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Conserved domains on  [gi|125887166|ref|XP_001331914|]
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protein-glutamine gamma-glutamyltransferase K [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
170-283 1.48e-38

Transglutaminase family;


:

Pssm-ID: 459971  Cd Length: 114  Bit Score: 138.91  E-value: 1.48e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125887166  170 VDLMKcwkSQNRQEHHTNGFRGDHLIVRRGQCFQMWVELSRPFNPKCDQLHLELKLGNVPSIPNGTLVIVPLVEEFKKNR 249
Cdd:pfam00868   3 VDLQK---NENAKAHHTDEYSSDRLIVRRGQPFTITLRFNRPFDPQLDKLTLEFETGPKPSESKGTLVVFPLGKSGDASS 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 125887166  250 WEAKIVEKCQNRIKLSVYSLPTACIGRYSLTIVT 283
Cdd:pfam00868  80 WSARVESISGNSLSVSITSPANAPVGRYTLTVET 113
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 429-520 2.76e-16

Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish covalent links between proteins. A subset of transglutaminase homologues appear to catalyse the reverse reaction, the hydrolysis of peptide bonds. Proteins with this domain are both extracellular and intracellular, and it is likely that the eukaryotic intracellular proteins are involved in signalling events.


:

Pssm-ID: 214673  Cd Length: 68  Bit Score: 73.96  E-value: 2.76e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125887166   429 PVKYGQSLAFAGVTNTLLRCFGIPARPVTNFCSAHDTDVsmtvdiyldenydlidslNRDSIWTFHVWNEAWMArsdlpa 508
Cdd:smart00460   3 KTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIG------------------GLRSIWEAHAWAEVYLE------ 58

                           90
                   ....*....|..
gi 125887166   509 gfGGWQAIDATP 520
Cdd:smart00460  59 --GGWVPVDPTP 68
Transglut_C super family cl08295
Transglutaminase family, C-terminal ig like domain;
761-846 1.17e-09

Transglutaminase family, C-terminal ig like domain;


The actual alignment was detected with superfamily member pfam00927:

Pssm-ID: 460002  Cd Length: 106  Bit Score: 56.20  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125887166  761 VVGKEVPVKITFQNPLPCVLKNAIFRI-----EGLGLKHC---RSINYGDIAGLATVNLTEKFIPKCHGPHKLLASLDCP 832
Cdd:pfam00927  12 VVGQDLTVSVTLSNPLSEPLKDVVLSLsaqtvEYNGVLGAefkKKSLELTLEPGEEKSVPIKITPSKYGPRQLLVEFSSD 91

                          90
                  ....*....|....
gi 125887166  833 QLTQVHGFTDVVVK 846
Cdd:pfam00927  92 ALAKVKGYRNVLVA 105
Cornifin super family cl25524
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
 42-128 5.13e-07

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.


The actual alignment was detected with superfamily member pfam02389:

Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 49.67  E-value: 5.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125887166   42 KPCVDPCWNPCVKPVVDPCG----NPCVKPVVDHCGKPVISPCGKPIVDPCGKPVVDPCGKPIFDPCGKPVVDLCGKPVV 117
Cdd:pfam02389   7 QPCQPPPQEPCVPTTKEPCHskvpEPCNPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCYPKVPEPCSPKVP 86

                          90
                  ....*....|.
gi 125887166  118 GPCVVPLPKPC 128
Cdd:pfam02389  87 EPCHPKAPEPC 97
Transglut_C super family cl08295
Transglutaminase family, C-terminal ig like domain;
639-730 3.33e-04

Transglutaminase family, C-terminal ig like domain;


The actual alignment was detected with superfamily member pfam00927:

Pssm-ID: 460002  Cd Length: 106  Bit Score: 40.79  E-value: 3.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125887166  639 DITMKGDGVcVGKDAVLCIALKNKCSST-RSVTLHSQLSAAYYTGIHKSLVKKDQTCFELKATETKVLEWSLKYEDY--K 715
Cdd:pfam00927   4 KIEVLGSAV-VGQDLTVSVTLSNPLSEPlKDVVLSLSAQTVEYNGVLGAEFKKKSLELTLEPGEEKSVPIKITPSKYgpR 82

