1DQ3,1AM2,1EF0,1AT0


Conserved Protein Domain Family
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Hedgehog/Intein domain, found in Hedgehog proteins as well as proteins which contain inteins and undergo protein splicing (e.g. DnaB, RIR1-2, GyrA and Pol). In protein splicing an intervening polypeptide sequence - the intein - is excised from a protein, and the flanking polypeptide sequences - the exteins - are joined by a peptide bond. In addition to the autocatalytic splicing domain, many inteins contain an inserted endonuclease domain, which plays a role in spreading inteins. Hedgehog proteins are a major class of intercellular signaling molecules, which control inductive interactions during animal development. The mature signaling forms of hedgehog proteins are the N-terminal fragments, which are covalently linked to cholesterol at their C-termini. This modification is the result of an autoprocessing step catalyzed by the C-terminal fragments, which are aligned here.
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Statistics
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PSSM-Id: 238035
Aligned: 77 rows
Threshold Bit Score: 41.1006
Created: 1-Nov-2000
Updated: 2-Oct-2020
Structure
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protein-splic..thioester
Conserved site includes 4 residues -Click on image for an interactive view with Cn3D
Feature 1:protein-splicing catalytic site
Evidence:
  • Comment:The conserved C, H, H, and N are almost invariant among inteins
  • Comment:Step1 of protein splicing is an N-O or N-S shift that leads to an ester or thioester intermediate. As a result, the N-extein binds to the oxygen of a serine or the sulfur of a cysteine sidechain at the amino-terminal splice junction.
  • Comment:Step 2 of protein splicing is a transesterification in which a nucleophilic residue at the carboxy-terminal splice site attacks the ester/thioester formed in step 1. The result is a branched protein intermediate.
  • Comment:Step 3 of protein splicing is an asparagine cyclization at the C-terminal end of the intein, which causes excision of the intein and results in splicing of the two exteins by an ester bond.
  • Comment:Step 4 of protein splicing is a spontaneous rearrangement in the spliced exteins, which results in formation of a peptide bond.
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Sequence Alignment
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Feature 1      #                                                                             # 
1DQ3_A       1 CIDGKAKIIFE.[4].EHLTTMEEM.[26].IYVKSF.[5].RVVKGKVNVI.[9].TKYEIITN.[2].TKILTSPWHP 100  Pyrococcus furiosus
1168975    448 CLTSDHTVLTT     RGWIPIADV.[ 3].DKVAVL.[5].EMSYQNPQKV.[7].PMYEVKTA.[1].VDLFVTPNHR 517  Chlamydomonas eugametos
1532153    291 CFTGNSKVMTP     AGEKSMADL.[ 3].DMVMTY.[3].KMTYTRVASW.[9].AFIKLTTE.[2].AIIDMTPQHF 361  Caenorhabditis elegans
1532155    346 CFPGDAMVNVY.[1].GGFKRMDEL.[ 3].DWVQAL.[5].QVTFIPVQYW.[9].DFVEFTLD.[2].ETFSLTEKHL 419  Caenorhabditis elegans
7503532    664 CFSSDTLVTTP     SGKKRMDEI.[ 3].DYVLTA.[3].KTHFTPVTLW.[9].EFLTITTE.[2].STLQLTPLHF 734  Caenorhabditis elegans
7510875    314 CFPNDAVVNVY.[1].KAVKRMDEL.[ 3].DWVEAL.[5].DITFLPVKYW.[9].EFLEFSLD.[2].ETFTLTEKHL 387  Caenorhabditis elegans
7521621    230 CFIEGTEVLTK     RGFVDFREL.[ 3].DLVAQY.[5].EISWTKPYAY.[7].SMYRLKHP.[3].WEVVATEGHE 301  Aquifex aeolicus
7496666    421 CFPADAEVNVY.[1].KGVKRMDEL.[ 3].DWVQAL.[3].ETTYSPVKYW.[9].EFVEFLLE.[2].ESFTLTEKHL 492  Caenorhabditis elegans
7507168    961 CFSADSLVTTV     TGQKRMDEL.[ 3].DYVLVP.[4].VLKYEKVEMF.[9].NFVVLYTK.[2].RKLSLTGRHL 1032 Caenorhabditis elegans
7469167    443 CFTAGTLIETP     RGPVPVESL.[ 3].DLVVTR.[5].PVLWSGGRSL.[9].GLLPVAIR.[7].GALLLSPQHA 520  Rhodobacter capsulatus


Feature 1                                                                                     
1DQ3_A     101 FFVL.[ 6].VEKRADEL     KEGDILIGG.[287].GLEVV.[1].HITTTN.[4].FYDLTVE.[1].YQNYLAG 445  Pyrococcus furiosus
1168975    518 MYVN.[10].NLVEASSI.[5].RYKNDAIWN.[306].VNPEV.[5].NDRFVY.[4].VYCLTGP     NNVFYVQ 893  Chlamydomonas eugametos
1532153    362 IYKA.[ 7].ELVYAEDM     TIGDCLMVK.[  1].NEKLV.[2].TISEKS.[6].VYAPMTE     TGDLIVD 423  Caenorhabditis elegans
1532155    420 VFVT.[14].NPVPAERV     NIGDCFYIA.[  8].QRVKV.[1].DINIVQ.[3].IYSPMTS     RGHLLVD 491  Caenorhabditis elegans
7503532    735 MYRT.[16].EAILASYL     EIGDCVILT.[  5].RQEKI.[1].QTTRGL.[3].IYSPLTK     NGRIIVN 805  Caenorhabditis elegans
7510875    388 VYTT.[13].ESISAGKV     NAGDCFYLA.[  8].RLVEI.[1].DIKRVK.[3].IYAPMTS     QGHLLVN 458  Caenorhabditis elegans
7521621    302 FIVR.[15].KLHPYSAI.[8].EVEEYDLWE.[122].ELVKW.[2].HIPKDR.[4].VYYYSTK.[3].NKDFVQA 501  Aquifex aeolicus
7496666    493 VFAT.[12].NPTSTGKI     NIGECFFMA.[  8].QKVQI.[1].DIQRVR.[3].IYAPMTS     LGHLLVN 562  Caenorhabditis elegans
7507168   1033 LPVA.[20].ESKYAEKA     RKGECVLSI.[  7].ADEIV     RVGRMT.[3].IYSPMTV     EGSLIVD 1108 Caenorhabditis elegans
7469167    521 VLAL.[ 5].RLVRARHL.[4].DPRFRIARG.[ 50].WLAGV     VLGTED.[3].VYGPTAR     PLALRRG 628  Rhodobacter capsulatus


Feature 1               ##
1DQ3_A     446 .[3].MIFVHN 454  Pyrococcus furiosus
1168975    894 .[4].AVWTGN 903  Chlamydomonas eugametos
1532153    424 .[2].YASCHN 431  Caenorhabditis elegans
1532155    492      RIHASC 497  Caenorhabditis elegans
7503532    806      DMLASC 811  Caenorhabditis elegans
7510875    459      KIHTSC 464  Caenorhabditis elegans
7521621    502 .[7].RTVVSR 514  Aquifex aeolicus
7496666    563      QIHTSC 568  Caenorhabditis elegans
7507168   1109      GVLSSC 1114 Caenorhabditis elegans
7469167    629 .[1].RLLDPG 635  Rhodobacter capsulatus

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