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Conserved domains on  [gi|26326697|dbj|BAC27092|]
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unnamed protein product, partial [Mus musculus]

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

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List of domain hits

Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
96-358 2.51e-07

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 2.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697     96 DELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRISEVLQKLQNEIlKDLSDGIHVVKDARER 175
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI-SRLEQQKQILRERLAN 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    176 DFTSLENtVEERLTELTKSINDNIAIFTDVQKRSQ----------KEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQ 245
Cdd:TIGR02168  314 LERQLEE-LEAQLEELESKLDELAEELAELEEKLEelkeelesleAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    246 ---ASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERL--ALQALTEKLLRSEESSSRLPEDIRR 320
Cdd:TIGR02168  393 lqiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELeeELEELQEELERLEEALEELREELEE 472
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 26326697    321 LEEELQQLKvgahgSEEGAVFKDSKALEELQRQIEGLG 358
Cdd:TIGR02168  473 AEQALDAAE-----RELAQLQARLDSLERLQENLEGFS 505
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
225-520 5.39e-06

DNA double-strand break repair ATPase Rad50;


The actual alignment was detected with superfamily member PRK03918:

Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 5.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  225 ESKGDRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERLALQALTEKL 304
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  305 LRSEESSSRLPEDIRRLEEELQQLKVGAHGSEegavfKDSKALEELQRQIEGL-GARLQYVEDGvysmqvasarhtESLE 383
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELK-----KEIEELEEKVKELKELkEKAEEYIKLS------------EFYE 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  384 SLLSKSQEYEQRLAMLQEHVGNLGSS-SDLASTVRSLGEtqlaLSSDLKELKQSLGELPGTVESLQE--QVLSLLSQDQA 460
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERiKELEEKEERLEE----LKKKLKELEKRLEELEERHELYEEakAKKEELERLKK 379
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  461 QAEGLPPQDFLDRLSSLDNLKssvSQVESDLKMLRTAVDSLVAYSVKIETNENNLESAKG 520
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAK---EEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
96-358 2.51e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 2.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697     96 DELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRISEVLQKLQNEIlKDLSDGIHVVKDARER 175
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI-SRLEQQKQILRERLAN 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    176 DFTSLENtVEERLTELTKSINDNIAIFTDVQKRSQ----------KEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQ 245
Cdd:TIGR02168  314 LERQLEE-LEAQLEELESKLDELAEELAELEEKLEelkeelesleAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    246 ---ASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERL--ALQALTEKLLRSEESSSRLPEDIRR 320
Cdd:TIGR02168  393 lqiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELeeELEELQEELERLEEALEELREELEE 472
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 26326697    321 LEEELQQLKvgahgSEEGAVFKDSKALEELQRQIEGLG 358
Cdd:TIGR02168  473 AEQALDAAE-----RELAQLQARLDSLERLQENLEGFS 505
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
93-362 9.39e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 9.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  93 RQRDELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRISEVLQKLQNEILKDLSDGIHVVKDA 172
