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Conserved domains on  [gi|808154220|ref|NP_001294869|]
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protein POF1B isoform 2 [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 ...
275-531 8.72e-11

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: 65.09  E-value: 8.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   275 LLEHLQRIGGSKQDFES-TDESEDIESLIPKGLSEFT--KQQIRYILQMRGMSDKSLRLVLSTFSNIREELGHLQNDMTS 351
Cdd:TIGR02169  676 LQRLRERLEGLKRELSSlQSELRRIENRLDELSQELSdaSRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   352 LENDKMRLEKDLSFKDTQLKEYEELLASVRAN-NHQQQQGLQDSSSKcqaLEENNLSLRHTLSDMEYRLKELEYCKRNLE 430
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQAELSK---LEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   431 QENQNLRMQVSEtctgpmLQAKMDEIGNHYTEMVKNLRmEKDREICRLRSQLNQY-------HKDVSKREGSCSDFQFKL 503
Cdd:TIGR02169  833 KEIQELQEQRID------LKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLesrlgdlKKERDELEAQLRELERKI 905
                          250       260
                   ....*....|....*....|....*...
gi 808154220   504 HELTSLLEEKDSLIKRQSEELSKLRQEI 531
Cdd:TIGR02169  906 EELEAQIEKKRKRLSELKAKLEALEEEL 933
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
275-531 8.72e-11

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: 65.09  E-value: 8.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   275 LLEHLQRIGGSKQDFES-TDESEDIESLIPKGLSEFT--KQQIRYILQMRGMSDKSLRLVLSTFSNIREELGHLQNDMTS 351
Cdd:TIGR02169  676 LQRLRERLEGLKRELSSlQSELRRIENRLDELSQELSdaSRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   352 LENDKMRLEKDLSFKDTQLKEYEELLASVRAN-NHQQQQGLQDSSSKcqaLEENNLSLRHTLSDMEYRLKELEYCKRNLE 430
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQAELSK---LEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   431 QENQNLRMQVSEtctgpmLQAKMDEIGNHYTEMVKNLRmEKDREICRLRSQLNQY-------HKDVSKREGSCSDFQFKL 503
Cdd:TIGR02169  833 KEIQELQEQRID------LKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLesrlgdlKKERDELEAQLRELERKI 905
                          250       260
                   ....*....|....*....|....*...
gi 808154220   504 HELTSLLEEKDSLIKRQSEELSKLRQEI 531
Cdd:TIGR02169  906 EELEAQIEKKRKRLSELKAKLEALEEEL 933
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
335-531 4.95e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 4.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220 335 FSNIREELGHLQNDMTSLENDKMR---LEKDLSFKDTQLKEYEELLASVraNNHQQQQG---LQDSSSKCQALEE---NN 405
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAELEKKLDELEEELAEL--LKELEELGfesVEELEERLKELEPfynEY 604
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220 406 LSLRHTLSDMEYRLKELEYCKRNLEQENQNLRMQVSETctgPMLQAKMDEIGNHYTE----MVKNLRMEKDREICRLRSQ 481
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL---EELRKELEELEKKYSEeeyeELREEYLELSRELAGLRAE 681
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 808154220 482 LNQYHKdvskregscsdfqfKLHELTSLLEEkdslIKRQSEELSKLRQEI 531
Cdd:PRK03918 682 LEELEK--------------RREEIKKTLEK----LKEELEEREKAKKEL 713
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
336-443 3.15e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.01  E-value: 3.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   336 SNIREELGHLQNDMTSLENDKMRLEKDLSFKDTQLKEYEELLAsvrannHQQQQGLQdSSSKCQALEENNLSLRHtlsdm 415
Cdd:pfam01576  436 SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ------EETRQKLN-LSTRLRQLEDERNSLQE----- 503
                           90       100
                   ....*....|....*....|....*...
