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Conserved domains on  [gi|41054117|ref|NP_956147|]
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pre-mRNA-splicing regulator WTAP [Danio rerio]

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 1.22e-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: 209.46  E-value: 1.22e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117    68 ESARRENILVMRLATKEQEMQECTTQIQYLKQVQQPSAAQLRSSMVDPAINLFFLKMKAELEQTKDKLEQAQNELSAWKF 147
Cdd:pfam17098   1 ESKRRENLLLARLAEKEQEIQELKAQLQDLKQSLQPPSSQLRSLLLDPAVNLEFLRLKKELEEKKKKLKEAQLELAAWKF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41054117   148 TPDSQTGKKLMAKCRMLIQENQELGRQLSQGRIAQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTI 222
Cdd:pfam17098  81 TPDSTTGKRLMAKCRLLQQENEELGRQLSEGRIAKLEIELALQKKVVEELKKSLEELDEFLIELDEELEGLQSTL 155
PTZ00108 super family cl36510
DNA topoisomerase 2-like protein; Provisional
 179-419 4.83e-03

DNA topoisomerase 2-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00108:

Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 39.26  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117   179 RIAQLEAELALQKKYSEELKSSQ------DELNDFIIQLDEEVEGMQSTILvlqqqlreTRQQLSQMnqtqgTSSGAGPS 252
Cdd:PTZ00108 1103 KVEKLNAELEKKEKELEKLKNTTpkdmwlEDLDKFEEALEEQEEVEEKEIA--------KEQRLKSK-----TKGKASKL 1169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117   253 RTSPST-ASEPSTQSEPANASSSNVGKDCGRVSNGPSNGNSSQRGASGSSLYrEASSADEDYPPSPSVSSPTHDGISKLS 331
Cdd:PTZ00108 1170 RKPKLKkKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSS-GSDQEDDEEQKTKPKKSSVKRLKSKKN 1248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117   332 NHSEDAVSQRGGEGYVTQLSAGYESVDSPTGSETSVTQHSNDT-----DSNADSHEAAAVPKGSRTAGTRHSTQNGLDSS 406
Cdd:PTZ00108 1249 NSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRpdgesNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSE 1328

                         250
                  ....*....|...
gi 41054117   407 AAAVATNTSNASA 419
Cdd:PTZ00108 1329 KKTARKKKSKTRV 1341
 
Name Accession Description Interval E-value
Wtap pfam17098
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ...
 68-222 1.22e-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: 209.46  E-value: 1.22e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117    68 ESARRENILVMRLATKEQEMQECTTQIQYLKQVQQPSAAQLRSSMVDPAINLFFLKMKAELEQTKDKLEQAQNELSAWKF 147
Cdd:pfam17098   1 ESKRRENLLLARLAEKEQEIQELKAQLQDLKQSLQPPSSQLRSLLLDPAVNLEFLRLKKELEEKKKKLKEAQLELAAWKF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41054117   148 TPDSQTGKKLMAKCRMLIQENQELGRQLSQGRIAQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTI 222
Cdd:pfam17098  81 TPDSTTGKRLMAKCRLLQQENEELGRQLSEGRIAKLEIELALQKKVVEELKKSLEELDEFLIELDEELEGLQSTL 155
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 49-240 1.03e-06

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: 51.22  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117     49 SNDVTGLKESEEKLKQQQQESARRENILVMRLATKEQEMQECTTQIQYLkqvqQPSAAQLRSSMVDPAINLFFLKMKaEL 128
Cdd:TIGR02169  722 EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL----EEDLHKLEEALNDLEARLSHSRIP-EI 796

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117    129 EQTKDKLEQAQNELSAWKFTPDSQTGKKLMAK--CRMLIQENQELGRQLsQGRIAQLEAELALQKKYSEELKSSQDELND 206
Cdd:TIGR02169  797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKeyLEKEIQELQEQRIDL-KEQIKSIEKEIENLNGKKEELEEELEELEA 875

                          170       180       190
                   ....*....|....*....|....*....|....
gi 41054117    207 FIIQLDEEVEGMQSTILVLQQQLRETRQQLSQMN 240
Cdd:TIGR02169  876 ALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
PRK11281 PRK11281
mechanosensitive channel MscK;
60-247 5.93e-06

