1SZH


Conserved Protein Domain Family
Caenor_Her-1
?
pfam09232: Caenor_Her-1 
Click on image for an interactive view with Cn3D
Caenorhabditis elegans Her-1
Her-1 adopts an all-helical structure with two subdomains: residues 19-80 comprise a left-handed three-helix bundle with an overhand connection between the second and third helices, whilst residues 81-164 comprise a left-handed anti-parallel four-helix bundle in which the first helix consists of four consecutive turns of 3-10-helix. Fourteen Cys are conserved in all known HER-1 sequences and form seven disulfide bonds. The protein dictates male development in Caenorhabditis elegans, probably by playing a direct role in cell signaling during C. elegans sex determination. It also inhibits the function of tra-2a.
Links
?
Statistics
?
PSSM-Id: 370376
Aligned: 6 rows
Threshold Bit Score: 181.553
Created: 23-Mar-2022
Updated: 17-Oct-2022
Structure
?
Program:
Drawing:
Aligned Rows:
Download Cn3D
PubMed ReferencesClick to see Conserved Features Help
Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection: 
1SZH_A        18 CCTRNRQECCIEIMKFGTPIRC-GYDRDPKLPGYVYKCLQNVLFAKEPKK--KINLDDSVCCSVFGNDQEDSGRRCENRC 94  Caenorhabditis ...
EGT35368      32 CCTPKRQECCMEMIKFGSPINC-GYEKHPKFPKVVYDCLQGQLFPNEPEK--RMELEDSGCCSVYHHDQNDPNRRCEHIC 108
CAP36615      33 CCTPNRYECCMDMIKFGTPIKC-GYERDLKIPALVYNCMQQELFAQEPEK--RMNLDDSVCCTVFGQDLNDPNRRCESIC 109
EFO96721      29 CCVKK-EECCREVIRFGLPVRC-RYEKEKELPRIVYNCLQKELFDKEEEKhqRVELDDIVCCQVFLKDKFDPKGRCERIC 106
XP_001899958  38 CCSKEYAECCTESVNFAKPLRCdGMKLGARIN--VTLCIQKELHGEYQPM---LNLTDTVCCDVFADDDNDEKEYCLTEC 112
PDM84004      32 CCPAAAFQCCYNAIDFNLRLSCaQIPDVNRTDNEMIRCVQTELHGENDTM--ETGIGHLGCCQTFKNDQTDPRSMCYVTC 109

1SZH_A        95 KNLMTSPSIDAATRLDSIKSCSLL--DNVLYKCFEKCRSLRKD-GIKIEVLQFEEYC 148 Caenorhabditis elegans
EGT35368     109 KTSLTSPALDAATKISRIQSCTLLdnDNALYGCFEKCQARRRK-GQKIEVLQFSEYC 164
CAP36615     110 KTTMQSPSLDAATKLQKIKDCTLS--ENVLYQCFTKCQMLRRQ-DIKIEVLHFNEYC 163
EFO96721     107 KTAMESPSYSETVKLQRIKECTIV--ENPRFQCFNQCRALRRE-GINIEVMRQDEYC 160
XP_001899958 113 ITVMQIPALRNDRKLKRIKECRRT---NPLYKCFNRCLQWLHS-RTEDEAFDFEQEC 165
PDM84004     110 RFFLHTPSFNSSEKLYMIEECRLT---NPLYTCFNDCRTVHNEnKAKGEMLtmynet 163
| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap