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Conserved domains on  [gi|62526118|ref|NP_780660|]
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cytoskeleton-associated protein 4 [Mus musculus]

Protein Classification

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 ...
128-390 5.74e-08

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 5.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    128 DELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRISEVLQKLQNEIlKDLSDGIHVVKDARER 207
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI-SRLEQQKQILRERLAN 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    208 DFTSLENtVEERLTELTKSINDNIAIFTDVQKRSQ----------KEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQ 277
Cdd:TIGR02168  314 LERQLEE-LEAQLEELESKLDELAEELAELEEKLEelkeelesleAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    278 ---ASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERL--ALQALTEKLLRSEESSSRLPEDIRR 352
Cdd:TIGR02168  393 lqiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELeeELEELQEELERLEEALEELREELEE 472
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 62526118    353 LEEELQQLKvgahgSEEGAVFKDSKALEELQRQIEGLG 390
Cdd:TIGR02168  473 AEQALDAAE-----RELAQLQARLDSLERLQENLEGFS 505
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
257-552 9.21e-07

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: 51.99  E-value: 9.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  257 ESKGDRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERLALQALTEKL 336
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  337 LRSEESSSRLPEDIRRLEEELQQLKVGAHGSEegavfKDSKALEELQRQIEGL-GARLQYVEDGvysmqvasarhtESLE 415
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELK-----KEIEELEEKVKELKELkEKAEEYIKLS------------EFYE 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  416 SLLSKSQEYEQRLAMLQEHVGNLGSS-SDLASTVRSLGEtqlaLSSDLKELKQSLGELPGTVESLQE--QVLSLLSQDQA 492
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERiKELEEKEERLEE----LKKKLKELEKRLEELEERHELYEEakAKKEELERLKK 379
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  493 QAEGLPPQDFLDRLSSLDNLKssvSQVESDLKMLRTAVDSLVAYSVKIETNENNLESAKG 552
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 ...
128-390 5.74e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 5.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    128 DELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRISEVLQKLQNEIlKDLSDGIHVVKDARER 207
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI-SRLEQQKQILRERLAN 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    208 DFTSLENtVEERLTELTKSINDNIAIFTDVQKRSQ----------KEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQ 277
Cdd:TIGR02168  314 LERQLEE-LEAQLEELESKLDELAEELAELEEKLEelkeelesleAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    278 ---ASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERL--ALQALTEKLLRSEESSSRLPEDIRR 352
Cdd:TIGR02168  393 lqiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELeeELEELQEELERLEEALEELREELEE 472
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 62526118    353 LEEELQQLKvgahgSEEGAVFKDSKALEELQRQIEGLG 390
Cdd:TIGR02168  473 AEQALDAAE-----RELAQLQARLDSLERLQENLEGFS 505
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
125-394 4.36e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 4.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 125 RQRDELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRISEVLQKLQNEILKDLSDGIHVVKDA 204
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 205 RErdftslENTVEERLTELTKSINDNIAIFTDVQKRSQKEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQASMMSRE 284
Cdd:COG1196 312 RE------LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 285 RDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERLALQALTEKLLRSEESSSRLPEDIRRLEEELQQLKVgA 364
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE-L 464
                       250       260       270
                ....*....|....*....|....*....|
gi 62526118 365 HGSEEGAVFKDSKALEELQRQIEGLGARLQ 394
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLL 494
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
257-552 9.21e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 9.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  257 ESKGDRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERLALQALTEKL 336
