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Conserved domains on  [gi|1939160219|ref|NP_036962|]
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T-cell surface antigen CD2 precursor [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IgV_CD2_like_N cd05775
N-terminal immunoglobulin (Ig)-like domain of T-cell surface antigen CD2, and similar domains; ...
 24-120 6.45e-30

N-terminal immunoglobulin (Ig)-like domain of T-cell surface antigen CD2, and similar domains; The members here are composed of the N-terminal immunoglobulin (Ig)-like domain (or domain 1) of T-cell surface antigen Clusters of Differentiation (CD) 2 and similar proteins. CD2 is a T-cell specific surface glycoprotein and is critically important for mediating adhesion between T cells and antigen-presenting cells or between cytolytic T cells and target cells. CD2 is located on chromosome 1 at 1p13 in humans and on chromosome 3 in mice. CD2 contains an extracellular domain with two or Ig-like domains, a single transmembrane segment, and a cytoplasmic region rich in proline and basic residues.


:

Pssm-ID: 409431  Cd Length: 98  Bit Score: 109.74  E-value: 6.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219  24 DSGTVWGALGHGINLNIPNFQmtDDIDEVRWERGSTLVAEFKRKMKPFL---KSGAFEILAN-GDLKIKNLTRDDSGTYN 99
Cdd:cd05775     1 SSGEVYGALGGNVTLTISSLQ--DDIDEIKWKKTKDKIVEWENNIGPTYfgsFKDRVLLDKEsGSLTIKNLTKEDSGTYE 78

                          90       100
                  ....*....|....*....|.
gi 1939160219 100 VTVYSTNGtRILNKALDLRIL 120
Cdd:cd05775    79 LEITSTNG-KVLSSKFTLEVL 98
C2-set pfam05790
Immunoglobulin C2-set domain;
128-198 5.51e-15

Immunoglobulin C2-set domain;


:

Pssm-ID: 399065  Cd Length: 80  Bit Score: 69.30  E-value: 5.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219 128 IYWECSNATLTCEVLEGT-------DVELKLYQGKEHLRSLRQKTMSYQWT-NLRAPFKCKA-VNRVSQESEMEVVNCPE 198
Cdd:pfam05790   1 VTVSCSNNLLTCEVLELTlpkgskmDPSLKLKGQEAKSLETKKLESTFQPTtEDSGTWVCLAsDNDQKKLESVIEVLVLE 80
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 256-343 1.29e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 47.07  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219 256 PKPHSTQASAPASQNPVA------------SQAPPPPG----HHLQTPGHRPLPPSHRNREHQPKKRP-PPSGTQVHQQK 318
Cdd:pfam03154 277 PMPHSLQTGPSHMQHPVPpqpfpltpqssqSQVPPGPSpaapGQSQQRIHTPPSQSQLQSQQPPREQPlPPAPLSMPHIK 356

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1939160219 319 GPP------LPRPRVQPKPPCGSG------DVSLPPP 343
Cdd:pfam03154 357 PPPttpipqLPNPQSHKHPPHLSGpspfqmNSNLPPP 393
 
Name Accession Description Interval E-value
IgV_CD2_like_N cd05775
N-terminal immunoglobulin (Ig)-like domain of T-cell surface antigen CD2, and similar domains; ...
 24-120 6.45e-30

N-terminal immunoglobulin (Ig)-like domain of T-cell surface antigen CD2, and similar domains; The members here are composed of the N-terminal immunoglobulin (Ig)-like domain (or domain 1) of T-cell surface antigen Clusters of Differentiation (CD) 2 and similar proteins. CD2 is a T-cell specific surface glycoprotein and is critically important for mediating adhesion between T cells and antigen-presenting cells or between cytolytic T cells and target cells. CD2 is located on chromosome 1 at 1p13 in humans and on chromosome 3 in mice. CD2 contains an extracellular domain with two or Ig-like domains, a single transmembrane segment, and a cytoplasmic region rich in proline and basic residues.


