ID W4VC03_9FIRM Unreviewed; 2354 AA.
AC W4VC03;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Dockerin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=JCM21531_3920 {ECO:0000313|EMBL:GAE90323.1};
OS Acetivibrio straminisolvens JCM 21531.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=1294263 {ECO:0000313|EMBL:GAE90323.1, ECO:0000313|Proteomes:UP000019109};
RN [1] {ECO:0000313|EMBL:GAE90323.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 21531 {ECO:0000313|EMBL:GAE90323.1};
RA Yuki M., Oshima K., Suda W., Sakamoto M., Kitamura K., Iida T., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequence of Clostridium straminisolvens Strain JCM 21531T,
RT Isolated from a Cellulose-Degrading Bacterial Community.";
RL Genome Announc. 2:e00110-14(2014).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, 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:GAE90323.1}.
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DR EMBL; BAVR01000064; GAE90323.1; -; Genomic_DNA.
DR RefSeq; WP_038290891.1; NZ_BAVR01000064.1.
DR STRING; 1294263.JCM21531_3920; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000019109; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; 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; cd07473; Peptidases_S8_Subtilisin_like; 1.
DR CDD; cd08547; Type_II_cohesin; 1.
DR Gene3D; 2.60.120.380; -; 3.
DR Gene3D; 2.60.40.4130; -; 1.
DR Gene3D; 2.60.40.680; -; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR045351; DUF6531.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
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 InterPro; IPR034204; PfSUB1-like_cat_dom.
DR InterPro; IPR003646; SH3-like_bac-type.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF20148; DUF6531; 1.
DR Pfam; PF01344; Kelch_1; 5.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF08239; SH3_3; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00612; Kelch; 5.
DR SMART; SM00287; SH3b; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF89260; Collagen-binding domain; 3.
DR SUPFAM; SSF50965; Galactose oxidase, central domain; 1.
DR SUPFAM; SSF117074; Hypothetical protein PA1324; 1.
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; PS51781; SH3B; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000019109};
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 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1275..1350
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
FT DOMAIN 1958..2032
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT REGION 63..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 260
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 317
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 471
