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Conserved domains on  [gi|50539822|ref|NP_001002377|]
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coiled-coil domain-containing protein 62 [Danio rerio]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000095)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
87-329 9.92e-12

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 67.00  E-value: 9.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822     87 EVSTVQRQRLELQLLIAELKDRDQELNTMAAAHHKQMLIWEQERQRvliLEQRSARLEDELQKRNDVIRALSRRLQLSEA 166
Cdd:TIGR02168  699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ---LEERIAQLSKELTELEAEIEELEERLEEAEE 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    167 REKHSERELNSTQQQLHELsQRQMNTSRHEQDledrneSLKSTVLMLSTQVGQLQVREEELSSMLKLKDKDVIEATNHIL 246
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQL-KEELKALREALD------ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    247 ELSGRVCELEKTLEELRTRDGKTQRDAEEHKQRFRESRYQNTQLKAELQEKTIENNSQREELIRLKQENQLLRKEISAVE 326
Cdd:TIGR02168  849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928

                   ...
gi 50539822    327 LQM 329
Cdd:TIGR02168  929 LRL 931
Golgin_A5 super family cl25511
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
288-378 2.02e-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.


The actual alignment was detected with superfamily member pfam09787:

Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 40.13  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822   288 TQLKAELQEKTIENNSQREELIRLKQENQLLRKEISAVELQMINEDKSWRDEL------LELSRSKQTRADSELLCLRQV 361
Cdd:pfam09787  43 TALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLqeleeqLATERSARREAEAELERLQEE 122
                          90
                  ....*....|....*..
gi 50539822   362 CENQQNDLQLLKLNLES 378
Cdd:pfam09787 123 LRYLEEELRRSKATLQS 139
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
87-329 9.92e-12

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: 67.00  E-value: 9.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822     87 EVSTVQRQRLELQLLIAELKDRDQELNTMAAAHHKQMLIWEQERQRvliLEQRSARLEDELQKRNDVIRALSRRLQLSEA 166
Cdd:TIGR02168  699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ---LEERIAQLSKELTELEAEIEELEERLEEAEE 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    167 REKHSERELNSTQQQLHELsQRQMNTSRHEQDledrneSLKSTVLMLSTQVGQLQVREEELSSMLKLKDKDVIEATNHIL 246
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQL-KEELKALREALD------ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    247 ELSGRVCELEKTLEELRTRDGKTQRDAEEHKQRFRESRYQNTQLKAELQEKTIENNSQREELIRLKQENQLLRKEISAVE 326
Cdd:TIGR02168  849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928

                   ...
gi 50539822    327 LQM 329
Cdd:TIGR02168  929 LRL 931
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
93-399 1.79e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 1.79e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822  93 RQRLE-LQLLIAELKDRDQELNTMA--AAHHKQMLIWEQERQRVLIL------EQRSARLEDELQKRNDVIRALSRRL-- 161
Cdd:COG1196 185 EENLErLEDILGELERQLEPLERQAekAERYRELKEELKELEAELLLlklrelEAELEELEAELEELEAELEELEAELae 264
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822 162 ---QLSEAREKHSE--RELNSTQQQLHELSQRQMNTSRHEQDLEDRNESLKSTVLMLSTQVGQLQVREEELSSMLKLKDK 236
Cdd:COG1196 265 leaELEELRLELEEleLELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822 237 DVIEATNHILELSGRVCELEKTLEELRTRDGKTQRDAEEHKQRFRESRYQNTQLKAELQEKTIENNSQREELIRLKQENQ 316
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822 317 LLRKEISAVELQMINEDKSWRDELLELSRSKQTRADSELLCLRQVCENQQNDLQLLKLNLESTREALRHHEGQRSRDSTD 396
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504

                ...
gi 50539822 397 LDL 399
Cdd:COG1196 505 GFL 507
PRK12704 PRK12704
phosphodiesterase; Provisional
129-275 1.49e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822  129 ERQRVLILEQrsARLEDELQKRNDVIRALSRRLQLSEAREKHSERELNSTQQQLHELSQRQMNTSRHEQDLEDRNESLKS 208
Cdd:PRK12704  37 EEEAKRILEE--AKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEK 114
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50539822  209 TVLMLSTQVGQLQVREEELSSMLKlkdkdviEATNHILELSGRVCE------LEKTLEELRTRDGKTQRDAEE 275
Cdd:PRK12704 115 KEKELEQKQQELEKKEEELEELIE-------EQLQELERISGLTAEeakeilLEKVEEEARHEAAVLIKEIEE 180
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
120-402 1.25e-03

