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Conserved domains on  [gi|193794853|ref|NP_079197|]
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protein POF1B isoform 1 [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 1.11e-10

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: 64.70  E-value: 1.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   275 LLEHLQRIGGSKQDFES-TDESEDIESLIPKGLSEFT--KQQIRYILQMRGMSDKSLRLVLSTFSNIREELGHLQNDMTS 351
Cdd:TIGR02169  676 LQRLRERLEGLKRELSSlQSELRRIENRLDELSQELSdaSRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   352 LENDKMRLEKDLSFKDTQLKEYEELLASVRAN-NHQQQQGLQDSSSKcqaLEENNLSLRHTLSDMEYRLKELEYCKRNLE 430
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQAELSK---LEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   431 QENQNLRMQVSEtctgpmLQAKMDEIGNHYTEMVKNLRmEKDREICRLRSQLNQY-------HKDVSKREGSCSDFQFKL 503
Cdd:TIGR02169  833 KEIQELQEQRID------LKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLesrlgdlKKERDELEAQLRELERKI 905
                          250       260
                   ....*....|....*....|....*...
gi 193794853   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 1.11e-10

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: 64.70  E-value: 1.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   275 LLEHLQRIGGSKQDFES-TDESEDIESLIPKGLSEFT--KQQIRYILQMRGMSDKSLRLVLSTFSNIREELGHLQNDMTS 351
Cdd:TIGR02169  676 LQRLRERLEGLKRELSSlQSELRRIENRLDELSQELSdaSRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   352 LENDKMRLEKDLSFKDTQLKEYEELLASVRAN-NHQQQQGLQDSSSKcqaLEENNLSLRHTLSDMEYRLKELEYCKRNLE 430
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQAELSK---LEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   431 QENQNLRMQVSEtctgpmLQAKMDEIGNHYTEMVKNLRmEKDREICRLRSQLNQY-------HKDVSKREGSCSDFQFKL 503
Cdd:TIGR02169  833 KEIQELQEQRID------LKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLesrlgdlKKERDELEAQLRELERKI 905
                          250       260
                   ....*....|....*....|....*...
gi 193794853   504 HELTSLLEEKDSLIKRQSEELSKLRQEI 531
Cdd:TIGR02169  906 EELEAQIEKKRKRLSELKAKLEALEEEL 933
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
335-531 5.69e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 5.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853 335 FSNIREELGHLQNDMTSLENDKMR---LEKDLSFKDTQLKEYEELLASVraNNHQQQQG---LQDSSSKCQALEE---NN 405
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAELEKKLDELEEELAEL--LKELEELGfesVEELEERLKELEPfynEY 604
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853 406 LSLRHTLSDMEYRLKELEYCKRNLEQENQNLRMQVSETctgPMLQAKMDEIGNHYTE----MVKNLRMEKDREICRLRSQ 481
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL---EELRKELEELEKKYSEeeyeELREEYLELSRELAGLRAE 681
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 193794853 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 3.81e-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: 43.63  E-value: 3.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   336 SNIREELGHLQNDMTSLENDKMRLEKDLSFKDTQLKEYEELLAsvrannHQQQQGLQdSSSKCQALEENNLSLRHtlsdm 415
Cdd:pfam01576  436 SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ------EETRQKLN-LSTRLRQLEDERNSLQE----- 503
                           90       100
                   ....*....|....*....|....*...
