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3.E.1.8.3 Homologue of anion-specific light-gated channel rhodopsin of 461 aas and 7 putative TMSs, lacking apparent channel activity (Govorunova et al. 2015). There are 7 N-terminal TMSs followed by a hydrophilic C-terminal half, residues 241 to end.
Accession Number:	L1JUU4
Protein Name:	Uncharacterized protein
Length:	461
Molecular Weight:	51474.00
Species:	Guillardia theta CCMP2712 [905079]
Number of TMSs:	4
Substrate

UniProt (Universal Protein Resource)
CDD Search (Conserved Domain Database)

Predict TMSs (Predict number of transmembrane segments)

FASTA formatted sequence

1:	MSVVYGEWAA QNPSCVTLSN IDLGVRTFEL CWGIMCACQA VFFALRYPRG TWEFVLVPLT 
61:	ECFVYGLGYS EIGYILLWDG RQVLWTRTVL WLATVPIILN QINGMAAVRI YGVDLNVMQM 
121:	YFSTLMICFG HTAALTHNQS LKWLFFIIAM AIFGLICFIN YHTFTAAEKH YKESGSEIDL 
181:	IIAKRIRLLA VIFFTSWTMY PLFFVLSVEG ACVASESVIL VCFALADLLS KNVFGVLFWD 
241:	TLWNLQDGKW SSYGTVTFFK TTDSVTKTAI STAMEEEFAK QKASRSDNPP AQYPFALPDA 
301:	ENSIEQELSQ LKQMNHTMMA TRQFSSLDHL NDFEHSDQRY APGVNAMPNG SPGSAGSQGV 
361:	ENPVQLSAIT KTGAIHSMDD VVDHVRSLNQ ALSDLLVTDD QPIRPPRRSN VGSTQPTGLT 
421:	GSENSTTGMY NVNTTPVLHS FTRNSFVRNS QTESPAPEYL R

3.E.1.8.3
Homologue of anion-specific light-gated channel rhodopsin of 461 aas and 7 putative TMSs, lacking apparent channel activity (Govorunova et al. 2015). There are 7 N-terminal TMSs followed by a hydrophilic C-terminal half, residues 241 to end.

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3.E.1.8.3Homologue of anion-specific light-gated channel rhodopsin of 461 aas and 7 putative TMSs, lacking apparent channel activity (Govorunova et al. 2015). There are 7 N-terminal TMSs followed by a hydrophilic C-terminal half, residues 241 to end.

Cross database links:

External Searches:

Analyze:

3.E.1.8.3
Homologue of anion-specific light-gated channel rhodopsin of 461 aas and 7 putative TMSs, lacking apparent channel activity (Govorunova et al. 2015). There are 7 N-terminal TMSs followed by a hydrophilic C-terminal half, residues 241 to end.