ID A0A0S4KG35_BODSA Unreviewed; 2590 AA.
AC A0A0S4KG35;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Carbohydrate-binding/sugar hydrolysis domain-containing protein {ECO:0000259|SMART:SM00722};
GN ORFNames=BSAL_01105 {ECO:0000313|EMBL:CUI14657.1};
OS Bodo saltans (Flagellated protozoan).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Eubodonida; Bodonidae; Bodo.
OX NCBI_TaxID=75058 {ECO:0000313|EMBL:CUI14657.1, ECO:0000313|Proteomes:UP000051952};
RN [1] {ECO:0000313|Proteomes:UP000051952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CYKH01001474; CUI14657.1; -; Genomic_DNA.
DR VEuPathDB; TriTrypDB:BSAL_01105; -.
DR OrthoDB; 2901654at2759; -.
DR Proteomes; UP000051952; Unassembled WGS sequence.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 7.
DR InterPro; IPR039448; Beta_helix.
DR InterPro; IPR006633; Carb-bd_sugar_hydrolysis-dom.
DR InterPro; IPR007742; NosD_dom.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR PANTHER; PTHR22990; F-BOX ONLY PROTEIN; 1.
DR PANTHER; PTHR22990:SF15; F-BOX ONLY PROTEIN 10; 1.
DR Pfam; PF13229; Beta_helix; 8.
DR Pfam; PF05048; NosD; 1.
DR SMART; SM00722; CASH; 4.
DR SMART; SM00710; PbH1; 34.
DR SUPFAM; SSF51126; Pectin lyase-like; 8.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000051952}.
FT DOMAIN 54..200
FT /note="Carbohydrate-binding/sugar hydrolysis"
FT /evidence="ECO:0000259|SMART:SM00722"
FT DOMAIN 490..628
FT /note="Carbohydrate-binding/sugar hydrolysis"
FT /evidence="ECO:0000259|SMART:SM00722"
FT DOMAIN 1746..1874
FT /note="Carbohydrate-binding/sugar hydrolysis"
FT /evidence="ECO:0000259|SMART:SM00722"
FT DOMAIN 2235..2367
FT /note="Carbohydrate-binding/sugar hydrolysis"
FT /evidence="ECO:0000259|SMART:SM00722"
FT REGION 658..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1397..1457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1659..1682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2360..2393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2460..2491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2544..2590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2370..2393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2590 AA; 275251 MW; 985FCA234C57900E CRC64;
MRDQDAITCR MTMSKWRPNT SVPTYFVSSK PRKGCFTQIN DAIQYAQQYS RIELLSGTFT
EAVVINKSIE IGSEKGDEQA VIAYHMTAVV LQTKEAYIEG VTIRNTENQA AMRIDRGSPI
IARCDIAGIE VGGDATPHIE ECKIESSAVH GLSILQVAGG MYKGNSILNS GWYGIHVEST
GPVTFVHNSI TESAQGQILV QGGSDVTPVF QYNRVIDQVK SAVDPALLHQ TQAYKLEHLP
VKKAGQTVVI MPLELTTAVR VALNEDNIDD AVVNSVDARC AIDIRGNTHP SFVRNTIVGS