gi 808154220   416 eyRLKELEYCKRNLEQENQNLRMQVSET 443
Cdd:pfam01576  504 --QLEEEEEAKRNVERQLSTLQAQLSDM 529
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
326-531 7.17e-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: 7.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220 326 KSLRLVLSTFSNIREELGHLQNDMTSLENDKMRLEKDLSFKDTQLKEYEELLASVRANNHQQQQGLQDSSSKCQALEENN 405
Cdd:COG1196  225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220 406 LSLRHTLSDMEYRLKELEYCKRNLEQENQNLRMQVSEtctgpmLQAKMDEIGNHYTEMVKNLRMEKDREIcRLRSQLNQY 485
Cdd:COG1196  305 ARLEERRRELEERLEELEEELAELEEELEELEEELEE------LEEELEEAEEELEEAEAELAEAEEALL-EAEAELAEA 377
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 808154220 486 HKDVSKREGSCSDFQFKLHELTSLLEEKDSLIKRQSEELSKLRQEI 531
Cdd:COG1196  378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
275-531 8.72e-11

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: 65.09  E-value: 8.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   275 LLEHLQRIGGSKQDFES-TDESEDIESLIPKGLSEFT--KQQIRYILQMRGMSDKSLRLVLSTFSNIREELGHLQNDMTS 351
Cdd:TIGR02169  676 LQRLRERLEGLKRELSSlQSELRRIENRLDELSQELSdaSRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   352 LENDKMRLEKDLSFKDTQLKEYEELLASVRAN-NHQQQQGLQDSSSKcqaLEENNLSLRHTLSDMEYRLKELEYCKRNLE 430
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQAELSK---LEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   431 QENQNLRMQVSEtctgpmLQAKMDEIGNHYTEMVKNLRmEKDREICRLRSQLNQY-------HKDVSKREGSCSDFQFKL 503
Cdd:TIGR02169  833 KEIQELQEQRID------LKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLesrlgdlKKERDELEAQLRELERKI 905
                          250       260
                   ....*....|....*....|....*...
gi 808154220   504 HELTSLLEEKDSLIKRQSEELSKLRQEI 531
Cdd:TIGR02169  906 EELEAQIEKKRKRLSELKAKLEALEEEL 933
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
335-531 4.95e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 4.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220 335 FSNIREELGHLQNDMTSLENDKMR---LEKDLSFKDTQLKEYEELLASVraNNHQQQQG---LQDSSSKCQALEE---NN 405
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAELEKKLDELEEELAEL--LKELEELGfesVEELEERLKELEPfynEY 604
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220 406 LSLRHTLSDMEYRLKELEYCKRNLEQENQNLRMQVSETctgPMLQAKMDEIGNHYTE----MVKNLRMEKDREICRLRSQ 481
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL---EELRKELEELEKKYSEeeyeELREEYLELSRELAGLRAE 681
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 808154220 482 LNQYHKdvskregscsdfqfKLHELTSLLEEkdslIKRQSEELSKLRQEI 531
Cdd:PRK03918 682 LEELEK--------------RREEIKKTLEK----LKEELEEREKAKKEL 713
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
297-537 5.26e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 5.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   297 DIESLIpKGLSEFTKQQIRYILQMR------GMSDKSLRLVLSTFSNIREELGHLQ-------NDMTSLENDKMRLEKDL 363
Cdd:TIGR02168  233 RLEELR-EELEELQEELKEAEEELEeltaelQELEEKLEELRLEVSELEEEIEELQkelyalaNEISRLEQQKQILRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   364 SFKDTQLKEYEELLASVRANNHQQQQGLQDSSSKCQALEENNLSLRHTLSDMEYRLKELEYCKRNLEQENQNLRMQVSEt 443
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ- 390
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   444 ctgpmLQAKMDEIGNHYTEMVKNLRMEKDReICRLRSQLNQYHK-----DVSKREGSCSDFQFKLHELTSLLEEKDSLIK 518
Cdd:TIGR02168  391 -----LELQIASLNNEIERLEARLERLEDR-RERLQQEIEELLKkleeaELKELQAELEELEEELEELQEELERLEEALE 464
                          250
                   ....*....|....*....
gi 808154220   519 RQSEELSKLRQEIYSSHNQ 537
Cdd:TIGR02168  465 ELREELEEAEQALDAAERE 483
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
336-443 3.15e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.01  E-value: 3.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   336 SNIREELGHLQNDMTSLENDKMRLEKDLSFKDTQLKEYEELLAsvrannHQQQQGLQdSSSKCQALEENNLSLRHtlsdm 415
Cdd:pfam01576  436 SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ------EETRQKLN-LSTRLRQLEDERNSLQE----- 503
                           90       100
                   ....*....|....*....|....*...