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697 173 RErdftslENTVEERLTELTKSINDNIAIFTDVQKRSQKEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQASMMSRE 252
Cdd:COG1196 312 RE------LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697 253 RDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERLALQALTEKLLRSEESSSRLPEDIRRLEEELQQLKVgA 332
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE-L 464
                       250       260       270
                ....*....|....*....|....*....|
gi 26326697 333 HGSEEGAVFKDSKALEELQRQIEGLGARLQ 362
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLL 494
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
225-520 5.39e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 5.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  225 ESKGDRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERLALQALTEKL 304
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  305 LRSEESSSRLPEDIRRLEEELQQLKVGAHGSEegavfKDSKALEELQRQIEGL-GARLQYVEDGvysmqvasarhtESLE 383
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELK-----KEIEELEEKVKELKELkEKAEEYIKLS------------EFYE 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  384 SLLSKSQEYEQRLAMLQEHVGNLGSS-SDLASTVRSLGEtqlaLSSDLKELKQSLGELPGTVESLQE--QVLSLLSQDQA 460
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERiKELEEKEERLEE----LKKKLKELEKRLEELEERHELYEEakAKKEELERLKK 379
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  461 QAEGLPPQDFLDRLSSLDNLKssvSQVESDLKMLRTAVDSLVAYSVKIETNENNLESAKG 520
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAK---EEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
243-516 6.69e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 6.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    243 EVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERLALQALTEKLLRSEESSSRLPEDIRRLE 322
Cdd:TIGR02168  667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    323 EELQQLkvgahgseEGAVFKDSKALEELQRQIEGLGARLQYVEDGVYSMQVASARHTESLESLLSKSQEYEQRLAMLQEH 402
Cdd:TIGR02168  747 ERIAQL--------SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    403 VGNL-----GSSSDLASTVRSLGETQLA---LSSDLKELKQSLGELPGTVESLQEQVLSLLSQDQAQAEGLPpqdflDRL 474
Cdd:TIGR02168  819 AANLrerleSLERRIAATERRLEDLEEQieeLSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA-----LLR 893
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 26326697    475 SSLDNLKSSVSQVESDLKMLRTAVDSLVAYSVKIETNENNLE 516
Cdd:TIGR02168  894 SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
92-448 9.80e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.58  E-value: 9.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697     92 SRQRDELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRI---------SEVLQKLQNEILKDL 162
Cdd:pfam15921  327 SQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladlhkrekELSLEKEQNKRLWDR 406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    163 SDGIHVVKDARERDFTSlENTVEERLTELTKSINDNIAIFTDVQKRSQKEINEVKMKVASLE--------------ESKG 228
Cdd:pfam15921  407 DTGNSITIDHLRRELDD-RNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTaqlestkemlrkvvEELT 485
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    229 DRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQA-ADSERLALQaLTEKllrs 307
Cdd:pfam15921  486 AKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVqTECEALKLQ-MAEK---- 560
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    308 eessSRLPEDIRRLEEELQQLkVGAHGSEEGAVFKDSKALE-----------ELQRQIEGLGARLQYVEDGVYSMQVASA 376
Cdd:pfam15921  561 ----DKVIEILRQQIENMTQL-VGQHGRTAGAMQVEKAQLEkeindrrlelqEFKILKDKKDAKIRELEARVSDLELEKV 635
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    377 R----HTESLESLLSKSQEYEQRLAMLQEHVGNLGSSSD----LASTVRSLGETQLALSSDLK-ELKQSLGELPGTVESL 447
Cdd:pfam15921  636 KlvnaGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEdyevLKRNFRNKSEEMETTTNKLKmQLKSAQSELEQTRNTL 715