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  337 LRSEESSSRLPEDIRRLEEELQQLKVGAHGSEegavfKDSKALEELQRQIEGL-GARLQYVEDGvysmqvasarhtESLE 415
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELK-----KEIEELEEKVKELKELkEKAEEYIKLS------------EFYE 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  416 SLLSKSQEYEQRLAMLQEHVGNLGSS-SDLASTVRSLGEtqlaLSSDLKELKQSLGELPGTVESLQE--QVLSLLSQDQA 492
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERiKELEEKEERLEE----LKKKLKELEKRLEELEERHELYEEakAKKEELERLKK 379
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  493 QAEGLPPQDFLDRLSSLDNLKssvSQVESDLKMLRTAVDSLVAYSVKIETNENNLESAKG 552
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAK---EEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
275-548 2.09e-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: 50.83  E-value: 2.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    275 EVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERLALQALTEKLLRSEESSSRLPEDIRRLE 354
Cdd:TIGR02168  667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    355 EELQQLkvgahgseEGAVFKDSKALEELQRQIEGLGARLQYVEDGVYSMQVASARHTESLESLLSKSQEYEQRLAMLQEH 434
Cdd:TIGR02168  747 ERIAQL--------SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    435 VGNL-----GSSSDLASTVRSLGETQLA---LSSDLKELKQSLGELPGTVESLQEQVLSLLSQDQAQAEGLPpqdflDRL 506
Cdd:TIGR02168  819 AANLrerleSLERRIAATERRLEDLEEQieeLSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA-----LLR 893
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 62526118    507 SSLDNLKSSVSQVESDLKMLRTAVDSLVAYSVKIETNENNLE 548
Cdd:TIGR02168  894 SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
124-480 2.21e-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: 50.89  E-value: 2.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    124 SRQRDELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRI---------SEVLQKLQNEILKDL 194
Cdd:pfam15921  327 SQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladlhkrekELSLEKEQNKRLWDR 406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    195 SDGIHVVKDARERDFTSlENTVEERLTELTKSINDNIAIFTDVQKRSQKEINEVKMKVASLE--------------ESKG 260
Cdd:pfam15921  407 DTGNSITIDHLRRELDD-RNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTaqlestkemlrkvvEELT 485
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    261 DRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQA-ADSERLALQaLTEKllrs 339
Cdd:pfam15921  486 AKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVqTECEALKLQ-MAEK---- 560
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    340 eessSRLPEDIRRLEEELQQLkVGAHGSEEGAVFKDSKALE-----------ELQRQIEGLGARLQYVEDGVYSMQVASA 408
Cdd:pfam15921  561 ----DKVIEILRQQIENMTQL-VGQHGRTAGAMQVEKAQLEkeindrrlelqEFKILKDKKDAKIRELEARVSDLELEKV 635
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    409 R----HTESLESLLSKSQEYEQRLAMLQEHVGNLGSSSD----LASTVRSLGETQLALSSDLK-ELKQSLGELPGTVESL 479
Cdd:pfam15921  636 KlvnaGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEdyevLKRNFRNKSEEMETTTNKLKmQLKSAQSELEQTRNTL 715

                   .
gi 62526118    480 Q 480
Cdd:pfam15921  716 K 716
PLN02939 PLN02939
transferase, transferring glycosyl groups
120-442 2.38e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 44.12  E-value: 2.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  120 HQDFSRQRDELG-----QGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRI---SEVLQKLQNEIL 191
Cdd:PLN02939  97 HNRASMQRDEAIaaidnEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKIlteKEALQGKINILE 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  192 KDLSDGIHVVKDARERDFTSleNTVEERLTELTKSINDNIAIFTDVQKRSQKEINEVKMKVASLEeskgDRSQDVKTLKD 271
Cdd:PLN02939 177 MRLSETDARIKLAAQEKIHV--EILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLK----DDIQFLKAELI 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  272 AVKEVQASMMSRERDIEALKSSLQTMES---DVYTEVRELVSLKQEqqAFKQAADSERLALQALT---EKLLRSEESSSR 345
Cdd:PLN02939 251 EVAETEERVFKLEKERSLLDASLRELESkfiVAQEDVSKLSPLQYD--CWWEKVENLQDLLDRATnqvEKAALVLDQNQD 328
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  346 LPEDIRRLEEELqqlkvgahgsEEGAVFKDSKALEELQRQieglgaRLQYVEDgvysmqvasaRHTESLESLLSKSQEYE 425
Cdd:PLN02939 329 LRDKVDKLEASL----------KEANVSKFSSYKVELLQQ------KLKLLEE----------RLQASDHEIHSYIQLYQ 382
                        330
                 ....*....|....*..
