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Conserved domains on  [gi|1370485281|ref|XP_024309548|]
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centrosomal protein of 70 kDa isoform X1 [Homo sapiens]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

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

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
64-347 1.72e-05

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  64 QRMRQNLKLLVEETSCQQNMIQELIETNQQLRNELQLEQSRAANQEQRANDLEQIMESVKSKIGELEDESLsracHQQNK 143
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA----RLEER 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281 144 IKDLQKEQKTLQVKCQHYKKKRTEQEETIASLQMEVCRLKKEEEDRIVTQNRVfaylckrvphtvldrqllclidyyESK 223
Cdd:COG1196   311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA------------------------EEA 366
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281 224 IRKIHTQRQYKEDESQSEEENDYRNLDASPTYKGLLMSLQNQLKESKSKIDALSSEKLNLQKDLETrptqhELRLYKQQV 303
Cdd:COG1196   367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE-----LEEEEEEEE 441
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1370485281 304 KKLEKALKKNVKLQELINHKKAEDTEKKDEpskYNQQQALIDQR 347
Cdd:COG1196   442 EALEEAAEEEAELEEEEEALLELLAELLEE---AALLEAALAEL 482
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
64-347 1.72e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  64 QRMRQNLKLLVEETSCQQNMIQELIETNQQLRNELQLEQSRAANQEQRANDLEQIMESVKSKIGELEDESLsracHQQNK 143
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA----RLEER 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281 144 IKDLQKEQKTLQVKCQHYKKKRTEQEETIASLQMEVCRLKKEEEDRIVTQNRVfaylckrvphtvldrqllclidyyESK 223
Cdd:COG1196   311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA------------------------EEA 366
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281 224 IRKIHTQRQYKEDESQSEEENDYRNLDASPTYKGLLMSLQNQLKESKSKIDALSSEKLNLQKDLETrptqhELRLYKQQV 303
Cdd:COG1196   367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE-----LEEEEEEEE 441
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1370485281 304 KKLEKALKKNVKLQELINHKKAEDTEKKDEpskYNQQQALIDQR 347
Cdd:COG1196   442 EALEEAAEEEAELEEEEEALLELLAELLEE---AALLEAALAEL 482
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
70-333 1.69e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  70 LKLLVEETSCQQNMIQELIETNQQLRNELQLEQSRAANQEQRANDLEQIMESVKSKIGELED--ESLSRACHQQNKIKDL 147
Cdd:PRK03918  298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEErhELYEEAKAKKEELERL 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281 148 QKEQKTLQV-----KCQHYKKKRTEQEETIASLQMEVCRLKKEEEDRIVTQNRVFAY-----LCKRvPHTVLDRqlLCLI 217
Cdd:PRK03918  378 KKRLTGLTPeklekELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGR-ELTEEHR--KELL 454
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281 218 DYYESKIRKIHTQRQyKEDESQSEEENDYRNLDASPTYKGLLMSLQ---NQLKESKSKIDALSSEKLNlQKDLETRPTQH 294
Cdd:PRK03918  455 EEYTAELKRIEKELK-EIEEKERKLRKELRELEKVLKKESELIKLKelaEQLKELEEKLKKYNLEELE-KKAEEYEKLKE 532
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1370485281 295 ELRLYKQQVKKLEKALKknvKLQELINhKKAEDTEKKDE 333
Cdd:PRK03918  533 KLIKLKGEIKSLKKELE---KLEELKK-KLAELEKKLDE 567
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
71-319 1.14e-03

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: 42.08  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281   71 KLLVEETSCQQNMIQELIETNQQLRNEL--QLEQSRAANQeqranDLEQIMESVKSKIGELEDE--SLSRACHQ-QNKIK 145
Cdd:pfam01576  334 KALEEETRSHEAQLQEMRQKHTQALEELteQLEQAKRNKA-----NLEKAKQALESENAELQAElrTLQQAKQDsEHKRK 408
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  146 DLQKEQKTLQVKCQHYKKKRTEQEETIASLQME---VCRLKKEEEdrivTQNRVFAYLCKRVPHTVLDRQLLcLIDYYES 222
Cdd:pfam01576  409 KLEGQLQELQARLSESERQRAELAEKLSKLQSElesVSSLLNEAE----GKNIKLSKDVSSLESQLQDTQEL-LQEETRQ 483
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  223 KIRKIHTQRQYKED-----ESQSEEENDYRNLDASptykglLMSLQNQLKESKSK-------IDALSSEKLNLQKDLETR 290
Cdd:pfam01576  484 KLNLSTRLRQLEDErnslqEQLEEEEEAKRNVERQ------LSTLQAQLSDMKKKleedagtLEALEEGKKRLQRELEAL 557
                          250       260
                   ....*....|....*....|....*....
