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Conserved domains on  [gi|165377291|ref|NP_001107005|]
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pre-mRNA-splicing regulator WTAP isoform a [Mus musculus]

Protein Classification

WTAP/Mum2p family protein( domain architecture ID 12181585)

WTAP/Mum2p (Wtap) family protein similar to Homo sapiens pre-mRNA-splicing regulator WTAP which is an associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Wtap pfam17098
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ...
68-222 2.61e-67

WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and pre-mRNA-splicing regulator WTAP from mammals. The former is required for female-specific splicing of Sex-lethal RNA, and the latter is a regulatory subunit of the RNA N6-methyladenosine methyltransferase. The family also includes the yeast Mum2p protein which is part of the Mis complex.


:

Pssm-ID: 465345 [Multi-domain]  Cd Length: 155  Bit Score: 210.23  E-value: 2.61e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291   68 ESARRENILVMRLATKEQEMQECTTQIQYLKQVQQPSVAQLRSTMVDPAINLFFLKMKGELEQTKDKLEQAQNELSAWKF 147
Cdd:pfam17098   1 ESKRRENLLLARLAEKEQEIQELKAQLQDLKQSLQPPSSQLRSLLLDPAVNLEFLRLKKELEEKKKKLKEAQLELAAWKF 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 165377291  148 TPDSQTGKKLMAKCRMLIQENQELGRQLSQGRIAQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTI 222
Cdd:pfam17098  81 TPDSTTGKRLMAKCRLLQQENEELGRQLSEGRIAKLEIELALQKKVVEELKKSLEELDEFLIELDEELEGLQSTL 155
 
Name Accession Description Interval E-value
Wtap pfam17098
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ...
68-222 2.61e-67

WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and pre-mRNA-splicing regulator WTAP from mammals. The former is required for female-specific splicing of Sex-lethal RNA, and the latter is a regulatory subunit of the RNA N6-methyladenosine methyltransferase. The family also includes the yeast Mum2p protein which is part of the Mis complex.


Pssm-ID: 465345 [Multi-domain]  Cd Length: 155  Bit Score: 210.23  E-value: 2.61e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291   68 ESARRENILVMRLATKEQEMQECTTQIQYLKQVQQPSVAQLRSTMVDPAINLFFLKMKGELEQTKDKLEQAQNELSAWKF 147
Cdd:pfam17098   1 ESKRRENLLLARLAEKEQEIQELKAQLQDLKQSLQPPSSQLRSLLLDPAVNLEFLRLKKELEEKKKKLKEAQLELAAWKF 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 165377291  148 TPDSQTGKKLMAKCRMLIQENQELGRQLSQGRIAQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTI 222
Cdd:pfam17098  81 TPDSTTGKRLMAKCRLLQQENEELGRQLSEGRIAKLEIELALQKKVVEELKKSLEELDEFLIELDEELEGLQSTL 155
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
29-233 1.24e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.32  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291  29 RWKQYEAYVQALEGKYTDL-NSNDVTGLrESEEKLKQQQQESARREnilvmrLATKEQEMQECTTQIQYLKQVQQPSVAQ 107
Cdd:COG3206  183 QLPELRKELEEAEAALEEFrQKNGLVDL-SEEAKLLLQQLSELESQ------LAEARAELAEAEARLAALRAQLGSGPDA 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291 108 LRSTMVDPAINlfflkmkgELEQTKDKLEQAQNELSAwKFTPDSQTGKKLMAKcrmlIQENQELGRQLSQGRIAQLEAEL 187
Cdd:COG3206  256 LPELLQSPVIQ--------QLRAQLAELEAELAELSA-RYTPNHPDVIALRAQ----IAALRAQLQQEAQRILASLEAEL 322
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 165377291 188 ALQKKYSEELKSSQDELNDFIIQLDEEvegmQSTILVLQQQLKETR 233
Cdd:COG3206  323 EALQAREASLQAQLAQLEARLAELPEL----EAELRRLEREVEVAR 364
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
23-233 5.02e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 5.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291    23 RDELILRWKQYEAYVQALEGKYTDLnSNDVTGLRESEEKLKQQQQESARRENILVMRLATKEQEMQECTTQIQYLkqvqQ 102
Cdd:TIGR02169  697 LRRIENRLDELSQELSDASRKIGEI-EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL----E 771
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291   103 PSVAQLRSTMVDPAINLFFLKMKgELEQTKDKLEQAQNELSAWKFTPDSQTGKKLMAK--CRMLIQENQELGRQLsQGRI 180
Cdd:TIGR02169  772 EDLHKLEEALNDLEARLSHSRIP-EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKeyLEKEIQELQEQRIDL-KEQI 849
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 165377291   181 AQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTILVLQQQLKETR 233
Cdd:TIGR02169  850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
PRK11281 PRK11281
mechanosensitive channel MscK;
60-231 7.32e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.90  E-value: 7.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291   60 EKLKQQQQESARreniLVMRLATKEQEMQECTTQIQYLKQVQQPSVAQLRSTMvdpaiNLFFLKMKgeLEQTKDKLEQAQ 139
Cdd:PRK11281   73 DKIDRQKEETEQ----LKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTL-----SLRQLESR--LAQTLDQLQNAQ 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291  140 NELSawkfTPDSQ----------------TGKKLMAKCRMLIQENQELGRQLSQGRIAQLEAELAL---QKKYSEE---- 196
Cdd:PRK11281  142 NDLA----EYNSQlvslqtqperaqaalyANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALlnaQNDLQRKsleg 217
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 165377291  197 -------LKSSQDELNDFIIQLDEEVEGMQSTI----LVL-QQQLKE 231
Cdd:PRK11281  218 ntqlqdlLQKQRDYLTARIQRLEHQLQLLQEAInskrLTLsEKTVQE 264
 