gi 62526118  426 QRLAMLQEHVGNLGSSS 442
Cdd:PLN02939 383 ESIKEFQDTLSKLKEES 399
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
314-550 7.76e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 7.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 314 EQQAFKQAADSERLALQALTEKLLRSEESSSRLPEDIRRLEEELQQLKvgahgseegavfkdsKALEELQRQIEGLGARL 393
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR---------------LELEELELELEEAQAEE 290
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 394 QYVEDGVYSMQVASARHTESLESLLSKSQEYEQRLAMLQEHVGNLgsSSDLASTVRSLGETQLALSSDLKELKQSLGELP 473
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL--EEELEELEEELEEAEEELEEAEAELAEAEEALL 368
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62526118 474 GTVESLQEQVLSLLSQDQAQAEGLppQDFLDRLSSLDNLKSSVSQVESDLKMLRTAVDSLVAYSVKIETNENNLESA 550
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEAL--RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
128-390 5.74e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 5.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    128 DELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRISEVLQKLQNEIlKDLSDGIHVVKDARER 207
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI-SRLEQQKQILRERLAN 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    208 DFTSLENtVEERLTELTKSINDNIAIFTDVQKRSQ----------KEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQ 277
Cdd:TIGR02168  314 LERQLEE-LEAQLEELESKLDELAEELAELEEKLEelkeelesleAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    278 ---ASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERL--ALQALTEKLLRSEESSSRLPEDIRR 352
Cdd:TIGR02168  393 lqiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELeeELEELQEELERLEEALEELREELEE 472
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 62526118    353 LEEELQQLKvgahgSEEGAVFKDSKALEELQRQIEGLG 390
Cdd:TIGR02168  473 AEQALDAAE-----RELAQLQARLDSLERLQENLEGFS 505
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
109-433 1.90e-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: 54.30  E-value: 1.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    109 VLEEVQQVRRGHQDFSRQRDELGQGLQGVE------QKVQSLQATFGTFESLLRNSQHKQDLTEKavKEGESELNRISEV 182
Cdd:TIGR02169  175 ALEELEEVEENIERLDLIIDEKRQQLERLRrerekaERYQALLKEKREYEGYELLKEKEALERQK--EAIERQLASLEEE 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    183 LQKLQNEIlkdlsdgihvvkDARERDFTSLEntveERLTELTKSINDniaIFTDVQKRSQKEINEVKMKVASLEESKGDR 262
Cdd:TIGR02169  253 LEKLTEEI------------SELEKRLEEIE----QLLEELNKKIKD---LGEEEQLRVKEKIGELEAEIASLERSIAEK 313
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    263 SQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERLALQALTEKLLRSEES 342
Cdd:TIGR02169  314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    343 SSRLPEDI-------RRLEEELQQLkvgahgseegavfkdSKALEELQRQIEGLGARLQYVEDGVYSMQVASARHTESLE 415
Cdd:TIGR02169  394 LEKLKREInelkrelDRLQEELQRL---------------SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
                          330
                   ....*....|....*...
gi 62526118    416 SLLSKSQEYEQRLAMLQE 433
Cdd:TIGR02169  459 QLAADLSKYEQELYDLKE 476
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
111-390 2.80e-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: 2.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    111 EEVQQVRRGHQDFSRQRDELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRISEVLQKLQNEI 190
Cdd:TIGR02168  712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI 791
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    191 LKDLSDgihvvKDARERDFTSLEN----------TVEERLTELTKSINDNIAIFTDVQKRS---QKEINEVKMKVASLEE 257
Cdd:TIGR02168  792 EQLKEE-----LKALREALDELRAeltllneeaaNLRERLESLERRIAATERRLEDLEEQIeelSEDIESLAAEIEELEE 866
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    258 SKGDRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESdvytevrELVSLKQEQQAFKQAADSERLALQALTEKLL 337
Cdd:TIGR02168  867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELES-------KRSELRRELEELREKLAQLELRLEGLEVRID 939
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 62526118    338 RSEEsssRLPEDIRRLEEELQQLKVGAHGSEEGAvfkdSKALEELQRQIEGLG 390
Cdd:TIGR02168  940 NLQE---RLSEEYSLTLEEAEALENKIEDDEEEA----RRRLKRLENKIKELG 985
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
125-394 4.36e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 4.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 125 RQRDELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRISEVLQKLQNEILKDLSDGIHVVKDA 204
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 205 RErdftslENTVEERLTELTKSINDNIAIFTDVQKRSQKEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQASMMSRE 284
Cdd:COG1196 312 RE------LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 285 RDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERLALQALTEKLLRSEESSSRLPEDIRRLEEELQQLKVgA 364
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE-L 464
                       250       260       270
                ....*....|....*....|....*....|
gi 62526118 365 HGSEEGAVFKDSKALEELQRQIEGLGARLQ 394
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLL 494
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
125-364 7.49e-07

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: 51.69  E-value: 7.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 125 RQRDELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRISEVLQKLQNEIlkdlsdgihvvkDA 204
Cdd:COG4942  27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI------------AE 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 205 RERDFTSLENTVEERLTELTK-SINDNIAIFTdvqkrSQKEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQAsmmsR 283
Cdd:COG4942  95 LRAELEAQKEELAELLRALYRlGRQPPLALLL-----SPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA----L 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 284 ERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERLALQALTEKLLRSEESSSRLPEDIRRLEEELQQLKVG 363
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245

                .