                   .
gi 26326697    448 Q 448
Cdd:pfam15921  716 K 716
PLN02939 PLN02939
transferase, transferring glycosyl groups
102-410 3.76e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 43.35  E-value: 3.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  102 LQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRI---SEVLQKLQNEILKDLSDGIHVVKDARERDFT 178
Cdd:PLN02939 116 QTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKIlteKEALQGKINILEMRLSETDARIKLAAQEKIH 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  179 SleNTVEERLTELTKSINDNIAIFTDVQKRSQKEINEVKMKVASLEeskgDRSQDVKTLKDAVKEVQASMMSRERDIEAL 258
Cdd:PLN02939 196 V--EILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLK----DDIQFLKAELIEVAETEERVFKLEKERSLL 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  259 KSSLQTMES---DVYTEVRELVSLKQEqqAFKQAADSERLALQALT---EKLLRSEESSSRLPEDIRRLEEELqqlkvga 332
Cdd:PLN02939 270 DASLRELESkfiVAQEDVSKLSPLQYD--CWWEKVENLQDLLDRATnqvEKAALVLDQNQDLRDKVDKLEASL------- 340
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26326697  333 hgsEEGAVFKDSKALEELQRQieglgaRLQYVEDgvysmqvasaRHTESLESLLSKSQEYEQRLAMLQEHVGNLGSSS 410
Cdd:PLN02939 341 ---KEANVSKFSSYKVELLQQ------KLKLLEE----------RLQASDHEIHSYIQLYQESIKEFQDTLSKLKEES 399
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
96-358 2.51e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 2.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697     96 DELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRISEVLQKLQNEIlKDLSDGIHVVKDARER 175
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI-SRLEQQKQILRERLAN 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    176 DFTSLENtVEERLTELTKSINDNIAIFTDVQKRSQ----------KEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQ 245
Cdd:TIGR02168  314 LERQLEE-LEAQLEELESKLDELAEELAELEEKLEelkeelesleAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    246 ---ASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERL--ALQALTEKLLRSEESSSRLPEDIRR 320
Cdd:TIGR02168  393 lqiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELeeELEELQEELERLEEALEELREELEE 472
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 26326697    321 LEEELQQLKvgahgSEEGAVFKDSKALEELQRQIEGLG 358
Cdd:TIGR02168  473 AEQALDAAE-----RELAQLQARLDSLERLQENLEGFS 505
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
77-401 8.61e-07

