ID A0A0M9UBM1_9CHLR Unreviewed; 1346 AA.
AC A0A0M9UBM1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ARMA_0417 {ECO:0000313|EMBL:GAP61994.1};
OS Ardenticatena maritima.
OC Bacteria; Chloroflexota; Ardenticatenia; Ardenticatenales;
OC Ardenticatenaceae; Ardenticatena.
OX NCBI_TaxID=872965 {ECO:0000313|EMBL:GAP61994.1, ECO:0000313|Proteomes:UP000037784};
RN [1] {ECO:0000313|EMBL:GAP61994.1, ECO:0000313|Proteomes:UP000037784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=110S {ECO:0000313|EMBL:GAP61994.1,
RC ECO:0000313|Proteomes:UP000037784};
RA Kawaichi S., Yoshida T., Sako Y., Nakamura R.;
RT "Draft Genome Sequence of a Heterotrophic Facultative Anaerobic
RT Thermophilic Bacterium, Ardenticatena maritima Strain 110ST.";
RL Genome Announc. 3:e01145-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000037784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=110S {ECO:0000313|Proteomes:UP000037784};
RA Kawaichi S., Yoshida T., Sako Y., Nakamura R.;
RT "Draft Genome Sequence of a Heterotrophic Facultative Anaerobic Bacterium
RT Ardenticatena maritima Strain 110S.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC 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:GAP61994.1}.
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DR EMBL; BBZA01000023; GAP61994.1; -; Genomic_DNA.
DR RefSeq; WP_054491919.1; NZ_LGKN01000005.1.
DR InParanoid; A0A0M9UBM1; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000037784; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd15482; Sialidase_non-viral; 1.
DR Gene3D; 2.120.10.10; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR011635; CARDB.
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 InterPro; IPR036278; Sialidase_sf.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF07705; CARDB; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF50939; Sialidases; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 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};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000037784};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 59..173
FT /note="CARDB"
FT /evidence="ECO:0000259|Pfam:PF07705"
FT DOMAIN 964..1230
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 32..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 973
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 1006
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 1182
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1346 AA; 146114 MW; 6EFD14DACD779314 CRC64;
MRSTKTIALV LVGVLALFLG LGRALVMADQ PDRATPTPYA PPEGLDSQGD APASPDALPD
LVVTHVNVFP TTPVVSQTVV IQVAIKNQGE VNLPAGNNFF VDLYIDPPLP PQPGIDIGPP
TYSWGVQSWY VDNGNVWTLS FSTAFTDTGH HSVYAVIDPT GVVVESDEEN NVTGPTQFEV
ITSAYWQQSS HADFQKGFSN LDLSHSRGLM QIGRFYDRYI GSQGTQVNYA LQYFDQPEFD
RDIYFPDYAV VTEPGLQIAP IMTKGPNNTD EVAVVWEDWR NGTADADIYF SRSTDRGRTW
GTPVRITSDA DSIHVQRSPS LIYNEACGTY HVVWADNRLG SFDIWHAYSA DNGATWIEDP
APINDTNVNP TADQTAPAIG VDAFGNLFVA WQDRRNGNDD IYFAYGSGGC LNWTWGANVF
VTDDPEATAQ DQRLPQLSVA TYGTSPNDVY VFIVWQDMRY DGGDIFLGVG RPSPAPLYFT
FDIDIQMNTD GTTALQLDPA LDSIPLLVEV DYQMSDDNNE PVSCKAVLQT NVAHVAWQDY
RYGNPDIFYA WMFTDYAVLS VTGDDPLLCA AGGAIVETEF DPFTPYGNVN VSAYQVEPLS
AACWGPDSNT EEPMQSRWQG EPTVAVGNPY QVFIGWSDGR SSDDLNYDIH IAGMSNLTED
GTPTTDFTQR VGVANVNDNV KRLDLLVASD DQHYNTLYEE YAPAGVRQRR PSLVTQVSTV
ITPSLNPPSS WVPFAIAWDD TRNDDSFSGT VTNRDIFAAP FVSEMACAEG TPLCLINGRK
LGYYSEQEAL DQGYQAWGTY ISPVFDAGSE AVWFDIQWWG ATQFDSSLLL QVRLGNTPTP
PLDDINDGNW TRWSGVGGAG GYYDAPGQNI RDEDGSLFPR YRYAQYRVLI NQNRPTTGLT
SPLNGACVSQ VKLAYEPIRH DVYLPMVVNG TYQPIAQPDD PYYDALQWNM QISNFEAAWA
QSSGNGVTVA VIDTGVDLNH PELQPNLVSG WDFGNNDAVP QDVNGHGTHV AGLVAAVGNN
GQGIAGAAWN AKIMPLKVFA DGSSLASDAA IASAIQYAVD HGAKVINLSL GSQDDSQAIR
DAIAYARSKG AVVVAAAGNL YEAGNPVVYP AAIPEVIAVA AVTNERQRAS YSSVHSYVDV
AAGGGDPSSP TDPVIQHWVW STYPRALGGV PETGYNAISG TSQAAAHVSG VAALLLSRNS
SLSPDAVANL ITGTADDLGT PGKDSEFGYG LLNAGNAVSN AVVTTMQDRF APLRKQVFVY
KDTPDLLRQE NNWVSGELLV AYEETTTQAA VDALLSEYGA KRVEQVLATG VWRVQVPKGQ
EVAVRDALRA QPGIRYAELN YLRPLQ
//