gi 62526118 364 A 364
Cdd:COG4942 246 A 246
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
257-552 9.21e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 9.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  257 ESKGDRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERLALQALTEKL 336
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  337 LRSEESSSRLPEDIRRLEEELQQLKVGAHGSEegavfKDSKALEELQRQIEGL-GARLQYVEDGvysmqvasarhtESLE 415
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELK-----KEIEELEEKVKELKELkEKAEEYIKLS------------EFYE 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  416 SLLSKSQEYEQRLAMLQEHVGNLGSS-SDLASTVRSLGEtqlaLSSDLKELKQSLGELPGTVESLQE--QVLSLLSQDQA 492
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERiKELEEKEERLEE----LKKKLKELEKRLEELEERHELYEEakAKKEELERLKK 379
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  493 QAEGLPPQDFLDRLSSLDNLKssvSQVESDLKMLRTAVDSLVAYSVKIETNENNLESAKG 552
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAK---EEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
275-548 2.09e-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: 50.83  E-value: 2.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    275 EVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERLALQALTEKLLRSEESSSRLPEDIRRLE 354
Cdd:TIGR02168  667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    355 EELQQLkvgahgseEGAVFKDSKALEELQRQIEGLGARLQYVEDGVYSMQVASARHTESLESLLSKSQEYEQRLAMLQEH 434
Cdd:TIGR02168  747 ERIAQL--------SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    435 VGNL-----GSSSDLASTVRSLGETQLA---LSSDLKELKQSLGELPGTVESLQEQVLSLLSQDQAQAEGLPpqdflDRL 506
Cdd:TIGR02168  819 AANLrerleSLERRIAATERRLEDLEEQieeLSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA-----LLR 893
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 62526118    507 SSLDNLKSSVSQVESDLKMLRTAVDSLVAYSVKIETNENNLE 548
Cdd:TIGR02168  894 SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
124-480 2.21e-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: 50.89  E-value: 2.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    124 SRQRDELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRI---------SEVLQKLQNEILKDL 194
Cdd:pfam15921  327 SQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladlhkrekELSLEKEQNKRLWDR 406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    195 SDGIHVVKDARERDFTSlENTVEERLTELTKSINDNIAIFTDVQKRSQKEINEVKMKVASLE--------------ESKG 260
Cdd:pfam15921  407 DTGNSITIDHLRRELDD-RNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTaqlestkemlrkvvEELT 485
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    261 DRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQA-ADSERLALQaLTEKllrs 339
Cdd:pfam15921  486 AKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVqTECEALKLQ-MAEK---- 560
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    340 eessSRLPEDIRRLEEELQQLkVGAHGSEEGAVFKDSKALE-----------ELQRQIEGLGARLQYVEDGVYSMQVASA 408
Cdd:pfam15921  561 ----DKVIEILRQQIENMTQL-VGQHGRTAGAMQVEKAQLEkeindrrlelqEFKILKDKKDAKIRELEARVSDLELEKV 635
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    409 R----HTESLESLLSKSQEYEQRLAMLQEHVGNLGSSSD----LASTVRSLGETQLALSSDLK-ELKQSLGELPGTVESL 479
Cdd:pfam15921  636 KlvnaGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEdyevLKRNFRNKSEEMETTTNKLKmQLKSAQSELEQTRNTL 715

                   .