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 48.75  E-value: 5.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117    60 EKLKQQQQESARreniLVMRLATKEQEMQECTTQIQYLKQVQQPSAAQLRSSMVDPainlfflKMKAELEQTKDKLEQAQ 139
Cdd:PRK11281   73 DKIDRQKEETEQ----LKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSLR-------QLESRLAQTLDQLQNAQ 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117   140 NELSawkfTPDSQ----------------TGKKLMAKCRMLIQENQELGRQLSQGRIAQLEAELAL---QKKYSEE---- 196
Cdd:PRK11281  142 NDLA----EYNSQlvslqtqperaqaalyANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALlnaQNDLQRKsleg 217

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 41054117   197 -------LKSSQDELNDFIIQLDEEVEGMQStiLVLQQQLRETRQQLSQMNQTQGTSS 247
Cdd:PRK11281  218 ntqlqdlLQKQRDYLTARIQRLEHQLQLLQE--AINSKRLTLSEKTVQEAQSQDEAAR 273
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
55-238 2.31e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.55  E-value: 2.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117  55 LKESEEKLKQQQQES-----ARRENILVMRLATKEQEMQECTTQIQYLKQvqqpSAAQLRSSMVDPAINLFFLKMKAELE 129
Cdd:COG3206 191 LEEAEAALEEFRQKNglvdlSEEAKLLLQQLSELESQLAEARAELAEAEA----RLAALRAQLGSGPDALPELLQSPVIQ 266

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117 130 QTKDKLEQAQNELSAW--KFTPDSQTGKKLMAKCRMLIQE-NQELGRQLS---------QGRIAQLEAELALQKKYSEEL 197
Cdd:COG3206 267 QLRAQLAELEAELAELsaRYTPNHPDVIALRAQIAALRAQlQQEAQRILAsleaelealQAREASLQAQLAQLEARLAEL 346

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 41054117 198 KSSQDELNdfiiQLDEEVEGMQSTILVLQQQLRETRQQLSQ 238
Cdd:COG3206 347 PELEAELR----RLEREVEVARELYESLLQRLEEARLAEAL 383
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 179-419 4.83e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 39.26  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117   179 RIAQLEAELALQKKYSEELKSSQ------DELNDFIIQLDEEVEGMQSTILvlqqqlreTRQQLSQMnqtqgTSSGAGPS 252
Cdd:PTZ00108 1103 KVEKLNAELEKKEKELEKLKNTTpkdmwlEDLDKFEEALEEQEEVEEKEIA--------KEQRLKSK-----TKGKASKL 1169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117   253 RTSPST-ASEPSTQSEPANASSSNVGKDCGRVSNGPSNGNSSQRGASGSSLYrEASSADEDYPPSPSVSSPTHDGISKLS 331
Cdd:PTZ00108 1170 RKPKLKkKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSS-GSDQEDDEEQKTKPKKSSVKRLKSKKN 1248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117   332 NHSEDAVSQRGGEGYVTQLSAGYESVDSPTGSETSVTQHSNDT-----DSNADSHEAAAVPKGSRTAGTRHSTQNGLDSS 406
Cdd:PTZ00108 1249 NSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRpdgesNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSE 1328

                         250
                  ....*....|...
gi 41054117   407 AAAVATNTSNASA 419
Cdd:PTZ00108 1329 KKTARKKKSKTRV 1341
 
Name Accession Description Interval E-value
Wtap pfam17098
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ...
 68-222 1.22e-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: 209.46  E-value: 1.22e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117    68 ESARRENILVMRLATKEQEMQECTTQIQYLKQVQQPSAAQLRSSMVDPAINLFFLKMKAELEQTKDKLEQAQNELSAWKF 147
Cdd:pfam17098   1 ESKRRENLLLARLAEKEQEIQELKAQLQDLKQSLQPPSSQLRSLLLDPAVNLEFLRLKKELEEKKKKLKEAQLELAAWKF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41054117   148 TPDSQTGKKLMAKCRMLIQENQELGRQLSQGRIAQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTI 222
Cdd:pfam17098  81 TPDSTTGKRLMAKCRLLQQENEELGRQLSEGRIAKLEIELALQKKVVEELKKSLEELDEFLIELDEELEGLQSTL 155
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 49-240 1.03e-06

