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Conserved domains on  [gi|289547556|ref|NP_689618|]
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junction-mediating and -regulatory protein [Homo sapiens]

Protein Classification

WHAMM-JMY_N and JMY domain-containing protein( domain architecture ID 13869955)

protein containing domains WHAMM-JMY_N, JMY, and SMC_prok_B

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
JMY pfam15871
Junction-mediating and -regulatory protein; JMY, Junction-mediating and -regulatory protein is ...
229-582 0e+00

Junction-mediating and -regulatory protein; JMY, Junction-mediating and -regulatory protein is also a WASP homolog-associated protein with actin, membranes and microtubules. This middle region is the coiled-coil region that putatively binds microtubules to the scaffold. This ability to interact with microtubules plays a role in membrane tubulation.


:

Pssm-ID: 464915  Cd Length: 357  Bit Score: 556.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556  229 WAGLFSFQDLRAVHQQLCSVNSQLEPCLPVFPE-EPSGMWTVLFGGAPEMTEQEIDTLCYQLQVYLGHGLDTCGWKILSQ 307
Cdd:pfam15871   1 WAGLFSFQDLRAIHRQLCAVHPALEPCFPALPEgESEGLWTLLFPGRPEPGEAELQELCRQLEEYLGYALDICGRKILLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556  308 VLFT-ETDDPEEYYESLSELRQKGYEEVLQRARKRIQELLDKHKNTESMVELLDLYQMEDEAYSSLAEATTELYQYLLQP 386
Cdd:pfam15871  81 VLFAaDGDDAEEYFENLSELRKKGYEEVLQRAKERLRQVLQQHKNADTMVELMKVYQEEDEAYQELVTAATEFYQYLLQP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556  387 FRDMRELAMLRRQQIKISMENDYLGPRRIESLQKEDADWQRKAHMAVLSIQDLTVKYFEITAKAQKAVYDRMRADQKKFG 466
Cdd:pfam15871 161 FRDMRELATLRKLEIKKSLENDDLGPKRVEALQKEAEEWQRRAEEAVVSIQDITVNYFKETVKALSGMQKQMEQDQKRFG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556  467 KASWAAAAERMEKLQYAVSKETLQMMRAKEICLEQRKHALKEEMQSLRGGTEAIARLDQLEADYYDLQLQLYEVQFEILK 546
Cdd:pfam15871 241 KAAWAAAAPRLEKLKYMLAKETLQLMRAKELCLEQKRAEIRKEMESLEEGEKAVAVVDELEIQYYEAQLELYEVQLEILK 320
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 289547556  547 CEELLLTAQLESIKRLISEKRDEVVYYDTYESMEAM 582
Cdd:pfam15871 321 NEELLLTAQLDSLRRQIKEKQDEVVYYDTCESPEEL 356
WHAMM-JMY_N pfam15920
N-terminal of Junction-mediating and WASP homolog-associated; WHAMM-JMY_N is the very ...
6-54 3.95e-24

N-terminal of Junction-mediating and WASP homolog-associated; WHAMM-JMY_N is the very N-terminus of WHAMM and JMY proteins. The function of this conserved region is not known; there are two highly conserved tryptophan residues.


:

Pssm-ID: 464942  Cd Length: 49  Bit Score: 95.97  E-value: 3.95e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 289547556    6 EETLEsDWVAVRPHVFDEREKHKFVFIVAWNEIEGKFAITCHNRTAQRQ 54
Cdd:pfam15920   2 PDSLE-GWVAVKENLFEEPEKHKLRFIVAWNEIEGKFAVTCHNRTLQRQ 49
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
446-720 8.08e-04

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 8.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556   446 ITAKAQKAV-YDRMRADQKKFGKASWAAAAERMEKlQYAVSKETLQMMRAKEICLEQRKHALKEEMQSLRGG-TEAIARL 523
Cdd:TIGR02168  205 LERQAEKAErYKELKAELRELELALLVLRLEELRE-ELEELQEELKEAEEELEELTAELQELEEKLEELRLEvSELEEEI 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556   524 DQLEADYYDL---------QLQLYEVQFEILKCEELLLTAQLESIKRLISEKRDEVVYYDT--------YESMEAMLEK- 585
Cdd:TIGR02168  284 EELQKELYALaneisrleqQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEkleelkeeLESLEAELEEl 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556   586 ----EEMAASAYLQREELQKLQQKARQLEARRGRVSAKKSYLRNKKEIcIAKHNEKIQQRTRIEDEYRTHHTVQLKREKL 661
Cdd:TIGR02168  364 eaelEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELKELQAEL 442
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556   662 hDEEERKSAWVSQERQRTLDRLRTFKQRY-PGQVILKSTRLRLAHARRKGAASPVLQEDH 720
Cdd:TIGR02168  443 -EELEEELEELQEELERLEEALEELREELeEAEQALDAAERELAQLQARLDSLERLQENL 501
 