gi 193794853   416 eyRLKELEYCKRNLEQENQNLRMQVSET 443
Cdd:pfam01576  504 --QLEEEEEAKRNVERQLSTLQAQLSDM 529
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
326-531 8.18e-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: 8.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853 326 KSLRLVLSTFSNIREELGHLQNDMTSLENDKMRLEKDLSFKDTQLKEYEELLASVRANNHQQQQGLQDSSSKCQALEENN 405
Cdd:COG1196  225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853 406 LSLRHTLSDMEYRLKELEYCKRNLEQENQNLRMQVSEtctgpmLQAKMDEIGNHYTEMVKNLRMEKDREIcRLRSQLNQY 485
Cdd:COG1196  305 ARLEERRRELEERLEELEEELAELEEELEELEEELEE------LEEELEEAEEELEEAEAELAEAEEALL-EAEAELAEA 377
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 193794853 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 1.11e-10

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: 64.70  E-value: 1.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   275 LLEHLQRIGGSKQDFES-TDESEDIESLIPKGLSEFT--KQQIRYILQMRGMSDKSLRLVLSTFSNIREELGHLQNDMTS 351
Cdd:TIGR02169  676 LQRLRERLEGLKRELSSlQSELRRIENRLDELSQELSdaSRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   352 LENDKMRLEKDLSFKDTQLKEYEELLASVRAN-NHQQQQGLQDSSSKcqaLEENNLSLRHTLSDMEYRLKELEYCKRNLE 430
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQAELSK---LEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   431 QENQNLRMQVSEtctgpmLQAKMDEIGNHYTEMVKNLRmEKDREICRLRSQLNQY-------HKDVSKREGSCSDFQFKL 503
Cdd:TIGR02169  833 KEIQELQEQRID------LKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLesrlgdlKKERDELEAQLRELERKI 905
                          250       260
                   ....*....|....*....|....*...
gi 193794853   504 HELTSLLEEKDSLIKRQSEELSKLRQEI 531
Cdd:TIGR02169  906 EELEAQIEKKRKRLSELKAKLEALEEEL 933
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
335-531 5.69e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 5.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853 335 FSNIREELGHLQNDMTSLENDKMR---LEKDLSFKDTQLKEYEELLASVraNNHQQQQG---LQDSSSKCQALEE---NN 405
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAELEKKLDELEEELAEL--LKELEELGfesVEELEERLKELEPfynEY 604
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853 406 LSLRHTLSDMEYRLKELEYCKRNLEQENQNLRMQVSETctgPMLQAKMDEIGNHYTE----MVKNLRMEKDREICRLRSQ 481
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL---EELRKELEELEKKYSEeeyeELREEYLELSRELAGLRAE 681
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 193794853 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 5.99e-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: 5.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   297 DIESLIpKGLSEFTKQQIRYILQMR------GMSDKSLRLVLSTFSNIREELGHLQ-------NDMTSLENDKMRLEKDL 363
Cdd:TIGR02168  233 RLEELR-EELEELQEELKEAEEELEeltaelQELEEKLEELRLEVSELEEEIEELQkelyalaNEISRLEQQKQILRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   364 SFKDTQLKEYEELLASVRANNHQQQQGLQDSSSKCQALEENNLSLRHTLSDMEYRLKELEYCKRNLEQENQNLRMQVSEt 443
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ- 390
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   444 ctgpmLQAKMDEIGNHYTEMVKNLRMEKDReICRLRSQLNQYHK-----DVSKREGSCSDFQFKLHELTSLLEEKDSLIK 518
Cdd:TIGR02168  391 -----LELQIASLNNEIERLEARLERLEDR-RERLQQEIEELLKkleeaELKELQAELEELEEELEELQEELERLEEALE 464
                          250
                   ....*....|....*....
gi 193794853   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 3.81e-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: 43.63  E-value: 3.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   336 SNIREELGHLQNDMTSLENDKMRLEKDLSFKDTQLKEYEELLAsvrannHQQQQGLQdSSSKCQALEENNLSLRHtlsdm 415
Cdd:pfam01576  436 SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ------EETRQKLN-LSTRLRQLEDERNSLQE----- 503
                           90       100
                   ....*....|....*....|....*...
