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Conserved domains on  [gi|1622398923|ref|XP_028741787|]
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amelogenin, X isoform isoform X5 [Peromyscus leucopus]

Protein Classification

type IV secretion system protein( domain architecture ID 12220051)

type IV secretion system (T4SS) protein functions as a virulence factor that plays important roles in mediating intracellular survival and manipulating host immune response to infection

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 28-196 1.71e-53

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: 168.43  E-value: 1.71e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622398923   28 YINLSYEVLTPLKWYQSMIRQPYPSYGYEPMGGWLHHQIIPVlSQQHPPSHTLQPHHHLPVVPAQQPVAPQQPMMPVPGH 107
Cdd:smart00818   1 YINFSYEVLTPLKWYQSMIRHPYPSYGYEPMGGWLHHQIIPV-SQQHPPTHTLQPHHHIPVLPAQQPVVPQQPLMPVPGQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622398923  108 HSMTPTQHHQPNIPPSAQQPFQQPFQpqaIPPQSHQPMQPQSPLHPMQPLAPQPPLPPLFSMQPLSPILPELPLEAWPAT 187
Cdd:smart00818  80 HSMTPTQHHQPNLPQPAQQPFQPQPL---QPPQPQQPMQPQPPVHPIPPLPPQPPLPPMFPMQPLPPLLPDLPLEAWPAT 156


                   ....*....
gi 1622398923  188 DKTKREEVD 196
Cdd:smart00818 157 DKTKREEVD 165
 
Name Accession Description Interval E-value
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 28-196 1.71e-53

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: 168.43  E-value: 1.71e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622398923   28 YINLSYEVLTPLKWYQSMIRQPYPSYGYEPMGGWLHHQIIPVlSQQHPPSHTLQPHHHLPVVPAQQPVAPQQPMMPVPGH 107
Cdd:smart00818   1 YINFSYEVLTPLKWYQSMIRHPYPSYGYEPMGGWLHHQIIPV-SQQHPPTHTLQPHHHIPVLPAQQPVVPQQPLMPVPGQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622398923  108 HSMTPTQHHQPNIPPSAQQPFQQPFQpqaIPPQSHQPMQPQSPLHPMQPLAPQPPLPPLFSMQPLSPILPELPLEAWPAT 187
Cdd:smart00818  80 HSMTPTQHHQPNLPQPAQQPFQPQPL---QPPQPQQPMQPQPPVHPIPPLPPQPPLPPMFPMQPLPPLLPDLPLEAWPAT 156


                   ....*....
gi 1622398923  188 DKTKREEVD 196
Cdd:smart00818 157 DKTKREEVD 165
Amelogenin pfam02948
Amelogenin; Amelogenins play a role in biomineralization. They seem to regulate the formation ...
 21-196 6.66e-45

Amelogenin; Amelogenins play a role in biomineralization. They seem to regulate the formation of crystallites during the secretory stage of tooth enamel development. thought to play a major role in the structural organization and mineralization of developing enamel. They are found in the extracellular matrix. Mutations in X-chromosomal amelogenin can cause Amelogenesis imperfecta.


Pssm-ID: 460761 [Multi-domain]  Cd Length: 179  Bit Score: 146.82  E-value: 6.66e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622398923  21 PHPGSPGYINLSYEVLTPLKWYQSMIRQPYPSYGYEPMGGWLHHQIIPVLS----QQHPPSHTLQPHHHLPVVPAQQPV- 95
Cdd:pfam02948   1 PHPGHPGYINFSYEVLTPLKWYQSLIGHAYPRYGFEPMGGWLHHAAGPTLHqttfQQHPPTHSLLPHHHIPPHPALNPHm 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622398923  96 --APQQPMMPVPGHHSMTPTQHHQPNIPPSAQQPFQQPfqpqAIPPQSHQPMQPQSPLHPMQPLAPQPPLPPLFSMQPLS 173
Cdd:pfam02948  81 qpSGHNPFGPMPGQHSLIPTQHFQPAHGGPAHHPFQPH----AGEPHPHHPMQPGNPVHPMHPLPPANPLPPIFPMQPLP 156

                         170       180
                  ....*....|....*....|...
gi 1622398923 174 PILPELPLEAWPATDKTKREEVD 196
Cdd:pfam02948 157 PLIPDLPLEAWPAADKTKQEEVD 179
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 75-154 1.05e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 39.30  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622398923   75 PPSHTLQPHHhlPVVPAQQPVAPQQPMMPVPghhsmtptQHHQPNIPPSAQQPFQQPFQPQAIPPQSHQPMQPQSP---- 150
Cdd:PRK10263   774 PQPQYQQPQQ--PVAPQPQYQQPQQPVAPQP--------QYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPqpqd 843


                   ....*.
gi 1622398923  151 --LHPM 154
Cdd:PRK10263   844 tlLHPL 849
KLF1_2_4_N-like cd22056
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ...
 72-192 7.89e-03

N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of Kruppel-like factor (KLF)1, KLF2, and KLF4; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domains of an unknown subfamily of KLFs, predominantly found in fish, related to the N-terminal domains of KLF1, KLF2, and KLF4.