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: 51.99  E-value: 8.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697     77 VLEEVQQVRRGHQDFSRQRDELGQGLQGVE------QKVQSLQATFGTFESLLRNSQHKQDLTEKavKEGESELNRISEV 150
Cdd:TIGR02169  175 ALEELEEVEENIERLDLIIDEKRQQLERLRrerekaERYQALLKEKREYEGYELLKEKEALERQK--EAIERQLASLEEE 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    151 LQKLQNEIlkdlsdgihvvkDARERDFTSLEntveERLTELTKSINDniaIFTDVQKRSQKEINEVKMKVASLEESKGDR 230
Cdd:TIGR02169  253 LEKLTEEI------------SELEKRLEEIE----QLLEELNKKIKD---LGEEEQLRVKEKIGELEAEIASLERSIAEK 313
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    231 SQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERLALQALTEKLLRSEES 310
Cdd:TIGR02169  314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    311 SSRLPEDI-------RRLEEELQQLkvgahgseegavfkdSKALEELQRQIEGLGARLQYVEDGVYSMQVASARHTESLE 383
Cdd:TIGR02169  394 LEKLKREInelkrelDRLQEELQRL---------------SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
                          330
                   ....*....|....*...
gi 26326697    384 SLLSKSQEYEQRLAMLQE 401
Cdd:TIGR02169  459 QLAADLSKYEQELYDLKE 476
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
93-362 9.39e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 9.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  93 RQRDELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRISEVLQKLQNEILKDLSDGIHVVKDA 172
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697 173 RErdftslENTVEERLTELTKSINDNIAIFTDVQKRSQKEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQASMMSRE 252
Cdd:COG1196 312 RE------LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697 253 RDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERLALQALTEKLLRSEESSSRLPEDIRRLEEELQQLKVgA 332
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE-L 464
                       250       260       270
                ....*....|....*....|....*....|
gi 26326697 333 HGSEEGAVFKDSKALEELQRQIEGLGARLQ 362
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLL 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
79-358 1.14e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697     79 EEVQQVRRGHQDFSRQRDELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRISEVLQKLQNEI 158
Cdd:TIGR02168  712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI 791
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    159 LKDLSDgihvvKDARERDFTSLEN----------TVEERLTELTKSINDNIAIFTDVQKRS---QKEINEVKMKVASLEE 225
Cdd:TIGR02168  792 EQLKEE-----LKALREALDELRAeltllneeaaNLRERLESLERRIAATERRLEDLEEQIeelSEDIESLAAEIEELEE 866
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    226 SKGDRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESdvytevrELVSLKQEQQAFKQAADSERLALQALTEKLL 305
Cdd:TIGR02168  867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELES-------KRSELRRELEELREKLAQLELRLEGLEVRID 939
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 26326697    306 RSEEsssRLPEDIRRLEEELQQLKVGAHGSEEGAvfkdSKALEELQRQIEGLG 358
Cdd:TIGR02168  940 NLQE---RLSEEYSLTLEEAEALENKIEDDEEEA----RRRLKRLENKIKELG 985
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
93-332 1.81e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.15  E-value: 1.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  93 RQRDELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRISEVLQKLQNEIlkdlsdgihvvkDA 172
Cdd:COG4942  27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI------------AE 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697 173 RERDFTSLENTVEERLTELTK-SINDNIAIFTdvqkrSQKEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQAsmmsR 251
Cdd:COG4942  95 LRAELEAQKEELAELLRALYRlGRQPPLALLL-----SPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA----L 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697 252 ERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERLALQALTEKLLRSEESSSRLPEDIRRLEEELQQLKVG 331
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245