Name Accession Description Interval E-value
JMY pfam15871
Junction-mediating and -regulatory protein; JMY, Junction-mediating and -regulatory protein is ...
229-582 0e+00

Junction-mediating and -regulatory protein; JMY, Junction-mediating and -regulatory protein is also a WASP homolog-associated protein with actin, membranes and microtubules. This middle region is the coiled-coil region that putatively binds microtubules to the scaffold. This ability to interact with microtubules plays a role in membrane tubulation.


Pssm-ID: 464915  Cd Length: 357  Bit Score: 556.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556  229 WAGLFSFQDLRAVHQQLCSVNSQLEPCLPVFPE-EPSGMWTVLFGGAPEMTEQEIDTLCYQLQVYLGHGLDTCGWKILSQ 307
Cdd:pfam15871   1 WAGLFSFQDLRAIHRQLCAVHPALEPCFPALPEgESEGLWTLLFPGRPEPGEAELQELCRQLEEYLGYALDICGRKILLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556  308 VLFT-ETDDPEEYYESLSELRQKGYEEVLQRARKRIQELLDKHKNTESMVELLDLYQMEDEAYSSLAEATTELYQYLLQP 386
Cdd:pfam15871  81 VLFAaDGDDAEEYFENLSELRKKGYEEVLQRAKERLRQVLQQHKNADTMVELMKVYQEEDEAYQELVTAATEFYQYLLQP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556  387 FRDMRELAMLRRQQIKISMENDYLGPRRIESLQKEDADWQRKAHMAVLSIQDLTVKYFEITAKAQKAVYDRMRADQKKFG 466
Cdd:pfam15871 161 FRDMRELATLRKLEIKKSLENDDLGPKRVEALQKEAEEWQRRAEEAVVSIQDITVNYFKETVKALSGMQKQMEQDQKRFG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556  467 KASWAAAAERMEKLQYAVSKETLQMMRAKEICLEQRKHALKEEMQSLRGGTEAIARLDQLEADYYDLQLQLYEVQFEILK 546
Cdd:pfam15871 241 KAAWAAAAPRLEKLKYMLAKETLQLMRAKELCLEQKRAEIRKEMESLEEGEKAVAVVDELEIQYYEAQLELYEVQLEILK 320
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 289547556  547 CEELLLTAQLESIKRLISEKRDEVVYYDTYESMEAM 582
Cdd:pfam15871 321 NEELLLTAQLDSLRRQIKEKQDEVVYYDTCESPEEL 356
WHAMM-JMY_N pfam15920
N-terminal of Junction-mediating and WASP homolog-associated; WHAMM-JMY_N is the very ...
6-54 3.95e-24

N-terminal of Junction-mediating and WASP homolog-associated; WHAMM-JMY_N is the very N-terminus of WHAMM and JMY proteins. The function of this conserved region is not known; there are two highly conserved tryptophan residues.


