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Conserved domains on  [gi|1958793318|ref|XP_038936322|]
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keratin, type II cytoskeletal 79 isoform X3 [Rattus norvegicus]

Protein Classification

intermediate filament family protein( domain architecture ID 705869)

intermediate filament (IF) family protein is a primordial component of the cytoskeleton and the nuclear envelope; such as type I keratins

CATH:  1.20.5.170
Gene Ontology:  GO:0005882

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Filament super family cl25641
Intermediate filament protein;
1-197 2.54e-85

Intermediate filament protein;


The actual alignment was detected with superfamily member pfam00038:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 257.54  E-value: 2.54e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318   1 MGRMDLQSKVESLIQEIDFLQQLHEMELSQVQTSVSDTNVILSMDNNRSLDLDSIIAEVKAQYELIAQKSRAEAESWYQT 80
Cdd:pfam00038 117 LARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQS 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318  81 KYEELQVTAGKHGDSLRDTKNEISELTRTIQRLQGEVDAVKKQCQQLQTAIAESEQNGEMALKDAKKKLGDLDTALHQAK 160
Cdd:pfam00038 197 KLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETR 276
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958793318 161 EDLARMLREYQDLVSVKLALDMEIATYRKLLESEESR 197
Cdd:pfam00038 277 QEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
1-197 2.54e-85

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 257.54  E-value: 2.54e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318   1 MGRMDLQSKVESLIQEIDFLQQLHEMELSQVQTSVSDTNVILSMDNNRSLDLDSIIAEVKAQYELIAQKSRAEAESWYQT 80
Cdd:pfam00038 117 LARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQS 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318  81 KYEELQVTAGKHGDSLRDTKNEISELTRTIQRLQGEVDAVKKQCQQLQTAIAESEQNGEMALKDAKKKLGDLDTALHQAK 160
Cdd:pfam00038 197 KLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETR 276
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958793318 161 EDLARMLREYQDLVSVKLALDMEIATYRKLLESEESR 197
Cdd:pfam00038 277 QEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
99-197 3.57e-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: 41.97  E-value: 3.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318   99 TKNEISELTRTIQRLQGEVDAVKKQCQQLQTAIAESEQNgemaLKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKL 178
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEE----LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
                           90
                   ....*....|....*....
gi 1958793318  179 ALDMEIATYRKLLESEESR 197
Cdd:TIGR02168  751 QLSKELTELEAEIEELEER 769
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
6-173 1.96e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318   6 LQSKVESLIQEIDFLQQLHEmELSQVQTSVSDTNVILSMdnnrsldldsiIAEVKAQYELIAQKSRAEAE-SWYQTKYEE 84
Cdd:COG4717    83 AEEKEEEYAELQEELEELEE-ELEELEAELEELREELEK-----------LEKLLQLLPLYQELEALEAElAELPERLEE 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318  85 LQvtagKHGDSLRDTKNEISELTRTIQRLQgevdavkkqcQQLQTAIAESEQNGEMALKDAKKKLGDLDTALHQAKEDLA 164
Cdd:COG4717   151 LE----ERLEELRELEEELEELEAELAELQ----------EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216

                  ....*....
gi 1958793318 165 RMLREYQDL 173
Cdd:COG4717   217 EAQEELEEL 225
46 PHA02562
endonuclease subunit; Provisional
49-197 4.06e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 38.46  E-value: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318  49 SLDLDSIIAEVKAQYELI--AQKSRAEAESWYQTKYEELQVTAGKHGDSLRDTKNEISELTRT-------IQRLQGEVDA 119
Cdd:PHA02562  187 DMKIDHIQQQIKTYNKNIeeQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDiedpsaaLNKLNTAAAK 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318 120 VKKQCQQLQTAIAESEQNGE-----MALKDAKKKLGDLDTALHQ----------AKEDLARMLREYQDLVSVKLALDMEI 184
Cdd:PHA02562  267 IKSKIEQFQKVIKMYEKGGVcptctQQISEGPDRITKIKDKLKElqhslekldtAIDELEEIMDEFNEQSKKLLELKNKI 346
                         170
                  ....*....|...
gi 1958793318 185 ATYRKLLESEESR 197
Cdd:PHA02562  347 STNKQSLITLVDK 359
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
1-197 2.54e-85