                          90
                  ....*....|....*.
gi 125887166  716 NHLVD-HSTMMVTVAG 730
Cdd:pfam00927  83 QLLVEfSSDALAKVKG 98
 
Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
170-283 1.48e-38

Transglutaminase family;


Pssm-ID: 459971  Cd Length: 114  Bit Score: 138.91  E-value: 1.48e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125887166  170 VDLMKcwkSQNRQEHHTNGFRGDHLIVRRGQCFQMWVELSRPFNPKCDQLHLELKLGNVPSIPNGTLVIVPLVEEFKKNR 249
Cdd:pfam00868   3 VDLQK---NENAKAHHTDEYSSDRLIVRRGQPFTITLRFNRPFDPQLDKLTLEFETGPKPSESKGTLVVFPLGKSGDASS 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 125887166  250 WEAKIVEKCQNRIKLSVYSLPTACIGRYSLTIVT 283
Cdd:pfam00868  80 WSARVESISGNSLSVSITSPANAPVGRYTLTVET 113
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 429-520 2.76e-16

Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish covalent links between proteins. A subset of transglutaminase homologues appear to catalyse the reverse reaction, the hydrolysis of peptide bonds. Proteins with this domain are both extracellular and intracellular, and it is likely that the eukaryotic intracellular proteins are involved in signalling events.


Pssm-ID: 214673  Cd Length: 68  Bit Score: 73.96  E-value: 2.76e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125887166   429 PVKYGQSLAFAGVTNTLLRCFGIPARPVTNFCSAHDTDVsmtvdiyldenydlidslNRDSIWTFHVWNEAWMArsdlpa 508
Cdd:smart00460   3 KTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIG------------------GLRSIWEAHAWAEVYLE------ 58

                           90
                   ....*....|..
gi 125887166   509 gfGGWQAIDATP 520
Cdd:smart00460  59 --GGWVPVDPTP 68
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
761-846 1.17e-09

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 56.20  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125887166  761 VVGKEVPVKITFQNPLPCVLKNAIFRI-----EGLGLKHC---RSINYGDIAGLATVNLTEKFIPKCHGPHKLLASLDCP 832
Cdd:pfam00927  12 VVGQDLTVSVTLSNPLSEPLKDVVLSLsaqtvEYNGVLGAefkKKSLELTLEPGEEKSVPIKITPSKYGPRQLLVEFSSD 91

                          90
                  ....*....|....
gi 125887166  833 QLTQVHGFTDVVVK 846
Cdd:pfam00927  92 ALAKVKGYRNVLVA 105
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 431-518 4.76e-09

Transglutaminase-like superfamily; This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterized transglutaminase, the human blood clotting factor XIIIa'. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase, it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease.


Pssm-ID: 376628 [Multi-domain]  Cd Length: 108  Bit Score: 54.72  E-value: 4.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125887166  431 KYGQSLAFAGVTNTLLRCFGIPARPVTNFCSAHDTdvsmtvdiyldenydlidslnrDSIWTFHVWNEAWMarsdlpaGF 510
Cdd:pfam01841  50 GKGDCEDFASLFVALLRALGIPARYVTGYLRGPDT----------------------VRGGDAHAWVEVYL-------PG 100


                  ....*...
gi 125887166  511 GGWQAIDA 518
Cdd:pfam01841 101 YGWVPVDP 108
Cornifin pfam02389
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
 42-128 5.13e-07

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.


Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 49.67  E-value: 5.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125887166   42 KPCVDPCWNPCVKPVVDPCG----NPCVKPVVDHCGKPVISPCGKPIVDPCGKPVVDPCGKPIFDPCGKPVVDLCGKPVV 117
Cdd:pfam02389   7 QPCQPPPQEPCVPTTKEPCHskvpEPCNPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCYPKVPEPCSPKVP 86

                          90
                  ....*....|.
gi 125887166  118 GPCVVPLPKPC 128
Cdd:pfam02389  87 EPCHPKAPEPC 97
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 431-519 7.98e-05

Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 44.23  E-value: 7.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125887166 431 KYGQSLAFAGVTNTLLRCFGIPARPVTNFCSAHDTDVSMTVDiyldenydlidslnrdsiwTFHVWNEAWmarsdLPAgf 510
Cdd:COG1305  112 RRGVCRDFAHLLVALLRALGIPARYVSGYLPGEPPPGGGRAD-------------------DAHAWVEVY-----LPG-- 165


                 ....*....
gi 125887166 511 GGWQAIDAT 519
Cdd:COG1305  166 AGWVPFDPT 174
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
639-730 3.33e-04

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 40.79  E-value: 3.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125887166  639 DITMKGDGVcVGKDAVLCIALKNKCSST-RSVTLHSQLSAAYYTGIHKSLVKKDQTCFELKATETKVLEWSLKYEDY--K 715
Cdd:pfam00927   4 KIEVLGSAV-VGQDLTVSVTLSNPLSEPlKDVVLSLSAQTVEYNGVLGAEFKKKSLELTLEPGEEKSVPIKITPSKYgpR 82

                          90
                  ....*....|....*.
gi 125887166  716 NHLVD-HSTMMVTVAG 730
Cdd:pfam00927  83 QLLVEfSSDALAKVKG 98
 
Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
170-283 1.48e-38

Transglutaminase family;


Pssm-ID: 459971  Cd Length: 114  Bit Score: 138.91  E-value: 1.48e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125887166  170 VDLMKcwkSQNRQEHHTNGFRGDHLIVRRGQCFQMWVELSRPFNPKCDQLHLELKLGNVPSIPNGTLVIVPLVEEFKKNR 249
Cdd:pfam00868   3 VDLQK---NENAKAHHTDEYSSDRLIVRRGQPFTITLRFNRPFDPQLDKLTLEFETGPKPSESKGTLVVFPLGKSGDASS 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 125887166  250 WEAKIVEKCQNRIKLSVYSLPTACIGRYSLTIVT 283
Cdd:pfam00868  80 WSARVESISGNSLSVSITSPANAPVGRYTLTVET 113
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 429-520 2.76e-16

Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish covalent links between proteins. A subset of transglutaminase homologues appear to catalyse the reverse reaction, the hydrolysis of peptide bonds. Proteins with this domain are both extracellular and intracellular, and it is likely that the eukaryotic intracellular proteins are involved in signalling events.


Pssm-ID: 214673  Cd Length: 68  Bit Score: 73.96  E-value: 2.76e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125887166   429 PVKYGQSLAFAGVTNTLLRCFGIPARPVTNFCSAHDTDVsmtvdiyldenydlidslNRDSIWTFHVWNEAWMArsdlpa 508
Cdd:smart00460   3 KTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIG------------------GLRSIWEAHAWAEVYLE------ 58

                           90
                   ....*....|..
gi 125887166   509 gfGGWQAIDATP 520
Cdd:smart00460  59 --GGWVPVDPTP 68
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
761-846 1.17e-09

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 56.20  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125887166  761 VVGKEVPVKITFQNPLPCVLKNAIFRI-----EGLGLKHC---RSINYGDIAGLATVNLTEKFIPKCHGPHKLLASLDCP 832
Cdd:pfam00927  12 VVGQDLTVSVTLSNPLSEPLKDVVLSLsaqtvEYNGVLGAefkKKSLELTLEPGEEKSVPIKITPSKYGPRQLLVEFSSD 91

                          90
                  ....*....|....
gi 125887166  833 QLTQVHGFTDVVVK 846
Cdd:pfam00927  92 ALAKVKGYRNVLVA 105
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 431-518 4.76e-09

Transglutaminase-like superfamily; This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterized transglutaminase, the human blood clotting factor XIIIa'. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase, it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease.


Pssm-ID: 376628 [Multi-domain]  Cd Length: 108  Bit Score: 54.72  E-value: 4.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125887166  431 KYGQSLAFAGVTNTLLRCFGIPARPVTNFCSAHDTdvsmtvdiyldenydlidslnrDSIWTFHVWNEAWMarsdlpaGF 510
Cdd:pfam01841  50 GKGDCEDFASLFVALLRALGIPARYVTGYLRGPDT----------------------VRGGDAHAWVEVYL-------PG 100


                  ....*...
gi 125887166  511 GGWQAIDA 518
Cdd:pfam01841 101 YGWVPVDP 108
Cornifin pfam02389
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
 42-128 5.13e-07

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.


Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 49.67  E-value: 5.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125887166   42 KPCVDPCWNPCVKPVVDPCG----NPCVKPVVDHCGKPVISPCGKPIVDPCGKPVVDPCGKPIFDPCGKPVVDLCGKPVV 117
Cdd:pfam02389   7 QPCQPPPQEPCVPTTKEPCHskvpEPCNPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCYPKVPEPCSPKVP 86

                          90
                  ....*....|.
gi 125887166  118 GPCVVPLPKPC 128
Cdd:pfam02389  87 EPCHPKAPEPC 97
Cornifin pfam02389
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
 32-136 1.21e-06

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.


Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 48.51  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125887166   32 YVPVYSNPCVKPCVDPCW----NPCVKPVVDPCG----NPCVKPVVDHCGKPVISPCGKPIVDPCGKPVVDPCGKPIFDP 103
Cdd:pfam02389  17 CVPTTKEPCHSKVPEPCNpkvpEPCCPKVPEPCCpkvpEPCCPKVPEPCCPKVPEPCYPKVPEPCSPKVPEPCHPKAPEP 96

                          90       100       110
                  ....*....|....*....|....*....|...
gi 125887166  104 CGKPVVDLCGKPVVGPCVVPLPKPCvnPCDVRP 136
Cdd:pfam02389  97 CHPKVPEPCYPKAPEPCQPKVPEPC--PSTVTP 127
Cornifin pfam02389
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
 39-128 1.36e-06

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.


Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 48.51  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125887166   39 PCVKPCVDPCWNPCVKPVVDPCG----NPCVKPVVDHCGKPVISPCGKPIVDPCGKPVVDPCGKPIFDPCGKPVVDLCGK 114
Cdd:pfam02389  12 PPQEPCVPTTKEPCHSKVPEPCNpkvpEPCCPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCYPKVPEPCSPKVPEPCHP 91

                          90
                  ....*....|....
gi 125887166  115 PVVGPCVVPLPKPC 128
Cdd:pfam02389  92 KAPEPCHPKVPEPC 105
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 431-519 7.98e-05

Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 44.23  E-value: 7.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125887166 431 KYGQSLAFAGVTNTLLRCFGIPARPVTNFCSAHDTDVSMTVDiyldenydlidslnrdsiwTFHVWNEAWmarsdLPAgf 510
Cdd:COG1305  112 RRGVCRDFAHLLVALLRALGIPARYVSGYLPGEPPPGGGRAD-------------------DAHAWVEVY-----LPG-- 165


                 ....*....
gi 125887166 511 GGWQAIDAT 519
Cdd:COG1305  166 AGWVPFDPT 174
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
639-730 3.33e-04

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 460002  Cd Length: 106  Bit Score: 40.79  E-value: 3.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125887166  639 DITMKGDGVcVGKDAVLCIALKNKCSST-RSVTLHSQLSAAYYTGIHKSLVKKDQTCFELKATETKVLEWSLKYEDY--K 715
Cdd:pfam00927   4 KIEVLGSAV-VGQDLTVSVTLSNPLSEPlKDVVLSLSAQTVEYNGVLGAEFKKKSLELTLEPGEEKSVPIKITPSKYgpR 82

                          90
                  ....*....|....*.
gi 125887166  716 NHLVD-HSTMMVTVAG 730
Cdd:pfam00927  83 QLLVEfSSDALAKVKG 98
Cornifin pfam02389
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
 76-128 9.49e-03

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.


Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 37.34  E-value: 9.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 125887166   76 VISPCGKPIVDPCGKPVVDPCGKPIFDPCGKPVVDLCGKPVVGPCVVPLPKPC 128
Cdd:pfam02389   5 VKQPCQPPPQEPCVPTTKEPCHSKVPEPCNPKVPEPCCPKVPEPCCPKVPEPC 57
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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