Pssm-ID: 464942  Cd Length: 49  Bit Score: 95.97  E-value: 3.95e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 289547556    6 EETLEsDWVAVRPHVFDEREKHKFVFIVAWNEIEGKFAITCHNRTAQRQ 54
Cdd:pfam15920   2 PDSLE-GWVAVKENLFEEPEKHKLRFIVAWNEIEGKFAVTCHNRTLQRQ 49
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
302-690 1.94e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556 302 WKILSQVLFTETDDPEEYYESLSELRQKgyEEVLQRARKRIQELLDKHKNTESMVELLDLYQMEDEAYSSLAEATTELYQ 381
Cdd:COG4717   73 LKELEEELKEAEEKEEEYAELQEELEEL--EEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556 382 YL--LQPFRDMR--------ELAMLRRQQIKISMENDYLGPRRIESLQKEDADWQRKAHMAVLSIQDLTVKYFEITAKAQ 451
Cdd:COG4717  151 LEerLEELRELEeeleeleaELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556 452 KAVYDRMRADQKK---FGKASWAAAAERMEKLQYAVSKETLQMMRAKEICLEQRKHAL--------KEEMQSLRGGTEAI 520
Cdd:COG4717  231 QLENELEAAALEErlkEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALlflllareKASLGKEAEELQAL 310
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556 521 ARLDQLEADYYDLQLQLYEVQFEILKCEELLLTAQLESIKRLISEKRDE------VVYYDTYESM--EAMLEKEEMAASA 592
Cdd:COG4717  311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELeeelqlEELEQEIAALlaEAGVEDEEELRAA 390
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556 593 YLQREELQKLQQKARQLEARRGRV--SAKKSYLRNKKEICIAKHNEKIQQRTRIEDEYRTHHTV--QLKREKLHDEEERK 668
Cdd:COG4717  391 LEQAEEYQELKEELEELEEQLEELlgELEELLEALDEEELEEELEELEEELEELEEELEELREElaELEAELEQLEEDGE 470
                        410       420
                 ....*....|....*....|..
gi 289547556 669 SAWVSQERQRTLDRLRTFKQRY 690
Cdd:COG4717  471 LAELLQELEELKAELRELAEEW 492
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
446-720 8.08e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 8.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556   446 ITAKAQKAV-YDRMRADQKKFGKASWAAAAERMEKlQYAVSKETLQMMRAKEICLEQRKHALKEEMQSLRGG-TEAIARL 523
Cdd:TIGR02168  205 LERQAEKAErYKELKAELRELELALLVLRLEELRE-ELEELQEELKEAEEELEELTAELQELEEKLEELRLEvSELEEEI 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556   524 DQLEADYYDL---------QLQLYEVQFEILKCEELLLTAQLESIKRLISEKRDEVVYYDT--------YESMEAMLEK- 585
Cdd:TIGR02168  284 EELQKELYALaneisrleqQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEkleelkeeLESLEAELEEl 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556   586 ----EEMAASAYLQREELQKLQQKARQLEARRGRVSAKKSYLRNKKEIcIAKHNEKIQQRTRIEDEYRTHHTVQLKREKL 661
Cdd:TIGR02168  364 eaelEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELKELQAEL 442
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556   662 hDEEERKSAWVSQERQRTLDRLRTFKQRY-PGQVILKSTRLRLAHARRKGAASPVLQEDH 720
Cdd:TIGR02168  443 -EELEEELEELQEELERLEEALEELREELeEAEQALDAAERELAQLQARLDSLERLQENL 501
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
317-690 1.94e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556 317 EEYYESLSELRQ---------KGYEEVLQRARKRIQELLDKHKNTESMVELLDLYQMEDEAYSSLAEattELYQYLLQPF 387
Cdd:PRK03918 234 EELKEEIEELEKeleslegskRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSE---FYEEYLDELR 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556 388 RDMRELAMLRRQ--QIKISMENDYLGPRRIESLQKEDADWQRKahmavLSIQDLTVKYFEiTAKAQKAVYDRMRADQKKF 465
Cdd:PRK03918 311 EIEKRLSRLEEEinGIEERIKELEEKEERLEELKKKLKELEKR-----LEELEERHELYE-EAKAKKEELERLKKRLTGL 384
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556 466 GKASWAAAAERMEKLQYAVSKEtLQMMRAKEICLEQRKHALKEEMQSLRG--GTEAIARLDQLEADYYDL----QLQLYE 539
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEE-ISKITARIGELKKEIKELKKAIEELKKakGKCPVCGRELTEEHRKELleeyTAELKR 463
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556 540 VQFEILKCEELL--LTAQLESIKRLISEKRDEVVYYDTYESMEAMLEKeemaasayLQREELQKLQQKARQLEARRGRVS 617
Cdd:PRK03918 464 IEKELKEIEEKErkLRKELRELEKVLKKESELIKLKELAEQLKELEEK--------LKKYNLEELEKKAEEYEKLKEKLI 535
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 289547556 618 AKKSYLRNKKEIcIAKHNEKIQQRTRIEDEYrthHTVQLKREKLHDEEERKSAWVSQERQRTLDRLRTFKQRY 690
Cdd:PRK03918 536 KLKGEIKSLKKE-LEKLEELKKKLAELEKKL---DELEEELAELLKELEELGFESVEELEERLKELEPFYNEY 604
 