                .
gi 26326697 332 A 332
Cdd:COG4942 246 A 246
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
225-520 5.39e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 5.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  225 ESKGDRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERLALQALTEKL 304
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  305 LRSEESSSRLPEDIRRLEEELQQLKVGAHGSEegavfKDSKALEELQRQIEGL-GARLQYVEDGvysmqvasarhtESLE 383
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELK-----KEIEELEEKVKELKELkEKAEEYIKLS------------EFYE 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  384 SLLSKSQEYEQRLAMLQEHVGNLGSS-SDLASTVRSLGEtqlaLSSDLKELKQSLGELPGTVESLQE--QVLSLLSQDQA 460
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERiKELEEKEERLEE----LKKKLKELEKRLEELEERHELYEEakAKKEELERLKK 379
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  461 QAEGLPPQDFLDRLSSLDNLKssvSQVESDLKMLRTAVDSLVAYSVKIETNENNLESAKG 520
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAK---EEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
243-516 6.69e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 6.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    243 EVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERLALQALTEKLLRSEESSSRLPEDIRRLE 322
Cdd:TIGR02168  667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    323 EELQQLkvgahgseEGAVFKDSKALEELQRQIEGLGARLQYVEDGVYSMQVASARHTESLESLLSKSQEYEQRLAMLQEH 402
Cdd:TIGR02168  747 ERIAQL--------SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    403 VGNL-----GSSSDLASTVRSLGETQLA---LSSDLKELKQSLGELPGTVESLQEQVLSLLSQDQAQAEGLPpqdflDRL 474
Cdd:TIGR02168  819 AANLrerleSLERRIAATERRLEDLEEQieeLSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA-----LLR 893
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 26326697    475 SSLDNLKSSVSQVESDLKMLRTAVDSLVAYSVKIETNENNLE 516
Cdd:TIGR02168  894 SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
92-448 9.80e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.58  E-value: 9.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697     92 SRQRDELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRI---------SEVLQKLQNEILKDL 162
Cdd:pfam15921  327 SQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladlhkrekELSLEKEQNKRLWDR 406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    163 SDGIHVVKDARERDFTSlENTVEERLTELTKSINDNIAIFTDVQKRSQKEINEVKMKVASLE--------------ESKG 228
Cdd:pfam15921  407 DTGNSITIDHLRRELDD-RNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTaqlestkemlrkvvEELT 485
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    229 DRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQA-ADSERLALQaLTEKllrs 307
Cdd:pfam15921  486 AKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVqTECEALKLQ-MAEK---- 560
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    308 eessSRLPEDIRRLEEELQQLkVGAHGSEEGAVFKDSKALE-----------ELQRQIEGLGARLQYVEDGVYSMQVASA 376
Cdd:pfam15921  561 ----DKVIEILRQQIENMTQL-VGQHGRTAGAMQVEKAQLEkeindrrlelqEFKILKDKKDAKIRELEARVSDLELEKV 635
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    377 R----HTESLESLLSKSQEYEQRLAMLQEHVGNLGSSSD----LASTVRSLGETQLALSSDLK-ELKQSLGELPGTVESL 447
Cdd:pfam15921  636 KlvnaGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEdyevLKRNFRNKSEEMETTTNKLKmQLKSAQSELEQTRNTL 715

