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Conserved domains on  [gi|1034604799|ref|XP_016881500|]
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coiled-coil domain-containing protein 68 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 68-253 5.47e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 47.76  E-value: 5.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799   68 KLQASREAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQK--LKQHVENLNQVAEKLEEKHSQITELE 145
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKerLEELEEDLSSLEQEIENVKSELKELE 764

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  146 NLVQRMEKEKRTLLERKLSLENKLLQLKSSaTYGKSCQDLQREISILQEQISHLQFVIHSQHQNLRSVIQEMEG------ 219
Cdd:TIGR02169  765 ARIEELEEDLHKLEEALNDLEARLSHSRIP-EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQElqeqri 843

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1034604799  220 -LKNNLKEQDKRIENLREKVNILEAQNKELKTQVA 253
Cdd:TIGR02169  844 dLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 68-253 5.47e-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: 47.76  E-value: 5.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799   68 KLQASREAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQK--LKQHVENLNQVAEKLEEKHSQITELE 145
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKerLEELEEDLSSLEQEIENVKSELKELE 764

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  146 NLVQRMEKEKRTLLERKLSLENKLLQLKSSaTYGKSCQDLQREISILQEQISHLQFVIHSQHQNLRSVIQEMEG------ 219
Cdd:TIGR02169  765 ARIEELEEDLHKLEEALNDLEARLSHSRIP-EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQElqeqri 843

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1034604799  220 -LKNNLKEQDKRIENLREKVNILEAQNKELKTQVA 253
Cdd:TIGR02169  844 dLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 25-253 2.87e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 2.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  25 STSAHIIEETEYVKKIRTTLQKIRTQmfKDEIRHDSTNHKLDAKLQASREAGAAALRNVAQRLFENYQTQSEEVRKKQED 104
Cdd:COG1196   219 KEELKELEAELLLLKLRELEAELEEL--EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799 105 SKQLlqvnklekEQKLKQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSAtygkscQD 184
Cdd:COG1196   297 LARL--------EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL------AE 362

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034604799 185 LQREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRIENLREKVNILEAQNKELKTQVA 253
Cdd:COG1196   363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 50-249 5.37e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 44.53  E-value: 5.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  50 QMFKDEIRhdSTNHKLDAKLQASREAGAAALRNVAQRLfENYQTqsEEVRKKQEDSKQLL-------QVNKLEKEQKLKQ 122
Cdd:PRK05771    5 RMKKVLIV--TLKSYKDEVLEALHELGVVHIEDLKEEL-SNERL--RKLRSLLTKLSEALdklrsylPKLNPLREEKKKV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799 123 HV-----------ENLNQVAEKLEEKHSQITELENLVQRMEKEKRtLLE--RKLSLENKLLQLKSSATYGKSCQDLQREI 189
Cdd:PRK05771   80 SVksleelikdveEELEKIEKEIKELEEEISELENEIKELEQEIE-RLEpwGNFDLDLSLLLGFKYVSVFVGTVPEDKLE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034604799 190 SILQEQISHLQFVIH--------------SQHQNLRSVIQEMEGLKNNLKEQ---DKRIENLREKVNILEAQNKELK 249
Cdd:PRK05771  159 ELKLESDVENVEYIStdkgyvyvvvvvlkELSDEVEEELKKLGFERLELEEEgtpSELIREIKEELEEIEKERESLL 235
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 6-244 1.95e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 39.64  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799   6 VTTEIPPRDKMEDNSALYESTSA-HIIEETEYVKKIRTTLQkirtqmfkdeirHDSTNHKLDA-KLQASREAGAAALRNV 83
Cdd:pfam10168 472 LIDAVPPSPPLLCSKEDVTVDEPlRGLQEDSFEDHIKSILQ------------RSVSNPILSAdKLSSPSPQECLQLLSR 539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  84 AQRLF-ENYQTQSEEVRKKQEDSKQLLQVNK---LEKEQKLKQHVENLNQVAEKLEEKHSQITE-LENLVQRMEKEKRTL 158
Cdd:pfam10168 540 ATQVFrEEYLKKHDLAREEIQKRVKLLKLQKeqqLQELQSLEEERKSLSERAEKLAEKYEEIKDkQEKLMRRCKKVLQRL 619

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799 159 LERKLSL------ENKLLQLKSSAT--YGKSCQDLQREISILQEQISHLQfvIHSQHQNLRSVIQEMEGLKNNLKEQDKR 230
Cdd:pfam10168 620 NSQLPVLsdaereMKKELETINEQLkhLANAIKQAKKKMNYQRYQIAKSQ--SIRKKSSLSLSEKQRKTIKEILKQLGSE 697