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: 51.22  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117     49 SNDVTGLKESEEKLKQQQQESARRENILVMRLATKEQEMQECTTQIQYLkqvqQPSAAQLRSSMVDPAINLFFLKMKaEL 128
Cdd:TIGR02169  722 EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL----EEDLHKLEEALNDLEARLSHSRIP-EI 796

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117    129 EQTKDKLEQAQNELSAWKFTPDSQTGKKLMAK--CRMLIQENQELGRQLsQGRIAQLEAELALQKKYSEELKSSQDELND 206
Cdd:TIGR02169  797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKeyLEKEIQELQEQRIDL-KEQIKSIEKEIENLNGKKEELEEELEELEA 875

                          170       180       190
                   ....*....|....*....|....*....|....
gi 41054117    207 FIIQLDEEVEGMQSTILVLQQQLRETRQQLSQMN 240
Cdd:TIGR02169  876 ALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
PRK11281 PRK11281
mechanosensitive channel MscK;
60-247 5.93e-06

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 48.75  E-value: 5.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117    60 EKLKQQQQESARreniLVMRLATKEQEMQECTTQIQYLKQVQQPSAAQLRSSMVDPainlfflKMKAELEQTKDKLEQAQ 139
Cdd:PRK11281   73 DKIDRQKEETEQ----LKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSLR-------QLESRLAQTLDQLQNAQ 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117   140 NELSawkfTPDSQ----------------TGKKLMAKCRMLIQENQELGRQLSQGRIAQLEAELAL---QKKYSEE---- 196
Cdd:PRK11281  142 NDLA----EYNSQlvslqtqperaqaalyANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALlnaQNDLQRKsleg 217

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 41054117   197 -------LKSSQDELNDFIIQLDEEVEGMQStiLVLQQQLRETRQQLSQMNQTQGTSS 247
Cdd:PRK11281  218 ntqlqdlLQKQRDYLTARIQRLEHQLQLLQE--AINSKRLTLSEKTVQEAQSQDEAAR 273
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
55-238 2.31e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.55  E-value: 2.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117  55 LKESEEKLKQQQQES-----ARRENILVMRLATKEQEMQECTTQIQYLKQvqqpSAAQLRSSMVDPAINLFFLKMKAELE 129
Cdd:COG3206 191 LEEAEAALEEFRQKNglvdlSEEAKLLLQQLSELESQLAEARAELAEAEA----RLAALRAQLGSGPDALPELLQSPVIQ 266

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117 130 QTKDKLEQAQNELSAW--KFTPDSQTGKKLMAKCRMLIQE-NQELGRQLS---------QGRIAQLEAELALQKKYSEEL 197
Cdd:COG3206 267 QLRAQLAELEAELAELsaRYTPNHPDVIALRAQIAALRAQlQQEAQRILAsleaelealQAREASLQAQLAQLEARLAEL 346

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 41054117 198 KSSQDELNdfiiQLDEEVEGMQSTILVLQQQLRETRQQLSQ 238
Cdd:COG3206 347 PELEAELR----RLEREVEVARELYESLLQRLEEARLAEAL 383
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 5-250 2.95e-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: 46.59  E-value: 2.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117      5 EPLPKKVRLSESDMKTLTRE--ELCTRWKQHETYVQMLEAKYADLNS--NDVTGLKESEEKLKQQQQESARRENILVMRL 80
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAElqELEEKLEELRLEVSELEEEIEELQKelYALANEISRLEQQKQILRERLANLERQLEEL 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117     81 AT-------KEQEMQECTTQIQYLKQVQQPSAAQLRSSMVDPAINLFFLKMK-----AELEQTKDKLEQAQNELSAW--K 146
Cdd:TIGR02168  322 EAqleelesKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleeleEQLETLRSKVAQLELQIASLnnE 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117    147 FTPDSQTGKKLMAKCRMLIQENQELGRQLSQGRIAQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTILVLQ 226
Cdd:TIGR02168  402 IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481