Name Accession Description Interval E-value
Wtap pfam17098
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ...
68-222 2.61e-67

WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and pre-mRNA-splicing regulator WTAP from mammals. The former is required for female-specific splicing of Sex-lethal RNA, and the latter is a regulatory subunit of the RNA N6-methyladenosine methyltransferase. The family also includes the yeast Mum2p protein which is part of the Mis complex.


Pssm-ID: 465345 [Multi-domain]  Cd Length: 155  Bit Score: 210.23  E-value: 2.61e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291   68 ESARRENILVMRLATKEQEMQECTTQIQYLKQVQQPSVAQLRSTMVDPAINLFFLKMKGELEQTKDKLEQAQNELSAWKF 147
Cdd:pfam17098   1 ESKRRENLLLARLAEKEQEIQELKAQLQDLKQSLQPPSSQLRSLLLDPAVNLEFLRLKKELEEKKKKLKEAQLELAAWKF 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 165377291  148 TPDSQTGKKLMAKCRMLIQENQELGRQLSQGRIAQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTI 222
Cdd:pfam17098  81 TPDSTTGKRLMAKCRLLQQENEELGRQLSEGRIAKLEIELALQKKVVEELKKSLEELDEFLIELDEELEGLQSTL 155
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
29-233 1.24e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.32  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291  29 RWKQYEAYVQALEGKYTDL-NSNDVTGLrESEEKLKQQQQESARREnilvmrLATKEQEMQECTTQIQYLKQVQQPSVAQ 107
Cdd:COG3206  183 QLPELRKELEEAEAALEEFrQKNGLVDL-SEEAKLLLQQLSELESQ------LAEARAELAEAEARLAALRAQLGSGPDA 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291 108 LRSTMVDPAINlfflkmkgELEQTKDKLEQAQNELSAwKFTPDSQTGKKLMAKcrmlIQENQELGRQLSQGRIAQLEAEL 187
Cdd:COG3206  256 LPELLQSPVIQ--------QLRAQLAELEAELAELSA-RYTPNHPDVIALRAQ----IAALRAQLQQEAQRILASLEAEL 322
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 165377291 188 ALQKKYSEELKSSQDELNDFIIQLDEEvegmQSTILVLQQQLKETR 233
Cdd:COG3206  323 EALQAREASLQAQLAQLEARLAELPEL----EAELRRLEREVEVAR 364
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
23-233 5.02e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 5.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291    23 RDELILRWKQYEAYVQALEGKYTDLnSNDVTGLRESEEKLKQQQQESARRENILVMRLATKEQEMQECTTQIQYLkqvqQ 102
Cdd:TIGR02169  697 LRRIENRLDELSQELSDASRKIGEI-EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL----E 771
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291   103 PSVAQLRSTMVDPAINLFFLKMKgELEQTKDKLEQAQNELSAWKFTPDSQTGKKLMAK--CRMLIQENQELGRQLsQGRI 180
Cdd:TIGR02169  772 EDLHKLEEALNDLEARLSHSRIP-EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKeyLEKEIQELQEQRIDL-KEQI 849
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 165377291   181 AQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTILVLQQQLKETR 233
Cdd:TIGR02169  850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
31-231 6.68e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 6.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291    31 KQYEAYVQALEGKYTDLN------SNDVTGLRESEEKLKQQQQESARRENILVMRLATKEQEMQECTTQIQYLKQVQQPS 104
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEkalaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291   105 VAQLRSTMVDPAINLFFLK-MKGELEQTKDKLEQAQNELSAWKftpdsqtgKKLMAKCRMLIQENQELGRQLSqgRIAQL 183
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAeAEAEIEELEAQIEQLKEELKALR--------EALDELRAELTLLNEEAANLRE--RLESL 829
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 165377291   184 EAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTILVLQQQLKE 231