                   .
gi 26326697    448 Q 448
Cdd:pfam15921  716 K 716
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
210-454 4.22e-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: 4.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    210 QKEINEVKMKVASLEEskgdrsqDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQA 289
Cdd:TIGR02168  676 RREIEELEEKIEELEE-------KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    290 ADSERLALQALTEKLLRSEESSSRLPEDIRRLEEELQQLKVGAHGSEEgAVFKDSKALEELQRQIEGLGARLQYVEDGVY 369
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE-ELKALREALDELRAELTLLNEEAANLRERLE 827
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    370 SMQVASARHTESLESLLSKSQEYEQRLAMLQEHVGNLGSSSD-LASTVRSLGETQLALSSDLKELKQSLGELPGTVESLQ 448
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEeLESELEALLNERASLEEALALLRSELEELSEELRELE 907

                   ....*.
gi 26326697    449 EQVLSL 454
Cdd:TIGR02168  908 SKRSEL 913
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
205-450 5.26e-05

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: 46.21  E-value: 5.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    205 VQKRSQKEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQ 284
Cdd:TIGR02169  668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    285 AFKQAADSERLALQALTEKLlrseessSRLPEDIRRLEEELQQLKVGAHGSEEGAVFKDSKALEELQRQIEglgARLQYV 364
Cdd:TIGR02169  748 SLEQEIENVKSELKELEARI-------EELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIE---ARLREI 817
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    365 EDGVYSMQVASARHTESLESLLSKSQEYEQRLAMLQEHVGNLgsSSDLASTVRSLGETQLAlssdLKELKQSLGELPGTV 444
Cdd:TIGR02169  818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL--NGKKEELEEELEELEAA----LRDLESRLGDLKKER 891

                   ....*.
gi 26326697    445 ESLQEQ 450
Cdd:TIGR02169  892 DELEAQ 897
PLN02939 PLN02939
transferase, transferring glycosyl groups
102-410 3.76e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 43.35  E-value: 3.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  102 LQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRI---SEVLQKLQNEILKDLSDGIHVVKDARERDFT 178
Cdd:PLN02939 116 QTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKIlteKEALQGKINILEMRLSETDARIKLAAQEKIH 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  179 SleNTVEERLTELTKSINDNIAIFTDVQKRSQKEINEVKMKVASLEeskgDRSQDVKTLKDAVKEVQASMMSRERDIEAL 258
Cdd:PLN02939 196 V--EILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLK----DDIQFLKAELIEVAETEERVFKLEKERSLL 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  259 KSSLQTMES---DVYTEVRELVSLKQEqqAFKQAADSERLALQALT---EKLLRSEESSSRLPEDIRRLEEELqqlkvga 332
Cdd:PLN02939 270 DASLRELESkfiVAQEDVSKLSPLQYD--CWWEKVENLQDLLDRATnqvEKAALVLDQNQDLRDKVDKLEASL------- 340
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26326697  333 hgsEEGAVFKDSKALEELQRQieglgaRLQYVEDgvysmqvasaRHTESLESLLSKSQEYEQRLAMLQEHVGNLGSSS 410
Cdd:PLN02939 341 ---KEANVSKFSSYKVELLQQ------KLKLLEE----------RLQASDHEIHSYIQLYQESIKEFQDTLSKLKEES 399
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
78-463 4.11e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 4.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  78 LEEVQQVRRGHQDFSRQRDELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLtekavKEGESELNRISEVLQKLQNE 157
Cdd:COG4717  80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL-----EALEAELAELPERLEELEER 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697 158 I---------LKDLSDGIHVVKDARERDFTSLENTVEERLTELTKSIND---NIAIFTDVQKRSQKEINEVKMKVASLEE 225
Cdd:COG4717 155 LeelreleeeLEELEAELAELQEELEELLEQLSLATEEELQDLAEELEElqqRLAELEEELEEAQEELEELEEELEQLEN 234
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697 226 SKgDRSQDVKTLKDA-------------VKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADS 292
Cdd:COG4717 235 EL-EAAALEERLKEArlllliaaallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL 313
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697 293 ERLALQALTEKLLRSEESSSRLPEDIRRLEEELQQLKVGAHGSEEgavFKDSKALEELQRQIEGLGARLQYVEDGVYSMQ 372
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE---LEEELQLEELEQEIAALLAEAGVEDEEELRAA 390
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697 373 VASARHTESLESLLSKSQEYEQRLAMLQEHVGNLGSSSDLASTVRSLGETQLALSSDLKELKQSLGELPGTVESLQE-QV 451
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEdGE 470
                       410
                ....*....|..
gi 26326697 452 LSLLSQDQAQAE 463
Cdd:COG4717 471 LAELLQELEELK 482
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
102-448 5.71e-04