                          250       260
                   ....*....|....*....|....
gi 41054117    227 QQLRETRQQLSQMNQTQGTSSGAG 250
Cdd:TIGR02168  482 RELAQLQARLDSLERLQENLEGFS 505
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 31-241 5.26e-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: 45.82  E-value: 5.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117     31 KQHETYVQMLEAKYADLN------SNDVTGLKESEEKLKQQQQESARRENILVMRLATKEQEMQECTTQIQYLKQVQQPS 104
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEkalaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117    105 AAQLRSSMVDPAINLFFLK-MKAELEQTKDKLEQAQNELSAWKFTPDSQTGK---------KLMAKCRMLIQENQELGRQ 174
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAeAEAEIEELEAQIEQLKEELKALREALDELRAEltllneeaaNLRERLESLERRIAATERR 839

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054117    175 L--SQGRIAQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTILVLQQQLRETRQQLSQMNQ 241
Cdd:TIGR02168  840 LedLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
59-243 7.21e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.01  E-value: 7.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117  59 EEKLKQQQQESARRENILVMRLATKEQEMQECTTQIQYLKQVQQPSAAQLRSSMVDPAINlfflKMKAELEQTKDKLEQA 138
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLS----ELESQLAEARAELAEA 238

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117 139 QNELSAWKftpdSQTGKKLMAKCRmlIQENQELGRQLSQgrIAQLEAELA-LQKKYSEE--------------LKSSQDE 203
Cdd:COG3206 239 EARLAALR----AQLGSGPDALPE--LLQSPVIQQLRAQ--LAELEAELAeLSARYTPNhpdvialraqiaalRAQLQQE 310

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 41054117 204 LNDFIIQLDEEVEGMQSTILVLQQQLRETRQQLSQMNQTQ 243
Cdd:COG3206 311 AQRILASLEAELEALQAREASLQAQLAQLEARLAELPELE 350
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
38-238 8.59e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 8.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117   38 QMLEAK--YADLNS--NDVTGLKESEEKLKQQQqesaRRENIL--VMRLATKEQEMQECTTQIQYLKQVQQPSAAQLRSS 111
Cdd:COG4913  216 YMLEEPdtFEAADAlvEHFDDLERAHEALEDAR----EQIELLepIRELAERYAAARERLAELEYLRAALRLWFAQRRLE 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117  112 MVDPAInlffLKMKAELEQTKDKLEQAQNELSAwkftpdsqtgkkLMAKCRMLIQENQELGRQlsqgRIAQLEAELALQK 191
Cdd:COG4913  292 LLEAEL----EELRAELARLEAELERLEARLDA------------LREELDELEAQIRGNGGD----RLEQLEREIERLE 351

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 41054117  192 KYSEELKSSQDELNDFIIQLDEEVEGMQSTILVLQQQLRETRQQLSQ 238
Cdd:COG4913  352 RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 60-243 1.60e-04

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: 44.28  E-value: 1.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117     60 EKLKQQQQESARRENILVMRLATKEQEMQECTTQIQYLKQVQQpsaaQLRSSMVDPAINLFFLKMKAE-LEQTKDKLEQA 138
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE----ELSRQISALRKDLARLEAEVEqLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117    139 QNELSAWKFTPDSQtgkklMAKCRMLIQEnQELGRQLSQGRIAQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGM 218
Cdd:TIGR02168  756 LTELEAEIEELEER-----LEEAEEELAE-AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829

                          170       180
                   ....*....|....*....|....*
gi 41054117    219 QSTILVLQQQLRETRQQLSQMNQTQ 243
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDI 854
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 37-216 2.41e-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: 43.21  E-value: 2.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117  37 VQMLEAKYADLNSNdvtgLKESEEKLKQQQQESARRENILVMRLATkeQEMQECTTQIQYLKQVQQPSAAQLRSSMVDpA 116
Cdd:COG4942  71 IRALEQELAALEAE----LAELEKEIAELRAELEAQKEELAELLRA--LYRLGRQPPLALLLSPEDFLDAVRRLQYLK-Y 143

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117 117 INLFFLKMKAELEQTKDKLEQAQNELSAWKftpdsqtgKKLMAKCRMLIQENQELGRQLSQGR--IAQLEAELALQKKYS 194
Cdd:COG4942 144 LAPARREQAEELRADLAELAALRAELEAER--------AELEALLAELEEERAALEALKAERQklLARLEKELAELAAEL 215

