ID A0A0Q9MEH2_9BACL Unreviewed; 2087 AA.
AC A0A0Q9MEH2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=BIG2 domain-containing protein {ECO:0000259|SMART:SM00635};
GN ORFNames=ASL11_21390 {ECO:0000313|EMBL:KRE64631.1};
OS Paenibacillus sp. Soil750.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736398 {ECO:0000313|EMBL:KRE64631.1, ECO:0000313|Proteomes:UP000051252};
RN [1] {ECO:0000313|EMBL:KRE64631.1, ECO:0000313|Proteomes:UP000051252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE64631.1,
RC ECO:0000313|Proteomes:UP000051252};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE64631.1, ECO:0000313|Proteomes:UP000051252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE64631.1,
RC ECO:0000313|Proteomes:UP000051252};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRE64631.1}.
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DR EMBL; LMSD01000023; KRE64631.1; -; Genomic_DNA.
DR RefSeq; WP_056619376.1; NZ_LMSD01000023.1.
DR STRING; 1736398.ASL11_21390; -.
DR OrthoDB; 9816424at2; -.
DR Proteomes; UP000051252; Unassembled WGS sequence.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:InterPro.
DR Gene3D; 2.60.40.1080; -; 2.
DR Gene3D; 3.30.1920.20; -; 1.
DR Gene3D; 3.30.457.10; Copper amine oxidase-like, N-terminal domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR012854; Cu_amine_oxidase-like_N.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR036582; Mao_N_sf.
DR InterPro; IPR032719; WbsX.
DR PANTHER; PTHR41244:SF1; GLYCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR41244; RHAMNAN SYNTHESIS F; 1.
DR Pfam; PF02368; Big_2; 2.
DR Pfam; PF02018; CBM_4_9; 2.
DR Pfam; PF07833; Cu_amine_oxidN1; 1.
DR Pfam; PF14307; Glyco_tran_WbsX; 1.
DR SMART; SM00635; BID_2; 2.
DR SUPFAM; SSF55383; Copper amine oxidase, domain N; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 2.
PE 4: Predicted;
FT DOMAIN 1360..1437
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
FT DOMAIN 1445..1522
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
SQ SEQUENCE 2087 AA; 225671 MW; F21ACC4FB8F02EF2 CRC64;
MIKKLLGMVV SVLIVCAFTT IFEPSRARAE GATPEVGYVI DEDFSFLSAL TPGNSQPSGW
DVRAAGGALV SMYNTNFKIS DTSTVLPVSM NKKFVSQSEG SLTMEFRIKP LSIIDGLKWQ
LLSNEVVGVS LITQNNTLSL ETGINTVVPL QTYAANIEYG IKVVINLNTH TTDVYINGVR
KANGATFKNT VADLNQFQVR TGDASMGEFY FGPLKIYRGY AVNERLISVV NGGAIPQDWT
AVTSGGAITV GSMLSSPQPD INSMKLSAST ATGSMSLTKT ISPMSDNFTY DYKVLFKQKE
DGLEAELKSG TTSVIKLTTA GDYLAYVNNS GQPVPLDYKY LANLWTHIQI KVNWATATAD
IYINDKLVKQ GVALASGVTA VDSIKFTTSS SYRGEMWLDD ILLYKTVPLP VDYVPAPVAV
SKNEGAPLVG VQSCPMWREG HHLGWDMIQP YPDRTPLLGF YDEGNPETAD WESKWLEEHG
IDFQMSCWFR PLGGDTDRMP IKDSYLSHAL DNGYFNGAYS DQTQFAIMFE NLNSKVKDIE
DFRTNLIPYW IEYYFKDSRY MKIDGKPVFT IYNYDELVNA FKDSNGNDHV KEELDNLRTE
VSNAGIPGII LLNVYNGTDY AQLKKRKDAG FDGVYAYSWG SFGGHPEFQK LKMTQEKDTG
AIDIIPGLSM GRDDTAWRLN FGYYATPSEF ESLAQWTKDS FMPSLPAGSL GKKLVMLDNW
NEFGEGHFIM PAGLAGFGYV DAIRNVFGSS APHTDSVPTQ TQKDRINTLY PAGRVVPNLN
QPQAVMTNVY GNMWEFNTPG DAEGWTVEKQ IVGVTVQDGT FSGVTNNTDP GIRSADHLGI
KAEDIPYIVI RMKNSANDID GRFFFTTETD GTWNEAKAVG FFVNPLDSGY TEYIIEAWRN
KNWTGTIRQM RIDPISAVGP ISIDYIRTIY SPQPGIRTYV DGTYKGFSQP ALLQDGIVMI
PMKDMYLQIG AKPEWDSATN TLLAVKDNVV YKVKVGDSIA YKGNQAITLE HAPVKLANGT
VMVPLSYLRQ AFGAVAKWDA TAQTVSVYPT AITWDFATSS GWTANSQIAN PVVANGVFSG
TSNGVSGSVQ PTILSPDNLE YAASDIRRIR VRMNNMTNGE EAKIYFTTTG DTTWNEAKMI
PSYILPNDSV YREYVFDTSS LAAWTGTIKQ LQVVPTTASG AFSLDSVQLE ITPTVALKGD
NLIEDPGFEG STTSQYKLQN ATAAKDTTQS HSGHQSVKIT KSTRYGSISF PVNVEKGKPY
TYSAWAKLAA GTTTNEFLRV GIQYNLDGGP PKQLIIFTSP GLKAGEWTQI EGTYTIQESG
VVTNVLMYLY TEINNPGGVY YVDDVAVKPI TNSGSSVWVH PSNISFGATS MTVGVGKTKA
LVPAYTPVNV SNKELIWRSS NPSAATVDVN GMVYGVSLGT ATITATTVDG GKVASVLVTV
DDTIAVTGVS LTPTSLSLPL GTQQTLVPTV TPANATNKLI KWESANPIVA VVDANGIVTG
VGTGTTQIKA TSDDSGKQAI ASVTVTAPTN VVKGSNLIVD PGMEGSILAA PNYAYQAVPS
LTSAEQHSGQ KSLLLTKTDK YGGVKFPVPL VKGKPYYYST WAKLASAPAS TETIRIGLQY
KLDGDPMPKQ YIMFVSPSLN AAEWKQVQGS LIINETGVVT ETTMFLYTET QGNGTPFYVD
DVEVRPLTVD DVPPVTVSDA PSGWQTTAQV VHLTASDSGS GVAGTFYSLD HSAYVVGNTI
SIAAEGVHTL DFYSKDLAGN QEATQTVNVR IDGTAPTTTS VVAPSAPDGP SGTYVSPVTV
TLSATDNVSS VGQVVYSVNN GATWTPYTAA LTFDKQGAYT LQYRATDLAG NSETAKSVSF
NLAASTVKVQ LKDSTGNPLN GGVVKYYDGG WKDFGVTDAL GNASKSLQDK GYTFGITYEG
TYKEIVQHTG TDAVVVFQTV KAKVQLKDSL GNPLDSGTVK YYAGSWRTIG NTSGGEISKE
VLPSSYTFGM TYGGRYKEIV QNTGTDPVVV FQTVKVTVQV KDSHGNLLDG GTASYYAGSW
QTIGVTTGGG ISKELLPGSY TFGMTYNGTY RELVRNVATD PTVIFQL
//