gi 1370485281  291 PTQHELRlyKQQVKKLEKAlkKNVKLQEL 319
Cdd:pfam01576  558 TQQLEEK--AAAYDKLEKT--KNRLQQEL 582
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
13-343 4.30e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.34  E-value: 4.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281   13 QPSDRLMTEKQQEEAEWESINVLLMMHGLKPLSLVKRTDLKDlIIFDKQSSQRMRQNLKLLVEETSCQQNMIQELIETNQ 92
Cdd:TIGR00618  307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ-TLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQ 385
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281   93 Q--------------LRNELQLEQSRAANQEQRANDLEQIMESVKSKIgELEDESLSRACHQQNKIKDLQKEQKTLQVKC 158
Cdd:TIGR00618  386 QqkttltqklqslckELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ-ELQQRYAELCAAAITCTAQCEKLEKIHLQES 464
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  159 QHYKKKRTEQEETIASLQMEVCRLKKEEEDRIVTQNRVFAYLCKRVPHTVLDRQLLCLIDYYESKIRKIhtqrQYKEDES 238
Cdd:TIGR00618  465 AQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRG----EQTYAQL 540
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  239 QSEEENDYRNLDA----SPTYKGLLMSLQNQLKESKSKIDALSSEKLNLQKDLEtrptqhELRLYKQQVKKLEKALKKNV 314
Cdd:TIGR00618  541 ETSEEDVYHQLTSerkqRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITV------RLQDLTEKLSEAEDMLACEQ 614
                          330       340
                   ....*....|....*....|....*....
gi 1370485281  315 KLQELINHKKAEDTEKKDEPSKYNQQQAL 343
Cdd:TIGR00618  615 HALLRKLQPEQDLQDVRLHLQQCSQELAL 643
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
64-347 1.72e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  64 QRMRQNLKLLVEETSCQQNMIQELIETNQQLRNELQLEQSRAANQEQRANDLEQIMESVKSKIGELEDESLsracHQQNK 143
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA----RLEER 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281 144 IKDLQKEQKTLQVKCQHYKKKRTEQEETIASLQMEVCRLKKEEEDRIVTQNRVfaylckrvphtvldrqllclidyyESK 223
Cdd:COG1196   311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA------------------------EEA 366
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281 224 IRKIHTQRQYKEDESQSEEENDYRNLDASPTYKGLLMSLQNQLKESKSKIDALSSEKLNLQKDLETrptqhELRLYKQQV 303
Cdd:COG1196   367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE-----LEEEEEEEE 441
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1370485281 304 KKLEKALKKNVKLQELINHKKAEDTEKKDEpskYNQQQALIDQR 347
Cdd:COG1196   442 EALEEAAEEEAELEEEEEALLELLAELLEE---AALLEAALAEL 482
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
70-333 1.69e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  70 LKLLVEETSCQQNMIQELIETNQQLRNELQLEQSRAANQEQRANDLEQIMESVKSKIGELED--ESLSRACHQQNKIKDL 147
Cdd:PRK03918  298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEErhELYEEAKAKKEELERL 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281 148 QKEQKTLQV-----KCQHYKKKRTEQEETIASLQMEVCRLKKEEEDRIVTQNRVFAY-----LCKRvPHTVLDRqlLCLI 217
Cdd:PRK03918  378 KKRLTGLTPeklekELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGR-ELTEEHR--KELL 454
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281 218 DYYESKIRKIHTQRQyKEDESQSEEENDYRNLDASPTYKGLLMSLQ---NQLKESKSKIDALSSEKLNlQKDLETRPTQH 294
Cdd:PRK03918  455 EEYTAELKRIEKELK-EIEEKERKLRKELRELEKVLKKESELIKLKelaEQLKELEEKLKKYNLEELE-KKAEEYEKLKE 532