Name Accession Description Interval E-value
JMY pfam15871
Junction-mediating and -regulatory protein; JMY, Junction-mediating and -regulatory protein is ...
229-582 0e+00

Junction-mediating and -regulatory protein; JMY, Junction-mediating and -regulatory protein is also a WASP homolog-associated protein with actin, membranes and microtubules. This middle region is the coiled-coil region that putatively binds microtubules to the scaffold. This ability to interact with microtubules plays a role in membrane tubulation.


Pssm-ID: 464915  Cd Length: 357  Bit Score: 556.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556  229 WAGLFSFQDLRAVHQQLCSVNSQLEPCLPVFPE-EPSGMWTVLFGGAPEMTEQEIDTLCYQLQVYLGHGLDTCGWKILSQ 307
Cdd:pfam15871   1 WAGLFSFQDLRAIHRQLCAVHPALEPCFPALPEgESEGLWTLLFPGRPEPGEAELQELCRQLEEYLGYALDICGRKILLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556  308 VLFT-ETDDPEEYYESLSELRQKGYEEVLQRARKRIQELLDKHKNTESMVELLDLYQMEDEAYSSLAEATTELYQYLLQP 386
Cdd:pfam15871  81 VLFAaDGDDAEEYFENLSELRKKGYEEVLQRAKERLRQVLQQHKNADTMVELMKVYQEEDEAYQELVTAATEFYQYLLQP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556  387 FRDMRELAMLRRQQIKISMENDYLGPRRIESLQKEDADWQRKAHMAVLSIQDLTVKYFEITAKAQKAVYDRMRADQKKFG 466
Cdd:pfam15871 161 FRDMRELATLRKLEIKKSLENDDLGPKRVEALQKEAEEWQRRAEEAVVSIQDITVNYFKETVKALSGMQKQMEQDQKRFG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556  467 KASWAAAAERMEKLQYAVSKETLQMMRAKEICLEQRKHALKEEMQSLRGGTEAIARLDQLEADYYDLQLQLYEVQFEILK 546
Cdd:pfam15871 241 KAAWAAAAPRLEKLKYMLAKETLQLMRAKELCLEQKRAEIRKEMESLEEGEKAVAVVDELEIQYYEAQLELYEVQLEILK 320
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 289547556  547 CEELLLTAQLESIKRLISEKRDEVVYYDTYESMEAM 582
Cdd:pfam15871 321 NEELLLTAQLDSLRRQIKEKQDEVVYYDTCESPEEL 356
WHAMM-JMY_N pfam15920
N-terminal of Junction-mediating and WASP homolog-associated; WHAMM-JMY_N is the very ...
6-54 3.95e-24

N-terminal of Junction-mediating and WASP homolog-associated; WHAMM-JMY_N is the very N-terminus of WHAMM and JMY proteins. The function of this conserved region is not known; there are two highly conserved tryptophan residues.


