ID A0A2A2YA15_9BACT Unreviewed; 1674 AA.
AC A0A2A2YA15;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Carbohydrate-binding protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CAK88_07985 {ECO:0000313|EMBL:PAZ05443.1};
OS Verrucomicrobiae bacterium AMD-G2.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae.
OX NCBI_TaxID=1982328 {ECO:0000313|EMBL:PAZ05443.1, ECO:0000313|Proteomes:UP000217571};
RN [1] {ECO:0000313|EMBL:PAZ05443.1, ECO:0000313|Proteomes:UP000217571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMD-G2 {ECO:0000313|EMBL:PAZ05443.1};
RA Cabello-Yeves P.J., Ghai R., Mehrshad M., Picazo A., Camacho A.,
RA Rodriguez-Valera F.;
RT "Genome diversity of Verrucomicrobia from freshwater lakes.";
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:PAZ05443.1}.
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DR EMBL; NEUM01000015; PAZ05443.1; -; Genomic_DNA.
DR Proteomes; UP000217571; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR013211; LVIVD.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR InterPro; IPR032812; SbsA_Ig.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR47197:SF3; PE-PGRS FAMILY PROTEIN PE_PGRS17; 1.
DR PANTHER; PTHR47197; PROTEIN NIRF; 1.
DR Pfam; PF13205; Big_5; 1.
DR Pfam; PF08309; LVIVD; 1.
DR Pfam; PF18911; PKD_4; 1.
DR Pfam; PF21419; RoxA-like_Cyt-c; 1.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF75011; 3-carboxy-cis,cis-mucoante lactonizing enzyme; 1.
DR SUPFAM; SSF46626; Cytochrome c; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR PROSITE; PS51175; CBM6; 2.
DR PROSITE; PS51007; CYTC; 2.
DR PROSITE; PS50093; PKD; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00433}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 475..537
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 545..673
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 676..802
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 1186..1311
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 1327..1434
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 1674 AA; 176261 MW; 9641A2A5B8F719EB CRC64;
MSHTLHRIVL MTSLMIGCLH AVDGVIPNRT YLPTEQFTAI SPQLSSLHLN QPSVYNGYVI
FAGNGVHEVW DIADPYAPLK RATFQSNFRS GEAESHQVTY ARKADGTAYM ATISGKGVDF
WNVTNTIEPV LLGEIQLPNI NYGDVTGGIW GVSWQGNYLY AGATTHGLYV LDVTNPAAPS
LVATMPRAAL GNVPAGPLFA VGSTLVVTTP KTFRGIATVD ISNPLQPRLL DSVIPASGDS
YIGGFYNGFA TLITPFRAYD VTTDPSNITL LGSTNTPYGE YTSFANNKMF FGGIRGGTHG
VYKFDVTNPA TPILEGRFIG RDTRWDDQFS CPIGNLLAVA DDQQVDGHYV GGLMVVHDTQ
PDTTGPSVLK VFPKDGSTGQ ALSGCVSVSL SEWPELATVD ASSFIVRPVG GTPIAGIWST
NHTILSFGPA QPLLPLTQYE IVLPANGIKD FVGNAIAAEY RSTFRTGIGG VSGFPGNAAI
AAVPPTELGQ ATTFSLAIAP AAATQYEWNF GDGNSATGSL VQHTYTAPGR YPVRLDAVPT
GPRVESYEAE SAVQSGGVAF GSSNQGYSGT GYADFPGGQG TNVAITWNLT LAEAAWIHLD
FRYANGGSAA RPLDVVVNGG DEIPLTFAST TAWNQYRSQP ASRAFYLPAG ANTIILRATN
GSAGGNIDRL DLVHLEPDEA EDADLSAGIS VRNWHAGFTG DGFADYDATG SAVRIRWTLD
LAAPLTLPLN FRYANGGTGD RALNLVIDGG TPQPLPFPAT GAWTAYGIQS SPVISFPAGV
HTIDLVCDAG SSGGNIDSLL LPTRSAPPAS VSFTHIVHRL LTTEPSSNSS PLALDGARTT
LWIANPDTDT VTRVRAADLV KLSEHPVGDQ PENLAVAPDG KLWVSNHSSA NLTVLNDDGT
LHATHPLPHG SRPYGLIISP DGNGAYLALQ AAGKIIRIDP ATGTITATIP LAPSADGRAA
NPRALALDAS GARLFVTRFI SPDSGGLVYE INTATFTLTR SYGLAADPGP DTSISSRGIA
NYLTGIGISP DGTRAWIPSK KDNILRGSLR NGNGLTHDQS VRSITSVIDL SNHTDIPAER
RDYDNLDRAH AVAFSPLGDL AFVTQPGNNL VEVVDAYTRS TVTQIPVGKV PTGILLDPVH
KRLFVLNFLD RSLSAFDVNS LVNGSGATAA ELAPAASLIA TETLTAQVLH GKRLFYDAAS
TRLNEEGYMS CASCHLDGAH DGRTWDFTGF GEGLRNTIDL RGRAGIAHGR LHWSGNFDEV
HDFENQIRNF GAGTGLMQSS DFSTRSDTLG TPKAGVSADL DALAAYVASL ATVPASPHRQ
PDGSLTAEAI AGREIYQSLN CASCHGGQTY TDSTTAALHD VGTLKSSSGT RLGVALTGID
TPTLRGIWDT APYFHDGSAP DLAAVLSSGP HHDVSNTLNA TQTAQLIAWL KQIDQIDPAT
ELIPGTIEFT ALPAKSPTDP PFPLTANASS GLVVAFTSSD PTVATIAGDL LTIQGPGTTT
ITATQPGNAL HPAALPVAQS LIITPLSPLF AHFLTDHFTP AQLADPLVTG PLADFDNDGI
SNLLEYALGS TDPTNRTGAF PVIHSSGPFR ITFLRRSSGT ETDGTYRSGD LTYQPLAATD
LANWNIAPDS VSNPSNLPTA PEGFEWTSYA IPHSAETSRR GFLKLNVTIQ NESN
//