Pssm-ID: 409431  Cd Length: 98  Bit Score: 109.74  E-value: 6.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219  24 DSGTVWGALGHGINLNIPNFQmtDDIDEVRWERGSTLVAEFKRKMKPFL---KSGAFEILAN-GDLKIKNLTRDDSGTYN 99
Cdd:cd05775     1 SSGEVYGALGGNVTLTISSLQ--DDIDEIKWKKTKDKIVEWENNIGPTYfgsFKDRVLLDKEsGSLTIKNLTKEDSGTYE 78

                          90       100
                  ....*....|....*....|.
gi 1939160219 100 VTVYSTNGtRILNKALDLRIL 120
Cdd:cd05775    79 LEITSTNG-KVLSSKFTLEVL 98
C2-set pfam05790
Immunoglobulin C2-set domain;
128-198 5.51e-15

Immunoglobulin C2-set domain;


Pssm-ID: 399065  Cd Length: 80  Bit Score: 69.30  E-value: 5.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219 128 IYWECSNATLTCEVLEGT-------DVELKLYQGKEHLRSLRQKTMSYQWT-NLRAPFKCKA-VNRVSQESEMEVVNCPE 198
Cdd:pfam05790   1 VTVSCSNNLLTCEVLELTlpkgskmDPSLKLKGQEAKSLETKKLESTFQPTtEDSGTWVCLAsDNDQKKLESVIEVLVLE 80
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 25-120 2.95e-13

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 65.17  E-value: 2.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219  25 SGTVWGALGHGINLNIP-NFQMTDDIDEVRWERG------STLVAEFKRKMKPFLKSGAFEILA-----NGDLKIKNLTR 92
Cdd:pfam07686   3 PREVTVALGGSVTLPCTySSSMSEASTSVYWYRQppgkgpTFLIAYYSNGSEEGVKKGRFSGRGdpsngDGSLTIQNLTL 82

                          90       100
                  ....*....|....*....|....*...
gi 1939160219  93 DDSGTYNVTVYsTNGTRILNKALDLRIL 120
Cdd:pfam07686  83 SDSGTYTCAVI-PSGEGVFGKGTRLTVL 109
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 256-343 1.29e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 47.07  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219 256 PKPHSTQASAPASQNPVA------------SQAPPPPG----HHLQTPGHRPLPPSHRNREHQPKKRP-PPSGTQVHQQK 318
Cdd:pfam03154 277 PMPHSLQTGPSHMQHPVPpqpfpltpqssqSQVPPGPSpaapGQSQQRIHTPPSQSQLQSQQPPREQPlPPAPLSMPHIK 356

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1939160219 319 GPP------LPRPRVQPKPPCGSG------DVSLPPP 343
Cdd:pfam03154 357 PPPttpipqLPNPQSHKHPPHLSGpspfqmNSNLPPP 393
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 267-332 3.28e-05

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 43.62  E-value: 3.28e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219  267 ASQNPVASQAP--PPPGHHLQTP--GHRPLPPSHRNREHQPKKRPPPSGTQVHQQKGPPLPRPRVQPKPP 332
Cdd:smart00818  62 PAQQPVVPQQPlmPVPGQHSMTPtqHHQPNLPQPAQQPFQPQPLQPPQPQQPMQPQPPVHPIPPLPPQPP 131
PHA03247 PHA03247
large tegument protein UL36; Provisional
 256-344 1.83e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 1.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219  256 PKPHSTQASAPASQNPVASQAPPPPGhhlqtPGHRPLPPSHRNREHQPKKRPPPSGTQVHQQkgPPLPRPRVQPKP-PCG 334
Cdd:PHA03247  2879 ARPPVRRLARPAVSRSTESFALPPDQ-----PERPPQPQAPPPPQPQPQPPPPPQPQPPPPP--PPRPQPPLAPTTdPAG 2951

                           90
                   ....*....|
gi 1939160219  335 SGDVSLPPPN 344
Cdd:PHA03247  2952 AGEPSGAVPQ 2961
 
Name Accession Description Interval E-value
IgV_CD2_like_N cd05775
N-terminal immunoglobulin (Ig)-like domain of T-cell surface antigen CD2, and similar domains; ...
 24-120 6.45e-30

N-terminal immunoglobulin (Ig)-like domain of T-cell surface antigen CD2, and similar domains; The members here are composed of the N-terminal immunoglobulin (Ig)-like domain (or domain 1) of T-cell surface antigen Clusters of Differentiation (CD) 2 and similar proteins. CD2 is a T-cell specific surface glycoprotein and is critically important for mediating adhesion between T cells and antigen-presenting cells or between cytolytic T cells and target cells. CD2 is located on chromosome 1 at 1p13 in humans and on chromosome 3 in mice. CD2 contains an extracellular domain with two or Ig-like domains, a single transmembrane segment, and a cytoplasmic region rich in proline and basic residues.