MNNGFYVHSG ARGTYEHNYV TSNRGWAFVL DGPTTKAHLV ANSLTGNGGG VKVVNSPSTI
DGKNEFVENR GPQLMLVNGH EDFRFTQNDV RSGSKIGVLC RDGGSGTIDT NSFDQCGTAI
RTEFGANPLV KDNVCTMTNI GVCSVRGGRG DFIDNEFGNL SVMCVLITTG ADPKFTNCRF
LTSNNGVLIT KGGKGTFQQC ILKDNKGVQL EISDRANPLI TDCFIADGRD DGVKVHHRGK
GTLRRNVIAG NERAQICIRA FGDPIIDENI ITRSHHDGIL IEDKGFGVIT NNVVERCRLS
GISVVAQSMP TIRGNMITLC REAGLFIGDE AGGGTYEKND IFNNRKANIQ IAGPGVVVAE
PEKSTSPKKK RQSVVAPSTE QSSSSVAAPP IAAVNPLSSS VNTTANDPAA MSMMSASVSV
VMPDKFRRVY VRANKIYDAV GCGILASSRC EAVVSKNLFL ANQVSAIRVA TGSEVTILQN
EFIAGVDGVV AVEDSKVRIL ANSFADLRGA AITFDEGSRA LAMWNTAEHC LHGLVVRNST
GMCFLNSILQ STNSAVVIGG QCRTNVKFNM MFEDEVGARV EHRARGSLSG NVIFESEING
IVIDGEEVHT VIDANIVLNA KQSGVVVKKG SPKMQNNVVM NCVTNGIEVS AGHTSPHFLG
TYVSCCQKGV LFGDGSGGRL DASIVGHCDI GVEFNGSHSG HLRGSVVHNC SAVGVYGTGG
ASCAGEIGDS ILFKNFINAL FTNHSKMHLA NSLIQAAVSF NIACTKSAAP TISRCVIASR
AVGTEEDQDE LREADKQSTT IFSNLKRKFG EQKIRDTWNS AYAYRIISLW DDVYATNSTS
VGGLPAGWIP AAEIAAANAA AALAAGNDEN GDAKDAELLS DGRGYSRSHT ASIYSSNTSR
PQSAMSSVSV VTESVDGDVI SGVSPNSKDH HDEAGSFEVL SVSDQSTAQQ HLDSAAPPRA
IQNVVTIADI LRSKAMPIAR RTAILFPSNI HDTTDEFIGP GGPFILHRML GGETNSYLKG
LFTYYCSGLR VDHAANPHVE GCVFRDHKFR EAKILSKRIP LRETADGGVG GAVGGSAAKT
LRHLLAERTL SDTAKKLRAR TQHQSNGNIK TPLSPPTGQP SSSRRTNKSK HTKRREVEIQ
QPLDDEGGLG MSNSGAFRAT HGDGGLLMLP GTPMMIDQSN FIDQILLTSS PCFYQHHNAP
HPIDALPALY DVPSERQARE EIQTSLSSGG AGRNVLTNTA ASKFLSTVAD HTMNMQDRAV
QAAAAAGTPQ GTFISTECTM EFTGFGAIFC DGGLGTVTRC QFYRNNCGLK IESRACPVIS
YCNIAHQQVD GVWIRYLGSG VLRANKVLKN KRTQIRLDDS KTTFPTTPST ANDAESTSSG
LSFKPPSLEE NEICDSHSPG VVVSGRELQC SLMHNTFANI TTNQVAAVIV ELGAEPQIRN
NDVTECTNGF LFRQGGCGVA DSNRLNLCSR TAIVVEGGYD PITAEPTIEQ NQITDCGECG
ISVIGQGTRP SVIGNQILNS RASGMNMTNG ASGSFLQNHI ENSFEHGISV TNGANGLIEG
NTIIASQQHG VYIAGDAAAP FVQRNVICFG KQYGIVIEDA AGTVSLNRIL SHIGDGNSTH
HESGGIRATG GSATTNIEQN EINHNTVGIY CTNGARPDCT NNVITRSHIG GMIVEGKLTQ
PNIKGGYFKL NQQFGVKYQL SGGGTMEETT IMCVYGNGIE LHSSSNPSIQ NCCVTMCTEN
GIFAGSGGAG VIHDSVIMQC DQVGVSLSDS SGQFRLKNCV ITDCKDAAVK GEASGRGTIH
SCTLLGKFFV AGAVLMPSSR IIFDATLFVD QKVGMLNHST QTQVLDALFQ SCVVGISDVV
TDGDRSSTGG VMAQNCEFRD CQTAGIQCNK GNAAIKQCQF IASVKHGVQV VGSDCAPVME
GCTLQRCRVG VSLDAGKGTL ESNEVFNCAD GIIISASLRD IIFFLESNEV FNCADGIIIS
ASDADIKNNT IYDCAASALT LRNGNPSITT NLVFDNFNAG VVLEGGGGLL EDNRIFFARD
DGALLVKPTS QTLQNRNTVK NAFSPPKEKS YAERTAHYKR QEQQEREKSS SVFKKFARSA
DSVCSEVLRA SMENAERLAE ATADSGAWVF EESFDDPQSA TAASSKSSLA PSPRAAAAAT
GSGLASAAPP PLSVTPRTGG GRASLFSPNP VAVTTSPGQA ALQLSANPVS TADASMSMAP
FLDHMPLTKA KDKLNSLLEP IRPAKSSGVV DPALSINTAP VPPTKPKGSR GASMVRRQSK
KSLSSPVPKD
//