                       170       180
                ....*....|....*....|..
gi 41054117 195 EELKSSQDELNDFIIQLDEEVE 216
Cdd:COG4942 216 AELQQEAEELEALIARLEAEAA 237
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
30-233 6.76e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 6.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117   30 WKQHETYVQMLEAKYADL--NSNDVTGLKESEEKLKQQQQESARRENILVMRLATKEQEMQECTTQIQYLKQVQQPS--- 104
Cdd:COG4913  663 VASAEREIAELEAELERLdaSSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAedl 742

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117  105 ---------AAQLRSSMVDPAINLFFLKMKAELEQTKDKLEQAQNEL--------SAWKF-TPDSQTGkkLMAkcrmlIQ 166
Cdd:COG4913  743 arlelrallEERFAAALGDAVERELRENLEERIDALRARLNRAEEELeramrafnREWPAeTADLDAD--LES-----LP 815

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41054117  167 ENQELGRQLSQGRIAQLEAELALQKKyseelKSSQDELNDFIIQLDEEVEGMQSTILVLQQQLRETR 233
Cdd:COG4913  816 EYLALLDRLEEDGLPEYEERFKELLN-----ENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRIP 877
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 124-241 8.53e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.61  E-value: 8.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117 124 MKAELEQTKDKLEQAQNELSAwkftpdsqtgkklmakcrmLIQENQELgrqlSQGRIAQLEAELALQKKYSEELKS---S 200
Cdd:COG0542 409 KPEELDELERRLEQLEIEKEA-------------------LKKEQDEA----SFERLAELRDELAELEEELEALKArweA 465

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 41054117 201 QDELNDFIIQLDEEVEGMQSTILVLQQQLRETRQQLSQMNQ 241
Cdd:COG0542 466 EKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAP 506
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
5-216 2.36e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117    5 EPLPKKVRLSESDMKTLtrEElctRWKQHETYVQMLEAKYADLNSN--DVTGLKESEE---KLKQQQQESARRENILVMR 79
Cdd:PRK03918 241 EELEKELESLEGSKRKL--EE---KIRELEERIEELKKEIEELEEKvkELKELKEKAEeyiKLSEFYEEYLDELREIEKR 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117   80 LATKEQEMQECTTQIQYLKqvqqpsaaqlrssmvdpainlfflKMKAELEQTKDKLEQAQNELSAWKftpdsqTGKKLMA 159
Cdd:PRK03918 316 LSRLEEEINGIEERIKELE------------------------EKEERLEELKKKLKELEKRLEELE------ERHELYE 365

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 41054117  160 KCRMLIQENQELGRQLSQGRIAQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVE 216
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK 422
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 61-243 3.02e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 3.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117  61 KLKQQQQESARRENILVMRLATKEQEMQEctTQIQYLKQVQQPSAAQLRssmvdpainlfflKMKAELEQTKDKLEQAQN 140
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELE--AELEELEAELEELEAELA-------------ELEAELEELRLELEELEL 281

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117 141 ELSAwkFTPDSQTGKKLMAKCRMLIQENQELGRQLSQgRIAQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQS 220
Cdd:COG1196 282 ELEE--AQAEEYELLAELARLEQDIARLEERRRELEE-RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358

                       170       180
                ....*....|....*....|...
gi 41054117 221 TILVLQQQLRETRQQLSQMNQTQ 243
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEEL 381
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 34-240 3.18e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 39.82  E-value: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117   34 ETYVQMLEAKYaDLNSNDVTG-LKESEEKLKQQQqesarrENILVMRLATKEQEMQECTTQIQYL-----KQVQ-QPSAA 106
Cdd:PRK04778 237 AGYRELVEEGY-HLDHLDIEKeIQDLKEQIDENL------ALLEELDLDEAEEKNEEIQERIDQLydileREVKaRKYVE 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117  107 QLRSSMVDpainlFFLKMKAELEQTKDKLEQAQN--ELSAwkftPDSQTGKKLMAKCRMLIQENQELGRQLSQGRIA--Q 182
Cdd:PRK04778 310 KNSDTLPD-----FLEHAKEQNKELKEEIDRVKQsyTLNE----SELESVRQLEKQLESLEKQYDEITERIAEQEIAysE 380

