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Database: UniProt
Entry: F2TWZ6_SALR5
LinkDB: F2TWZ6_SALR5
Original site: F2TWZ6_SALR5 
ID   F2TWZ6_SALR5            Unreviewed;      1724 AA.
AC   F2TWZ6;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Chitin-binding protein {ECO:0000313|EMBL:EGD75905.1};
GN   ORFNames=PTSG_00614 {ECO:0000313|EMBL:EGD75905.1};
OS   Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC   Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX   NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN   [1] {ECO:0000313|Proteomes:UP000007799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "Annotation of Salpingoeca rosetta.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; GL832956; EGD75905.1; -; Genomic_DNA.
DR   RefSeq; XP_004998081.1; XM_004998024.1.
DR   STRING; 946362.F2TWZ6; -.
DR   EnsemblProtists; EGD75905; EGD75905; PTSG_00614.
DR   GeneID; 16078677; -.
DR   KEGG; sre:PTSG_00614; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   InParanoid; F2TWZ6; -.
DR   OrthoDB; 1453590at2759; -.
DR   Proteomes; UP000007799; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 4.
DR   CDD; cd00110; LamG; 1.
DR   Gene3D; 2.60.120.200; -; 3.
DR   Gene3D; 2.10.25.10; Laminin; 8.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 1.
DR   Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
DR   InterPro; IPR026823; cEGF.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR003609; Pan_app.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   InterPro; IPR048287; TSPN-like_N.
DR   PANTHER; PTHR24034:SF195; CHITINASE; 1.
DR   PANTHER; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF07645; EGF_CA; 4.
DR   Pfam; PF14670; FXa_inhibition; 1.
DR   Pfam; PF13385; Laminin_G_3; 1.
DR   Pfam; PF00090; TSP_1; 1.
DR   SMART; SM00032; CCP; 3.
DR   SMART; SM00181; EGF; 7.
DR   SMART; SM00179; EGF_CA; 7.
DR   SMART; SM00209; TSP1; 2.
DR   SMART; SM00210; TSPN; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS01186; EGF_2; 4.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01187; EGF_CA; 4.
DR   PROSITE; PS50948; PAN; 1.
DR   PROSITE; PS50923; SUSHI; 1.
DR   PROSITE; PS50050; TNFR_NGFR_2; 1.
DR   PROSITE; PS50092; TSP1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007799};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..1724
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003290061"
FT   DOMAIN          293..337
FT                   /note="TNFR-Cys"
FT                   /evidence="ECO:0000259|PROSITE:PS50050"
FT   REPEAT          293..337
FT                   /note="TNFR-Cys"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT   DOMAIN          634..674
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          718..790
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          830..865
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          940..977
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          978..1019
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1639..1724
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DISULFID        834..844
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        988..1005
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1724 AA;  183047 MW;  CB246EF275DE2F19 CRC64;
     MRLAVASVVV AAAMLFAAAV TTVPVALAQS DPCSQTCTGD TYEETPCVDP VPSILLDYEA
     GVTQPDITVV GDWNEFEQSG DNAFFGFFGD HFYLLNRVRN TGYGMFSFSV DREADYNISI
     SYVYFSTSPG AFTDSQRYDV HTDGSRAGTF YIDQQQPPPD GNLTLLGQFH IEQSGYVFLN
     ATVKDTSQTT VTASLDAVYI TPADQAVADG SPPVCLPLRV CQDYEYETVA ATATSNRQCA
     LVRNCTVSVE YETVAPTATS NRDCATLRTC NATEYETVAP TPTSNRDCAI IEVCADDQYE
     TQAPTPTSDR FCDDCDVCDD ATQITDANCT STTNTMCRNI TEPYQYSPWS DWSQSCGTQE
     RTRVETCADV KCLDQKPTRQ TRSINGGCDD VCDDTMGQIE CSCTPPSYLI DAYNCSSVYC
     DIPTIANATA SATGQLRLDE QALITCSSGY ESVAYGTSFT ITCTEMGLMN DTETCDDVDE
     CAVNNGGCAD MCTNLPGTFC CSQDGVYVYS EWSDWSTTCG EGTRTRTRTC NATCGGSCTN
     DQPLMETRDI CCPVNANYTY GPFPDWMPTC ARQTRERPES CTASCGGVCT NRINTTQVLT
     NGGCEQICNA TSGAIVCDCD PGYRLTSDNA TCEEFNPCDE NNGGCSHTCV AMPLGQFECT
     CPSGFEAVDG FNCEDVDECA VNNGGCFQNC NNTAGDYFCS CVDGFMVDPS NSSHCVRINC
     ANPPPTLPAS IPSVTARLNG TGPYQFGDEL PYVCEDGFTV DGGAASATSF SLFCRASGMV
     DGQFADGCVD VDECSTNNGG CTDGCVNFAG GFNCTCPTGY RLTDGFRCVE INECMEDSPC
     DHICTNTAGS FECACRTGFF LETSDNRTCT RVPCGPPPAE QLNATASNSA PAVAVYEDVV
     VYNCYDGYTT NGDAGGSSFF FAVCQASGVL SPLVSIACLD VDECLSSPCD QLCDNTLGSF
     TCSCLPGYTN TSATTCEDID ECDDPSSCAL DDNTMCVNTD GAFTCECIAG YTRYNNTCQQ
     QTHNLLDPLL SSGVVASPTA PQRFADDWVY FDGKGALEIT QPLFIGETFS LTAQVQIVPG
     TGGYIFAVTS ATGSTRHFAL YVYELTQRVG VYYRTDSDAS TLAVFQLDSP LDDGALHNIV
     LNVQAQSVSL QIDANTTTYT QNLGATISFC DPGPDCKIYI GQRASSAGGA YRLEGIIRHL
     RINALSTSDL VPIEDYPSPS AAGPSVIDLL DASNRNVVGS VSADADGALV FDGQSAVVIP
     RFHAVPLGAT STFTVTLTVN QDRNTNGYFV AKTDAIGGRF WSLYSSATSN RVSFYYKTSG
     STAQQSASFS VSLADGLYHR VMLAVNNATA QLYVDGSLAG TSSLSGRVQD CSPPSSSCIL
     QLGRRTDASS SDGLFFLSGA IASASVYSGV FMTADPTAVA PTPALDQQLP ISNASGLAYL
     DLLNDTVGFS VGAVRGTEGA TFDGSSRLEV TEHSFSLGPT LSVVGTLRAD TGTAGYIFAK
     TSQDGNTRHL ALYMSALSRL TLYYTSTAST SSRNLLFFPD VQLADGVVHS FLLQLVYTAQ
     TDTTAVNLYV DGRMQTQQSF QGQLTDCGAR SATCGLAVGQ RLDDNAAGGA FGMTGLIQLL
     QLFPHGQLSL ADAPSVSLAS PPYFSVLPAH YIPGQNQGGA YREGVSLEAC ARMCLDDALC
     LSFDAGTVGG SMEGSCFLSY VAAGDTGATA LVESSLFAYY ERLS
//
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