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 2354 AA; 262060 MW; 98175DD99C9E4C8D CRC64;
MRLAGKAITS IAIVIAIIIQ CFSVTGMAYD KSIPVTKESH NSFRNESVNN EKADTLREDK
QAVKTEEISR TVSSEVYGEG NETSDIEENS DANIEEKNRK KIEELVPPNV IEIGEKNEID
INLNKNLNKT KKDIIVVYKD ISKANETKEK FKSKDNVRDV KTKYKSKRFE MEALEVSDQK
DMEKLIAEIK SDPNVKYVQP DYKLNTFDIP QDEHFDKQWG LLNNGQIVNG QTGLAGIDIN
VLDAWDITTG DEEIVVAVVD TGVDINHPDL AANIFSNTNE ILNGIDDDGN GLIDDVNGWD
FANNDNSVND SSTHDIHGTA VSGIIAAEMN DIGVTGAAPK VRILPVKFIE GSSGYTSDAI
KAIEYAVDMG ASIINCSWGG SEYNPALMDV ISQSNALFVC AAGNSSSNTI QNPVYPASFD
LDNIISVAAI GSDGNLAAFS NYGKNVDIAA PGTNILSTVT LERYDYLSGT SMAAPFVSAT
AALIKSNDTA LTATEIKERI LNNVTQSDKL SGKVKTSGRL NAYAALLNET PADEEPEPQE
ENEQINLREP RFVYDISAEG NNKVPKPIVR EGGFFDDSGD NRENANVILS GGREKIEKIT
KKYPTVASAT YNGQTPVSQL SLQDVSILSY VFDNNNNHTI DTAQAISECT VFGSMEESSQ
QDYYAINFEA GKRYTIRLTG MHTPDDFDLL LLNSSGGLLG FSYFGGSNEI ITHTAGYTGV
HYIVVEAYHV DDSTEHHNYQ LLVYSDNNKP DVYEPNDSSE TAQPITDGIP VYATLNINTD
EDWFVIDITE TGKLSITLKN IPAGCDYELE VYNSNLIKKY FSYASGNNDE KIDKIIDTSG
RYYIRVYSYS GANSVENYEL KVSVTEPDNY EVNDNIYDVR YYGSPLIDIG STIYATIDNI
DDCDIFKFNL NNHMNVGIRL QNIPEGNDYN LVVYSYSIYQ GFFEVVRSMN VGSLAETIIT
QLNSGDYYVM VYSAGGFSET ETYTLSIYDE DTVSKVYVEL DKTTASEGDI ITATVKVKQL
AELAGIELNL AYDPNVVMPV KDDLSPYGYS PILSGSDIFL DEEYLPFRFV SHAPNEGNIR
FSLCYVDIKA YRNSMPEPVD GTVAVIKFKV LRENQIQLKF YNAKEPDSSA IYLYDWYGNR
IREGFIVEQP QVINEDLPIY VPEYLSISNI MNTPQGTTLF GSSPRKISGY IDINFNSKNP
NIKEGFLVEL KGASPENQSI IQTVTTDSNG YFEFVQLPSG YYNITITKSR FVKREFINVA
TIFEETVIGY QEEPIIMFFG DLVGGDNDFD NPDNSVNLGD IMVIVKSFNT VIGDADYNPL
ADLNDNGAIN MEDVMILYIN FGKSTSNYSV IKYKLYKNEK VPSFTLPIGE LDLNGHTLIV
EGNLTIDEPT TTTYATLNIN GGSLYVTGNL LLSGNARLIM RNPGDYILVN GNFETRSLID
HEKNKEEIKG GDGKACLTDG VLEVKGNFTQ NSNEKYWVGT TYVREAYGDP RNFTALENHK
VIMSGDEVQH IKFDRVVIQA NIDHSHFYTL EITKPLETGY TLELMEPSTV AWIRLIEAFA
SSTPREGTTE DLEENAIARG GTVAATTGAK IYVFGGYNGD YLKVIEEYDP IRGKWTVIDG
SNQHRLELKV PRRDMGVVEV NNQIYVIGGE NANGYVGEVE EFSSVTGSRV LTNIDPVTGE
NKCEMPTPRA KVAVASFGNK IYAIGGFDGS YSNKVEVFDL DITKKEWTTQ CMVGGQTQTI
KNMPTARCGA AAVEFNGYIY VVGGYNASGY LATVEKYDPV NNIWTTCSSM QYKRANLGLE
VVEGKIYALG GYNGVDHLAV VEEYDPETNT WKKMTRSIVS PGSGYVEEPR SSFGTAVVYS
QIYIVGGENK GGYMNKAQKY VPSVLPGLKM YTGSIVKKTV GDVMLSGDYS TQVSDLKIDS
PGIPIELIRT YDSSDNEEKT VIGYGWRFNY DSKLVEISNY GKVTASALNV REKPTVNSKS
FGLVPRGAVL LFETVNGQPV TERDVNGNEW YKIKLSDGKT AYVASWYVTK HSSGVEIKLG
AGKTTVFEGN KTDGFTASYG NYDHLEYMTN TGEYVLVMSD TTRYGFKKIS TSDNAYRLVW
IEDKHKNRVN IQGEYVNSVY RITRVSDNAG RALTFNYSTS NTIIVSDNVG RTVQYLLNGT
TGHLEQVINV YGKATKYTYY TAENDISTDK KNVKKLREIQ TEQMNEETGV EEFTTIQRNY
YDEDTGRIYK QTDAYDKVKY WRYIDPVAGE NVDSEEISGT LERKFIDENN VSVSIQYSHF
LKQPIREEYS DGSVVEYKYE MEINDAWVDT TNLTREENES IGATSKNRLN RKYTKDKYGY
TTVQETDETV MLKW
//