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1370485281 295 ELRLYKQQVKKLEKALKknvKLQELINhKKAEDTEKKDE 333
Cdd:PRK03918  533 KLIKLKGEIKSLKKELE---KLEELKK-KLAELEKKLDE 567
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
64-347 2.44e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  64 QRMRQNLKLLVEETSCQQNMIQELIETNQQLRNELQLEQSRAANQEQRANDLEQIMESVKSKIGELEDESLSrachQQNK 143
Cdd:COG1196   270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE----LEEE 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281 144 IKDLQKEQKTLQVKCQHYKKKRTEQEETIASLQMEVCRLKKEEEDRivtqnrvfaylckrvphtvldrqllclidyyESK 223
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-------------------------------LRA 394
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281 224 IRKIHTQRQYKEDESQSEEENDYRNLDAsptykglLMSLQNQLKESKSKIDALSSEKLNLQKDLETrptqhELRLYKQQV 303
Cdd:COG1196   395 AAELAAQLEELEEAEEALLERLERLEEE-------LEELEEALAELEEEEEEEEEALEEAAEEEAE-----LEEEEEALL 462
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1370485281 304 KKLEKALKKNVKLQELINHKKAEDTEKKdepSKYNQQQALIDQR 347
Cdd:COG1196   463 ELLAELLEEAALLEAALAELLEELAEAA---ARLLLLLEAEADY 503
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
80-335 4.86e-04

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: 42.83  E-value: 4.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  80 QQNMIQELIETNQQLRNELQLEQSRAANQEQRANDLEQIMESVKSKIGELEDESLSrachQQNKIKDLQKEQKTLQvkcq 159
Cdd:COG4942    25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA----LEAELAELEKEIAELR---- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281 160 hykKKRTEQEETIASLQMEVCRLKKEEEDRIVTQNRVFAYLCKRV-PHTVLDRQLLCLIDYYESKIRKIHTQRQYKEDES 238
Cdd:COG4942    97 ---AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqYLKYLAPARREQAEELRADLAELAALRAELEAER 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281 239 QSeeendyrnldasptykglLMSLQNQLKESKSKIDALSSEKLNLQKDLETrptqhELRLYKQQVKKLEKALKknvKLQE 318
Cdd:COG4942   174 AE------------------LEALLAELEEERAALEALKAERQKLLARLEK-----ELAELAAELAELQQEAE---ELEA 227
                         250
                  ....*....|....*..
gi 1370485281 319 LINHKKAEDTEKKDEPS 335
Cdd:COG4942   228 LIARLEAEAAAAAERTP 244
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
71-319 1.14e-03

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: 42.08  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281   71 KLLVEETSCQQNMIQELIETNQQLRNEL--QLEQSRAANQeqranDLEQIMESVKSKIGELEDE--SLSRACHQ-QNKIK 145
Cdd:pfam01576  334 KALEEETRSHEAQLQEMRQKHTQALEELteQLEQAKRNKA-----NLEKAKQALESENAELQAElrTLQQAKQDsEHKRK 408
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  146 DLQKEQKTLQVKCQHYKKKRTEQEETIASLQME---VCRLKKEEEdrivTQNRVFAYLCKRVPHTVLDRQLLcLIDYYES 222
Cdd:pfam01576  409 KLEGQLQELQARLSESERQRAELAEKLSKLQSElesVSSLLNEAE----GKNIKLSKDVSSLESQLQDTQEL-LQEETRQ 483
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  223 KIRKIHTQRQYKED-----ESQSEEENDYRNLDASptykglLMSLQNQLKESKSK-------IDALSSEKLNLQKDLETR 290
Cdd:pfam01576  484 KLNLSTRLRQLEDErnslqEQLEEEEEAKRNVERQ------LSTLQAQLSDMKKKleedagtLEALEEGKKRLQRELEAL 557
                          250       260
                   ....*....|....*....|....*....