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.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.50  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    120 HKQMLIWEQERQRVLILEQRSARLEDELQKRN----DVIRALSRRLQLSEAREKHSERELNSTQQQLHELSQRQMNTSRH 195
Cdd:pfam02463  187 ELIIDLEELKLQELKLKEQAKKALEYYQLKEKleleEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEK 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    196 EQDLEDRNESLKSTVLMLSTQVGQLQVREEELSSMLKLKDKDVIEATNHILELSGRVCELEKTLEELRTrDGKTQRDAEE 275
Cdd:pfam02463  267 LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE-EIEELEKELK 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    276 HKQRFRESRYQNTQLKAELQEKTIENNSQREELIRLKQENQLLRKEISAVELQMINEDKSWRDELLELSRSK-------Q 348
Cdd:pfam02463  346 ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLedllkeeK 425
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 50539822    349 TRADSELLCLRQVCENQQNDLQLLKLNLESTREALRHHEGQRSRDSTDLDLLHL 402
Cdd:pfam02463  426 KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
288-378 2.02e-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: 40.13  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822   288 TQLKAELQEKTIENNSQREELIRLKQENQLLRKEISAVELQMINEDKSWRDEL------LELSRSKQTRADSELLCLRQV 361
Cdd:pfam09787  43 TALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLqeleeqLATERSARREAEAELERLQEE 122
                          90
                  ....*....|....*..
gi 50539822   362 CENQQNDLQLLKLNLES 378
Cdd:pfam09787 123 LRYLEEELRRSKATLQS 139
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
87-329 9.92e-12

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: 67.00  E-value: 9.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822     87 EVSTVQRQRLELQLLIAELKDRDQELNTMAAAHHKQMLIWEQERQRvliLEQRSARLEDELQKRNDVIRALSRRLQLSEA 166
Cdd:TIGR02168  699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ---LEERIAQLSKELTELEAEIEELEERLEEAEE 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    167 REKHSERELNSTQQQLHELsQRQMNTSRHEQDledrneSLKSTVLMLSTQVGQLQVREEELSSMLKLKDKDVIEATNHIL 246
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQL-KEELKALREALD------ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    247 ELSGRVCELEKTLEELRTRDGKTQRDAEEHKQRFRESRYQNTQLKAELQEKTIENNSQREELIRLKQENQLLRKEISAVE 326
Cdd:TIGR02168  849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928

                   ...
gi 50539822    327 LQM 329
Cdd:TIGR02168  929 LRL 931
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
92-392 1.06e-11

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: 67.00  E-value: 1.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822     92 QRQRLELQlliAELKDRDQELNTMAAAHHKQMLI--WEQERQRVLILEQRSARLEDELQKRNDVIRALSrrLQLSEAREK 169
Cdd:TIGR02168  201 QLKSLERQ---AEKAERYKELKAELRELELALLVlrLEELREELEELQEELKEAEEELEELTAELQELE--EKLEELRLE 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    170 HSERE--LNSTQQQLHELSQRQMNTSRHEQDLEDRNESLKSTVLMLSTQVGQLQVREEELSSMLKLKDKDVIEATNHILE 247
Cdd:TIGR02168  276 VSELEeeIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    248 LSGRVCELEKTLEELRTRDGKTQRDAEEHKQRFRESRYQNTQLKAELQEKTIENNSQREELIRLKQENQLLRKEISAVEL 327
Cdd:TIGR02168  356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50539822    328 QMINEDKSWRDELLELSRSKQTRADSELLCLRQVCENQQNDLQLLKLNLESTREALRHHEGQRSR 392
Cdd:TIGR02168  436 KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
93-399 1.79e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 1.79e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822  93 RQRLE-LQLLIAELKDRDQELNTMA--AAHHKQMLIWEQERQRVLIL------EQRSARLEDELQKRNDVIRALSRRL-- 161
Cdd:COG1196 185 EENLErLEDILGELERQLEPLERQAekAERYRELKEELKELEAELLLlklrelEAELEELEAELEELEAELEELEAELae 264
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822 162 ---QLSEAREKHSE--RELNSTQQQLHELSQRQMNTSRHEQDLEDRNESLKSTVLMLSTQVGQLQVREEELSSMLKLKDK 236
Cdd:COG1196 265 leaELEELRLELEEleLELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822 237 DVIEATNHILELSGRVCELEKTLEELRTRDGKTQRDAEEHKQRFRESRYQNTQLKAELQEKTIENNSQREELIRLKQENQ 316
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822 317 LLRKEISAVELQMINEDKSWRDELLELSRSKQTRADSELLCLRQVCENQQNDLQLLKLNLESTREALRHHEGQRSRDSTD 396
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504