Pssm-ID: 464942  Cd Length: 49  Bit Score: 95.97  E-value: 3.95e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 289547556    6 EETLEsDWVAVRPHVFDEREKHKFVFIVAWNEIEGKFAITCHNRTAQRQ 54
Cdd:pfam15920   2 PDSLE-GWVAVKENLFEEPEKHKLRFIVAWNEIEGKFAVTCHNRTLQRQ 49
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
302-690 1.94e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556 302 WKILSQVLFTETDDPEEYYESLSELRQKgyEEVLQRARKRIQELLDKHKNTESMVELLDLYQMEDEAYSSLAEATTELYQ 381
Cdd:COG4717   73 LKELEEELKEAEEKEEEYAELQEELEEL--EEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556 382 YL--LQPFRDMR--------ELAMLRRQQIKISMENDYLGPRRIESLQKEDADWQRKAHMAVLSIQDLTVKYFEITAKAQ 451
Cdd:COG4717  151 LEerLEELRELEeeleeleaELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556 452 KAVYDRMRADQKK---FGKASWAAAAERMEKLQYAVSKETLQMMRAKEICLEQRKHAL--------KEEMQSLRGGTEAI 520
Cdd:COG4717  231 QLENELEAAALEErlkEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALlflllareKASLGKEAEELQAL 310
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556 521 ARLDQLEADYYDLQLQLYEVQFEILKCEELLLTAQLESIKRLISEKRDE------VVYYDTYESM--EAMLEKEEMAASA 592
Cdd:COG4717  311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELeeelqlEELEQEIAALlaEAGVEDEEELRAA 390
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556 593 YLQREELQKLQQKARQLEARRGRV--SAKKSYLRNKKEICIAKHNEKIQQRTRIEDEYRTHHTV--QLKREKLHDEEERK 668
Cdd:COG4717  391 LEQAEEYQELKEELEELEEQLEELlgELEELLEALDEEELEEELEELEEELEELEEELEELREElaELEAELEQLEEDGE 470
                        410       420
                 ....*....|....*....|..
gi 289547556 669 SAWVSQERQRTLDRLRTFKQRY 690
Cdd:COG4717  471 LAELLQELEELKAELRELAEEW 492
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
446-720 8.08e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 8.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556   446 ITAKAQKAV-YDRMRADQKKFGKASWAAAAERMEKlQYAVSKETLQMMRAKEICLEQRKHALKEEMQSLRGG-TEAIARL 523
Cdd:TIGR02168  205 LERQAEKAErYKELKAELRELELALLVLRLEELRE-ELEELQEELKEAEEELEELTAELQELEEKLEELRLEvSELEEEI 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556   524 DQLEADYYDL---------QLQLYEVQFEILKCEELLLTAQLESIKRLISEKRDEVVYYDT--------YESMEAMLEK- 585
Cdd:TIGR02168  284 EELQKELYALaneisrleqQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEkleelkeeLESLEAELEEl 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556   586 ----EEMAASAYLQREELQKLQQKARQLEARRGRVSAKKSYLRNKKEIcIAKHNEKIQQRTRIEDEYRTHHTVQLKREKL 661
Cdd:TIGR02168  364 eaelEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELKELQAEL 442
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556   662 hDEEERKSAWVSQERQRTLDRLRTFKQRY-PGQVILKSTRLRLAHARRKGAASPVLQEDH 720
Cdd:TIGR02168  443 -EELEEELEELQEELERLEEALEELREELeEAEQALDAAERELAQLQARLDSLERLQENL 501
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
317-690 1.94e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556 317 EEYYESLSELRQ---------KGYEEVLQRARKRIQELLDKHKNTESMVELLDLYQMEDEAYSSLAEattELYQYLLQPF 387
Cdd:PRK03918 234 EELKEEIEELEKeleslegskRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSE---FYEEYLDELR 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556 388 RDMRELAMLRRQ--QIKISMENDYLGPRRIESLQKEDADWQRKahmavLSIQDLTVKYFEiTAKAQKAVYDRMRADQKKF 465
Cdd:PRK03918 311 EIEKRLSRLEEEinGIEERIKELEEKEERLEELKKKLKELEKR-----LEELEERHELYE-EAKAKKEELERLKKRLTGL 384
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556 466 GKASWAAAAERMEKLQYAVSKEtLQMMRAKEICLEQRKHALKEEMQSLRG--GTEAIARLDQLEADYYDL----QLQLYE 539
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEE-ISKITARIGELKKEIKELKKAIEELKKakGKCPVCGRELTEEHRKELleeyTAELKR 463
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289547556 540 VQFEILKCEELL--LTAQLESIKRLISEKRDEVVYYDTYESMEAMLEKeemaasayLQREELQKLQQKARQLEARRGRVS 617
Cdd:PRK03918 464 IEKELKEIEEKErkLRKELRELEKVLKKESELIKLKELAEQLKELEEK--------LKKYNLEELEKKAEEYEKLKEKLI 535
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 289547556 618 AKKSYLRNKKEIcIAKHNEKIQQRTRIEDEYrthHTVQLKREKLHDEEERKSAWVSQERQRTLDRLRTFKQRY 690
Cdd:PRK03918 536 KLKGEIKSLKKE-LEKLEELKKKLAELEKKL---DELEEELAELLKELEELGFESVEELEERLKELEPFYNEY 604
 
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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