gi 62526118    480 Q 480
Cdd:pfam15921  716 K 716
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
242-533 1.33e-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: 48.13  E-value: 1.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    242 QKEINEVKMKVASLEEskgdrsqDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQA 321
Cdd:TIGR02168  676 RREIEELEEKIEELEE-------KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    322 ADSERLALQALTEKLLRSEESSSRLPEDIRRLEEELQQLKVGAHGSEEgAVFKDSKALEELQRQIEGLGARLQYVEDGVY 401
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE-ELKALREALDELRAELTLLNEEAANLRERLE 827
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    402 SMQVASARHTESLESLlsksqeyEQRLAMLQEHVgnlgssSDLASTVRSLGETQLALSSDLKELKQSLGELPGTVESLQE 481
Cdd:TIGR02168  828 SLERRIAATERRLEDL-------EEQIEELSEDI------ESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 62526118    482 QvLSLLSQDQAQAEglppQDFLDRLSSLDNLKSSVSQVESDLKMLRTAVDSL 533
Cdd:TIGR02168  895 E-LEELSEELRELE----SKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
237-497 2.00e-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: 47.76  E-value: 2.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    237 VQKRSQKEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQ 316
Cdd:TIGR02169  668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    317 AFKQAADSERLALQALTEKLlrseessSRLPEDIRRLEEELQQLKVGAHGSEEGAVFKDSKALEELQRQIEglgARLQYV 396
Cdd:TIGR02169  748 SLEQEIENVKSELKELEARI-------EELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIE---ARLREI 817
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    397 EDGVYSMQVASARHTESLESLLSKSQEYEQRLAMLQEHVGNLgsSSDLASTVRSLGETQLA-----------------LS 459
Cdd:TIGR02169  818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL--NGKKEELEEELEELEAAlrdlesrlgdlkkerdeLE 895
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 62526118    460 SDLKELKQSLGELPGTVESLQEQVLSLLSQDQAQAEGL 497
Cdd:TIGR02169  896 AQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
110-495 4.11e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 4.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 110 LEEVQQVRRGHQDFSRQRDELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLtekavKEGESELNRISEVLQKLQNE 189
Cdd:COG4717  80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL-----EALEAELAELPERLEELEER 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 190 I---------LKDLSDGIHVVKDARERDFTSLENTVEERLTELTKSIND---NIAIFTDVQKRSQKEINEVKMKVASLEE 257
Cdd:COG4717 155 LeelreleeeLEELEAELAELQEELEELLEQLSLATEEELQDLAEELEElqqRLAELEEELEEAQEELEELEEELEQLEN 234
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 258 SKgDRSQDVKTLKDA-------------VKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADS 324
Cdd:COG4717 235 EL-EAAALEERLKEArlllliaaallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL 313
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 325 ERLALQALTEKLLRSEESSSRLPEDIRRLEEELQQLKVGAHGSEEgavFKDSKALEELQRQIEGLGARLQYVEDGVYSMQ 404
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE---LEEELQLEELEQEIAALLAEAGVEDEEELRAA 390
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 405 VASARHTESLESLLSKSQEYEQRLAMLQEHVGNLGSSSDLASTVRSLGETQLALSSDLKELKQSLGELPGTVESLQE-QV 483
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEdGE 470
                       410
                ....*....|..
gi 62526118 484 LSLLSQDQAQAE 495
Cdd:COG4717 471 LAELLQELEELK 482
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
134-497 1.79e-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: 44.65  E-value: 1.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    134 LQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRISEVLQKLQNEILKDLSDGIHVVKDARERDFTSLE 213
Cdd:TIGR00606  711 LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTD 790
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    214 NTVEERLTELTKSINDNIAiftdvQKRSQKEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQASMMSRERDIEALKSS 293
Cdd:TIGR00606  791 VTIMERFQMELKDVERKIA-----QQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSK 865
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    294 LQTMEsdvyTEVRELVSLKQEQQAFKQAADSERLALQALTEKLLRSEESSSRLPEDIRRLEEELQQLKVGAHGSEEGAVF 373
Cdd:TIGR00606  866 TNELK----SEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQD 941
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    374 KDSKALEELQRQIEGLGARLQYVEDGVYSMQVASARHTESLESLLSKSQEYEQRlamLQEHVGNLGSSSDLASTVRSLGE 453
Cdd:TIGR00606  942 KVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEK---INEDMRLMRQDIDTQKIQERWLQ 1018
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 62526118    454 TQLAL---SSDLKELKQSLGELPGTVEslQEQVLSLLSQDQAQAEGL 497
Cdd:TIGR00606 1019 DNLTLrkrENELKEVEEELKQHLKEMG--QMQVLQMKQEHQKLEENI 1063
PLN02939 PLN02939
transferase, transferring glycosyl groups
120-442 2.38e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 44.12  E-value: 2.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  120 HQDFSRQRDELG-----QGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELNRI---SEVLQKLQNEIL 191
Cdd:PLN02939  97 HNRASMQRDEAIaaidnEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKIlteKEALQGKINILE 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  192 KDLSDGIHVVKDARERDFTSleNTVEERLTELTKSINDNIAIFTDVQKRSQKEINEVKMKVASLEeskgDRSQDVKTLKD 271
Cdd:PLN02939 177 MRLSETDARIKLAAQEKIHV--EILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLK----DDIQFLKAELI 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  272 AVKEVQASMMSRERDIEALKSSLQTMES---DVYTEVRELVSLKQEqqAFKQAADSERLALQALT---EKLLRSEESSSR 345
Cdd:PLN02939 251 EVAETEERVFKLEKERSLLDASLRELESkfiVAQEDVSKLSPLQYD--CWWEKVENLQDLLDRATnqvEKAALVLDQNQD 328
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  346 LPEDIRRLEEELqqlkvgahgsEEGAVFKDSKALEELQRQieglgaRLQYVEDgvysmqvasaRHTESLESLLSKSQEYE 425
Cdd:PLN02939 329 LRDKVDKLEASL----------KEANVSKFSSYKVELLQQ------KLKLLEE----------RLQASDHEIHSYIQLYQ 382
                        330
                 ....*....|....*..