Pssm-ID: 409431  Cd Length: 98  Bit Score: 109.74  E-value: 6.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219  24 DSGTVWGALGHGINLNIPNFQmtDDIDEVRWERGSTLVAEFKRKMKPFL---KSGAFEILAN-GDLKIKNLTRDDSGTYN 99
Cdd:cd05775     1 SSGEVYGALGGNVTLTISSLQ--DDIDEIKWKKTKDKIVEWENNIGPTYfgsFKDRVLLDKEsGSLTIKNLTKEDSGTYE 78

                          90       100
                  ....*....|....*....|.
gi 1939160219 100 VTVYSTNGtRILNKALDLRIL 120
Cdd:cd05775    79 LEITSTNG-KVLSSKFTLEVL 98
C2-set pfam05790
Immunoglobulin C2-set domain;
128-198 5.51e-15

Immunoglobulin C2-set domain;


Pssm-ID: 399065  Cd Length: 80  Bit Score: 69.30  E-value: 5.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219 128 IYWECSNATLTCEVLEGT-------DVELKLYQGKEHLRSLRQKTMSYQWT-NLRAPFKCKA-VNRVSQESEMEVVNCPE 198
Cdd:pfam05790   1 VTVSCSNNLLTCEVLELTlpkgskmDPSLKLKGQEAKSLETKKLESTFQPTtEDSGTWVCLAsDNDQKKLESVIEVLVLE 80
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 25-120 2.95e-13

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 65.17  E-value: 2.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219  25 SGTVWGALGHGINLNIP-NFQMTDDIDEVRWERG------STLVAEFKRKMKPFLKSGAFEILA-----NGDLKIKNLTR 92
Cdd:pfam07686   3 PREVTVALGGSVTLPCTySSSMSEASTSVYWYRQppgkgpTFLIAYYSNGSEEGVKKGRFSGRGdpsngDGSLTIQNLTL 82

                          90       100
                  ....*....|....*....|....*...
gi 1939160219  93 DDSGTYNVTVYsTNGTRILNKALDLRIL 120
Cdd:pfam07686  83 SDSGTYTCAVI-PSGEGVFGKGTRLTVL 109
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 256-343 1.29e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 47.07  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219 256 PKPHSTQASAPASQNPVA------------SQAPPPPG----HHLQTPGHRPLPPSHRNREHQPKKRP-PPSGTQVHQQK 318
Cdd:pfam03154 277 PMPHSLQTGPSHMQHPVPpqpfpltpqssqSQVPPGPSpaapGQSQQRIHTPPSQSQLQSQQPPREQPlPPAPLSMPHIK 356

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1939160219 319 GPP------LPRPRVQPKPPCGSG------DVSLPPP 343
Cdd:pfam03154 357 PPPttpipqLPNPQSHKHPPHLSGpspfqmNSNLPPP 393
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 253-343 2.07e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 46.30  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219 253 ERGPKPHST--QASAPASQNPVASQAPPPPGHHLQTPghrPLP-PSHRNREHQPKKRPP---PSGTQVHQQKGPPLPRPR 326
Cdd:pfam03154 240 QRLPSPHPPlqPMTQPPPPSQVSPQPLPQPSLHGQMP---PMPhSLQTGPSHMQHPVPPqpfPLTPQSSQSQVPPGPSPA 316

                          90       100
                  ....*....|....*....|....
gi 1939160219 327 V-------QPKPPCGSGDVSLPPP 343
Cdd:pfam03154 317 ApgqsqqrIHTPPSQSQLQSQQPP 340
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 267-332 3.28e-05

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 43.62  E-value: 3.28e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219  267 ASQNPVASQAP--PPPGHHLQTP--GHRPLPPSHRNREHQPKKRPPPSGTQVHQQKGPPLPRPRVQPKPP 332
Cdd:smart00818  62 PAQQPVVPQQPlmPVPGQHSMTPtqHHQPNLPQPAQQPFQPQPLQPPQPQQPMQPQPPVHPIPPLPPQPP 131
PHA03247 PHA03247
large tegument protein UL36; Provisional
 256-344 1.83e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 1.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219  256 PKPHSTQASAPASQNPVASQAPPPPGhhlqtPGHRPLPPSHRNREHQPKKRPPPSGTQVHQQkgPPLPRPRVQPKP-PCG 334
Cdd:PHA03247  2879 ARPPVRRLARPAVSRSTESFALPPDQ-----PERPPQPQAPPPPQPQPQPPPPPQPQPPPPP--PPRPQPPLAPTTdPAG 2951

