ID L8LSM8_9CYAN Unreviewed; 1446 AA.
AC L8LSM8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Putative calcium-binding protein {ECO:0000313|EMBL:ELS00659.1};
GN ORFNames=Xen7305DRAFT_00003600 {ECO:0000313|EMBL:ELS00659.1};
OS Xenococcus sp. PCC 7305.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Xenococcaceae;
OC Xenococcus.
OX NCBI_TaxID=102125 {ECO:0000313|EMBL:ELS00659.1, ECO:0000313|Proteomes:UP000011203};
RN [1] {ECO:0000313|EMBL:ELS00659.1, ECO:0000313|Proteomes:UP000011203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7305 {ECO:0000313|EMBL:ELS00659.1,
RC ECO:0000313|Proteomes:UP000011203};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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:ELS00659.1}.
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DR EMBL; ALVZ01000231; ELS00659.1; -; Genomic_DNA.
DR RefSeq; WP_006512211.1; NZ_ALVZ01000231.1.
DR STRING; 102125.Xen7305DRAFT_00003600; -.
DR PATRIC; fig|102125.3.peg.5123; -.
DR eggNOG; COG2755; Bacteria.
DR eggNOG; COG2931; Bacteria.
DR OrthoDB; 504400at2; -.
DR Proteomes; UP000011203; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:InterPro.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 4.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR005638; Pest_crys_C.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR NCBIfam; NF038122; metallo_LGF; 1.
DR PANTHER; PTHR38340; S-LAYER PROTEIN; 1.
DR PANTHER; PTHR38340:SF1; S-LAYER PROTEIN; 1.
DR Pfam; PF03944; Endotoxin_C; 1.
DR Pfam; PF00353; HemolysinCabind; 7.
DR Pfam; PF00059; Lectin_C; 1.
DR PRINTS; PR00313; CABNDNGRPT.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF51120; beta-Roll; 2.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 4.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000011203};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 1082..1193
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
SQ SEQUENCE 1446 AA; 157818 MW; C6BD9B5761FF612C CRC64;
MKINFVYTPD VSFEQMIGYE IASIIWGKLF ADDVEVNILA KTTDQLNSNV IGGAIPEFHE
QHYALFLEYY EADITSIEDQ MAFNALQKGN TIDFLLDGDL VGGNTKLKLT TALAKALGMT
EAISLDRYVL DESENFIDGT IMMNQDFAWD FNYLRDSEGE EDTLDFLSVA LHETGHILGF
TSSLDFSLQE ETLHSGRTEL SNFSPLDLFR FSAGSLAQEN PDGKVNDLSI GETAWFSTDG
GETLSAKMST GKKGDGFQAS HWERRYDPLG IMDPTLWYQE RVSITDLDVL AFDLMGYDLS
SEAENVEDLF ASESLEVLLA QAKVQLADKL GLSVEYLEEH ADVPVSSLEL IGELENAYLD
NNPTEDSSSV DNSSGSDLEN LDDKELKDFF KDLSNLMKKT YEWWAQNNGG GSSSWQELYE
WWAQNNGEGS SSWQELYEWW AQNNGGGSSS WQELYEWWAQ NNDGGSSAWQ ELYEWWSQDN
DGEGSWWQEV FFASQDDGNW EDVELPGASD SKEVGANYYK EITGGNDDDI IGGDLSDDEI
NAKQGDDLID GAEGHDTIKG GAGFDTIFGF DGNDSIMGGE GDDVISGESD NDVLLGEAGA
DVLMGGDHDD YLDGGAGRDF LSGNTGHDVL IGGTEDDALE GGAGKDLLVG GAGEDIGNGG
SGDDFIFGDG YSESFNHNLG DDLSNLKQIF DPANTENAEV TANTNGNDNE TDSMVAGQNP
IRIEAEDLSW SGNYKVMKKN FASGGRLIKN KNNNQAIAGT TTFTGETGTY KIIIGYHDID
LKTGEIQFKL NDNLIDSWQL NKDIDGNKPS SENFTTHTIE NISLTKNQFF TIQNIVSSDK
GGEGSLDYIE FVPVVDLIAT NNLVLGQDPI TVEAESLSWS GNYRATNKGY ASGGGLIQNN
TNDQWIAGED VFTGKTGVYD IVIGYHDIEI DNGTIQFQVN NTQIDSWDLS QNLHTDILAA
GNFTTHRISN VSLNNNDSFT LRSMVNESYY GEGSLDYVKF ILVENPESKD SRDSSPEDID
SPPEAISITP EFELGLNSDV LRGGAGNDGI DGGEGNDMIF GEDELNDSSN ITPPLIENAL
HYGHSSYILS QAGTWEEAQA EAQSYGGNLV TINDAGEEQW LVDNFGFDQN GNFVNEAFWI
GLTDQETEGQ WQWTNGEAMT YNNQSSYSHI ANNEDYGVIN LYEVALNTSW WSNNQTHYST
EWGAESLTAD YSWNGTAWLA PEGHRGIIEI DWSSVGGNDT IFGGNGDDQV YGNTGNDVIY
GDDLSTSISV EFVSTGDSAT SSIETYNDNI FGNGGHDIIK GGAGDDVING TDGIVAGRLE
RDTLEGGAGA DKFILGDGTK AFYATGGAQD YVVIQDFNSS EDTVQLFGVA GDYQKIQQGN
NIHITRNGDL VAILENNNTL SINGSGDWQT TPYLSTFNGS SDLATILGVY STLDLNDSAF
EYVRTV
//