                ...
gi 50539822 397 LDL 399
Cdd:COG1196 505 GFL 507
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
91-328 3.01e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.73  E-value: 3.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822  91 VQRQRLELQLLIAELKDRDQELNTMAAAHHKQMLIWEQERQRVLILEQRSARLEDELQKRNDVIRALSRRLQLSEAREKH 170
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822 171 SERELNSTQQQLHELSQRQMNTSRHEQDLEDRNESLKSTVLMLSTQVGQLQVREEELSSMLKLKDKDVIEATNHILELSG 250
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50539822 251 RVCELEKTLEELRTRDGKTQRDAEEHKQRFRESRYQNTQLKAELQEKTIENNSQREELIRLKQENQLLRKEISAVELQ 328
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
86-356 1.69e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 1.69e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822  86 VEVSTVQRQRLELQLLIAELKDRDQELNTMAAAHHKQMLIWEQERQRVLI----LEQRSARLEDELQKRNDVIRALSRRL 161
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrreLEERLEELEEELAELEEELEELEEEL 339
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822 162 QLSEAREKHSERELNSTQQQLHELSQRQMNTSRHEQDLEDRNESLKSTVLMLSTQVGQLQVREEELSSMLKLKDKDVIEA 241
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822 242 TNHILELSgrvcELEKTLEELRTRDGKTQRDAEEHKQRFRESRYQNTQLKAELQEKTIENNSQREELIRLKQENQLLRKE 321
Cdd:COG1196 420 EEELEELE----EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
                       250       260       270
                ....*....|....*....|....*....|....*
gi 50539822 322 ISAVELQMINEDKSWRDELLELSRSKQTRADSELL 356
Cdd:COG1196 496 LLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
154-400 3.25e-08

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: 55.83  E-value: 3.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    154 IRALSRRLQLSEAREKHSERELNSTQQQLHELSQRQMNTSRHEQDLEDRNESLKSTVLMLSTQVGQLQVREEELSSMLKL 233
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    234 KDKDVIEATNHILELSGRVCELEKTLEELRTRDGKTQRDAEEHKQRFRESRYQNTQLKAELQEKTIENNSQREELIRLKQ 313
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    314 ENQLLRKEISAVELQMINEDKSWRDelLELSRSKQTRADSELLCLRQVcenQQNDLQLLKLNLESTREALRHHEGQRSRD 393
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEIEE--LEELIEELESELEALLNERAS---LEEALALLRSELEELSEELRELESKRSEL 913

                   ....*..
gi 50539822    394 STDLDLL 400
Cdd:TIGR02168  914 RRELEEL 920
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
92-332 4.00e-08

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: 55.83  E-value: 4.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822     92 QRQRLELQLLIAELKDRDQELNTMAAAHHKQMLIWEQERQRVLI----LEQRSARLEDELQKRNDVIRALSRRLQLSEAR 167
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEelkaLREALDELRAELTLLNEEAANLRERLESLERR 832
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    168 EKHSERELNSTQQQLHELSQRQMNTSRHEQDLEDRNESLKSTVLMLSTQVGQLQVREEELSSMLKLKDKDVIEATNHILE 247
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    248 LSGRVCELEKTLEELRTRDGKTQRDAEEHKQRFREsRYQNTQLKAELQEKTIENNSQ--REELIRLKQEnqllRKEISAV 325
Cdd:TIGR02168  913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLSE-EYSLTLEEAEALENKIEDDEEeaRRRLKRLENK----IKELGPV 987

                   ....*..
gi 50539822    326 ELQMINE 332
Cdd:TIGR02168  988 NLAAIEE 994
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
87-329 4.14e-08

