ID A0A1Y4NMZ9_9FIRM Unreviewed; 1884 AA.
AC A0A1Y4NMZ9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=CBM6 domain-containing protein {ECO:0000259|PROSITE:PS51175};
GN ORFNames=B5F07_14825 {ECO:0000313|EMBL:OUP82196.1};
OS Lachnoclostridium sp. An169.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1965569 {ECO:0000313|EMBL:OUP82196.1, ECO:0000313|Proteomes:UP000195962};
RN [1] {ECO:0000313|Proteomes:UP000195962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An169 {ECO:0000313|Proteomes:UP000195962};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUP82196.1}.
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DR EMBL; NFKT01000022; OUP82196.1; -; Genomic_DNA.
DR Proteomes; UP000195962; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR CDD; cd04080; CBM6_cellulase-like; 2.
DR CDD; cd04084; CBM6_xylanase-like; 1.
DR Gene3D; 2.60.40.1080; -; 2.
DR Gene3D; 1.20.1270.90; AF1782-like; 3.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 4.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR InterPro; IPR039448; Beta_helix.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR PANTHER; PTHR36453:SF1; BETA_HELIX DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR36453; SECRETED PROTEIN-RELATED; 1.
DR Pfam; PF13229; Beta_helix; 1.
DR Pfam; PF02368; Big_2; 2.
DR Pfam; PF03422; CBM_6; 4.
DR Pfam; PF07554; FIVAR; 3.
DR SMART; SM00635; BID_2; 2.
DR SMART; SM00606; CBD_IV; 4.
DR SMART; SM00710; PbH1; 7.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 4.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 2.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS51175; CBM6; 3.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000195962};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1857..1877
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 915..1033
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 1041..1155
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 1159..1288
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT REGION 1727..1855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1738..1805
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1813..1855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1884 AA; 205644 MW; F4F43EC7C7EC507E CRC64;
MGNKEEVRRE DMKKRKKAAG RKRLIAKLMS GLLAVTWAVP PAGIALADEG SPSLQENTAA
VYVATDGSDE KGDGTLENPY ATIQAAQEAV RKAIREGLDG DTYIYIREGT YYLDEGIQID
GDDFDPEYKV IYKNYNNEKV RIVGGEKVTG WTDPDGDGIY EADVTGRTEL YSLFADGKRL
TNARESNWGG IEVEDQSHMQ AVYGGPTNWF GEVLKVESVN GGQVSTTYPA GAWSGSIQYL
QGAKEYINES GEWAVSGNTL YYKPLEGTDP EESEIIAPTA DRIFYLNGTQ ENPVENIVID
GLDLEMTAFG ENLLAHSGRY GDKTEEYECN LKGIVDLNNT ENITVSNCIL KNGGYMAVVL
NHYSQNNLIY GNDIEDTGYA GIFMIGENPG SLNYINKNNT VSNNRIQNVG HFVSHGSGVY
LMNSGENTIT YNNISGTPRY GISMKGIRYG VFEANGVEDV PFEEHWKYNQ TTKNYIGYNV
IYNTGSYSGD GGGVESWGIG RDNWIDHNII YNAYRGQPST GWRGHSIFAD DGSHYLMVTN
NIVYDESAVT VNAGTMIKGI SSYVKNNVFD VGYQTNGSAD IEPYIEPCGY MTFENNIIYN
GTGGSLAGNG TWSESGSGDR LYLKVNDNAN STGTPAMEAL RKMDENVYFN SVGTGKLDIM
GNILSLEEWK NFDKNINSYD QNSVEQDPEF IDPADRDYRL SADSPARAMG ISSIDISTIG
LLKDFRYSDQ EDQPKELFLS FENKPGVASV AEVGEKLAGE AVIRTESGYA LTDVEGTVFS
SSDESVASVD TDGTVTAKKA GKAVITAKNG ELSDTYTLYV GDEGSELIAD DINLTAGKDE
IAYINTQIKT ENGHYIDCAD LTYESEDESV ASVDENGYVK AEGKGNTTIT VTTAVNGKKL
EKEISVYVGK ESIPGKVEAE NYKSMEGIEK EACSDEGGGD NLTAIDPGDW FEYSSDVWKS
GVYNVDFRVN IPAGSKAEFE LSSGGENITV ICLDSTDGEW KTLTEAVTLP KGEQTIRITA
QSGDWKLNWM EYSFGGQVIP GRVEAEDFTA QQDVQIEDGD HVGYIDDGDW MEYTITVKEP
GTYHLTYYVS VNDSEGIVEF ILDGELLRTT TLPGTGGWKN WINVRDTIVI EETGTHTVRL
NVPNGKWNLD YFELYTDSSQ VETKTPYEWI TGDEADRYQN GANKQSGKAG LDPDGSYIVF
ENIDFKDGAK RVTATYETGN LERVGDLELR LDGINGTLIG VIDCKTTGAW GIQEQSWLKT
DPDIVNGVHD LYAVASPGAL NLVGLKFSQA DAGTDIEGLE IGGQDIVTAP EQETCNYEFS
AQLLDDLGEA VETEDVIWSL ETPDNNIELD EESGILTVGI PAVRETKIKL KAVSRTDETV
WNEKEVLVYD GKIVELTGLD ADEKYGRIEQ DGTSGIVFWN TDSYVQYNDV DFGNGIEKYA
VEFSYPNSEN IMELHADSKE ESAFSSIALS SGSWSDYLQK EQQVTDSPQG KHNLIITQSD
ALHFQWIRLY VPYERKTDVE TDRTLLQKTY DYALTLNTDG VVDSAKAYFE KVLAEAQAVL
EDETATQEEV NTAWNNLLEG IWGLGIYQGD KTNLNLLIET AEAMTAEADR YVTEKWDLLT
AALEEAKAVA ADGDALEEDI TPAADALLDA ILAQRYKADK ANLQKLVDSL KDLDLTKYTE
ESVAVFNVAL TQANAVLADE TLSVDDQAVV DQAETELVAA RNALVLIEEK DPSEPGDPSE
PGDPSDPSDP SDPSDPGDPS DPSDPSDPSD PSDPSDPSDP SDPSDPSDPS DPSDPSEPGN
PSDPGDPSKP GDTGSSDDVN KPGTNDGNST TQDQNSQKTP DNQNGQHTVQ TGDVSPIGAT
AGVMVLAVVA AGAVFVIRRM KFRR
//
