25443.1};
KW Protease {ECO:0000313|EMBL:EGF25443.1}.
FT DOMAIN 673..750
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 337..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 274..326
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 342..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 762 AA; 82882 MW; CC51B7657AD3FC88 CRC64;
MMTRRNTIRM FGNSLTQTIR QLGSLSRVTI ALLGVGIATH CFYAVETFAE DRASGSEAAS
KTEPDANPNQ VLLVADSIAK DLRYLTSEEL AGRSAVGPEI LKAADYIADR YRQMGLETRL
YGDSPMQPVE MATGSQPTSA EDNGLRWWST GEEPDEIQLD DQFMPLAIGA TRGDIEADIV
WVGYGIQAPD RGYDDYAAVK QSQDAKNADS KGSVEGKIVM MLRKEPGFAD PNSPFDGLKN
TRHAFFDTKI STAIDEGAVG VLFVNDPASV ELALKAVDNQ YAAEDRRLEA LLAQRNALPA
EATNLRSSLT EKIDQVQEML SNREREQARA NWGLLGSAEA GTRPRKGDEK ITDPETGKTA
RRPAIPVASI SREVADRLLK QMASITAADE ESKSDNKESR TLFANGLAAV EAAIDSDYKP
RTIDSPGLRG RLRVGLTNAT ATSPNVIGVL EGKGKLADET VVIGAHYDHV GMGGIGSLAP
GTIEIHNGAD DNASGTATML AVAERVISEL AVASEHRRIV FIAFTGEERG LLGSKYYCSQ
PRFPMSKTVT MLNMDMVGRL RDNELTVYGT GTSDGFESLI QGLNSDMEQT SRPFKLNLVS
TGYGPSDHAS FYEAGVPVLF FFTGLHSDYH RPSDDFEKLN LDGMTRITDI VSQAANRVAT
MEQRPSYTQT NKDFQIRRQL SVVLGIQLDP DTNAVAAVMD PSAAKEGGIQ VGDQLIKAGD
KTIQTINDLR DELRPKSPGD SLRLTIQRDG NEMELDVRLR AR
//