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 257.54  E-value: 2.54e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318   1 MGRMDLQSKVESLIQEIDFLQQLHEMELSQVQTSVSDTNVILSMDNNRSLDLDSIIAEVKAQYELIAQKSRAEAESWYQT 80
Cdd:pfam00038 117 LARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQS 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318  81 KYEELQVTAGKHGDSLRDTKNEISELTRTIQRLQGEVDAVKKQCQQLQTAIAESEQNGEMALKDAKKKLGDLDTALHQAK 160
Cdd:pfam00038 197 KLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETR 276
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958793318 161 EDLARMLREYQDLVSVKLALDMEIATYRKLLESEESR 197
Cdd:pfam00038 277 QEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
99-197 3.57e-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: 41.97  E-value: 3.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318   99 TKNEISELTRTIQRLQGEVDAVKKQCQQLQTAIAESEQNgemaLKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKL 178
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEE----LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
                           90
                   ....*....|....*....
gi 1958793318  179 ALDMEIATYRKLLESEESR 197
Cdd:TIGR02168  751 QLSKELTELEAEIEELEER 769
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
3-199 1.43e-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: 40.05  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318    3 RMDLQSKVESLIQEIDFLqqlhEMELSQVQTSVSDTNVILSMDNNRSLDLDSIIAEVKAQYELIA--QKSRAEAESWYQT 80
Cdd:TIGR02169  786 ARLSHSRIPEIQAELSKL----EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKeqIKSIEKEIENLNG 861
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318   81 KYEELQVTAGKHGDSLRDTKNEISELTRTIQRLQGEVDAVKKQCQQLQTAIaeseqngemalKDAKKKLGDLDTALHQAK 160
Cdd:TIGR02169  862 KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI-----------EKKRKRLSELKAKLEALE 930
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1958793318  161 EDLARMLREYQDLVSVKlALDMEIATYRKLLESEESRMS 199
Cdd:TIGR02169  931 EELSEIEDPKGEDEEIP-EEELSLEDVQAELQRVEEEIR 968
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
6-173 1.96e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318   6 LQSKVESLIQEIDFLQQLHEmELSQVQTSVSDTNVILSMdnnrsldldsiIAEVKAQYELIAQKSRAEAE-SWYQTKYEE 84
Cdd:COG4717    83 AEEKEEEYAELQEELEELEE-ELEELEAELEELREELEK-----------LEKLLQLLPLYQELEALEAElAELPERLEE 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318  85 LQvtagKHGDSLRDTKNEISELTRTIQRLQgevdavkkqcQQLQTAIAESEQNGEMALKDAKKKLGDLDTALHQAKEDLA 164
Cdd:COG4717   151 LE----ERLEELRELEEELEELEAELAELQ----------EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216