gi 1370485281  291 PTQHELRlyKQQVKKLEKAlkKNVKLQEL 319
Cdd:pfam01576  558 TQQLEEK--AAAYDKLEKT--KNRLQQEL 582
PTZ00121 PTZ00121
MAEBL; Provisional
88-336 1.57e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281   88 IETNQQLRNELQLEQSRAANQEQRANDLEQImESVKSKIGELEDESLSRACHQQNKIKDLQKEQKTLQVKCQHYKKKRTE 167
Cdd:PTZ00121  1202 AEAARKAEEERKAEEARKAEDAKKAEAVKKA-EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA 1280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  168 QEETIASLQMEVCRLKKEEEDRIVTQNRVFAYLCKRVPHTVLDRQllclidyyESK-----IRKIHTQRQYKEDESQSEE 242
Cdd:PTZ00121  1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAE--------EAKkkadaAKKKAEEAKKAAEAAKAEA 1352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  243 ENDYRNLDASPTYKgllMSLQNQLKESKSKIDALSSEKLNLQKDLETRPTQHELRLYKQQVKKLEKALKKNVKLQelinh 322
Cdd:PTZ00121  1353 EAAADEAEAAEEKA---EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK----- 1424
                          250
                   ....*....|....
gi 1370485281  323 KKAEDTEKKDEPSK 336
Cdd:PTZ00121  1425 KKAEEKKKADEAKK 1438
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
13-343 4.30e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.34  E-value: 4.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281   13 QPSDRLMTEKQQEEAEWESINVLLMMHGLKPLSLVKRTDLKDlIIFDKQSSQRMRQNLKLLVEETSCQQNMIQELIETNQ 92
Cdd:TIGR00618  307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ-TLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQ 385
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281   93 Q--------------LRNELQLEQSRAANQEQRANDLEQIMESVKSKIgELEDESLSRACHQQNKIKDLQKEQKTLQVKC 158
Cdd:TIGR00618  386 QqkttltqklqslckELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ-ELQQRYAELCAAAITCTAQCEKLEKIHLQES 464
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  159 QHYKKKRTEQEETIASLQMEVCRLKKEEEDRIVTQNRVFAYLCKRVPHTVLDRQLLCLIDYYESKIRKIhtqrQYKEDES 238
Cdd:TIGR00618  465 AQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRG----EQTYAQL 540
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  239 QSEEENDYRNLDA----SPTYKGLLMSLQNQLKESKSKIDALSSEKLNLQKDLEtrptqhELRLYKQQVKKLEKALKKNV 314
Cdd:TIGR00618  541 ETSEEDVYHQLTSerkqRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITV------RLQDLTEKLSEAEDMLACEQ 614
                          330       340
                   ....*....|....*....|....*....
gi 1370485281  315 KLQELINHKKAEDTEKKDEPSKYNQQQAL 343
Cdd:TIGR00618  615 HALLRKLQPEQDLQDVRLHLQQCSQELAL 643
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
92-179 4.59e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 4.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281   92 QQLRNELQLEQSRAANQEQRANDLEQIMESVKSKIGELEDEslsRACHQQNKIKDLQKEQKTLQVKCQHYKKKRTEQEET 171
Cdd:COG4913    291 ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ---IRGNGGDRLEQLEREIERLERELEERERRRARLEAL 367

                   ....*...
