ID M0MTD5_9EURY Unreviewed; 1540 AA.
AC M0MTD5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:EMA47740.1};
GN ORFNames=C450_20506 {ECO:0000313|EMBL:EMA47740.1};
OS Halococcus salifodinae DSM 8989.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halococcus.
OX NCBI_TaxID=1227456 {ECO:0000313|EMBL:EMA47740.1, ECO:0000313|Proteomes:UP000011625};
RN [1] {ECO:0000313|EMBL:EMA47740.1, ECO:0000313|Proteomes:UP000011625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8989 {ECO:0000313|EMBL:EMA47740.1,
RC ECO:0000313|Proteomes:UP000011625};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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:EMA47740.1}.
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DR EMBL; AOME01000108; EMA47740.1; -; Genomic_DNA.
DR RefSeq; WP_005046961.1; NZ_AOME01000108.1.
DR STRING; 1227456.C450_20506; -.
DR PATRIC; fig|1227456.3.peg.4139; -.
DR OrthoDB; 214857at2157; -.
DR Proteomes; UP000011625; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 3.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR011635; CARDB.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
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; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF13620; CarboxypepD_reg; 3.
DR Pfam; PF07705; CARDB; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 2.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 428..495
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
FT REGION 50..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1511..1540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 105
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 152
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 359
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1540 AA; 160037 MW; EBCB3110DFCF1F98 CRC64;
MAGTRDLGGV DVTNRFWIAN LVAVTVDTDR TSVRSLAEIK GVNAVVKSRE ISVPKPPENV
QPADDRSETS PSDVNTTYGL DQINATQTWN EFDTRGEGTK VAVLDTGVDI DHPDIDLYTE
NESNATYPGG WAEFDENGNQ VPGSEPRDSA EHGTHVSGTV SGGDASGTAI GVAPNVQLMH
GMVIPGGSGS TTQVIGGVQW AVSEGADVAS LSLGAGCGLF GPVYSQAWIP VVENTKASGT
SFVAAAGNSG EGCVGSPGND FKTFSIGASN ADGDIADFSS GQVIDKSEWD DPPAEWPDTF
IKPNVSAPGV NVLSSVPGGG YDDTFSGTTF IKPNVSAPGV NVLSSVPGGG YDDTFSGTSM
ATPHVAGATA LIHSANPDAS VSEIQQALNS TAWKPDDAPA PDDEKDTRYG MGIIDVYNAT
QQLAVSAPES ELGDVNENGD VNVQDVRLTQ QYLYGEEPES FNANLADMNR DGEVTTDDLR
LLQRKVQGTL DEGAIQVSNL TAPDEVAENE TITVTATLTN PGDEGAIQAV SLHVSENESD
LGDGTPVTNK TIDMAPAGVD DPVDRPHETT VTFEVDADEI GAGDYHVGVF SEDDSASDEI
TVLGSNFAVS DLSAPSEVEQ GNAFDVNATV TNTGNQEDTQ TVEYRFRGSS ERTTNVTLGA
GESTTVGFED IETEGVNAGT YQHGVHTEDD SATANIMVLE GFFDVNITDA PDEASLGETI
NVSASVENTG NATDEQTVTY DLMQGETAVA VVDSDEGYGE QVASTLRKEL PDQYNVTMVE
DQNAMEAVGE YDTFVMQDLD PAELDVQSFV EATNGQQTGV VWLDGWGSGS DAIPELSAAT
GNPSGATDGD GGSTPVYYNV TQDHPIFEGM ADPGETVPIH TADYADRSWF SGYSGEVIAD
VGAESSTIGG SGLGADSANS TVLASSLGRE SFVQNPDFTE AANQTLANTV TYVTGPGGTG
AGEVASQDDT SANVTLDPGE SETIEFTYTI GDDLDISADW FHTVTSEDDV DTAPVTIDVD
RGAVEGTVVN NATGDPIEDA PANISVAVDD GNYTAVTDED GTYRIEDVPA GTHNVTVSPD
GYTNETTAVE VPANGTVTQD FSLAPMDGSI SGTVTASDTG EPVANVTVAA EDNEGNVHEA
TTADNGTYTL DVPPGNYVVN VADTPGEYRP QEVVTVAPGE EVTGVDFQIT PRNGSITGYV
ENAAGVPIEG AHVVDADQGA FNVTTDEDGS YEINDLDRGT YALRANADGY NATDISFVEV
PANGTATQNF TVGSFLAVSD LSAPDTAAQG ETINVSATIT NTGAEQTTRT VFYFPPGTDF
GGEMFTASSH LSERVTLDGG ESTTVTFTYD VSTSREPGEY RHGASADEVA STTITIEESE
TPGEANYSVS DLSAPTTAEP GAEIGVNATI TNTGNTTGTQ TVEYLFNGST ANTSNVTLGP
GESTTVAFSP TVPATEGTYE HGIETADDSA IANISVEGGE PEPAYFAVSN LTGPSEVGQG
EEFTATATIT NTXRGLEPDR SLGSRPGRGV HGDRHHHQHW
//
