(data stored in ACNUC9306 zone)

HOGENOM: TRIAD_1217_PE298

ID   TRIAD_1217_PE298                     STANDARD;      PRT;   553 AA.
AC   TRIAD_1217_PE298; B3RY21;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   Flags: Fragments;
DE   SubName: Full=Putative uncharacterized protein;Flags: Fragment;
DE   (TRIAD_1217.PE298).
GN   ORFNames=TRIADDRAFT_25177;
OS   TRICHOPLAX ADHAERENS.
OC   Eukaryota; Metazoa; Placozoa; Trichoplax.
OX   NCBI_TaxID=10228;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS TRIAD_1217.PE298.
CC       Trichoplax adhaerens scaffold scaffold_5 TRIAD1  sequence 1..8573113
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:B3RY21_TRIAD
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- GENE_FAMILY: HOG000007113 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Trichoplax_adhaerens;TRIADG25177;TRIADT25177;TRIADP25177.
DR   EMBL; DS985245; - ;
DR   UniProtKB/Swiss-Prot; B3RY21; -.
DR   EMBL; DS985245; EDV24958.1; -; Genomic_DNA.
DR   RefSeq; XP_002112848.1; XM_002112812.1.
DR   EnsemblMetazoa; TriadT25177; TriadP25177; TriadG25177.
DR   GeneID; 6754061; -.
DR   KEGG; tad:TRIADDRAFT_25177; -.
DR   OMA; AIQPNTS; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR011174; ERM.
DR   InterPro; IPR011259; ERM_C.
DR   InterPro; IPR000798; Ez/rad/moesin.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR008954; Moesin.
DR   InterPro; IPR011993; PH_type.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00769; ERM; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   PIRSF; PIRSF002305; ERM; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   SUPFAM; SSF48678; Moesin; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   HOGENOMDNA; TRIAD_1217.PE298; -.
KW   TriadG251773.19671820036002503210000011;
KW   B3RY21; DS985245.
SQ   SEQUENCE   553 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     VNVRVTSLDS ELEFAIQPNT SGKQLFDQVC KTLGIREVWY FGLRFLDSKG QLSWLRLEKK
     VSAQDIKKEV PLQFKFRVEF FPEDVSEELI EDVTQKLFFL QVKEGIINDD VYCPPETAVL
     LASYAVQAKF GDYDKDTHKD GYLSNEKLLP KRVLDQHKLD SRQWEERISN WHSEHKNMLK
     EEAMMEYLKI AQDLEMYGVN YYDIKNKKGS DLWLGVDALG INVYEHEDRL TPKIGFPWSE
     IRNISFSEKK FVIKPIDRKS PDFNFYVPRV KLNKHILALC MGNHELFIRR RKPDTVEIQQ
     MKTTAKDLRN AKRSEKAQFL REQQARLDAE KQRLELEEKM KKFEEDQKIV QNSLKKTEEG
     SKELAEKARK AEEETRRLEE IKKQIEEEKK KLEKIAAEDR ERLLEKNEEI KRLSEAAARA
     EEAVAMAEEA AAKAAEEARA RAAEEAYQNN NLAEPQYEEG TDAGSSQLID DETDEVPMTQ
     EIDRVALAER NKRLMEQLKL LGNELIGIRD NSKDTTMDHL HAENVKQGRD KYKTLKQIRQ
     GNTKKRVNDF EQL
//

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