gi 62526118  426 QRLAMLQEHVGNLGSSS 442
Cdd:PLN02939 383 ESIKEFQDTLSKLKEES 399
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
105-547 4.05e-04

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: 43.57  E-value: 4.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    105 YVHHVLEEVQQVRRGHQDFSRQRDELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQDLTEKAVKEGESELnrisEVLQ 184
Cdd:pfam15921   83 YSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHEL----EAAK 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    185 KLQNEILKDLSDGIhvvkDARERDFTSLENTVEERLTeltksindniaIFTDVQKRSQKEINEV-KMKVASLEESKGDRS 263
Cdd:pfam15921  159 CLKEDMLEDSNTQI----EQLRKMMLSHEGVLQEIRS-----------ILVDFEEASGKKIYEHdSMSTMHFRSLGSAIS 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    264 QDVKTLKDAVKEVQASMMSRERDIEALKSSLQT------------MESDVYTEVRELVSLKQEQQAFKQAADSERLALQA 331
Cdd:pfam15921  224 KILRELDTEISYLKGRIFPVEDQLEALKSESQNkielllqqhqdrIEQLISEHEVEITGLTEKASSARSQANSIQSQLEI 303
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    332 LTEKllrSEESSSRLPEDIRRLEEELQQLKvgAHGSEEGAVFKDSkaLEELQRQIEGLGARLQYVEDGVYSMQVASARHT 411
Cdd:pfam15921  304 IQEQ---ARNQNSMYMRQLSDLESTVSQLR--SELREAKRMYEDK--IEELEKQLVLANSELTEARTERDQFSQESGNLD 376
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    412 ESLESLLSKSQEYEQRLAMLQEHVgnlgsssdlastvRSLGETQLALSSDLKELKQSLGELPGTVESLQEQVLSLLSQDQ 491
Cdd:pfam15921  377 DQLQKLLADLHKREKELSLEKEQN-------------KRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQ 443
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 62526118    492 AQAEGLPPQdFLDRLSSLDNLKSSVSQVESDLKMLRTAVDSLVAYSVKIETNENNL 547
Cdd:pfam15921  444 GQMERQMAA-IQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTV 498
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
111-387 4.63e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 42.90  E-value: 4.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  111 EEVQQVRRGHQDFSR----QRDELGQGLQGVEQKVQSLQATFGTFESLLRNSQHKQ-----DLTEKAVKEGESELNRISE 181
Cdd:PRK04778 140 EEVEQLKDLYRELRKsllaNRFSFGPALDELEKQLENLEEEFSQFVELTESGDYVEareilDQLEEELAALEQIMEEIPE 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  182 VLQKLQNEI---LKDLSDGIhvvKDARERDFTSLENTVEERLTELTKSINDNIAIFTDVqkrsqkEINEVKMKVASLEE- 257
Cdd:PRK04778 220 LLKELQTELpdqLQELKAGY---RELVEEGYHLDHLDIEKEIQDLKEQIDENLALLEEL------DLDEAEEKNEEIQEr 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  258 -------------SKGDRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTeVRELvsLKQEQQAFKQA-AD 323
Cdd:PRK04778 291 idqlydilerevkARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELES-VRQL--EKQLESLEKQYdEI 367
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  324 SERLALQALT-----EKLLRSEESSSRLPEDIRRLEEELQQL-KVGAHGSEEGAVFKdsKALEELQRQIE 387
Cdd:PRK04778 368 TERIAEQEIAyselqEELEEILKQLEEIEKEQEKLSEMLQGLrKDELEAREKLERYR--NKLHEIKRYLE 435
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
184-361 7.38e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 7.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  184 QKLQNEILKDLSDGIHVVKDARERDftsLENTVEERLTELTKSINDNIAIFTDVQKRSQKEINEVKmkvASLEESKGDRs 263
Cdd:COG4913  267 ARERLAELEYLRAALRLWFAQRRLE---LLEAELEELRAELARLEAELERLEARLDALREELDELE---AQIRGNGGDR- 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  264 qdVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQAADSERlalQALTEKLLRSEESS 343
Cdd:COG4913  340 --LEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL---EALEEALAEAEAAL 414
                        170
                 ....*....|....*...