                         250
                  ....*....|....
gi 1034604799 231 IENLREKVNILEAQ 244
Cdd:pfam10168 698 IDELIKQVKDINKH 711
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 68-253 5.47e-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: 47.76  E-value: 5.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799   68 KLQASREAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQK--LKQHVENLNQVAEKLEEKHSQITELE 145
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKerLEELEEDLSSLEQEIENVKSELKELE 764

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  146 NLVQRMEKEKRTLLERKLSLENKLLQLKSSaTYGKSCQDLQREISILQEQISHLQFVIHSQHQNLRSVIQEMEG------ 219
Cdd:TIGR02169  765 ARIEELEEDLHKLEEALNDLEARLSHSRIP-EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQElqeqri 843

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1034604799  220 -LKNNLKEQDKRIENLREKVNILEAQNKELKTQVA 253
Cdd:TIGR02169  844 dLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 114-253 6.55e-06

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: 47.36  E-value: 6.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  114 LEKEQKLKQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSA--------TYGKSCQDL 185
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLarleaeveQLEERIAQL 752

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034604799  186 QREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRIENLREKVNILEAQNKELKTQVA 253
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 34-257 7.55e-06

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: 47.36  E-value: 7.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799   34 TEYVKKIRTtLQKIRTQMFKDEIRHDSTNHKLDAKLQASREAGAAALRNVAQ---RLFENYQTQSEEVRKKQEDSKQLLQ 110
Cdd:TIGR02168  235 EELREELEE-LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkELYALANEISRLEQQKQILRERLAN 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  111 VNK---------LEKEQKLKQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKS-SATYGK 180
Cdd:TIGR02168  314 LERqleeleaqlEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkVAQLEL 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  181 SCQDLQREISILQEQISHLQFVIHSQHQNLRSVIQ-----EMEGLKNNLKEQDKRIENLREKVNILEAQNKELKTQVALS 255
Cdd:TIGR02168  394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKkleeaELKELQAELEELEEELEELQEELERLEEALEELREELEEA 473


                   ..
gi 1034604799  256 SE 257
Cdd:TIGR02168  474 EQ 475
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 37-251 1.68e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 1.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799   37 VKKIRTTLQKIRTQMFKDEIRHDSTNHKLDAKLQASREAGAAALRNVAQRLFEnyQTQSEEVRKKQEDSKQLLQVNKLEK 116
Cdd:TIGR02168  703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE--LTELEAEIEELEERLEEAEEELAEA 780

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  117 EQKLKQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSATY-GKSCQDLQREISILQEQ 195
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDlEEQIEELSEDIESLAAE 860

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034604799  196 ISHLQFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRIENLREKVNILEAQNKELKTQ 251
Cdd:TIGR02168  861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 25-253 2.87e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 2.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  25 STSAHIIEETEYVKKIRTTLQKIRTQmfKDEIRHDSTNHKLDAKLQASREAGAAALRNVAQRLFENYQTQSEEVRKKQED 104
Cdd:COG1196   219 KEELKELEAELLLLKLRELEAELEEL--EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799 105 SKQLlqvnklekEQKLKQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSAtygkscQD 184
Cdd:COG1196   297 LARL--------EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL------AE 362

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034604799 185 LQREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRIENLREKVNILEAQNKELKTQVA 253
Cdd:COG1196   363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 50-249 5.37e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 44.53  E-value: 5.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  50 QMFKDEIRhdSTNHKLDAKLQASREAGAAALRNVAQRLfENYQTqsEEVRKKQEDSKQLL-------QVNKLEKEQKLKQ 122
Cdd:PRK05771    5 RMKKVLIV--TLKSYKDEVLEALHELGVVHIEDLKEEL-SNERL--RKLRSLLTKLSEALdklrsylPKLNPLREEKKKV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799 123 HV-----------ENLNQVAEKLEEKHSQITELENLVQRMEKEKRtLLE--RKLSLENKLLQLKSSATYGKSCQDLQREI 189
Cdd:PRK05771   80 SVksleelikdveEELEKIEKEIKELEEEISELENEIKELEQEIE-RLEpwGNFDLDLSLLLGFKYVSVFVGTVPEDKLE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034604799 190 SILQEQISHLQFVIH--------------SQHQNLRSVIQEMEGLKNNLKEQ---DKRIENLREKVNILEAQNKELK 249
Cdd:PRK05771  159 ELKLESDVENVEYIStdkgyvyvvvvvlkELSDEVEEELKKLGFERLELEEEgtpSELIREIKEELEEIEKERESLL 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 68-253 1.94e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  68 KLQASREAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQKLKQHVENLNQVAEKLEEKHSQITELENL 147
Cdd:COG1196   217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799 148 VQRMEKEKRTLLERKLSLENKLLQLKSS-ATYGKSCQDLQREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNLKE 226
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLEELEEElAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376