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: 55.83  E-value: 4.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822     87 EVSTVQRQRLELQLLIAELKDRDQELNTMAAAHHKqmlIWEQERQRVLILEQRSARLEDELQKRNDVIRALSRRLQLSEA 166
Cdd:TIGR02168  254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQK---ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    167 REKHSERELNSTQQQLHELSQRQmntsrheQDLEDRNESLKSTVLMLSTQVGQLQVREEELSSMLKLKDKDVIEATNHIL 246
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEEL-------ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    247 ELSGRVCELEKTLEELRTRdgKTQRDAEEHKQRFRESRYQNTQLKAELQEKTIENNSQREELIRLKQENQLLRKEISAVE 326
Cdd:TIGR02168  404 RLEARLERLEDRRERLQQE--IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481

                   ...
gi 50539822    327 LQM 329
Cdd:TIGR02168  482 REL 484
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
92-415 6.61e-08

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: 55.07  E-value: 6.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822     92 QRQRLELQLLIAE----LKDRDQELNTMAAAHHKQMLIWEQER--QRVLILEQRSARLEDELQKRNDVIRALSRRL-QLS 164
Cdd:TIGR02169  199 QLERLRREREKAEryqaLLKEKREYEGYELLKEKEALERQKEAieRQLASLEEELEKLTEEISELEKRLEEIEQLLeELN 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    165 EAREKHSERELNSTQQQLHELSQRQMNTSRHEQDLEDRNESLKSTVLMLSTQVGQLQVREEELSSMLKLKDKDVIeatnh 244
Cdd:TIGR02169  279 KKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD----- 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    245 ilELSGRVCELEKTLEELRtrdgktqRDAEEHKQRFRESRYQNTQLKAELQEKTIENNSQREELIRLKQENQLLRKEISa 324
Cdd:TIGR02169  354 --KLTEEYAELKEELEDLR-------AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA- 423
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    325 velQMINEDKSWRDELLELSRSKQTRADsELLCLRQVCENQQNDLQLLKLNLESTREALRHHEGQRSRDSTDLDLLHLDC 404
Cdd:TIGR02169  424 ---DLNAAIAGIEAKINELEEEKEDKAL-EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
                          330
                   ....*....|.
gi 50539822    405 PASSHGSRRSS 415
Cdd:TIGR02169  500 RASEERVRGGR 510
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
130-384 3.15e-07

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: 52.75  E-value: 3.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    130 RQRVLILEQRSARLEDELQKRNDVIRALSRRLQLSEAREKHSERELNSTQQQLHELSQRQMNTSRHEQDLEDRNESLKST 209
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    210 VLMLSTQVGQLQVREEELSSMLKLKDKDVIEATNH-------ILELSGRVCELEKTLEELRTRDGKTQRDAEEHKQRFRE 282
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEElkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    283 SRYQNTQLKAELQEKTIENNSQREELIRLKQENQLLRKEISAVELQM--INEDKSWRDELLELSRSKQTRADSELLCLRQ 360
Cdd:TIGR02168  843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALalLRSELEELSEELRELESKRSELRRELEELRE 922
                          250       260
                   ....*....|....*....|....
gi 50539822    361 VCENQQNDLQLLKLNLESTREALR 384
Cdd:TIGR02168  923 KLAQLELRLEGLEVRIDNLQERLS 946
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
87-323 1.20e-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: 50.84  E-value: 1.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822     87 EVSTVQRQRLELQLLIAELKDRDQELNTMAAAHHKQMLIWEQERQRvliLEQRSARLEDELQKRNDVIRALSRRLQLSEA 166
Cdd:TIGR02169  689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK---LKERLEELEEDLSSLEQEIENVKSELKELEA 765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    167 REKHSERELNSTQQQLHELSQRqMNTSRHEQdLEDRNESLKSTVLMLSTQVGQLQVREEELSSMLKLKDKDVIEATNHIL 246
Cdd:TIGR02169  766 RIEELEEDLHKLEEALNDLEAR-LSHSRIPE-IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50539822    247 ELSGRVCELEKTLEELRTRDGKTQRDAEEHKQRFRESRYQNTQLKAELQEKTIENNSQREELIRLKQENQLLRKEIS 323
Cdd:TIGR02169  844 DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
127-334 2.03e-06

