(data stored in ACNUC32233 zone)

SWISSPROT: B3SAU0_TRIAD

ID   B3SAU0_TRIAD            Unreviewed;      1964 AA.
AC   B3SAU0;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   11-DEC-2019, entry version 62.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDV20211.1};
GN   ORFNames=TRIADDRAFT_32391 {ECO:0000313|EMBL:EDV20211.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Trichoplacidae; Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV20211.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV20211.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
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DR   EMBL; DS985262; EDV20211.1; -; Genomic_DNA.
DR   RefSeq; XP_002117372.1; XM_002117336.1.
DR   STRING; 10228.TriadP32391; -.
DR   EnsemblMetazoa; TriadT32391; TriadP32391; TriadG32391.
DR   GeneID; 6758584; -.
DR   KEGG; tad:TRIADDRAFT_32391; -.
DR   eggNOG; KOG0035; Eukaryota.
DR   eggNOG; COG5069; LUCA.
DR   HOGENOM; HOG000007281; -.
DR   InParanoid; B3SAU0; -.
DR   OMA; FMLNREV; -.
DR   OrthoDB; 543832at2759; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   CDD; cd00014; CH; 2.
DR   Gene3D; 1.10.418.10; -; 2.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF00435; Spectrin; 12.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00150; SPEC; 14.
DR   SUPFAM; SSF47576; SSF47576; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
PE   4: Predicted;
DR   PRODOM; B3SAU0.
DR   SWISS-2DPAGE; B3SAU0.
KW   Actin-binding {ECO:0000256|SAAS:SAAS00782879};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW   Repeat {ECO:0000256|SAAS:SAAS00782917}.
FT   DOMAIN          32..136
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          153..258
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   COILED          592..612
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          767..794
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1297..1317
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1410..1430
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1964 AA;  228390 MW;  40029DFC64B6935A CRC64;
     MNKSTTSPNS DVSRASHFER ARIRTLAAEL EKVQKKTFTK WVNSCLSRVG LNIDNLYSDL
     CDGTVLLRLL EVLSGEKLPK PARGRMRIHL IQNLNAVLKF LIHKHVKLEN IGAHDIVDGN
     QRIILGLIWT IILRFQIQDI RIEGETTEST EKRSAKDALL VWCKLKTANY TNVRVTNFTS
     SWRNGLAFNA LIHKHRPDVV DYDRLSPDNA LENLRLAFTV ADECFGIAPL LDAEDICVEN
     PDEKSIMTYV ASYYQSFSKL KAENVVERRI WKVMNCIMDL EKMMQEYDTL ASNLLKWIRA
     MIVILSDRQF ENNLDGVQRQ LSEFKTYRTV DKPLRYLEKG TLEEKFFTIQ SKLRSNNRKG
     FIPVADKTIS DINKSWEQLE NAEHDREQAL REEIIRQERL ERLADKFTKK AEMRVQWICD
     SVRLVDNDIF GDSGSSVSAA LKKQEAFEAD VYEYQKRIRA MEDLVQELKI GNYHAIQKIQ
     DKRDKVIILW NELLELIKIR EGKVSQHVEL HDHIQELEDF MGWSRDVKNS LESEDYGLEL
     HDVEDLLQKN LILENEILAQ EEPLTRALLE AENFKAPSKE DGVNFFNSNP MNDLLKERIN
     SLSRLYDQIS ELLYIRKTRL EDSRQLLQFY QNVDDELDWM KGKNQSLSLT DLTKATDCSY
     VIHKLRSHQA LEAEVNNNET LLRNIIDTGN QLSKNNNYDS SMILSKINNL ASAWNNLVDS
     MSKRKDRIAE ILSMQQFLSE ADYLEGQISL HTGLLSVDQN RIDEDNIDSL LKHHANLEFE
     VENYKDQLHL LDNMADDLNP NDQSFEMALG KKAVITEKYQ VLMAEVGYRR EKLIAQQSLF
     RYLSEIDIVF SWIGDKEAVL FSFEPPTNLI EAELILQKFK GIERDIVTYQ DRYNNTLKAG
     NDLAVQITDG NDEIANAQGE LNEKWIRLLE LHGLKKEELS KLLILLRLFY EVDEVKNWIA
     DKGTGLSSCS YTTDPAAVLQ MQRQINVIER ETPAIEERIE DVESKRDALA EEQPDKLEIV
     NDKLDSLYEV WDDLRNLVRN QIATIGECSN IQKLMFDVED LEDWLKFQLG QLSLETDGLN
     SLPDVEKLQA EHNELLEEFT NRKIILDRIN STAPMHYTGD AAGRRLEQRV EDINHDWNDL
     DSLCHKRKVL LQQIQQYLIF QRDCKYIEGI LQKQDVFLAE VMTELGTSNK SANQLKNKDD
     QHLKRLDSCI QRVAQADQFA KLSVDDDHYA KESLMSKAAT LSERVERNRG LFTEIAFRLD
     KAVHLQSFYQ RCNELIDWIN EKFNIISGDI VTDQAYISRL LQKHRTFEAE LAATRDQKNV
     VNELGKSLVQ DQPDARPEVE IHLTDIEDRW ITLMDACSTR SQLLTDRYNE VQFIRIIDNL
     QAWMSDAENT LANMETCKDL ASCNKSMTKL TSLESDIISR KDRLDQLEQQ VQNFLDINHR
     GADDMQDLFE SVSQRYAALQ RPLKERRKLL EASRRMFQFY RDVDDELLWI EDKKQQLQSN
     ETGNNLHEVQ ILRTVQQNIQ NEIRVHEQII NEIFKSGSKV ISDADSSADK IRHNTELLKE
     KWLELEICSR EREAIIEQSA TAHKLLFDTE EMEGWIMEKA AILITKDKPK DQIRAMSMMK
     HHELLEQSVK SYAQNIKSLH QSGQAFLDQS TIKSKEIVEA LDVIDDSYNS LLILASERRN
     FIDELLRFYR YNSEVDEVEQ WIKEREVFSK SKDYGSNLEQ IQRIAETFHS WVVNTKNSGV
     SKVKEVNLIA DQLIITGHPE AATICEWKSG INDLWNQLLE TIQERTKNIE NVATIRDHYA
     AGNDFLHRIR TKGQCLPDDL GNNFDSTECL LHRHSIVQSD VLGIELEYNN LQEYAAQLKV
     DFPNEKQAID ELHGKISDAW ELLKDKCNWR KSQLEQTLDL FRLLLLVENH ALWINDMYDD
     INSLEDPRYW LPSRFCSYSI GFLFKHIIRE FIANSIVQLI RIIK
//

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