gi 1370485281  172 IASLQMEV 179
Cdd:COG4913    368 LAALGLPL 375
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
64-195 5.94e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.72  E-value: 5.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  64 QRMRQNLKLLVEETSCQQNMIQELIETNQQLRNELQLE---QSRAANQEQRANDLEQIMESVKSKIGEledeslsrachQ 140
Cdd:pfam17380 443 ERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEkekRDRKRAEEQRRKILEKELEERKQAMIE-----------E 511
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370485281 141 QNKIKDLQKEQKTLQVKCQHYKKKRTEQEETIASLQMEVcRLKKEEEDRIVTQNR 195
Cdd:pfam17380 512 ERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE-RRRIQEQMRKATEER 565
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
60-361 6.84e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.62  E-value: 6.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  60 KQSSQRMRQNLKLLVEETSCQQNMIQELIETNQQLRNELQLEQSRAANQEQRANDLEQIMESVKSKIGELEDESlsrach 139
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK------ 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281 140 QQNKIKDLQKEQKTLQVKCQHYKKKRTEQEETIASLQMEVCRLKKEEEDrivtqnrvfaylcKRVPHTVLDRQLlcliDY 219
Cdd:TIGR04523 305 EQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTN-------------SESENSEKQREL----EE 367
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281 220 YESKIRKIHTQRQYKEDESQseeendyrnldasptykgllmSLQNQLKESKSKIDalSSEKLNLQKDLETRPTQHELRLY 299
Cdd:TIGR04523 368 KQNEIEKLKKENQSYKQEIK---------------------NLESQINDLESKIQ--NQEKLNQQKDEQIKKLQQEKELL 424
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370485281 300 KQQVKKLekaLKKNVKLQELINHKKAEDTEKKDEPSKYNQQQALIDQRYFQVLCSINSIIHN 361
Cdd:TIGR04523 425 EKEIERL---KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
20-306 7.13e-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: 7.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281   20 TEKQQEEAEWESINVLLMMHGLKPLSLVKRTDLKDL---IIFDKQSSQRMRQNLKLLVEETSCQQNMIQELIETNQQLRN 96
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281   97 ELQLEQSRAANQEQRANDLEQIMESVKSKIGELEDE--SLSRACH-QQNKIKDLQKEQKTLQVKCQHYKKKRTEQEETIA 173
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAEltLLNEEAAnLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  174 SLQMEvcrLKKEEEDRIVTQNRVFAYLCKRVPHTVLDRQLLCLIDYYESKIRKIHTQRQYKEDESQS--EEENDYRNlda 251
Cdd:TIGR02168  856 SLAAE---IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEElrEKLAQLEL--- 929
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370485281  252 spTYKGLLMSLQNQLKE--SKSKIDALSSEKLNLQKDLETRPTQHELRLYKQQVKKL 306
Cdd:TIGR02168  930 --RLEGLEVRIDNLQERlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
51-311 8.74e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.28  E-value: 8.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281   51 DLKDLIIFDKQSSQRMRQNLKLLVEETSCQQNMIQELIETNQQLRNELQLEQSRAANQEQRANDLEQIMESVKSKIGELE 130
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  131 ------DESLSRACHQQNKIKD--LQKEQKTLQVKCQHYKKKRTEQEETIASLQMEVCRLKKEEEdrivtqnrvfaYLCK 202
Cdd:TIGR02169  765 arieelEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE-----------YLEK 833
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370485281  203 RVPHtvLDRQLLCLIDYYESKIRKIHTQRQYKEDESQSEEENDYRNLDASPTYKGL---LMSLQNQLKESKSKIDALSSE 279
Cdd:TIGR02169  834 EIQE--LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLkkeRDELEAQLRELERKIEELEAQ 911
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1370485281  280 KLNLQKDLETRPTQheLRLYKQQVKKLEKALK 311
Cdd:TIGR02169  912 IEKKRKRLSELKAK--LEALEEELSEIEDPKG 941
 
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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