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Conserved domains on  [gi|21361159|ref|NP_004897|]
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pre-mRNA-splicing regulator WTAP isoform 1 [Homo sapiens]

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 2.05e-66

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: 207.92  E-value: 2.05e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159    68 ESARRENILVMRLATKEQEMQECTTQIQYLKQVQQPSVAQLRSTMVDPAINLFFLKMKGELEQTKDKLEQAQNELSAWKF 147
Cdd:pfam17098   1 ESKRRENLLLARLAEKEQEIQELKAQLQDLKQSLQPPSSQLRSLLLDPAVNLEFLRLKKELEEKKKKLKEAQLELAAWKF 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21361159   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 2.05e-66

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: 207.92  E-value: 2.05e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159    68 ESARRENILVMRLATKEQEMQECTTQIQYLKQVQQPSVAQLRSTMVDPAINLFFLKMKGELEQTKDKLEQAQNELSAWKF 147
Cdd:pfam17098   1 ESKRRENLLLARLAEKEQEIQELKAQLQDLKQSLQPPSSQLRSLLLDPAVNLEFLRLKKELEEKKKKLKEAQLELAAWKF 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21361159   148 TPDSQTGKKLMAKCRMLIQENQELGRQLSQGRIAQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTI 222
Cdd:pfam17098  81 TPDSTTGKRLMAKCRLLQQENEELGRQLSEGRIAKLEIELALQKKVVEELKKSLEELDEFLIELDEELEGLQSTL 155
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
29-233 2.45e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.63  E-value: 2.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159  29 RWKQYEAYVQALEGKYTDL-NSNDVTGLrESEEKLKQQQQESARREnilvmrLATKEQEMQECTTQIQYLKQVQQPSVAQ 107
Cdd:COG3206 183 QLPELRKELEEAEAALEEFrQKNGLVDL-SEEAKLLLQQLSELESQ------LAEARAELAEAEARLAALRAQLGSGPDA 255
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159 108 LRSTMVDPAINlfflkmkgELEQTKDKLEQAQNELSAwKFTPDSQTGKKLMAKCRMLIQE-NQELGRQLS---------Q 177
Cdd:COG3206 256 LPELLQSPVIQ--------QLRAQLAELEAELAELSA-RYTPNHPDVIALRAQIAALRAQlQQEAQRILAsleaelealQ 326
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21361159 178 GRIAQLEAELALQKKYSEELKSSQDELNdfiiQLDEEVEGMQSTILVLQQQLKETR 233
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPELEAELR----RLEREVEVARELYESLLQRLEEAR 378
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
23-233 7.47e-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: 45.06  E-value: 7.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159     23 RDELILRWKQYEAYVQALEGKYTDLnSNDVTGLRESEEKLKQQQQESARRENILVMRLATKEQEMQECTTQIQYLkqvqQ 102
Cdd:TIGR02169  697 LRRIENRLDELSQELSDASRKIGEI-EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL----E 771
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159    103 PSVAQLRSTMVDPAINLFFLKMKgELEQTKDKLEQAQNELSAWKFTPDSQTGKKLMAK--CRMLIQENQELGRQLsQGRI 180
Cdd:TIGR02169  772 EDLHKLEEALNDLEARLSHSRIP-EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKeyLEKEIQELQEQRIDL-KEQI 849
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 21361159    181 AQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTILVLQQQLKETR 233
Cdd:TIGR02169  850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
PRK11281 PRK11281
mechanosensitive channel MscK;
60-231 1.03e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.52  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159    60 EKLKQQQQESARreniLVMRLATKEQEMQECTTQIQYLKQVQQPSVAQLRSTMvdpaiNLFFLKMKgeLEQTKDKLEQAQ 139
Cdd:PRK11281   73 DKIDRQKEETEQ----LKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTL-----SLRQLESR--LAQTLDQLQNAQ 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159   140 NELSawkfTPDSQ----------------TGKKLMAKCRMLIQENQELGRQLSQGRIAQLEAELAL---QKKYSEE---- 196
Cdd:PRK11281  142 NDLA----EYNSQlvslqtqperaqaalyANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALlnaQNDLQRKsleg 217
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 21361159   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 2.05e-66