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: 42.73  E-value: 5.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    102 LQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRISEVLQKLQNEILKDLSDGIHVVKDARERDFTSLE 181
Cdd:TIGR00606  711 LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTD 790
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    182 NTVEERLTELTKSINDNIAiftdvQKRSQKEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQASMMSRERDIEALKSS 261
Cdd:TIGR00606  791 VTIMERFQMELKDVERKIA-----QQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSK 865
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    262 LQTMEsdvyTEVRELVSLKQEQQAFKQAADSERLALQALTEKLLRSEESSSRLPEDIRRLEEELQQLKVGAHGSEEGAVF 341
Cdd:TIGR00606  866 TNELK----SEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQD 941
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    342 KDSKALEELQRQIEGLGARLQYVEDGVYSMQVASARHTESLESLLSKSQEYEQRlamLQEHVGNLGSSSDLASTVRSLGE 421
Cdd:TIGR00606  942 KVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEK---INEDMRLMRQDIDTQKIQERWLQ 1018
                          330       340       350
                   ....*....|....*....|....*....|
gi 26326697    422 TQLAL---SSDLKELKQSLGELPGTVESLQ 448
Cdd:TIGR00606 1019 DNLTLrkrENELKEVEEELKQHLKEMGQMQ 1048
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
152-329 1.29e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  152 QKLQNEILKDLSDGIHVVKDARERDftsLENTVEERLTELTKSINDNIAIFTDVQKRSQKEINEVKmkvASLEESKGDRs 231
Cdd:COG4913  267 ARERLAELEYLRAALRLWFAQRRLE---LLEAELEELRAELARLEAELERLEARLDALREELDELE---AQIRGNGGDR- 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  232 qdVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERlalQALTEKLLRSEESS 311
Cdd:COG4913  340 --LEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL---EALEEALAEAEAAL 414
                        170
                 ....*....|....*...
gi 26326697  312 SRLPEDIRRLEEELQQLK 329
Cdd:COG4913  415 RDLRRELRELEAEIASLE 432
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
73-515 1.85e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.26  E-value: 1.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697     73 YVHHVLEEVQQVRRGHQDFSRQRDELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELnrisEVLQ 152
Cdd:pfam15921   83 YSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHEL----EAAK 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    153 KLQNEILKDLSDGIhvvkDARERDFTSLENTVEERLTeltksindniaIFTDVQKRSQKEINEV-KMKVASLEESKGDRS 231
Cdd:pfam15921  159 CLKEDMLEDSNTQI----EQLRKMMLSHEGVLQEIRS-----------ILVDFEEASGKKIYEHdSMSTMHFRSLGSAIS 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    232 QDVKTLKDAVKEVQASMMSRERDIEALKSSLQT------------MESDVYTEVRELVSLKQEQQAFKQAADSERLALQA 299
Cdd:pfam15921  224 KILRELDTEISYLKGRIFPVEDQLEALKSESQNkielllqqhqdrIEQLISEHEVEITGLTEKASSARSQANSIQSQLEI 303
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    300 LTEKllrSEESSSRLPEDIRRLEEELQQLKvgAHGSEEGAVFKDSkaLEELQRQIEGLGARLQYVEDGVYSMQVASARHT 379
Cdd:pfam15921  304 IQEQ---ARNQNSMYMRQLSDLESTVSQLR--SELREAKRMYEDK--IEELEKQLVLANSELTEARTERDQFSQESGNLD 376
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697    380 ESLESLLSKSQEYEQRLAMLQEHVgnlgsssdlastvRSLGETQLALSSDLKELKQSLGELPGTVESLQEQVLSLLSQDQ 459
Cdd:pfam15921  377 DQLQKLLADLHKREKELSLEKEQN-------------KRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQ 443
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 26326697    460 AQAEGLPPQdFLDRLSSLDNLKSSVSQVESDLKMLRTAVDSLVAYSVKIETNENNL 515
Cdd:pfam15921  444 GQMERQMAA-IQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTV 498
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
203-406 3.06e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 3.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697 203 TDVQKRSQKEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQE 282
Cdd:COG4942  19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697 283 QQAfKQAADSERLAL-----QALTEKLLRSEESSSRLPEDIRRLEEELQQLKvgahgSEEGAVFKDSKALEELQRQIEGL 357
Cdd:COG4942  99 LEA-QKEELAELLRAlyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR-----EQAEELRADLAELAALRAELEAE 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 26326697 358 GARLQYVEDGV----YSMQVASARHTESLESLLSKSQEYEQRLAMLQEHVGNL 406
Cdd:COG4942 173 RAELEALLAELeeerAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
79-355 3.61e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.20  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697   79 EEVQQVRRGHQDFSR----QRDELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQ-----DLTEKAVKEGESELNRISE 149
Cdd:PRK04778 140 EEVEQLKDLYRELRKsllaNRFSFGPALDELEKQLENLEEEFSQFVELTESGDYVEareilDQLEEELAALEQIMEEIPE 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  150 VLQKLQNEI---LKDLSDGIhvvKDARERDFTSLENTVEERLTELTKSINDNIAIFTDVqkrsqkEINEVKMKVASLEE- 225
Cdd:PRK04778 220 LLKELQTELpdqLQELKAGY---RELVEEGYHLDHLDIEKEIQDLKEQIDENLALLEEL------DLDEAEEKNEEIQEr 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  226 -------------SKGDRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTeVRELvsLKQEQQAFKQA-AD 291
Cdd:PRK04778 291 idqlydilerevkARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELES-VRQL--EKQLESLEKQYdEI 367
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  292 SERLALQALT-----EKLLRSEESSSRLPEDIRRLEEELQQL-KVGAHGSEEGAVFKdsKALEELQRQIE 355
Cdd:PRK04778 368 TERIAEQEIAyselqEELEEILKQLEEIEKEQEKLSEMLQGLrKDELEAREKLERYR--NKLHEIKRYLE 435
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
209-399 9.72e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 9.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  209 SQKEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQ 288
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26326697  289 AADSERLALQALTEKLLRSEESSSRLPEDIRRLEEELQQLKVGAHGSEEgAVFKDSKALEELQRQIEGLGARLQYVEdgv 368
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE-AVEDRREEIEELEEEIEELRERFGDAP--- 404
                        170       180       190
                 ....*....|....*....|....*....|.
gi 26326697  369 ysmqVASARHTESLESLLSKSQEYEQRLAML 399
Cdd:PRK02224 405 ----VDLGNAEDFLEELREERDELREREAEL 431
 
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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