ID   K5EEA2_RHOBT            Unreviewed;      1901 AA.
AC   K5EEA2;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=C-type lectin {ECO:0000313|EMBL:EKK04206.1};
GN   ORFNames=RBSH_00401 {ECO:0000313|EMBL:EKK04206.1};
OS   Rhodopirellula baltica SH28.
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=993517 {ECO:0000313|EMBL:EKK04206.1, ECO:0000313|Proteomes:UP000007993};
RN   [1] {ECO:0000313|EMBL:EKK04206.1, ECO:0000313|Proteomes:UP000007993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH28 {ECO:0000313|EMBL:EKK04206.1,
RC   ECO:0000313|Proteomes:UP000007993};
RX   PubMed=23273849;
RA   Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., Richter M.,
RA   Achstetter T., Glockner F.O., Harder J.;
RT   "Expression of sulfatases in Rhodopirellula baltica and the diversity of
RT   sulfatases in the genus Rhodopirellula.";
RL   Mar. Genomics 0:0-0(2012).
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:EKK04206.1}.
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DR   EMBL; AMCW01000012; EKK04206.1; -; Genomic_DNA.
DR   PATRIC; fig|993517.3.peg.445; -.
DR   Proteomes; UP000007993; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR   CDD; cd03603; CLECT_VCBS; 1.
DR   Gene3D; 2.60.120.380; -; 4.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR034007; CTLD_bac.
DR   InterPro; IPR002105; Dockerin_1_rpt.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR007280; Peptidase_C_arc/bac.
DR   InterPro; IPR011506; Planctomycete_extracellular.
DR   PANTHER; PTHR35533; CONSERVED REPEAT DOMAIN PROTEIN; 1.
DR   PANTHER; PTHR35533:SF13; CONSERVED REPEAT DOMAIN PROTEIN; 1.
DR   Pfam; PF00404; Dockerin_1; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF07595; Planc_extracel; 1.
DR   Pfam; PF04151; PPC; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF89260; Collagen-binding domain; 1.
DR   SUPFAM; SSF63446; Type I dockerin domain; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   4: Predicted;
KW   Lectin {ECO:0000313|EMBL:EKK04206.1}.
FT   DOMAIN          285..383
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1859..1883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..43
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1901 AA;  207145 MW;  DDC70CD383922642 CRC64;
     MADTGSKSPS QQVTQDEGRA LIPGRAQRNR RGRSTHRRNA AANRRRARLE QLESRWMLAA
     DAISDMPEST PLVFASVAEG RDLQIARSTG DLRQTSNRFS LSTEEQTELS LYVNSGGLAL
     TFSATLFDED GNYVTSSDPH AQHDHKSILV PEAGEYLLEV DPSFSSDYAS DYQLRVLQGS
     LPFETESLAP LLSDLQGIGT ASVAGVIASG LHDEDIDSYS LGFLGEGTRV DLTASIPSGG
     TAAPIIELRG PRGIVVDQNP ARGKVEAVVP SAGTYEVRVR QETVFGDSQY KSRGRNTKIE
     AEQLAHESGG HLLAINSAEE QSLFEPIESE TWIGISLGEH ESVDSLRWSS GEEITYTNWR
     EGEPALHSHE SRGDGVMDQS GKWALKQVFS YISKTTIIEL PRNEDDPVSS FAGPDALYLL
     DVVVTDADAP QVVSVSGIPT HDIVADSPLI ELGFEFSEPV QATGDLKHIV DLREAGVDGE
     FFTDDDRLFQ TTSKLDSPTE LVVCIMDGPI ADGHYQISIS DQLTDLFGNP LAAGAGYSKS
     FEIAIDTKRF IFEGVDNDTM ETATPIPLTP DLGGTGLSHT TRTGLGLISQ YGDPDYWTFD
     VAAASEIAVR ITGSGRGLTL LDADENVLAQ GNNVINAVSL PKAGQYFVLL SGSLGSDANA
     PYQLSLDVSQ SITLETDSRQ SNINPTTEDI EFNETTNPRL ATVAGALSVG SDSPQDRFSL
     GTLNAGSTVS LRSILPHWST LKPFVELYRG YERVLDINVS EEVFEGTIAT DGMYYAVVRA
     DTGYGLHGQY ILDIEIDDDI APKLLGTPGL PAADEAGTEL IGRFALNFSE EVLLENDSID
     LREAGDDGQF DTDDDRSFYV ELTGDETNSY FEFIVSDGPL DTGQFRLKLD ADITDLSGNT
     LDGDNAVTQF FQLNAVDNTE IFEGFDNGQR DRATVLPLEL DPTGTGFSRT PRSGVGLIET
     FNDTDWWSFE AEASQTIRVT LTTEMIKSLD LTVTDSEGHT IAGTLAMHQQ VDESTLVNRF
     QVPSDGEYYI QIQKRHLIYS EHQRDYELRI DTVAGQALES REQANQHKGH GNTIVLNSTP
     DGSLKGSIAG TLLTADRDTY KLGSLEPNLQ VRFTIDRPEW SQVEPVIGLY GVGSAFTEIS
     PDEDGSFRAL TTDRGEYEVL VAANPEGNGA GFDGQYVLNV EVIETVPFRV TEIRGLPSGN
     GETDQMLSDF EVTFNRNLSE DSFESSDVAI VEAGADGQFG TSDDHSYALR HEFAYAHGKA
     QRDRLLFSVD SGVNVLREGN YRLHLPASFQ SRYGEPLEEG DGYSTDFSIG ELPDGYLVEG
     PTNDDRTGAV HLDPEAPGSN WLVRGIGSLE RDDDIDHWSI DASAGDWVTV WTPNRSSSYF
     ATSGLSNEAG QYMTASSRHH QYPQQGAFQH YVIPTDGTYF VAVEGNTAQL PNDRLYELWV
     HIAPLADGGT PVEGYHRDHP IFQTTDRGET AVVADSFISD ESGSFYPYHE TTYDIGHLPE
     HTDIRIDTRS TTWTFANPFL LLDPIANRKS QRFVVTGTIT DQLGTELTIG PSNLYPGHVP
     NSQQRADYIV EIQSFDVTAP KISLDIETDS DTHYVRASAS DSDELGRQGS GVAQLSLFSI
     HDGLLSHRQA GTTNRIEHTI TSAHASHFFA TATDRIGNRS ILDLSDQDLG PISIDSAIAD
     NSLVTWPSQI IVGSGTSLTW SGQWDVLLPI VRDNRLYHRV TAGDQVIELE AVSEDQNPVL
     AYDVDRSGSV SAIDALLVIN HLNSEQAQTG TWLSLGGLYF DVNGDSRFSP LDALQIINQL
     RFGPTSGESE FIPIEQTAPQ TFICRFAPSD DSHETIHSVN DPAIQAQATN QFIDATPAVP
     ASQSLSELGT STRDEPRMPL DPTTVDEVLT SSISSDLKHL V
//