Pssm-ID: 409231 [Multi-domain]  Cd Length: 339  Bit Score: 36.18  E-value: 7.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622398923  72 QQHPPSHTLQPHHHLPVVPAQQPVAPQQPMMPVPGHHSMTPTQHHQPNIPPSAQQPFQQPFQPQAIPPQSHQPMQPQSPL 151
Cdd:cd22056   206 QQKPKHQMHSVHPQAFTHHQAAGPGALQGRGGRGGPDCHLLHSSHHHHHHHHLQYQYMNAPYPPHYAHQGAPQFHGQYSV 285

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1622398923 152 HPMQPLAPQPPLPPLFSMQPLSPILPELPLEAWPATDKTKR 192
Cdd:cd22056   286 FREPMRVHHQGHPGSMLTPPSSPPLLEFYAQDEPEDIKPKR 326
 
Name Accession Description Interval E-value
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 28-196 1.71e-53

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: 168.43  E-value: 1.71e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622398923   28 YINLSYEVLTPLKWYQSMIRQPYPSYGYEPMGGWLHHQIIPVlSQQHPPSHTLQPHHHLPVVPAQQPVAPQQPMMPVPGH 107
Cdd:smart00818   1 YINFSYEVLTPLKWYQSMIRHPYPSYGYEPMGGWLHHQIIPV-SQQHPPTHTLQPHHHIPVLPAQQPVVPQQPLMPVPGQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622398923  108 HSMTPTQHHQPNIPPSAQQPFQQPFQpqaIPPQSHQPMQPQSPLHPMQPLAPQPPLPPLFSMQPLSPILPELPLEAWPAT 187
Cdd:smart00818  80 HSMTPTQHHQPNLPQPAQQPFQPQPL---QPPQPQQPMQPQPPVHPIPPLPPQPPLPPMFPMQPLPPLLPDLPLEAWPAT 156


                   ....*....
gi 1622398923  188 DKTKREEVD 196
Cdd:smart00818 157 DKTKREEVD 165
Amelogenin pfam02948
Amelogenin; Amelogenins play a role in biomineralization. They seem to regulate the formation ...
 21-196 6.66e-45

Amelogenin; Amelogenins play a role in biomineralization. They seem to regulate the formation of crystallites during the secretory stage of tooth enamel development. thought to play a major role in the structural organization and mineralization of developing enamel. They are found in the extracellular matrix. Mutations in X-chromosomal amelogenin can cause Amelogenesis imperfecta.


Pssm-ID: 460761 [Multi-domain]  Cd Length: 179  Bit Score: 146.82  E-value: 6.66e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622398923  21 PHPGSPGYINLSYEVLTPLKWYQSMIRQPYPSYGYEPMGGWLHHQIIPVLS----QQHPPSHTLQPHHHLPVVPAQQPV- 95
Cdd:pfam02948   1 PHPGHPGYINFSYEVLTPLKWYQSLIGHAYPRYGFEPMGGWLHHAAGPTLHqttfQQHPPTHSLLPHHHIPPHPALNPHm 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622398923  96 --APQQPMMPVPGHHSMTPTQHHQPNIPPSAQQPFQQPfqpqAIPPQSHQPMQPQSPLHPMQPLAPQPPLPPLFSMQPLS 173
Cdd:pfam02948  81 qpSGHNPFGPMPGQHSLIPTQHFQPAHGGPAHHPFQPH----AGEPHPHHPMQPGNPVHPMHPLPPANPLPPIFPMQPLP 156

                         170       180
                  ....*....|....*....|...
gi 1622398923 174 PILPELPLEAWPATDKTKREEVD 196
Cdd:pfam02948 157 PLIPDLPLEAWPAADKTKQEEVD 179
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 43-153 1.45e-04

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: 41.95  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622398923  43 QSMIRQPYPSYGYEPMGGWLHHQIIPVLSQQHPPSHTLQPHHHLPVVPAQQPVAPQQPMMPVPGHHSMTPTQHHQPNIPP 122
Cdd:pfam09770 230 AQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQILQNPNRL 309

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1622398923 123 SAQQPFQQPFQPQAIPPQSHQPMQPQSPLHP 153
Cdd:pfam09770 310 SAARVGYPQNPQPGVQPAPAHQAHRQQGSFG 340
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 73-152 2.93e-04