gi 808154220   416 eyRLKELEYCKRNLEQENQNLRMQVSET 443
Cdd:pfam01576  504 --QLEEEEEAKRNVERQLSTLQAQLSDM 529
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
279-531 7.11e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 7.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220 279 LQRIGGSKQDFESTDE-SEDIESLIPkgLSEFT-----KQ-QIRYILQMRGMSDKSLRLVLS--TFSNIREELGHLqndM 349
Cdd:PRK03918  97 LKYLDGSEVLEEGDSSvREWVERLIP--YHVFLnaiyiRQgEIDAILESDESREKVVRQILGldDYENAYKNLGEV---I 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220 350 TSLENDKMRLEKDLSFK---DTQLKEYEELLASVRANNHQQQQGLQDSSSKCQALEENNLSLRHT---LSDMEYRLKELE 423
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTeniEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEELEKELESLE 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220 424 YCKRNLEQENQNLRMQVSEtctgpmLQAKMDEIGNHYTEmVKNLRMEKD--REICRLRSQLNQYHKDVSKREGSCSDFQF 501
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEE------LKKEIEELEEKVKE-LKELKEKAEeyIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
                        250       260       270
                 ....*....|....*....|....*....|
gi 808154220 502 KLHELTSLLEEKDSLIKRQSEELSKLRQEI 531
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRL 354
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
326-531 7.17e-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: 7.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220 326 KSLRLVLSTFSNIREELGHLQNDMTSLENDKMRLEKDLSFKDTQLKEYEELLASVRANNHQQQQGLQDSSSKCQALEENN 405
Cdd:COG1196  225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220 406 LSLRHTLSDMEYRLKELEYCKRNLEQENQNLRMQVSEtctgpmLQAKMDEIGNHYTEMVKNLRMEKDREIcRLRSQLNQY 485
Cdd:COG1196  305 ARLEERRRELEERLEELEEELAELEEELEELEEELEE------LEEELEEAEEELEEAEAELAEAEEALL-EAEAELAEA 377
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 808154220 486 HKDVSKREGSCSDFQFKLHELTSLLEEKDSLIKRQSEELSKLRQEI 531
Cdd:COG1196  378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
280-532 9.75e-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: 42.35  E-value: 9.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   280 QRIGGSKQDFESTDESEDIESLIPKGLS-EFTKQQIRYILQMRGMSDKSLRLVlstfsNIREELGHLQNDMTSLENDKMR 358
Cdd:TIGR02168  789 AQIEQLKEELKALREALDELRAELTLLNeEAANLRERLESLERRIAATERRLE-----DLEEQIEELSEDIESLAAEIEE 863
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   359 LEKDLSFKDTQLKEYEELLASVRANNHQQQQGLQDSSSKCQALEENNLSLRHTLSDMEYRLKELEYCKRNLEQENQNLRM 438
Cdd:TIGR02168  864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   439 QVSEtctgpMLQAKMDEIGNHYtEMVKNLRMEKDREICRLRSQLNQY----------HKDVSKRegscsdFQFKLHELTS 508
Cdd:TIGR02168  944 RLSE-----EYSLTLEEAEALE-NKIEDDEEEARRRLKRLENKIKELgpvnlaaieeYEELKER------YDFLTAQKED 1011
                          250       260
                   ....*....|....*....|....*..
gi 808154220   509 LLEEKDSL---IKRQSEELSKLRQEIY 532
Cdd:TIGR02168 1012 LTEAKETLeeaIEEIDREARERFKDTF 1038
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
333-530 1.02e-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: 42.35  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   333 STFSNIREELGHLQNDMTSLENDKMRLEKDLSFKDTQLKEYEELLASVRANNHQQQQGLQDSSSKCQALEENNLSLRHTL 412
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   413 SDMEYRLKELEYCKRNLEQENQNLRMQVSETCTgpMLQAKMDEIGNHYT---------EMVKNLRMEKDREICRLRSQLN 483
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALRE--ALDELRAELTLLNEeaanlrerlESLERRIAATERRLEDLEEQIE 848
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 808154220   484 QYHKDVSKREGSCSDFQFKLHELTSLLEEKDSLIKRQSEELSKLRQE 530
Cdd:TIGR02168  849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
290-529 1.06e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220 290 ESTDESEDIESLIpKGLSEFTKQQIRYILQMRGMSD--KSLRLVLSTFSNIREELGHLQNDMTSLENDKMRLEKDLSFKD 367
Cdd:PRK03918 270 ELKKEIEELEEKV-KELKELKEKAEEYIKLSEFYEEylDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220 368 TQLKEYEELLASVRAnnHQQQQGLQDSSSKCQALEENNlslrhTLSDMEYRLKELEYCKRNLEQENQNLRmqvsetctgp 447
Cdd:PRK03918 349 ELEKRLEELEERHEL--YEEAKAKKEELERLKKRLTGL-----TPEKLEKELEELEKAKEEIEEEISKIT---------- 411
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220 448 mlqAKMDEIGNHYTEMVKNL-RMEKDREIC----RLRSQ------LNQYHKDVSKREGSCSDFQFKLHELTSLLEEKDSL 516
Cdd:PRK03918 412 ---ARIGELKKEIKELKKAIeELKKAKGKCpvcgRELTEehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKV 488
                        250
                 ....*....|...