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 41054117  183 LEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTILVLQQQLRETRQQLSQMN 240
Cdd:PRK04778 381 LQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKSN 438
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 56-238 3.92e-03

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: 39.67  E-value: 3.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117     56 KESEEKLKQQQQESARRE---NILVMRLATKEQEMQECTTQIQYLKQVQQPSAAQLRssmvdpainlfflKMKAELEQTK 132
Cdd:TIGR02169  205 REREKAERYQALLKEKREyegYELLKEKEALERQKEAIERQLASLEEELEKLTEEIS-------------ELEKRLEEIE 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117    133 DKLEQAQNELSAWKFTPDSQTGKKL------MAKCRMLIQENQELGRQLsQGRIAQLEAELALQKKYSEELKSSQDELND 206
Cdd:TIGR02169  272 QLLEELNKKIKDLGEEEQLRVKEKIgeleaeIASLERSIAEKERELEDA-EERLAKLEAEIDKLLAEIEELEREIEEERK 350

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 41054117    207 FIIQLDEEVEGMQSTILVLQQQL-------RETRQQLSQ 238
Cdd:TIGR02169  351 RRDKLTEEYAELKEELEDLRAELeevdkefAETRDELKD 389
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 71-240 4.41e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.23  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117    71 RRENILVMRLATKEQEMQECTTQIQYLKQVQ---QPSAAQLRSSMVDpaINLFFLKMKAELEQTKDKLEQAQNELSAwKF 147
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNnqlKDNIEKKQQEINE--KTTEISNTQTQLNQLKDEQNKIKKQLSE-KQ 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117   148 TPDSQTGKKLMAKCRMLIQ---ENQELGRQLSQGRIAQLEAELALQKKYSEELKS-------SQDELNDFIIQLDEEVEG 217
Cdd:TIGR04523 274 KELEQNNKKIKELEKQLNQlksEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNqisqnnkIISQLNEQISQLKKELTN 353

                         170       180
                  ....*....|....*....|...
gi 41054117   218 MQSTILVLQQQLRETRQQLSQMN 240
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLK 376
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 179-419 4.83e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 39.26  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117   179 RIAQLEAELALQKKYSEELKSSQ------DELNDFIIQLDEEVEGMQSTILvlqqqlreTRQQLSQMnqtqgTSSGAGPS 252
Cdd:PTZ00108 1103 KVEKLNAELEKKEKELEKLKNTTpkdmwlEDLDKFEEALEEQEEVEEKEIA--------KEQRLKSK-----TKGKASKL 1169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117   253 RTSPST-ASEPSTQSEPANASSSNVGKDCGRVSNGPSNGNSSQRGASGSSLYrEASSADEDYPPSPSVSSPTHDGISKLS 331
Cdd:PTZ00108 1170 RKPKLKkKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSS-GSDQEDDEEQKTKPKKSSVKRLKSKKN 1248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117   332 NHSEDAVSQRGGEGYVTQLSAGYESVDSPTGSETSVTQHSNDT-----DSNADSHEAAAVPKGSRTAGTRHSTQNGLDSS 406
Cdd:PTZ00108 1249 NSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRpdgesNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSE 1328

                         250
                  ....*....|...
gi 41054117   407 AAAVATNTSNASA 419
Cdd:PTZ00108 1329 KKTARKKKSKTRV 1341
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
125-238 5.07e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 5.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117 125 KAELEQTKDKLEQAQNELSAWKftpDSQTGKKLMAKCRMLIQENQELGRQLS--QGRIAQLEAELALQKKYSEELKSSQD 202
Cdd:COG4717  94 QEELEELEEELEELEAELEELR---EELEKLEKLLQLLPLYQELEALEAELAelPERLEELEERLEELRELEEELEELEA 170

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 41054117 203 ELNDFIIQLDEEVEGMQSTILVLQQQLRETRQQLSQ 238
Cdd:COG4717 171 ELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 123-238 5.58e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.37  E-value: 5.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117 123 KMKAELEQTKDKLEQAQNELSAWKftpDSQTGKKL-MAKCRMLIQENQElgrQLSQGR----IAQLEAELALQKKyseel 197
Cdd:COG1579  35 ELEDELAALEARLEAAKTELEDLE---KEIKRLELeIEEVEARIKKYEE---QLGNVRnnkeYEALQKEIESLKR----- 103