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: 49.76  E-value: 2.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822 127 EQERQRVLILEQRSARLEDELQKRNDVIRALSRRLQLSEAREKHSERELNSTQQQLHELSQRQmntSRHEQDLED----- 201
Cdd:COG4942  37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL---EAQKEELAEllral 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822 202 -RNESLKSTVLMLSTQVGQLQVREEELSSMLKLKDKDVIEATNHILElsgRVCELEKTLEELRTRDGKTQRDAEEHKQRF 280
Cdd:COG4942 114 yRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA---ELAALRAELEAERAELEALLAELEEERAAL 190
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 50539822 281 RESRYQNTQLKAELQEKTienNSQREELIRLKQENQLLRKEISAVELQMINEDK 334
Cdd:COG4942 191 EALKAERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEAAAAAE 241
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
130-384 6.29e-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: 48.51  E-value: 6.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    130 RQRVLILEQRSARLEDELQKRNDVIRALSRRLQLSEAREKHSER------ELNSTQ-----QQLHELSQRQMNTSRHEQD 198
Cdd:TIGR02168  171 KERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaELRELElallvLRLEELREELEELQEELKE 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    199 LEDRNESLKSTVLMLSTQVGQLQVREEELSSMLKLKDKDVIEATNHILELSGRVCELEKTLEELRTRDGKTQRDAEEHKQ 278
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    279 RFRESRYQNTQLKAELQEKTIENNSQREELIRLKQENQLLRKEISAVELQMINEdkswRDELLELsRSKQTRADSELlcl 358
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL----RSKVAQL-ELQIASLNNEI--- 402
                          250       260
                   ....*....|....*....|....*.
gi 50539822    359 rQVCENQQNDLQLLKLNLESTREALR 384
Cdd:TIGR02168  403 -ERLEARLERLEDRRERLQQEIEELL 427
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
240-384 1.32e-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: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    240 EATNHILELSGRVCELEKTLEELRTRDGKTQRDAEEHKQRFRESRYQNTQLKAELQEKTIENNSQREELIRLKQENQLLR 319
Cdd:TIGR02168  667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50539822    320 KEIS--AVELQMINEDKSWRDELLELSRSKQTRADSELLCLRQVCENQQNDLQLLKLNLESTREALR 384
Cdd:TIGR02168  747 ERIAqlSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
PRK12704 PRK12704
phosphodiesterase; Provisional
129-275 1.49e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822  129 ERQRVLILEQrsARLEDELQKRNDVIRALSRRLQLSEAREKHSERELNSTQQQLHELSQRQMNTSRHEQDLEDRNESLKS 208
Cdd:PRK12704  37 EEEAKRILEE--AKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEK 114
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50539822  209 TVLMLSTQVGQLQVREEELSSMLKlkdkdviEATNHILELSGRVCE------LEKTLEELRTRDGKTQRDAEE 275
Cdd:PRK12704 115 KEKELEQKQQELEKKEEELEELIE-------EQLQELERISGLTAEeakeilLEKVEEEARHEAAVLIKEIEE 180
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
136-369 2.58e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 2.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822  136 LEQRSARLEDELQKRNDV-IRALSRRLQLSEAREKHSER--ELNSTQQQLHELSQRQMNTSRHEQDLEDRNESLKSTVLM 212
Cdd:PRK02224 211 LESELAELDEEIERYEEQrEQARETRDEADEVLEEHEERreELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822  213 LSTqvgqlqvREEELSSMLKLKDKDVIEATNHILELSGRVCELEKTLEELRTRDGKTQRDAEEHKQRFRESRYQNTQLKA 292
Cdd:PRK02224 291 LEE-------ERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE 363
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50539822  293 ELQEKTIENNSQREELIRLKQENQLLRKEISAVELQMIN--EDKSWRDELLELSRSKQTRADSELLCLRQVCENQQNDL 369
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDapVDLGNAEDFLEELREERDELREREAELEATLRTARERV 442
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
120-402 1.25e-03

