ID A0A0J1EL75_RHOIS Unreviewed; 996 AA.
AC A0A0J1EL75;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=DUF5117 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=RISK_001505 {ECO:0000313|EMBL:KLU06294.1};
OS Rhodopirellula islandica.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=595434 {ECO:0000313|EMBL:KLU06294.1, ECO:0000313|Proteomes:UP000036367};
RN [1] {ECO:0000313|EMBL:KLU06294.1, ECO:0000313|Proteomes:UP000036367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24040 / K833 {ECO:0000313|Proteomes:UP000036367};
RA Kizina J., Richter M., Glockner F.O., Harder J.;
RT "Permanent draft genome of Rhodopirellula islandicus K833.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KLU06294.1}.
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DR EMBL; LECT01000015; KLU06294.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1EL75; -.
DR STRING; 595434.RISK_001505; -.
DR PATRIC; fig|595434.4.peg.1440; -.
DR Proteomes; UP000036367; Unassembled WGS sequence.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR CDD; cd04276; ZnMc_MMP_like_2; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR033413; DUF5117.
DR InterPro; IPR032534; EcxA_zinc-bd.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR034032; Zn_MMP-like_bac.
DR PANTHER; PTHR38478; PEPTIDASE M1A AND M12B; 1.
DR PANTHER; PTHR38478:SF1; ZINC DEPENDENT METALLOPROTEASE DOMAIN LIPOPROTEIN; 1.
DR Pfam; PF16313; DUF4953; 1.
DR Pfam; PF17148; DUF5117; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..996
FT /note="DUF5117 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005250151"
FT DOMAIN 88..256
FT /note="DUF5117"
FT /evidence="ECO:0000259|Pfam:PF17148"
FT DOMAIN 558..874
FT /note="EcxA zinc-binding"
FT /evidence="ECO:0000259|Pfam:PF16313"
FT REGION 486..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 996 AA; 111863 MW; A12A62A12EF8470C CRC64;
MATIAAVTVT YVGSALTSSA ADLPPFAKIS EGYEQLPVSD QQAKKGLFNV WQNEKEASVI
AELPKNFAGK KYFVALTLSS GDRYAGLQSG DWVVQWRRYN NRLALIAPNL DIRATGDAES
KASVKRLFTD RVLLDVPILA MGPNGGPVVD MDSLLIGNAT TFFGASVRLA NSRLFTVEAA
KVFPENVELA FEVVGRGGQL QTLHYSFSEV PSSSSGFKPR EADERVGFFV TSFSDLSQYQ
DDETKVRYIN RWHLEKRDPK LKLSPPKEPI RFYVEHTAPV RYRRWIKKGV DYWNKAFEKV
GIVDAIVIEY QDAVSKIHME KDPEDVRYNF VRWLNNDVGT AIGPSRVHPE TGQILDADII
LTDGWIRHFN FNYNDLMPKL AMEGVSAETL AWLGSHPSWD PRVRMGATES ANSLRAKYAL
EAQQPMAGYA MAQADPALLG DDEFDGLMGQ VSQKNGLCMA ASGRSMDLAF ARMNWGLALM
ADEEAEKKKE EEAKEKAEAE NVDKDAKADA DAKDEDKKDK EEESEEEESD GDKKDDEKKD
DEKEDSDKEK DELLDGIPEW FVGPLLADLV AHEVGHTLGL RHNFKASGLY TIDEINSEEL
KGKKTFTASV MDYCPINYRY EAGDVQGDYG MIDIGPYDFW AIEYGYTFED SKIKDILKRC
SEPELQYATD EDTSGPDPYA RRYDFGKDPL TFAEEQMRLV QLYRERLLEK FVKEGDSWAK
ARRGYELTLA IQTKSVSMMA NWIGGAFVNR DKKGDPGNRV PVEVVPAADQ RAALQYVIDT
SFRDESYGLT TEILERLGVD KWLDSGRGGM SNEATWPIHD RVLGMQASTL TLIMNPTTLR
RVYDNELRLP AETDALTLPE LLDTVSNAVW EELDQPCPED RNDRKPMISS LRRNLQREHI
QRLVDLILEE GQDTAAYHPI SNLARMQLRT LASRMDSTIE KCGKKMDAYS LAHLTECKER
IERALEAGYT FGGGKAGAPM LMMLMGQEPA STSNND
//