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
PRK11281 PRK11281
mechanosensitive channel MscK;
60-231 7.32e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.90  E-value: 7.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291   60 EKLKQQQQESARreniLVMRLATKEQEMQECTTQIQYLKQVQQPSVAQLRSTMvdpaiNLFFLKMKgeLEQTKDKLEQAQ 139
Cdd:PRK11281   73 DKIDRQKEETEQ----LKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTL-----SLRQLESR--LAQTLDQLQNAQ 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291  140 NELSawkfTPDSQ----------------TGKKLMAKCRMLIQENQELGRQLSQGRIAQLEAELAL---QKKYSEE---- 196
Cdd:PRK11281  142 NDLA----EYNSQlvslqtqperaqaalyANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALlnaQNDLQRKsleg 217
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 165377291  197 -------LKSSQDELNDFIIQLDEEVEGMQSTI----LVL-QQQLKE 231
Cdd:PRK11281  218 ntqlqdlLQKQRDYLTARIQRLEHQLQLLQEAInskrLTLsEKTVQE 264
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
24-233 1.95e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291   24 DELILRWKQYEAYVQALEGKYTDL--NSNDVTGLRESEEKLKQQQQESARRENILVMRLATKEQEMQECTTQIQYLKQVQ 101
Cdd:COG4913   657 SWDEIDVASAEREIAELEAELERLdaSSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291  102 QPSV------------AQLRSTMVDPAINLFFLKMKGELEQTKDKLEQAQNEL--------SAWKF-TPDSQTGkkLMAk 160
Cdd:COG4913   737 EAAEdlarlelralleERFAAALGDAVERELRENLEERIDALRARLNRAEEELeramrafnREWPAeTADLDAD--LES- 813
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 165377291  161 crmlIQENQELGRQLSQGRIAQLEAELALQKKyseelKSSQDELNDFIIQLDEEVEGMQSTILVLQQQLKETR 233
Cdd:COG4913   814 ----LPEYLALLDRLEEDGLPEYEERFKELLN-----ENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRIP 877
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
34-216 2.29e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 2.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291  34 EAYVQALEGKYTDLNSNdvtgLRESEEKLKQQQQESARRENILVMRLATkeQEMQECTTQIQYLKQVQQPSVAQLRSTMV 113
Cdd:COG4942   68 ARRIRALEQELAALEAE----LAELEKEIAELRAELEAQKEELAELLRA--LYRLGRQPPLALLLSPEDFLDAVRRLQYL 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291 114 DpAINLFFLKMKGELEQTKDKLEQAQNELSAWKftpdsqtgKKLMAKCRMLIQENQELGRQLSQGR--IAQLEAELALQK 191
Cdd:COG4942  142 K-YLAPARREQAEELRADLAELAALRAELEAER--------AELEALLAELEEERAALEALKAERQklLARLEKELAELA 212
                        170       180
                 ....*....|....*....|....*
gi 165377291 192 KYSEELKSSQDELNDFIIQLDEEVE 216
Cdd:COG4942  213 AELAELQQEAEELEALIARLEAEAA 237
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
24-233 1.87e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291    24 DELILRWKQYEAYVQALEGKYTDLNS--NDVTG-LRESEEKLKQQQQESARRENILVmRLATKEQEMQECTTQIQYLKQV 100
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKELYALANeiSRLEQqKQILRERLANLERQLEELEAQLE-ELESKLDELAEELAELEEKLEE 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165377291   101 QQPSVAQLRSTMVDPAINLFFLK------------MKGELEQTKDKLEQAQNELSAWKftpdsQTGKKLMAKCRMLIQEN 168
Cdd:TIGR02168  349 LKEELESLEAELEELEAELEELEsrleeleeqletLRSKVAQLELQIASLNNEIERLE-----ARLERLEDRRERLQQEI 423
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 165377291   169 QELGRQLSQGRIAQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTILVLQQQLKETR 233
Cdd:TIGR02168  424 EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
 
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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