gi 62526118  344 SRLPEDIRRLEEELQQLK 361
Cdd:COG4913  415 RDLRRELRELEAEIASLE 432
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
235-438 1.38e-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: 41.29  E-value: 1.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 235 TDVQKRSQKEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQE 314
Cdd:COG4942  19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 315 QQAfKQAADSERLAL-----QALTEKLLRSEESSSRLPEDIRRLEEELQQLKvgahgSEEGAVFKDSKALEELQRQIEGL 389
Cdd:COG4942  99 LEA-QKEELAELLRAlyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR-----EQAEELRADLAELAALRAELEAE 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 62526118 390 GARLQYVEDGV----YSMQVASARHTESLESLLSKSQEYEQRLAMLQEHVGNL 438
Cdd:COG4942 173 RAELEALLAELeeerAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
152-549 1.38e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  152 ESLLRNSQHKQDLTEKAVKEGESELNRISEVLQKLQNEiLKDLsDGIHVVKDARERDFTSLENTV---EERLTELTKSIN 228
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKE-VKEL-EELKEEIEELEKELESLEGSKrklEEKIRELEERIE 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  229 DniaiftdvqkrSQKEINEVKMKVASLEESKGDRSQDVKtlkdaVKEVQASMMSRERDIEALKSSLQTMESDVYTEVREL 308
Cdd:PRK03918 270 E-----------LKKEIEELEEKVKELKELKEKAEEYIK-----LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  309 VSLKQEQQAFKQaadserlALQALTEKLLRSEEsSSRLPEDIRRLEEELQQLKVGAHGSEEGAVFKD----SKALEELQR 384
Cdd:PRK03918 334 EEKEERLEELKK-------KLKELEKRLEELEE-RHELYEEAKAKKEELERLKKRLTGLTPEKLEKEleelEKAKEEIEE 405
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  385 QIEGLGARLQYVEDGVYSMQVA--------------------------SARHTESLESLLSKSQEYEQRLAMLQEHVGNL 438
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAieelkkakgkcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELREL 485
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  439 gsssdlastvrslgETQLALSSDLKELKQSLGELPGTVESLQEQVLSLLSQDQAQAEGLppqdfldrLSSLDNLKSSVSQ 518
Cdd:PRK03918 486 --------------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKL--------KEKLIKLKGEIKS 543
                        410       420       430
                 ....*....|....*....|....*....|.
gi 62526118  519 VESDLKMLRTAVDSLVAYSVKIETNENNLES 549
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAE 574
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
212-458 1.96e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 1.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 212 LENTVEERLTELTKSINDNIAIFTDVQKRSQKEINEVKMKVASLEEskgdrsqdvktLKDAVKEVQASMMSRERDIEALK 291
Cdd:COG4717  47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAE-----------LQEELEELEEELEELEAELEELR 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 292 SSLQTMEsdvytEVRELVSLKQEqqafKQAADSERLALQALTEKLLRSEESSSRLPEDIRRLEEELQQLKVGAHGSEEGA 371
Cdd:COG4717 116 EELEKLE-----KLLQLLPLYQE----LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 372 VFKDSKALEELQRQIEGLGARLQYVEDGVYSMQVASARHTESLESLLSK--SQEYEQRLAMLQEHVGNLGSSSDLASTVR 449
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEleAAALEERLKEARLLLLIAAALLALLGLGG 266

                ....*....