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: 40.79  E-value: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622398923  73 QHPPSHTLQPHHHLPVVPAQQPVAPQQPMMPVPGH-HSMTPTQHHQPNIPPSAQQPFQQPFQpqAIPPQSHQPMQPQSPL 151
Cdd:pfam09770 223 AAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPgQGHPVTILQRPQSPQPDPAQPSIQPQ--AQQFHQQPPPVPVQPT 300


                  .
gi 1622398923 152 H 152
Cdd:pfam09770 301 Q 301
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 75-154 1.05e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 39.30  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622398923   75 PPSHTLQPHHhlPVVPAQQPVAPQQPMMPVPghhsmtptQHHQPNIPPSAQQPFQQPFQPQAIPPQSHQPMQPQSP---- 150
Cdd:PRK10263   774 PQPQYQQPQQ--PVAPQPQYQQPQQPVAPQP--------QYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPqpqd 843


                   ....*.
gi 1622398923  151 --LHPM 154
Cdd:PRK10263   844 tlLHPL 849
EIF4E-T pfam10477
Nucleocytoplasmic shuttling protein for mRNA cap-binding EIF4E; EIF4E-T is the transporter ...
 62-146 3.66e-03

Nucleocytoplasmic shuttling protein for mRNA cap-binding EIF4E; EIF4E-T is the transporter protein for shuttling the mRNA cap-binding protein EIF4E protein, targeting it for nuclear import. EIF4E-T contains several key binding domains including two functional leucine-rich NESs (nuclear export signals) between residues 438-447 and 613-638 in the human protein. The other two binding domains are an EIF4E-binding site, between residues 27-42 in Q9EST3, and a bipartite NLS (nuclear localization signals) between 194-211, and these lie in family EIF4E-T_N. EIF4E is the eukaryotic translation initiation factor 4E that is the rate-limiting factor for cap-dependent translation initiation.


Pssm-ID: 371079  Cd Length: 646  Bit Score: 37.68  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622398923  62 LHHQIIPVLSQQHPPSHTLQPHHHLPV---VPAQQPVAPQQPMMPVPGHHSMTPTQHHQPNIPPSAQQPFQQPFQPQAIP 138
Cdd:pfam10477 530 LVRPDISHEFLEKELSNPSTLGHTKDViaaVLRECSNGMRNTMSPKPQQNVMTPQSLHQAQLQPLQQPQQLALQQDLFYQ 609


                  ....*...
gi 1622398923 139 PQSHQPMQ 146
Cdd:pfam10477 610 NDGNQNRQ 617
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 76-178 3.91e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 37.76  E-value: 3.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622398923   76 PSHTLQPHHHLPVVPAQQPVAPQQPMMPvpghhsmtPTQHHQPNIPPSAQQPFQQPFQPQAIPPQSHQPMQPQSPLHPMQ 155
Cdd:PRK10263   747 PIVEPVQQPQQPVAPQQQYQQPQQPVAP--------QPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQ 818

                           90       100
                   ....*....|....*....|...
gi 1622398923  156 PLAPQPPLPPLFSmQPLSPILPE 178
Cdd:PRK10263   819 QPQQPVAPQPQYQ-QPQQPVAPQ 840
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 66-150 5.63e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 36.99  E-value: 5.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622398923   66 IIPVLSQQHPPSHTLQPHH-HLPVVPAQQPVAPQQPMMPvpghhsmtPTQHHQPNIPPSAQQPFQQPFQPQAIPPQSHQP 144
Cdd:PRK10263   749 VEPVQQPQQPVAPQQQYQQpQQPVAPQPQYQQPQQPVAP--------QPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQP 820


                   ....*.
gi 1622398923  145 MQPQSP 150
Cdd:PRK10263   821 QQPVAP 826
KLF1_2_4_N-like cd22056
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ...
 72-192 7.89e-03

N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of Kruppel-like factor (KLF)1, KLF2, and KLF4; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domains of an unknown subfamily of KLFs, predominantly found in fish, related to the N-terminal domains of KLF1, KLF2, and KLF4.


Pssm-ID: 409231 [Multi-domain]  Cd Length: 339  Bit Score: 36.18  E-value: 7.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622398923  72 QQHPPSHTLQPHHHLPVVPAQQPVAPQQPMMPVPGHHSMTPTQHHQPNIPPSAQQPFQQPFQPQAIPPQSHQPMQPQSPL 151
Cdd:cd22056   206 QQKPKHQMHSVHPQAFTHHQAAGPGALQGRGGRGGPDCHLLHSSHHHHHHHHLQYQYMNAPYPPHYAHQGAPQFHGQYSV 285

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1622398923 152 HPMQPLAPQPPLPPLFSMQPLSPILPELPLEAWPATDKTKR 192
Cdd:cd22056   286 FREPMRVHHQGHPGSMLTPPSSPPLLEFYAQDEPEDIKPKR 326
 
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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