                         170       180
                  ....*....|....*....|....*..
gi 1034604799 227 QDKRIENLREKVNILEAQNKELKTQVA 253
Cdd:COG1196   377 AEEELEELAEELLEALRAAAELAAQLE 403
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
131-253 2.43e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 2.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  131 AEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSATYGKSCQD---LQREISILQEQISHLQfvihSQH 207
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasAEREIAELEAELERLD----ASS 684

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1034604799  208 QNLRSVIQEMEGLKNNLKEQDKRIENLREKVNILEAQNKELKTQVA 253
Cdd:COG4913    685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 24-248 3.59e-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: 3.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799   24 ESTSAHIIEETEYVKKIRTTLQKIRTQMFKDEIRHDSTNHKLDAkLQASREAGAAALRNVAQRLfENYQTQSEEVRKKQE 103
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE-LRAELTLLNEEAANLRERL-ESLERRIAATERRLE 841

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  104 DSKQllqvNKLEKEQKLKQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSATYGK-SC 182
Cdd:TIGR02168  842 DLEE----QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRrEL 917

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034604799  183 QDLQREISILQEQISHLQFVIHSQHQNLRSVIQ-EMEGLKNNLKEQDKRIENLREKVNILEAQNKEL 248
Cdd:TIGR02168  918 EELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
103-238 3.61e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.77  E-value: 3.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799 103 EDSKQLLQVNKLEKEQKLKQHVE-NLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSAtygKS 181
Cdd:COG2433   383 EELIEKELPEEEPEAEREKEHEErELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEE---RR 459

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034604799 182 CQDLQREISILQEQIShlqfvihsqhqNLRSVIQEMEGLKNNLKEQDKRIENLREKV 238
Cdd:COG2433   460 EIRKDREISRLDREIE-----------RLERELEEERERIEELKRKLERLKELWKLE 505
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
70-240 6.09e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 6.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799   70 QASREAGAAALRNVAQRLFEnyQTQSEEVRKKQEDSKQLLQVNKLEKEQkLKQHVENLNQVAEKLEEKHSQ-----ITEL 144
Cdd:COG4913    267 ARERLAELEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAELER-LEARLDALREELDELEAQIRGnggdrLEQL 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  145 ENLVQRMEKEKRTLLERKLSLENKLLQLKSSATYGKscQDLQREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNL 224
Cdd:COG4913    344 EREIERLERELEERERRRARLEALLAALGLPLPASA--EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421

                          170
                   ....*....|....*..
gi 1034604799  225 KEQDKRIENLRE-KVNI 240
Cdd:COG4913    422 RELEAEIASLERrKSNI 438
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
65-258 1.11e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  65 LDAKLQASREAGAAALRNVAQRLfENYQTQSEEVRKKQEDSKQLLQVNKLEKEQKlkQHVENLNQVAEKLEEKHSQITEL 144
Cdd:COG3206   162 LEQNLELRREEARKALEFLEEQL-PELRKELEEAEAALEEFRQKNGLVDLSEEAK--LLLQQLSELESQLAEARAELAEA 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799 145 ENLVQRMEKEKRT----------------LLERKLSLENKLLQLksSATYGKSCQDLQReisiLQEQISHLQFVIHSQHQ 208
Cdd:COG3206   239 EARLAALRAQLGSgpdalpellqspviqqLRAQLAELEAELAEL--SARYTPNHPDVIA----LRAQIAALRAQLQQEAQ 312

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034604799 209 NLRSVIQ-EMEGLKNNLKEQDKRIENLREKVNIL---EAQNKELKTQVALSSET 258
Cdd:COG3206   313 RILASLEaELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVAREL 366
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 109-253 1.36e-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: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  109 LQVNKLEKEQKLKQHVENLNQVAEKLEEKHSQITELENLVQRMEK-----------EKRTLLERKLSLENKLLQLKSSAT 177
Cdd:TIGR02168  170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQEELK 249

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034604799  178 -YGKSCQDLQREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRIENLREKVNILEAQNKELKTQVA 253
Cdd:TIGR02168  250 eAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 77-253 1.89e-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: 39.36  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  77 AAALRNVAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQKLKQhvenLNQVAEKLEEKHSQITELENLVQRMEKEKR 156
Cdd:COG4942    11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ----LAALERRIAALARRIRALEQELAALEAELA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799 157 TLLERKLSLENKLLQLKssatygkscQDLQREISILQ--EQISHLQFVIHSqhQNLRSVIQEMEGLKNNLKEQDKRIENL 234
Cdd:COG4942    87 ELEKEIAELRAELEAQK---------EELAELLRALYrlGRQPPLALLLSP--EDFLDAVRRLQYLKYLAPARREQAEEL 155