gi 193794853   416 eyRLKELEYCKRNLEQENQNLRMQVSET 443
Cdd:pfam01576  504 --QLEEEEEAKRNVERQLSTLQAQLSDM 529
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
326-531 8.18e-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: 8.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853 326 KSLRLVLSTFSNIREELGHLQNDMTSLENDKMRLEKDLSFKDTQLKEYEELLASVRANNHQQQQGLQDSSSKCQALEENN 405
Cdd:COG1196  225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853 406 LSLRHTLSDMEYRLKELEYCKRNLEQENQNLRMQVSEtctgpmLQAKMDEIGNHYTEMVKNLRMEKDREIcRLRSQLNQY 485
Cdd:COG1196  305 ARLEERRRELEERLEELEEELAELEEELEELEEELEE------LEEELEEAEEELEEAEAELAEAEEALL-EAEAELAEA 377
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 193794853 486 HKDVSKREGSCSDFQFKLHELTSLLEEKDSLIKRQSEELSKLRQEI 531
Cdd:COG1196  378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
279-531 8.62e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 8.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853 279 LQRIGGSKQDFESTDE-SEDIESLIPkgLSEFT-----KQ-QIRYILQMRGMSDKSLRLVLS--TFSNIREELGHLqndM 349
Cdd:PRK03918  97 LKYLDGSEVLEEGDSSvREWVERLIP--YHVFLnaiyiRQgEIDAILESDESREKVVRQILGldDYENAYKNLGEV---I 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853 350 TSLENDKMRLEKDLSFK---DTQLKEYEELLASVRANNHQQQQGLQDSSSKCQALEENNLSLRHT---LSDMEYRLKELE 423
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTeniEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEELEKELESLE 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853 424 YCKRNLEQENQNLRMQVSEtctgpmLQAKMDEIGNHYTEmVKNLRMEKD--REICRLRSQLNQYHKDVSKREGSCSDFQF 501
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEE------LKKEIEELEEKVKE-LKELKEKAEeyIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
                        250       260       270
                 ....*....|....*....|....*....|
gi 193794853 502 KLHELTSLLEEKDSLIKRQSEELSKLRQEI 531
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRL 354
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
280-532 1.01e-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: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   280 QRIGGSKQDFESTDESEDIESLIPKGLS-EFTKQQIRYILQMRGMSDKSLRLVlstfsNIREELGHLQNDMTSLENDKMR 358
Cdd:TIGR02168  789 AQIEQLKEELKALREALDELRAELTLLNeEAANLRERLESLERRIAATERRLE-----DLEEQIEELSEDIESLAAEIEE 863
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   359 LEKDLSFKDTQLKEYEELLASVRANNHQQQQGLQDSSSKCQALEENNLSLRHTLSDMEYRLKELEYCKRNLEQENQNLRM 438
Cdd:TIGR02168  864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   439 QVSEtctgpMLQAKMDEIGNHYtEMVKNLRMEKDREICRLRSQLNQY----------HKDVSKRegscsdFQFKLHELTS 508
Cdd:TIGR02168  944 RLSE-----EYSLTLEEAEALE-NKIEDDEEEARRRLKRLENKIKELgpvnlaaieeYEELKER------YDFLTAQKED 1011
                          250       260
                   ....*....|....*....|....*..
gi 193794853   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 1.09e-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: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   333 STFSNIREELGHLQNDMTSLENDKMRLEKDLSFKDTQLKEYEELLASVRANNHQQQQGLQDSSSKCQALEENNLSLRHTL 412
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   413 SDMEYRLKELEYCKRNLEQENQNLRMQVSETCTgpMLQAKMDEIGNHYT---------EMVKNLRMEKDREICRLRSQLN 483
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALRE--ALDELRAELTLLNEeaanlrerlESLERRIAATERRLEDLEEQIE 848
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 193794853   484 QYHKDVSKREGSCSDFQFKLHELTSLLEEKDSLIKRQSEELSKLRQE 530
Cdd:TIGR02168  849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
366-531 1.35e-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: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   366 KDTQLKEYEELLASVRANNHQQQQGLQDSSSKCQALEENNLSLRHTLSDMEYRLKELEYCKRNLEQENQNL--------- 436
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLeeriaqlsk 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   437 ---RMQVSETCTGPMLQAKMDEIGNHYTEMVK--------NLRMEKDREICR-LRSQLNQYHKDVSKREGSCSDFQFKLH 504
Cdd:TIGR02168  755 eltELEAEIEELEERLEEAEEELAEAEAEIEEleaqieqlKEELKALREALDeLRAELTLLNEEAANLRERLESLERRIA 834
                          170       180
                   ....*....|....*....|....*..