gi 808154220 517 IKRQSeELSKLRQ 529
Cdd:PRK03918 489 LKKES-ELIKLKE 500
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
324-442 1.09e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220 324 SDKSLRLVLSTFSNIREELGHLQNDMTSLENDKMRLEKDLSFKDTQLKEYEELLASVRANNHQQQQGLQDSSSKCQALEE 403
Cdd:COG4372   29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 808154220 404 NNLSLRHTLSDMEYRLKELEYCKRNLEQENQNLRMQVSE 442
Cdd:COG4372  109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAE 147
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
366-531 1.24e-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: 41.97  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   366 KDTQLKEYEELLASVRANNHQQQQGLQDSSSKCQALEENNLSLRHTLSDMEYRLKELEYCKRNLEQENQNL--------- 436
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLeeriaqlsk 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   437 ---RMQVSETCTGPMLQAKMDEIGNHYTEMVK--------NLRMEKDREICR-LRSQLNQYHKDVSKREGSCSDFQFKLH 504
Cdd:TIGR02168  755 eltELEAEIEELEERLEEAEEELAEAEAEIEEleaqieqlKEELKALREALDeLRAELTLLNEEAANLRERLESLERRIA 834
                          170       180
                   ....*....|....*....|....*..
gi 808154220   505 ELTSLLEEKDSLIKRQSEELSKLRQEI 531
Cdd:TIGR02168  835 ATERRLEDLEEQIEELSEDIESLAAEI 861
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
293-535 6.60e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 39.64  E-value: 6.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   293 DESEDIESLIPKglsefTKQQIRYILQMRGMSDKSLRLVLSTFSNIREELGHLQNDMTSLENDKMRLEKDLSFKDTQLKE 372
Cdd:TIGR00606  709 DKLKSTESELKK-----KEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEES 783
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   373 YEELLASVRANNHQQQQgLQDSSSKC--QALEENNLSLRHTLSDMEYRLKELEYCKRNLEQENQNLRMQVSETC-TGPML 449
Cdd:TIGR00606  784 AKVCLTDVTIMERFQME-LKDVERKIaqQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQeQIQHL 862
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   450 QAKMDEIGNHYTEMVKNLR---------MEKDREICRLRSQLNQYHKDVSKREGSCSDFQFKLHELTSLLEEKDsliKRQ 520
Cdd:TIGR00606  863 KSKTNELKSEKLQIGTNLQrrqqfeeqlVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSN---KKA 939
                          250
                   ....*....|....*
gi 808154220   521 SEELSKLRQEIYSSH 535
Cdd:TIGR00606  940 QDKVNDIKEKVKNIH 954
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
312-531 6.65e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 6.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   312 QQIRYILQMRGMSDKSLRLVLSTFSNIREELGHLQNDMTSLENDKMRLEKDLSFKDTQLKEYEELLASVRANNHQQQQGL 391
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   392 QDSSSKCQA--------------LEENNLSLRHTLSDMEYRLKELEyckRNLEqENQNLRMQvsetctgpmLQAKMDEIG 457
Cdd:TIGR02168  827 ESLERRIAAterrledleeqieeLSEDIESLAAEIEELEELIEELE---SELE-ALLNERAS---------LEEALALLR 893
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   458 NHYTEMVKNLR------MEKDREICRLRSQLNQYHKDVSKREGSCSDFQFKLHELTSLLEE--------KDSLIKRQSEE 523
Cdd:TIGR02168  894 SELEELSEELReleskrSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeaealenkIEDDEEEARRR 973

                   ....*...
gi 808154220   524 LSKLRQEI 531
Cdd:TIGR02168  974 LKRLENKI 981
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
318-565 9.35e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 39.26  E-value: 9.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   318 LQMRGMSDKSlRLVLSTFSNIREELGHLQNDMTSLENDKMRLEKDLSFKDTQLKEYEELLASVRANNHQQQQGLQDSSSK 397
Cdd:TIGR00606  398 LVIERQEDEA-KTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILEL 476
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   398 CQAL--EENNLSLRHTLSDMEYRLKELEYCKRNLEQENQNLRMQVSEtctgpMLQAKMDEIGNHYTEMVKNLRMEKDREI 475
Cdd:TIGR00606  477 DQELrkAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQE-----MEQLNHHTTTRTQMEMLTKDKMDKDEQI 551
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154220   476 CRLRSQ---------------------LNQYHKDVSKREGSCSDFQFKLHELTSLLEEKDSLIKRQSEELSKLRQEIY-- 532
Cdd:TIGR00606  552 RKIKSRhsdeltsllgyfpnkkqledwLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFdv 631
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 808154220   533 -SSHNQPSTGGRTTITTKKYRTQYPILG---LLYDDY 565
Cdd:TIGR00606  632 cGSQDEESDLERLKEEIEKSSKQRAMLAgatAVYSQF 668
 
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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