ID A0A1F6JRM3_9BACT Unreviewed; 1229 AA.
AC A0A1F6JRM3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Dockerin domain-containing protein {ECO:0000259|PROSITE:PS51766};
GN ORFNames=A3B44_02505 {ECO:0000313|EMBL:OGH37465.1};
OS Candidatus Levybacteria bacterium RIFCSPLOWO2_01_FULL_38_21.
OC Bacteria; Candidatus Levybacteria.
OX NCBI_TaxID=1798620 {ECO:0000313|EMBL:OGH37465.1, ECO:0000313|Proteomes:UP000178827};
RN [1] {ECO:0000313|EMBL:OGH37465.1, ECO:0000313|Proteomes:UP000178827}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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:OGH37465.1}.
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DR EMBL; MFOT01000027; OGH37465.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6JRM3; -.
DR STRING; 1798620.A3B44_02505; -.
DR Proteomes; UP000178827; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd14256; Dockerin_I; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1049..1117
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 261
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 445
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1229 AA; 132791 MW; 177B9886A5EEC86F CRC64;
MSKLFKAKPI LGLPIMQRSW WSVLPARIFF VFLFFSLFIF LSAPGIIKSQ EQEATDSARQ
ATESAQVVPQ ATESAKIAPS IPWKGLKKGQ LYLAPGEKMI SDKIDPTGEF FEDELVVHFK
SAVSDEEKAA ILNSKSLKTK WVSSYSKSHV IKVNPAQREK ILKELKADPK VEYAEPNYVV
RPLAVPRDVP NDPDFSKQWA LEKIKAPEAW SSQKGSGGKY IAVIDSGVDY NHPDLNYKVI
NGLNFIIYGL NPSMDDSFTS HGTKVAGIAA AITNNGTGIA GTAWFPKIVA IKALNVWDEL
PMDTPVTLGG APLLAAAILY AVDPCGSPWC PPDVPKADVI NISTAVPRHS QELQGSVNVA
LQSNVVIVAG VENDSGDCFM GYPAAYAGVI SVAATDQNDN QVSGCQNPRD VDNNQFVNGI
TVTAPGQDIY TTTRDGGYGA LSGTSAATAF VSGALATYLG YMPTEPNAAR NALIASVDDL
GVPGLDSTYG YGRLNFCKLV STNCPPSVSL YVSKNSNDPY QHEQNVNVGE TFYITVKAQR
GGTGSGVLQG IYLYDFYQQK WFLPPISCAP ETCEYKWPWS FGSSGDYKFI AGALDSNGNS
GFSHHSLGSP YIIHVGDGGM SVQGGLNRNS LPPYLQELTT SSGSVKVNLN WTDTQGESGL
ALQKKVGTGS FADFKNLSAG TTNYSDTLPT SQEGQNLTYR VRAKFSDNSY STSNEQSINT
PVATPSLQIT TSCNNGKVRY QLAWPDLPNE TQYRVVYWNI STTTLPANTT SYTRTDVDQI
SVPQNTVYWA VHADLQGGGI SSSGNIFAPP IDCGGGSLNL GVSTTCDGGK VHFWLSWGQV
QGASIYNLSV ATGGPGSPYS YIGTFSQTSF DYKSSLSSIS SNQVNFMAQA KNASGQVLAT
STRYASAKSC SLPPPPPASP PEIEITNVRV IEEPAAMDGI IEPGESLRLV FDIANKGNTN
SGWFDITTWW NRLSSAGCGT SGDYNWRYSA PSGYIGTLNI TGSGQFRAPA TPGTYKAWVF
ADSRCEVSES YENNNQGGGE YVVSAMPLSC DSFGDIDDSG YITSSDRNMM DRYLRGQTNL
TDEQKRRADV TGDGQINQSD IDKITAYLGG TASTFPVCED PDNDGLPNYE DQDDDNDKFT
DTKEIFIGTD PLDACSDNRS DPAWPFDINN DTRANVLDIN SFSVAGVLNT WEGNPKYNRR
YDLNADRKVN VLDINLYSAR GVLNTWCSN
//