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 41054117 198 ksSQDELNDFIIQLDEEVEGMQSTILVLQQQLRETRQQLSQ 238
Cdd:COG1579 104 --RISDLEDEILELMERIEELEEELAELEAELAELEAELEE 142
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 71-244 6.04e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 38.95  E-value: 6.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117     71 RRE----NILVMRLATKEQEMQ-ECTTQIQylkqvQQPSAAQLRSSMVDPAINLfflkmKAELEQTKDKLEQAQNELSAW 145
Cdd:pfam15921  418 RRElddrNMEVQRLEALLKAMKsECQGQME-----RQMAAIQGKNESLEKVSSL-----TAQLESTKEMLRKVVEELTAK 487

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117    146 KFTPDSQtgKKLMAKCRMLIQEnQELGRQLSQGRIAQLEAELALQKKYSEELKSSQDELNDFIIQLDE---EVEGMQSTI 222
Cdd:pfam15921  488 KMTLESS--ERTVSDLTASLQE-KERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEAlklQMAEKDKVI 564

                          170       180
                   ....*....|....*....|..
gi 41054117    223 LVLQQQLRETRQQLSQMNQTQG 244
Cdd:pfam15921  565 EILRQQIENMTQLVGQHGRTAG 586
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 50-255 6.86e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 38.20  E-value: 6.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117    50 NDVTGLKESEEKLKQQQQESarreNILVMRLATKEQEMQECTTQIQYLKQVQQPSAAQLRSSMVDPAINlfFLKMKAELE 129
Cdd:pfam09787  37 EGLDSSTALTLELEELRQER----DLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQ--LATERSARR 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117   130 QTKDKLEQAQNELSAwkftpdsqtgkklmakcrmlIQENQELGRQLSQGRIAQLEAE---LALQKKYSEELKSSQDELND 206
Cdd:pfam09787 111 EAEAELERLQEELRY--------------------LEEELRRSKATLQSRIKDREAEiekLRNQLTSKSQSSSSQSELEN 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 41054117   207 FIIQLDEEVEGMQSTILVLQQQLRETRQQLSQMNQTQGTSSGAGPSRTS 255
Cdd:pfam09787 171 RLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQQIKELQGEGSNGTS 219
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
55-243 7.42e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 7.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117  55 LKESEEKLKQQQQESARrenilvmrLATKEQEMQECTTQIQYLKQVQqpSAAQLRSSMVDPAINLFFL-----KMKAELE 129
Cdd:COG4717  73 LKELEEELKEAEEKEEE--------YAELQEELEELEEELEELEAEL--EELREELEKLEKLLQLLPLyqeleALEAELA 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117 130 QTKDKLEQAQNELSAWKftpdsqtgkKLMAKCRMLIQENQELgrqlsQGRIAQLEAELALQKKysEELKSSQDELNdfii 209
Cdd:COG4717 143 ELPERLEELEERLEELR---------ELEEELEELEAELAEL-----QEELEELLEQLSLATE--EELQDLAEELE---- 202

                       170       180       190
                ....*....|....*....|....*....|....
gi 41054117 210 QLDEEVEGMQSTILVLQQQLRETRQQLSQMNQTQ 243
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 55-243 8.04e-03

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: 38.21  E-value: 8.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117  55 LKESEEKLKQQQQESARRENILVMRLATKEQEMQECTTQIQYLKQVQQPSAAQLRSSMVDPAinlfflKMKAELEQTKDK 134
Cdd:COG4942  32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA------ELRAELEAQKEE 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054117 135 LEQ---------AQNELSAWKFTPDSQTGKKLMAKCRMLIQENQELGRQLsQGRIAQLEAELALQKKYSEELKSSQDELN 205
Cdd:COG4942 106 LAEllralyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL-RADLAELAALRAELEAERAELEALLAELE 184

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 41054117 206 DFIIQLDEEVEGMQSTILVLQQQLRETRQQLSQMNQTQ 243
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
 
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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