gi 62526118 450 SLGETQLAL 458
Cdd:COG4717 267 SLLSLILTI 275
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
129-433 3.66e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.21  E-value: 3.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    129 ELGQGLQGVEQKVQSLQATFGTFESLLRNSQHkqdlTEKAVKEGEselnRISEVLQKLQNEILKDLsdgihvvkdarERD 208
Cdd:pfam12128  231 QAIAGIMKIRPEFTKLQQEFNTLESAELRLSH----LHFGYKSDE----TLIASRQEERQETSAEL-----------NQL 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    209 FTSLENTVEERLTELTKSINDNIAIFTdvQKRSQKEINEVKMKV---ASLEESKGDRSQ--DVKTLKDAVKEVQASMMSR 283
Cdd:pfam12128  292 LRTLDDQWKEKRDELNGELSAADAAVA--KDRSELEALEDQHGAfldADIETAAADQEQlpSWQSELENLEERLKALTGK 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    284 ERDIEAlksSLQTMESDVYTE-VRELVSLKQEQQAFKQAADSERLALQALTEKL---LRS--EESSSRLPEDIRRLEEEL 357
Cdd:pfam12128  370 HQDVTA---KYNRRRSKIKEQnNRDIAGIKDKLAKIREARDRQLAVAEDDLQALeseLREqlEAGKLEFNEEEYRLKSRL 446
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62526118    358 QQLKV---GAHGSEEGAVFKDSKAlEELQRQIEGLGARLQYVEDGVYSMQVASARHTESLESLLSKSQEYEQRLAMLQE 433
Cdd:pfam12128  447 GELKLrlnQATATPELLLQLENFD-ERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE 524
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
166-398 5.39e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 5.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  166 EKAVKEGESELNRISEVLQKLQNEI-----LKDLSDGIHVVKDARErDFTSL----ENTVEE---RLTELTKSINDNIAI 233
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLeraedLVEAEDRIERLEERRE-DLEELiaerRETIEEkreRAEELRERAAELEAE 552
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  234 FTDVQKRSQK---EINEVKMKVASLEESKGDRSQDVKTLkDAVKEVQASMMSRERDIEALKSSLQTMeSDVYTEVRELVS 310
Cdd:PRK02224 553 AEEKREAAAEaeeEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREAL-AELNDERRERLA 630
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  311 LKQEQQAfKQAADSERLALQALTEKLLRSEESSSRLPEDIRRLEEELQQLKvgahgSEEGAVFKDSKALEELQRQIEGLG 390
Cdd:PRK02224 631 EKRERKR-ELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQ-----AEIGAVENELEELEELRERREALE 704

                 ....*...
gi 62526118  391 ARLQYVED 398
Cdd:PRK02224 705 NRVEALEA 712
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
241-431 5.57e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 5.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  241 SQKEINEVKMKVASLEESKGDRSQDVKTLKDAVKEVQASMMSRERDIEALKSSLQTMESDVYTEVRELVSLKQEQQAFKQ 320
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118  321 AADSERLALQALTEKLLRSEESSSRLPEDIRRLEEELQQLKVGAHGSEEgAVFKDSKALEELQRQIEGLGARLQYVEdgv 400
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE-AVEDRREEIEELEEEIEELRERFGDAP--- 404
                        170       180       190
                 ....*....|....*....|....*....|.
gi 62526118  401 ysmqVASARHTESLESLLSKSQEYEQRLAML 431
Cdd:PRK02224 405 ----VDLGNAEDFLEELREERDELREREAEL 431
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
125-310 6.13e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 39.65  E-value: 6.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    125 RQRDELGQGLQGVEQKVQSLQATFGTFESLLRNS-------------QHKQDLTEKAVKEGESELNRISEVLQKLQneiL 191
Cdd:TIGR01612 1019 HQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSiyniideiekeigKNIELLNKEILEEAEINITNFNEIKEKLK---H 1095
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118    192 KDLSDgihVVKDARERdFTSLENTVEERLTELTKSINDNIAIFTDVQKRSQKEINEVKMKVASLEESKgdrsqDVKTLKD 271
Cdd:TIGR01612 1096 YNFDD---FGKEENIK-YADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVA-----DKAISND 1166
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 62526118    272 AVKEVqasmmsrERDIEALKSSLQTmESDVYTEVRELVS 310
Cdd:TIGR01612 1167 DPEEI-------EKKIENIVTKIDK-KKNIYDEIKKLLN 1197
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
314-550 7.76e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 7.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 314 EQQAFKQAADSERLALQALTEKLLRSEESSSRLPEDIRRLEEELQQLKvgahgseegavfkdsKALEELQRQIEGLGARL 393
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR---------------LELEELELELEEAQAEE 290
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526118 394 QYVEDGVYSMQVASARHTESLESLLSKSQEYEQRLAMLQEHVGNLgsSSDLASTVRSLGETQLALSSDLKELKQSLGELP 473
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL--EEELEELEEELEEAEEELEEAEAELAEAEEALL 368
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62526118 474 GTVESLQEQVLSLLSQDQAQAEGLppQDFLDRLSSLDNLKSSVSQVESDLKMLRTAVDSLVAYSVKIETNENNLESA 550
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEAL--RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
 
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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