                         170
                  ....*....|....*....
gi 1034604799 235 REKVNILEAQNKELKTQVA 253
Cdd:COG4942   156 RADLAELAALRAELEAERA 174
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 6-244 1.95e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 39.64  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799   6 VTTEIPPRDKMEDNSALYESTSA-HIIEETEYVKKIRTTLQkirtqmfkdeirHDSTNHKLDA-KLQASREAGAAALRNV 83
Cdd:pfam10168 472 LIDAVPPSPPLLCSKEDVTVDEPlRGLQEDSFEDHIKSILQ------------RSVSNPILSAdKLSSPSPQECLQLLSR 539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  84 AQRLF-ENYQTQSEEVRKKQEDSKQLLQVNK---LEKEQKLKQHVENLNQVAEKLEEKHSQITE-LENLVQRMEKEKRTL 158
Cdd:pfam10168 540 ATQVFrEEYLKKHDLAREEIQKRVKLLKLQKeqqLQELQSLEEERKSLSERAEKLAEKYEEIKDkQEKLMRRCKKVLQRL 619

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799 159 LERKLSL------ENKLLQLKSSAT--YGKSCQDLQREISILQEQISHLQfvIHSQHQNLRSVIQEMEGLKNNLKEQDKR 230
Cdd:pfam10168 620 NSQLPVLsdaereMKKELETINEQLkhLANAIKQAKKKMNYQRYQIAKSQ--SIRKKSSLSLSEKQRKTIKEILKQLGSE 697

                         250
                  ....*....|....
gi 1034604799 231 IENLREKVNILEAQ 244
Cdd:pfam10168 698 IDELIKQVKDINKH 711
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 81-241 2.03e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.49  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  81 RNVAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKEQKLKQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLE 160
Cdd:pfam07888  43 RAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLA 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799 161 RKLSLENKLLQLKS-SATYGKSCQDLQREISILQEQI--------------SHLQFVIHSQHQNLRSVIQEMEGLKNNLK 225
Cdd:pfam07888 123 QRAAHEARIRELEEdIKTLTQRVLERETELERMKERAkkagaqrkeeeaerKQLQAKLQQTEEELRSLSKEFQELRNSLA 202

                         170
                  ....*....|....*.
gi 1034604799 226 EQDKRIENLREKVNIL 241
Cdd:pfam07888 203 QRDTQVLQLQDTITTL 218
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 125-249 2.41e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.42  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799 125 ENLNQVAEKLEEKH----SQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSATygkscQDLQREISILQEQISHLQ 200
Cdd:PRK00409  516 EKLNELIASLEELEreleQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAE-----KEAQQAIKEAKKEADEII 590

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1034604799 201 FVIHSQHQNLRSVIQEMEgLKNNLKEQDKRIENLREKVNILEAQNKELK 249
Cdd:PRK00409  591 KELRQLQKGGYASVKAHE-LIEARKRLNKANEKKEKKKKKQKEKQEELK 638
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 102-253 7.29e-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: 37.21  E-value: 7.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799 102 QEDSKQLLQVNKLEKE--QKLKQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLKSSATYg 179
Cdd:COG1579    13 QELDSELDRLEHRLKElpAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEY- 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034604799 180 kscQDLQREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNNLKEQDKRIENLREKvniLEAQNKELKTQVA 253
Cdd:COG1579    92 ---EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELE 159
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 67-252 9.34e-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: 37.74  E-value: 9.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799   67 AKLQASREAGAAALRNVAQRLfENYQTQSEEVR---KKQEDSKQLLQVNKLEKEQKLKQHVENLNQVAEKLEEKHSQITE 143
Cdd:TIGR02169  325 AKLEAEIDKLLAEIEELEREI-EEERKRRDKLTeeyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  144 LENLVQRMEKEKRTLLERKLSLENKLLQLKSSATygkscqDLQREISILQEQISHLQFVIHSQHQNLRSVIQEMEGLKNN 223
Cdd:TIGR02169  404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKIN------ELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477

                          170       180
                   ....*....|....*....|....*....
gi 1034604799  224 LKEQDKRIENLREKVNILEAQNKELKTQV 252
Cdd:TIGR02169  478 YDRVEKELSKLQRELAEAEAQARASEERV 506
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
44-230 9.44e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 37.44  E-value: 9.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799  44 LQKIRTQMFKDEIRHDSTNHKLDAKLQASREAGAAALRNVAQRLFENYQTQSEEVRKKQEDSKQLLQVNKLEKE------ 117
Cdd:COG4717    51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlqllpl 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034604799 118 -QKLKQHVENLNQVAEKLEEKHSQITELENLVQRMEKEKRTLLERKLSLENKLLQLksSATYGKSCQDLQREISILQEQI 196
Cdd:COG4717   131 yQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL--SLATEEELQDLAEELEELQQRL 208

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034604799 197 SHLQFVIHSQHQNLRSVIQEMEGLKNNLKEQDKR 230
Cdd:COG4717   209 AELEEELEEAQEELEELEEELEQLENELEAAALE 242
 
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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