                           90
                   ....*....|
gi 1939160219  335 SGDVSLPPPN 344
Cdd:PHA03247  2952 AGEPSGAVPQ 2961
PHA03247 PHA03247
large tegument protein UL36; Provisional
 252-343 3.57e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 3.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219  252 VERGPKPHSTQASAPASQNPVASQAPPPPGHhlQTPGHRPLPPSHRNREHQPKKRPPPSGTQVHQQKG------PPLPRP 325
Cdd:PHA03247  2862 VRRRPPSRSPAAKPAAPARPPVRRLARPAVS--RSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPqpqpppPPPPRP 2939

                           90
                   ....*....|....*...
gi 1939160219  326 RVQPKPPCGSGDVSLPPP 343
Cdd:PHA03247  2940 QPPLAPTTDPAGAGEPSG 2957
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 256-343 8.16e-04

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 39.64  E-value: 8.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219 256 PKPHSTQASAPASQNPVASQAPPPPGHHLQtpgHRPLPPSHRNREHQPKKRPPPSGTQVHQQKGPPLPRPRVQPKPPCGS 335
Cdd:pfam15240  83 QKPQGPPPQGGPRPPPGKPQGPPPQGGNQQ---QGPPPPGKPQGPPPQGGGPPPQGGNQQGPPPPPPGNPQGPPQRPPQP 159


                  ....*...
gi 1939160219 336 GDVSLPPP 343
Cdd:pfam15240 160 GNPQGPPQ 167
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 256-332 1.48e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.45  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219  256 PKPHSTQASAPASQNPVaSQAPPPPGHHLQTPgHRPLPPSHRNREHQPKKRPPPSGTQVHQQKGP----PLPRPRVQPKP 331
Cdd:PRK10263   751 PVQQPQQPVAPQQQYQQ-PQQPVAPQPQYQQP-QQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPqpqyQQPQQPVAPQP 828


                   .
gi 1939160219  332 P 332
Cdd:PRK10263   829 Q 829
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
 256-344 1.62e-03

Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteriztic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.


Pssm-ID: 464609 [Multi-domain]  Cd Length: 325  Bit Score: 39.80  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219 256 PKPHSTQASAPASQNPVASQAPPPPGHHLQtPGHRPLPPSHRNREHQPKKRPPPSgtqvhqQKGPPLPRPRVQPKPPCGS 335
Cdd:pfam15279 197 PPFLRPPPSIPQPNSPLSNPMLPGIGPPPK-PPRNLGPPSNPMHRPPFSPHHPPP------PPTPPGPPPGLPPPPPRGF 269


                  ....*....
gi 1939160219 336 GDVSLPPPN 344
Cdd:pfam15279 270 TPPFGPPFP 278
PHA03247 PHA03247
large tegument protein UL36; Provisional
 253-343 2.89e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 2.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219  253 ERGPKPHSTQASAPASQNPVASQAPPPPghhlQTPghrPLPPSHRNREHQPKKRPPPSGTQVHQQKGP------PLPRPR 326
Cdd:PHA03247  2906 ERPPQPQAPPPPQPQPQPPPPPQPQPPP----PPP---PRPQPPLAPTTDPAGAGEPSGAVPQPWLGAlvpgrvAVPRFR 2978

                           90
                   ....*....|....*...
gi 1939160219  327 V-QPKPPCGSGDVSLPPP 343
Cdd:PHA03247  2979 VpQPAPSREAPASSTPPL 2996
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 255-332 4.07e-03

