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Conserved domains on  [gi|215274164|sp|P16452|]
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RecName: Full=Erythrocyte membrane protein band 4.2; Short=Erythrocyte protein 4.2; Short=P4.2

Protein Classification

Transglut_N and Transglut_C domain-containing protein (domain architecture ID 10467682)

protein containing domains Transglut_N, TGc, and Transglut_C

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
5-124 2.04e-52

Transglutaminase family;


:

Pssm-ID: 334292  Cd Length: 117  Bit Score: 176.56  E-value: 2.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274164    5 LGIKSCDFQAARNNEEHHTKALSSRRLFVRRGQPFTIILYFRapvRAFLPALKKVALTAQTGEQPSKINRTQATFPISSL 84
Cdd:pfam00868   1 LEVKSVDLQKEENNKEHHTDEYESDRLIVRRGQPFTITLTFN---RPFDPSKDKLRLEFETGPNPSESKGTKAVFPLSSS 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 215274164   85 GDRKWWSAVVEERDAQSWTISVTTPADAVIGHYSLLLQVS 124
Cdd:pfam00868  78 RDPSGWSARVVESSGNSLTVSVTSPANAPIGRYRLTVETS 117
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
588-686 2.90e-25

Transglutaminase family, C-terminal ig like domain;


:

Pssm-ID: 307191  Cd Length: 106  Bit Score: 100.49  E-value: 2.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274164  588 PHLAIKMPEKAEQYQPLTASVSLQNSLDAPMEDCVISI-----LGRGLIHRE--RSYRFRSVWPENTMCAKFQFTPTHVG 660
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSLsaqtvEYNGVLGAEfkKKSLELTLEPGEEKSVPIKITPSKYG 80
                          90       100
                  ....*....|....*....|....*.
gi 215274164  661 LQRLTVEVDCNMFQNLTNYKSVTVVA 686
Cdd:pfam00927  81 LRQLLVEFSSDALKKVKGYRNVLVAQ 106
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
475-580 1.83e-20

Transglutaminase family, C-terminal ig like domain;


:

Pssm-ID: 307191  Cd Length: 106  Bit Score: 86.62  E-value: 1.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274164  475 LYLLLKAPSSLPLRGDAQISVTLVNHSEQE-KAVQLAIGVQAVHYNGVLAAKLWRKKLHLTLSANLEKIITIGLFFSNF- 552
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPlKDVVLSLSAQTVEYNGVLGAEFKKKSLELTLEPGEEKSVPIKITPSKYg 80
                          90       100
                  ....*....|....*....|....*....
gi 215274164  553 -ERNPPEntfLRLTAMATHSESNLSCFAQ 580
Cdd:pfam00927  81 lRQLLVE---FSSDALKKVKGYRNVLVAQ 106
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
261-352 1.08e-11

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 [Multi-domain]  Cd Length: 68  Bit Score: 60.47  E-value: 1.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274164   261 RPVYDGQAWVLAAVACTVLRCLGIPARVVTTFASAQGTGGRLLideyyneeglqngegqrgRIWIFQTSTECWMTrpalp 340
Cdd:smart00460   2 LKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLR------------------SIWEAHAWAEVYLE----- 58
                           90
                   ....*....|..
gi 215274164   341 qgyDGWQILHPS 352
Cdd:smart00460  59 ---GGWVPVDPT 67
 
Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
5-124 2.04e-52

Transglutaminase family;


Pssm-ID: 334292  Cd Length: 117  Bit Score: 176.56  E-value: 2.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274164    5 LGIKSCDFQAARNNEEHHTKALSSRRLFVRRGQPFTIILYFRapvRAFLPALKKVALTAQTGEQPSKINRTQATFPISSL 84
Cdd:pfam00868   1 LEVKSVDLQKEENNKEHHTDEYESDRLIVRRGQPFTITLTFN---RPFDPSKDKLRLEFETGPNPSESKGTKAVFPLSSS 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 215274164   85 GDRKWWSAVVEERDAQSWTISVTTPADAVIGHYSLLLQVS 124
Cdd:pfam00868  78 RDPSGWSARVVESSGNSLTVSVTSPANAPIGRYRLTVETS 117
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
588-686 2.90e-25

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 307191  Cd Length: 106  Bit Score: 100.49  E-value: 2.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274164  588 PHLAIKMPEKAEQYQPLTASVSLQNSLDAPMEDCVISI-----LGRGLIHRE--RSYRFRSVWPENTMCAKFQFTPTHVG 660
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSLsaqtvEYNGVLGAEfkKKSLELTLEPGEEKSVPIKITPSKYG 80
                          90       100
                  ....*....|....*....|....*.
gi 215274164  661 LQRLTVEVDCNMFQNLTNYKSVTVVA 686
Cdd:pfam00927  81 LRQLLVEFSSDALKKVKGYRNVLVAQ 106
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
475-580 1.83e-20

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 307191  Cd Length: 106  Bit Score: 86.62  E-value: 1.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274164  475 LYLLLKAPSSLPLRGDAQISVTLVNHSEQE-KAVQLAIGVQAVHYNGVLAAKLWRKKLHLTLSANLEKIITIGLFFSNF- 552
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPlKDVVLSLSAQTVEYNGVLGAEFKKKSLELTLEPGEEKSVPIKITPSKYg 80
                          90       100
                  ....*....|....*....|....*....
gi 215274164  553 -ERNPPEntfLRLTAMATHSESNLSCFAQ 580
Cdd:pfam00927  81 lRQLLVE---FSSDALKKVKGYRNVLVAQ 106
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
261-352 1.08e-11