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.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.50  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    120 HKQMLIWEQERQRVLILEQRSARLEDELQKRN----DVIRALSRRLQLSEAREKHSERELNSTQQQLHELSQRQMNTSRH 195
Cdd:pfam02463  187 ELIIDLEELKLQELKLKEQAKKALEYYQLKEKleleEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEK 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    196 EQDLEDRNESLKSTVLMLSTQVGQLQVREEELSSMLKLKDKDVIEATNHILELSGRVCELEKTLEELRTrDGKTQRDAEE 275
Cdd:pfam02463  267 LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE-EIEELEKELK 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822    276 HKQRFRESRYQNTQLKAELQEKTIENNSQREELIRLKQENQLLRKEISAVELQMINEDKSWRDELLELSRSK-------Q 348
Cdd:pfam02463  346 ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLedllkeeK 425
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 50539822    349 TRADSELLCLRQVCENQQNDLQLLKLNLESTREALRHHEGQRSRDSTDLDLLHL 402
Cdd:pfam02463  426 KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
87-265 1.68e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822   87 EVSTVQRQR------LELQLLIAELKDRDQELNTMAAAhhkqmLIWEQERQRVLILEQRSARLEDELQKRNDVIRALSRR 160
Cdd:COG4913  243 ALEDAREQIellepiRELAERYAAARERLAELEYLRAA-----LRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822  161 L--------QLSEAREKHSERELNSTQQQLH----ELSQRQMNTSRHEQDLEDRNESLKSTVLMLSTQVGQLQVREEELS 228
Cdd:COG4913  318 LdalreeldELEAQIRGNGGDRLEQLEREIErlerELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 50539822  229 SMLKLKDKDVIEATNHILELSGRVCELEKTLEELRTR 265
Cdd:COG4913  398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
130-346 1.85e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822  130 RQRVLILEQRSARLEDELQKRNDVIRALSRRLQLSEAREKHSERELNSTQQQlhelsqrqmntsRHEQDLEDRNESLKST 209
Cdd:COG4913  616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE------------REIAELEAELERLDAS 683
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822  210 vlmlSTQVGQLQVREEELssmlklkDKDVIEATNHILELSGRVCELEKTLEELRTRDGKTQRDAEEHKQRFREsrYQNTQ 289
Cdd:COG4913  684 ----SDDLAALEEQLEEL-------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRAL 750
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822  290 LKAELQEKTIENNSQ--REEL-IRLKQENQLLRKEISAVELQMINEDKSWRDELLELSRS 346
Cdd:COG4913  751 LEERFAAALGDAVERelRENLeERIDALRARLNRAEEELERAMRAFNREWPAETADLDAD 810
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
288-378 2.02e-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: 40.13  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822   288 TQLKAELQEKTIENNSQREELIRLKQENQLLRKEISAVELQMINEDKSWRDEL------LELSRSKQTRADSELLCLRQV 361
Cdd:pfam09787  43 TALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLqeleeqLATERSARREAEAELERLQEE 122
                          90
                  ....*....|....*..
gi 50539822   362 CENQQNDLQLLKLNLES 378
Cdd:pfam09787 123 LRYLEEELRRSKATLQS 139
46 PHA02562
endonuclease subunit; Provisional
142-328 3.62e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.61  E-value: 3.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822  142 RLEDELQKRNDVIRAlsrRLQ------LSEAREKHSEreLNSTQQQLHELSQRQMNTSRHEQDLEDRNESLKSTVLMLS- 214
Cdd:PHA02562 202 KNIEEQRKKNGENIA---RKQnkydelVEEAKTIKAE--IEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQk 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822  215 ---------------TQVGQLQVREEELSSMLKLKDKDVIEATNHILELSGRVCE---LEKTLEELRTrdgktqrDAEEH 276
Cdd:PHA02562 277 vikmyekggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEfneQSKKLLELKN-------KISTN 349
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 50539822  277 KQRFRESRYQNTQLKAELQEKTIENNSQREELIRLKQENQLLRKEISAVELQ 328
Cdd:PHA02562 350 KQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
127-343 8.56e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.48  E-value: 8.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822  127 EQERQRVLILEQRSARLEDeLQKRNDVIRALSRRLQLSEAREKHSERELNSTQQQLHELSQRQMNTSRHEQDLEDRNESL 206
Cdd:PRK02224 485 EDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539822  207 KSTVLMLSTQVGQLQVREEELssmlklkdKDVIEATNHILELSGRVCELEKTLEELRTRDGKTQRDAEEHKQRFRESRYQ 286
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAEL--------KERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRER 635
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50539822  287 NTQLKAELQEKTIENNSQR------------EELIRLKQENQLLRKEISAVELQmINEDKSWRDELLEL 343
Cdd:PRK02224 636 KRELEAEFDEARIEEAREDkeraeeyleqveEKLDELREERDDLQAEIGAVENE-LEELEELRERREAL 703
 
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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