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 37.71  E-value: 4.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939160219 255 GPKPHSTQASAPASQNPVASQAPPPPGHHLQTPGHRPLPPSHR-NREHQPKKRPPPSGTQVHQQKGPPLPRPRVQPKPP 332
Cdd:pfam15240  66 GPPPPGGPQQPPPQGGKQKPQGPPPQGGPRPPPGKPQGPPPQGgNQQQGPPPPGKPQGPPPQGGGPPPQGGNQQGPPPP 144
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 256-332 4.10e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 39.25  E-value: 4.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219 256 PKPHSTQASAPASQNPVASQAPPP---PGHHLQTPgHRPLPPSHRNREHQPKKRPPPSGTQVHQQKGPPLPRPRVQPKPP 332
Cdd:pfam09770 272 PQPDPAQPSIQPQAQQFHQQPPPVpvqPTQILQNP-NRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITHPQ 350
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 261-343 4.25e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 38.98  E-value: 4.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219 261 TQASAPASQNPVASQAPPPPGHHLQ------TPGHRPLPPSHRNREHQPKKRPPP---------SGTQVHQQKGP---PL 322
Cdd:pfam03154 169 TQPPVLQAQSGAASPPSPPPPGTTQaatagpTPSAPSVPPQGSPATSQPPNQTQStaaphtliqQTPTLHPQRLPsphPP 248

                          90       100
                  ....*....|....*....|.
gi 1939160219 323 PRPRVQPKPPCGSGDVSLPPP 343
Cdd:pfam03154 249 LQPMTQPPPPSQVSPQPLPQP 269
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 256-334 4.59e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 38.98  E-value: 4.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939160219 256 PKPHSTQASAPASQNPVASQappPPGHHLQTPGHRPLPPSHRNREHQPKKRPPPSGTQVHQQKGPPLPRPRVQPKPPCG 334
Cdd:pfam03154 151 PQDNESDSDSSAQQQILQTQ---PPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAA 226
PHA03247 PHA03247
large tegument protein UL36; Provisional
 246-343 5.43e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 38.77  E-value: 5.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219  246 ASRMSTVERGPKPHSTQASAPASQNPVASQAPPPPGHHLQTPGHRPLPPShrnrehqpkkrPPPSGTQvhqQKGPPLPRP 325
Cdd:PHA03247  2779 PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL-----------PPPTSAQ---PTAPPPPPG 2844

                           90       100
                   ....*....|....*....|...
gi 1939160219  326 RVQPK-PPCGS----GDVSLPPP 343
Cdd:PHA03247  2845 PPPPSlPLGGSvapgGDVRRRPP 2867
IgV_CEACAM_like cd05741
Immunoglobulin (Ig)-like domain of carcinoembryonic antigen (CEA) related cell adhesion ...
 28-109 6.14e-03

Immunoglobulin (Ig)-like domain of carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain in carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) and related domains. The CEA family is a group of anchored or secreted glycoproteins, expressed by epithelial cells, leukocytes, endothelial cells and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions: it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two (D1, D4) or four (D1-D4) Ig-like domains on the cell surface. This family corresponds to the D1 Ig-like domain. Also belonging to this group is the N-terminal immunoglobulin (Ig)-like domain of the signaling lymphocyte activation molecule (SLAM) family, CD84-like family. The SLAM family is a group of immune-cell specific receptors that can regulate both adaptive and innate immune responses. SLAM family proteins are organized as an extracellular domain with having two or four Ig-like domains, a single transmembrane segment, and a cytoplasmic region having Tyr-based motifs. The extracellular domain is organized as a membrane-distal Ig variable (IgV) domain that is responsible for ligand recognition and a membrane-proximal truncated Ig constant-2 (IgC2) domain.


Pssm-ID: 409403  Cd Length: 102  Bit Score: 35.96  E-value: 6.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219  28 VWGALGHGINLNIPNFQMTDDidEVRWERGSTL-----VAEFKRKMKPFLKSGAF----EILANGDLKIKNLTRDDSGTY 98
Cdd:cd05741     5 FYGAEGKNVLLLVPNLQTPLK--SVSWYKGKQVsrndeIAEYENSSDEFRAGSAFsgreYIYTNGSLLIQNITLSDTGFY 82

                          90
                  ....*....|.
gi 1939160219  99 NVTVYSTNGTR 109
Cdd:cd05741    83 TLESTNIGGKT 93
PHA03247 PHA03247
large tegument protein UL36; Provisional
 254-344 6.69e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 38.38  E-value: 6.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219  254 RGPKPHSTQASAPASQNPVA--SQAPPPPGHHLQTPGHRPLPPSHRNREHQPkkRPPPSGTQVHQQKGPPLPRPRVQPKP 331
Cdd:PHA03247   377 RASLPTRKRRSARHAATPFArgPGGDDQTRPAAPVPASVPTPAPTPVPASAP--PPPATPLPSAEPGSDDGPAPPPERQP 454