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: 207.92  E-value: 2.05e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159    68 ESARRENILVMRLATKEQEMQECTTQIQYLKQVQQPSVAQLRSTMVDPAINLFFLKMKGELEQTKDKLEQAQNELSAWKF 147
Cdd:pfam17098   1 ESKRRENLLLARLAEKEQEIQELKAQLQDLKQSLQPPSSQLRSLLLDPAVNLEFLRLKKELEEKKKKLKEAQLELAAWKF 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21361159   148 TPDSQTGKKLMAKCRMLIQENQELGRQLSQGRIAQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTI 222
Cdd:pfam17098  81 TPDSTTGKRLMAKCRLLQQENEELGRQLSEGRIAKLEIELALQKKVVEELKKSLEELDEFLIELDEELEGLQSTL 155
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
29-233 2.45e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.63  E-value: 2.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159  29 RWKQYEAYVQALEGKYTDL-NSNDVTGLrESEEKLKQQQQESARREnilvmrLATKEQEMQECTTQIQYLKQVQQPSVAQ 107
Cdd:COG3206 183 QLPELRKELEEAEAALEEFrQKNGLVDL-SEEAKLLLQQLSELESQ------LAEARAELAEAEARLAALRAQLGSGPDA 255
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159 108 LRSTMVDPAINlfflkmkgELEQTKDKLEQAQNELSAwKFTPDSQTGKKLMAKCRMLIQE-NQELGRQLS---------Q 177
Cdd:COG3206 256 LPELLQSPVIQ--------QLRAQLAELEAELAELSA-RYTPNHPDVIALRAQIAALRAQlQQEAQRILAsleaelealQ 326
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21361159 178 GRIAQLEAELALQKKYSEELKSSQDELNdfiiQLDEEVEGMQSTILVLQQQLKETR 233
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPELEAELR----RLEREVEVARELYESLLQRLEEAR 378
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
23-233 7.47e-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: 45.06  E-value: 7.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159     23 RDELILRWKQYEAYVQALEGKYTDLnSNDVTGLRESEEKLKQQQQESARRENILVMRLATKEQEMQECTTQIQYLkqvqQ 102
Cdd:TIGR02169  697 LRRIENRLDELSQELSDASRKIGEI-EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL----E 771
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159    103 PSVAQLRSTMVDPAINLFFLKMKgELEQTKDKLEQAQNELSAWKFTPDSQTGKKLMAK--CRMLIQENQELGRQLsQGRI 180
Cdd:TIGR02169  772 EDLHKLEEALNDLEARLSHSRIP-EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKeyLEKEIQELQEQRIDL-KEQI 849
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 21361159    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 9.62e-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: 44.66  E-value: 9.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159     31 KQYEAYVQALEGKYTDLN------SNDVTGLRESEEKLKQQQQESARRENILVMRLATKEQEMQECTTQIQYLKQVQQPS 104
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEkalaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159    105 VAQLRSTMVDPAINLFFLK-MKGELEQTKDKLEQAQNELSAWKftpdsqtgKKLMAKCRMLIQENQELGRQLSqgRIAQL 183
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAeAEAEIEELEAQIEQLKEELKALR--------EALDELRAELTLLNEEAANLRE--RLESL 829
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 21361159    184 EAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTILVLQQQLKE 231
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
PRK11281 PRK11281
mechanosensitive channel MscK;
60-231 1.03e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.52  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159    60 EKLKQQQQESARreniLVMRLATKEQEMQECTTQIQYLKQVQQPSVAQLRSTMvdpaiNLFFLKMKgeLEQTKDKLEQAQ 139
Cdd:PRK11281   73 DKIDRQKEETEQ----LKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTL-----SLRQLESR--LAQTLDQLQNAQ 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159   140 NELSawkfTPDSQ----------------TGKKLMAKCRMLIQENQELGRQLSQGRIAQLEAELAL---QKKYSEE---- 196
Cdd:PRK11281  142 NDLA----EYNSQlvslqtqperaqaalyANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALlnaQNDLQRKsleg 217
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 21361159   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 2.04e-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: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159   24 DELILRWKQYEAYVQALEGKYTDL--NSNDVTGLRESEEKLKQQQQESARRENILVMRLATKEQEMQECTTQIQYLKQVQ 101
Cdd:COG4913  657 SWDEIDVASAEREIAELEAELERLdaSSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159  102 QPSV------------AQLRSTMVDPAINLFFLKMKGELEQTKDKLEQAQNEL--------SAWKF-TPDSQTGkkLMAk 160
Cdd:COG4913  737 EAAEdlarlelralleERFAAALGDAVERELRENLEERIDALRARLNRAEEELeramrafnREWPAeTADLDAD--LES- 813
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361159  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 3.44e-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: 42.44  E-value: 3.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159  34 EAYVQALEGKYTDLNSNdvtgLRESEEKLKQQQQESARRENILVMRLATkeQEMQECTTQIQYLKQVQQPSVAQLRSTMV 113
Cdd:COG4942  68 ARRIRALEQELAALEAE----LAELEKEIAELRAELEAQKEELAELLRA--LYRLGRQPPLALLLSPEDFLDAVRRLQYL 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159 114 DpAINLFFLKMKGELEQTKDKLEQAQNELSAWKftpdsqtgKKLMAKCRMLIQENQELGRQLSQGR--IAQLEAELALQK 191
Cdd:COG4942 142 K-YLAPARREQAEELRADLAELAALRAELEAER--------AELEALLAELEEERAALEALKAERQklLARLEKELAELA 212
                       170       180
                ....*....|....*....|....*
gi 21361159 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 2.73e-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: 40.04  E-value: 2.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159     24 DELILRWKQYEAYVQALEGKYTDLNS--NDVTG-LRESEEKLKQQQQESARRENILVmRLATKEQEMQECTTQIQYLKQV 100
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKELYALANeiSRLEQqKQILRERLANLERQLEELEAQLE-ELESKLDELAEELAELEEKLEE 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159    101 QQPSVAQLRSTMVDPAINLFFLK------------MKGELEQTKDKLEQAQNELSAWKftpdsQTGKKLMAKCRMLIQEN 168
Cdd:TIGR02168  349 LKEELESLEAELEELEAELEELEsrleeleeqletLRSKVAQLELQIASLNNEIERLE-----ARLERLEDRRERLQQEI 423
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21361159    169 QELGRQLSQGRIAQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTILVLQQQLKETR 233
Cdd:TIGR02168  424 EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
31-233 4.96e-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: 39.27  E-value: 4.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159     31 KQYEAYVQALEGKYTDLNSNDVTGLRESEEKLKQQQQESARRENILVMRLATKEQEMQECTTQIQYLKQVQQPSVAQLRS 110
Cdd:TIGR02168  213 ERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361159    111 TMVDPAinlfflKMKGELEQTKDKLEQAQNELsawkftpdsqtgKKLMAKCRMLIQENQELGRQL--SQGRIAQLEAELA 188
Cdd:TIGR02168  293 LANEIS------RLEQQKQILRERLANLERQL------------EELEAQLEELESKLDELAEELaeLEEKLEELKEELE 354
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 21361159    189 LQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTILVLQQQLKETR 233
Cdd:TIGR02168  355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
 
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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