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 [Multi-domain]  Cd Length: 68  Bit Score: 60.47  E-value: 1.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274164   261 RPVYDGQAWVLAAVACTVLRCLGIPARVVTTFASAQGTGGRLLideyyneeglqngegqrgRIWIFQTSTECWMTrpalp 340
Cdd:smart00460   2 LKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLR------------------SIWEAHAWAEVYLE----- 58
                           90
                   ....*....|..
gi 215274164   341 qgyDGWQILHPS 352
Cdd:smart00460  59 ---GGWVPVDPT 67
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
225-351 8.83e-08

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: 334704  Cd Length: 108  Bit Score: 50.48  E-value: 8.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274164  225 QRVLPTPQTQATQEGALLNKRRGSVPILRQWLTGRGRPVYD------GQAWVLAAVACTVLRCLGIPARVVTTFASAQGT 298
Cdd:pfam01841   5 DRITGGATDPLEKARAIYDYVRKNITYDLDGRSPGDGDAEEflftgkGDCEDFASLFVALLRALGIPARYVTGYLRGPDT 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 215274164  299 ggrllideyyneeglqngegqrGRIWIFQTSTECWMtrpalpqGYDGWQILHP 351
Cdd:pfam01841  85 ----------------------VRGGDAHAWVEVYL-------PGYGWVPVDP 108
 
Name Accession Description Interval E-value
Transglut_N pfam00868
Transglutaminase family;
5-124 2.04e-52

Transglutaminase family;


Pssm-ID: 334292  Cd Length: 117  Bit Score: 176.56  E-value: 2.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274164    5 LGIKSCDFQAARNNEEHHTKALSSRRLFVRRGQPFTIILYFRapvRAFLPALKKVALTAQTGEQPSKINRTQATFPISSL 84
Cdd:pfam00868   1 LEVKSVDLQKEENNKEHHTDEYESDRLIVRRGQPFTITLTFN---RPFDPSKDKLRLEFETGPNPSESKGTKAVFPLSSS 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 215274164   85 GDRKWWSAVVEERDAQSWTISVTTPADAVIGHYSLLLQVS 124
Cdd:pfam00868  78 RDPSGWSARVVESSGNSLTVSVTSPANAPIGRYRLTVETS 117
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
588-686 2.90e-25

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 307191  Cd Length: 106  Bit Score: 100.49  E-value: 2.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274164  588 PHLAIKMPEKAEQYQPLTASVSLQNSLDAPMEDCVISI-----LGRGLIHRE--RSYRFRSVWPENTMCAKFQFTPTHVG 660
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPLKDVVLSLsaqtvEYNGVLGAEfkKKSLELTLEPGEEKSVPIKITPSKYG 80
                          90       100
                  ....*....|....*....|....*.
gi 215274164  661 LQRLTVEVDCNMFQNLTNYKSVTVVA 686
Cdd:pfam00927  81 LRQLLVEFSSDALKKVKGYRNVLVAQ 106
Transglut_C pfam00927
Transglutaminase family, C-terminal ig like domain;
475-580 1.83e-20

Transglutaminase family, C-terminal ig like domain;


Pssm-ID: 307191  Cd Length: 106  Bit Score: 86.62  E-value: 1.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274164  475 LYLLLKAPSSLPLRGDAQISVTLVNHSEQE-KAVQLAIGVQAVHYNGVLAAKLWRKKLHLTLSANLEKIITIGLFFSNF- 552
Cdd:pfam00927   1 PEMKIEVLGSAVVGQDLTVSVTLSNPLSEPlKDVVLSLSAQTVEYNGVLGAEFKKKSLELTLEPGEEKSVPIKITPSKYg 80
                          90       100
                  ....*....|....*....|....*....
gi 215274164  553 -ERNPPEntfLRLTAMATHSESNLSCFAQ 580
Cdd:pfam00927  81 lRQLLVE---FSSDALKKVKGYRNVLVAQ 106
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
261-352 1.08e-11

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 [Multi-domain]  Cd Length: 68  Bit Score: 60.47  E-value: 1.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274164   261 RPVYDGQAWVLAAVACTVLRCLGIPARVVTTFASAQGTGGRLLideyyneeglqngegqrgRIWIFQTSTECWMTrpalp 340
Cdd:smart00460   2 LKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLR------------------SIWEAHAWAEVYLE----- 58
                           90
                   ....*....|..
gi 215274164   341 qgyDGWQILHPS 352
Cdd:smart00460  59 ---GGWVPVDPT 67
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
225-351 8.83e-08

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: 334704  Cd Length: 108  Bit Score: 50.48  E-value: 8.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215274164  225 QRVLPTPQTQATQEGALLNKRRGSVPILRQWLTGRGRPVYD------GQAWVLAAVACTVLRCLGIPARVVTTFASAQGT 298
Cdd:pfam01841   5 DRITGGATDPLEKARAIYDYVRKNITYDLDGRSPGDGDAEEflftgkGDCEDFASLFVALLRALGIPARYVTGYLRGPDT 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 215274164  299 ggrllideyyneeglqngegqrGRIWIFQTSTECWMtrpalpqGYDGWQILHP 351
Cdd:pfam01841  85 ----------------------VRGGDAHAWVEVYL-------PGYGWVPVDP 108
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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