gi 193794853   505 ELTSLLEEKDSLIKRQSEELSKLRQEI 531
Cdd:TIGR02168  835 ATERRLEDLEEQIEELSEDIESLAAEI 861
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
324-442 1.36e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853 324 SDKSLRLVLSTFSNIREELGHLQNDMTSLENDKMRLEKDLSFKDTQLKEYEELLASVRANNHQQQQGLQDSSSKCQALEE 403
Cdd:COG4372   29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 193794853 404 NNLSLRHTLSDMEYRLKELEYCKRNLEQENQNLRMQVSE 442
Cdd:COG4372  109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAE 147
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
290-529 1.37e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853 290 ESTDESEDIESLIpKGLSEFTKQQIRYILQMRGMSD--KSLRLVLSTFSNIREELGHLQNDMTSLENDKMRLEKDLSFKD 367
Cdd:PRK03918 270 ELKKEIEELEEKV-KELKELKEKAEEYIKLSEFYEEylDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853 368 TQLKEYEELLASVRAnnHQQQQGLQDSSSKCQALEENNlslrhTLSDMEYRLKELEYCKRNLEQENQNLRmqvsetctgp 447
Cdd:PRK03918 349 ELEKRLEELEERHEL--YEEAKAKKEELERLKKRLTGL-----TPEKLEKELEELEKAKEEIEEEISKIT---------- 411
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853 448 mlqAKMDEIGNHYTEMVKNL-RMEKDREIC----RLRSQ------LNQYHKDVSKREGSCSDFQFKLHELTSLLEEKDSL 516
Cdd:PRK03918 412 ---ARIGELKKEIKELKKAIeELKKAKGKCpvcgRELTEehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKV 488
                        250
                 ....*....|...
gi 193794853 517 IKRQSeELSKLRQ 529
Cdd:PRK03918 489 LKKES-ELIKLKE 500
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
312-531 7.33e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 7.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   312 QQIRYILQMRGMSDKSLRLVLSTFSNIREELGHLQNDMTSLENDKMRLEKDLSFKDTQLKEYEELLASVRANNHQQQQGL 391
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   392 QDSSSKCQA--------------LEENNLSLRHTLSDMEYRLKELEyckRNLEqENQNLRMQvsetctgpmLQAKMDEIG 457
Cdd:TIGR02168  827 ESLERRIAAterrledleeqieeLSEDIESLAAEIEELEELIEELE---SELE-ALLNERAS---------LEEALALLR 893
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   458 NHYTEMVKNLR------MEKDREICRLRSQLNQYHKDVSKREGSCSDFQFKLHELTSLLEE--------KDSLIKRQSEE 523
Cdd:TIGR02168  894 SELEELSEELReleskrSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeaealenkIEDDEEEARRR 973

                   ....*...
gi 193794853   524 LSKLRQEI 531
Cdd:TIGR02168  974 LKRLENKI 981
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
293-535 7.52e-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: 7.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   293 DESEDIESLIPKglsefTKQQIRYILQMRGMSDKSLRLVLSTFSNIREELGHLQNDMTSLENDKMRLEKDLSFKDTQLKE 372
Cdd:TIGR00606  709 DKLKSTESELKK-----KEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEES 783
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   373 YEELLASVRANNHQQQQgLQDSSSKC--QALEENNLSLRHTLSDMEYRLKELEYCKRNLEQENQNLRMQVSETC-TGPML 449
Cdd:TIGR00606  784 AKVCLTDVTIMERFQME-LKDVERKIaqQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQeQIQHL 862
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193794853   450 QAKMDEIGNHYTEMVKNLR---------MEKDREICRLRSQLNQYHKDVSKREGSCSDFQFKLHELTSLLEEKDsliKRQ 520
Cdd:TIGR00606  863 KSKTNELKSEKLQIGTNLQrrqqfeeqlVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSN---KKA 939
                          250
                   ....*....|....*
gi 193794853   521 SEELSKLRQEIYSSH 535
Cdd:TIGR00606  940 QDKVNDIKEKVKNIH 954
 
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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