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Database: UniProt
Entry: A0A0Q9MEH2_9BACL
LinkDB: A0A0Q9MEH2_9BACL
Original site: A0A0Q9MEH2_9BACL 
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
//
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