                           90
                   ....*....|...
gi 1939160219  332 PCGSGDVSLPPPN 344
Cdd:PHA03247   455 PAPATEPAPDDPD 467
PHA03247 PHA03247
large tegument protein UL36; Provisional
 255-343 7.49e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 38.38  E-value: 7.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219  255 GPKPHSTQASAPASQN---PVASQAPPPPGHHLQTPGHRPLPPSHRNREHQP--------KKRPPPSGTQVHQQKGPPLP 323
Cdd:PHA03247  2550 DPPPPLPPAAPPAAPDrsvPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPvddrgdprGPAPPSPLPPDTHAPDPPPP 2629

                           90       100
                   ....*....|....*....|
gi 1939160219  324 RPRVQPKPPCGSGDVSLPPP 343
Cdd:PHA03247  2630 SPSPAANEPDPHPPPTVPPP 2649
Ig_SLAM-like_N cd16842
N-terminal immunoglobulin (Ig)-like domain of the signaling lymphocyte activation molecule ...
 27-119 7.91e-03

N-terminal immunoglobulin (Ig)-like domain of the signaling lymphocyte activation molecule (SLAM) family; The members here are composed of the N-terminal immunoglobulin (Ig)-like domain of the signaling lymphocyte activation molecule (SLAM) family and similar proteins. The SLAM family is a group of immune-cell specific receptors that can regulate both adaptive and innate immune responses. Members of this group include proteins such as CD84, SLAM (CD150), Ly-9 (CD229), NTB-A (ly-108, SLAM6), 19A (CRACC), and SLAMF9. The genes coding for the SLAM family are nested on chromosome 1, in humans at 1q23, and in mice at 1H2. The SLAM family is a subset of the CD2 family, which also includes CD2 and CD58 located on chromosome 1 at 1p13 in humans. In mice, CD2 is located on chromosome 3, and there is no CD58 homolog. The SLAM family proteins are organized as an extracellular domain with either two or four Ig-like domains, a single transmembrane segment, and a cytoplasmic region having Tyr-based motifs. The extracellular domain is organized as a membrane-distal Ig variable (IgV) domain that is responsible for ligand recognition and a membrane-proximal truncated Ig constant-2 (IgC2) domain.


Pssm-ID: 409517  Cd Length: 102  Bit Score: 35.37  E-value: 7.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219  27 TVWGALGHGINLNIpNFQMTDDIDEVRWERGSTLVAEFKRKMKP-----FLKS--GAFEILANG-DLKIKNLTRDDSGTY 98
Cdd:cd16842     2 EVNGILGGSVTFPL-NISDGQEIENITWSFKTSLAVIAPGEGGApeiiiTDKSykERLNISQNDySLQISNLTMEDAGSY 80

                          90       100
                  ....*....|....*....|.
gi 1939160219  99 NVTVYSTNGTRILNKALDLRI 119
Cdd:cd16842    81 RARINTKNSRVTITKEFTLHI 101
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 258-343 9.29e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 38.09  E-value: 9.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219 258 PHSTQASAPASQNPVASQAPPPPGHH---LQTPGHRPLP---PSHRNREHQPKKRPPPSGTQVHQQ-KGPPLPRPRVQPK 330
Cdd:pfam09770 237 PPQIQQQQQPQQQPQQPQQHPGQGHPvtiLQRPQSPQPDpaqPSIQPQAQQFHQQPPPVPVQPTQIlQNPNRLSAARVGY 316

                          90
                  ....*....|...
gi 1939160219 331 PPCGSGDVSLPPP 343
Cdd:pfam09770 317 PQNPQPGVQPAPA 329
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 261-343 9.74e-03

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 37.21  E-value: 9.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939160219 261 TQASAPASQNPVASQAPPPPGhhlqtpghrPLPPSHRNREHQPKKRPPPSGTQVhqqkGPPLPRPRVQPKPPCGSGDVSL 340
Cdd:pfam07174  24 AGASAVAVALPAVAHADPEPA---------PPPPSTATAPPAPPPPPPAPAAPA----PPPPPAAPNAPNAPPPPADPNA 90


                  ...
gi 1939160219 341 PPP 343
Cdd:pfam07174  91 PPP 93
 
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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