ID A0A139WWH3_9CYAN Unreviewed; 815 AA.
AC A0A139WWH3;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=DUF4347 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=WA1_44765 {ECO:0000313|EMBL:KYC36788.1};
OS Scytonema hofmannii PCC 7110.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC Scytonema.
OX NCBI_TaxID=128403 {ECO:0000313|EMBL:KYC36788.1, ECO:0000313|Proteomes:UP000076925};
RN [1] {ECO:0000313|EMBL:KYC36788.1, ECO:0000313|Proteomes:UP000076925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7110 {ECO:0000313|EMBL:KYC36788.1,
RC ECO:0000313|Proteomes:UP000076925};
RX PubMed=23221676; DOI=10.1093/gbe/evs117;
RA Dagan T., Roettger M., Stucken K., Landan G., Koch R., Major P.,
RA Gould S.B., Goremykin V.V., Rippka R., Tandeau de Marsac N., Gugger M.,
RA Lockhart P.J., Allen J.F., Brune I., Maus I., Puhler A., Martin W.F.;
RT "Genomes of Stigonematalean cyanobacteria (subsection V) and the evolution
RT of oxygenic photosynthesis from prokaryotes to plastids.";
RL Genome Biol. Evol. 5:31-44(2013).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:KYC36788.1}.
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DR EMBL; ANNX02000047; KYC36788.1; -; Genomic_DNA.
DR RefSeq; WP_017744833.1; NZ_KQ976354.1.
DR AlphaFoldDB; A0A139WWH3; -.
DR STRING; 128403.WA1_44765; -.
DR OrthoDB; 466259at2; -.
DR Proteomes; UP000076925; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR Gene3D; 2.60.40.2030; -; 1.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 1.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR025592; DUF4347.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR003995; RTX_toxin_determinant-A.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR NCBIfam; NF041518; choice_anch_Q; 1.
DR PANTHER; PTHR38340; S-LAYER PROTEIN; 1.
DR PANTHER; PTHR38340:SF1; S-LAYER PROTEIN; 1.
DR Pfam; PF03160; Calx-beta; 1.
DR Pfam; PF14252; DUF4347; 1.
DR Pfam; PF00353; HemolysinCabind; 2.
DR PRINTS; PR00313; CABNDNGRPT.
DR PRINTS; PR01488; RTXTOXINA.
DR SUPFAM; SSF51120; beta-Roll; 1.
DR SUPFAM; SSF141072; CalX-like; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000076925};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Toxin {ECO:0000256|ARBA:ARBA00022656};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 13..182
FT /note="DUF4347"
FT /evidence="ECO:0000259|Pfam:PF14252"
FT DOMAIN 510..601
FT /note="Calx-beta"
FT /evidence="ECO:0000259|Pfam:PF03160"
SQ SEQUENCE 815 AA; 84142 MW; 471519EA2AAD0286 CRC64;
MTQQNNHIQE LNLVFIDPTV LNYQNLIASV KSDHQVVILD STKDGVAQIS EFLQTNPFLK
EGGVVKSIHL TSHGIKAGLQ LGSTQLNSDT LKSHDKDLQH WAKALSDDAD ILLYGCDVAF
GEEGKTFILQ LSQLTGADII ASDDLTGNAA LGGDWNLEVV TGSIEASLAF QSEVMEAYGE
VLSQFIVTNT NDSGVGSLRQ AILNSNSTSG TQDIVFSLPT SAIVNLASAL PNLTDSVNII
NSTGAKNLTI RRNSGGDYSI LTINNGQTVN IEGLTLTNGN SEFGGGIYNE GTLAIADSII
SDNQVTQTGG GIYNEGTLTI SNSTISGNTA QVVGGGIGAA TGFSIANSTI SGNTAKFGGG
AIADVIATGT VNISNTTIYN NFSSAGGGGI DLITLTVNIK NSILAGNKND DGEQNFAAPG
NGKIVSFGHN IESGTDAGFT STGDLQNTNP LLAPLADNGG STLTHALLQG SPAINAGDNT
GVLTTDQRGN PRIVDGTVDI GAFEVNPYPS KVSFGAASYH KTEGNSDTTV TIPVTLDSIP
STTVTVPIAI SSSSTATSDN DYSFAPTTLS FNPGVTGTAL TQQLNITIKA DNLPENDETI
VFNFGTIQGA VVGTINTTTL TIAANDASPN TLVGTDGSDE ISGLAGNETI IGKLGSDTIN
AGEGEDTVFG DEIISVADVT SENNDTVKGA NGSDLIFGGD GDDKLYGDAG NDKIWGNDGF
DLIWGGEGND YLTGGQGNDV FVVSSNEGTD TINDFQEYDI IGLVGGLTYA QLSITQILDN
TFIFESSTQK ILAILTGVQS STLTSNRFQD ATANV
//