                  ....*....
gi 1958793318 165 RMLREYQDL 173
Cdd:COG4717   217 EAQEELEEL 225
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
52-197 2.21e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318  52 LDSIIAEVKAQYE-LIAQKSRAEAESW-YQTKYEELQVTAGKHGDSLRDTKNEISELTRTIQRLQGEVDAVKKQCQQLQT 129
Cdd:COG1196   244 LEAELEELEAELEeLEAELAELEAELEeLRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958793318 130 AIAESEQNGEMA---LKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKLALDMEIATYRKLLESEESR 197
Cdd:COG1196   324 ELAELEEELEELeeeLEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
48-198 2.28e-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: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318   48 RSLDLDSIIAEVKAQYELIAQKSRAEAEswYQTKYEELQVTAGKHGDSLRDTKNEISELTRTIQRLQGEVDAVKKQCQQL 127
Cdd:TIGR02168  223 RELELALLVLRLEELREELEELQEELKE--AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958793318  128 QTAIA---ESEQNGEMALKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKLALDMEIATYRKLLESEESRM 198
Cdd:TIGR02168  301 EQQKQilrERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
5-170 3.28e-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: 38.88  E-value: 3.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318    5 DLQSKVESLIQEIDFLQ---QLHEMELSQVQTSVSDTNVILSMDNNRSLDLDSIIAEVKAQYELI-------------AQ 68
Cdd:TIGR02168  285 ELQKELYALANEISRLEqqkQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELkeelesleaeleeLE 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318   69 KSRAEAESWYQTKYEELQVTAGK---HGDSLRDTKNEISELTRTIQRLQGEVDAVKKQCQQLQTAIAESEqngemaLKDA 145
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE------LKEL 438
                          170       180
                   ....*....|....*....|....*
gi 1958793318  146 KKKLGDLDTALHQAKEDLARMLREY 170
Cdd:TIGR02168  439 QAELEELEEELEELQEELERLEEAL 463
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
85-173 3.86e-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: 3.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318  85 LQVTAGKHGDSLRDTKNEISELTRTIQRLQGEVDAVKKQCQQLQTAIAESEQngemALKDAKKKLGDLDTALHQAKEDLA 164
Cdd:COG4942    11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER----RIAALARRIRALEQELAALEAELA 86

                  ....*....
gi 1958793318 165 RMLREYQDL 173
Cdd:COG4942    87 ELEKEIAEL 95
46 PHA02562
endonuclease subunit; Provisional
49-197 4.06e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 38.46  E-value: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318  49 SLDLDSIIAEVKAQYELI--AQKSRAEAESWYQTKYEELQVTAGKHGDSLRDTKNEISELTRT-------IQRLQGEVDA 119
Cdd:PHA02562  187 DMKIDHIQQQIKTYNKNIeeQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDiedpsaaLNKLNTAAAK 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318 120 VKKQCQQLQTAIAESEQNGE-----MALKDAKKKLGDLDTALHQ----------AKEDLARMLREYQDLVSVKLALDMEI 184
Cdd:PHA02562  267 IKSKIEQFQKVIKMYEKGGVcptctQQISEGPDRITKIKDKLKElqhslekldtAIDELEEIMDEFNEQSKKLLELKNKI 346
                         170
                  ....*....|...
gi 1958793318 185 ATYRKLLESEESR 197
Cdd:PHA02562  347 STNKQSLITLVDK 359
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-171 4.35e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 4.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318    7 QSKVESLIQEIDFLQQlhemELSQVQTSVSDTNVILSMDNNRSLDLDSI---------IAEVKAQY-ELIAQKSRAEAES 76
Cdd:COG4913    609 RAKLAALEAELAELEE----ELAEAEERLEALEAELDALQERREALQRLaeyswdeidVASAEREIaELEAELERLDASS 684
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318   77 wyqTKYEELQVTAGKHGDSLRDTKNEISELTRTIQRLQGEVDAVKKQCQQLQTAIAESEQNGEMAL-------------- 142
Cdd:COG4913    685 ---DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELralleerfaaalgd 761
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1958793318  143 -------KDAKKKLGDLDTALHQAKEDLARMLREYQ 171
Cdd:COG4913    762 averelrENLEERIDALRARLNRAEEELERAMRAFN 797
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
71-136 5.35e-03

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 36.51  E-value: 5.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958793318  71 RAEAESWyQTKYEELQVTAGKHGDSLRDTKNEISELTRTIQRLQGEVDAVKKQCQQLQTAIAESEQ 136
Cdd:pfam12718   6 KLEAENA-QERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEK 70
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
56-198 5.71e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.99  E-value: 5.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958793318  56 IAEVKAQYELIAQKSRAEaeswyQTKYEELQVTAGKHGDSLRDTKNEISELTRTIQRLQGEVDAVKKQCQQLQTAIA--- 132
Cdd:COG1196   234 LRELEAELEELEAELEEL-----EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIArle 308
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958793318 133 ESEQNGEMALKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKLALDMEIATYRKLLESEESRM 198
Cdd:COG1196   309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
 
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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