NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2056392211|ref|NP_001382253|]
View 

myomegalin isoform 43 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
123-713 1.19e-10

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 123 QQQVALLDLQSAlfcsQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEaswkhnqELRKALQQLQEELQNKS 202
Cdd:COG1196   226 EAELLLLKLREL----EAELEELEAELEELEAELEELEAELAELEAELEELRLELE-------ELELELEEAQAEEYELL 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 203 QQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEK 282
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 283 FSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKE 362
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 363 QESIIQQLQTSLHDRNKEDLSATLLCKLGPGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQ 442
Cdd:COG1196   455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEA 534
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 443 ESQAAAEklvqalmernSELQALRQYLGGRDSLMSQAPIsnqqaevtptgRLGKQTDQGSMQIPSRDDSTSLTAKEDVSI 522
Cdd:COG1196   535 AYEAALE----------AALAAALQNIVVEDDEVAAAAI-----------EYLKAAKAGRATFLPLDKIRARAALAAALA 593
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 523 PRSTLGDLDTVAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAADMESLTRNIQIKEDLIKDLQMQ 602
Cdd:COG1196   594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 603 LVDPEDIPAMERLTQEVLLLREKVASVESQGQEISGNRRQQLLLMLEGLVDERSRLNEALQAERQLYSSLvkfhAHPESS 682
Cdd:COG1196   674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE----EEELLE 749
                         570       580       590
                  ....*....|....*....|....*....|.
gi 2056392211 683 ERDRTLQVELEGAQVLRSRLEEvLGRSLERL 713
Cdd:COG1196   750 EEALEELPEPPDLEELERELER-LEREIEAL 779
CwlO1 super family cl25603
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
24-212 4.83e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


The actual alignment was detected with superfamily member COG3883:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  24 SDSHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKL-- 101
Cdd:COG3883    14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERar 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 102 ---REMLHQSQLGQLHSSEGTSPAQQQVALLDLQSALfcSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKE 178
Cdd:COG3883    94 alyRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADA--DADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2056392211 179 ASWKHNQELRKALQQLQEELQNKSQQLRAWEAEK 212
Cdd:COG3883   172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
123-713 1.19e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 123 QQQVALLDLQSAlfcsQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEaswkhnqELRKALQQLQEELQNKS 202
Cdd:COG1196   226 EAELLLLKLREL----EAELEELEAELEELEAELEELEAELAELEAELEELRLELE-------ELELELEEAQAEEYELL 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 203 QQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEK 282
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 283 FSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKE 362
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 363 QESIIQQLQTSLHDRNKEDLSATLLCKLGPGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQ 442
Cdd:COG1196   455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEA 534
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 443 ESQAAAEklvqalmernSELQALRQYLGGRDSLMSQAPIsnqqaevtptgRLGKQTDQGSMQIPSRDDSTSLTAKEDVSI 522
Cdd:COG1196   535 AYEAALE----------AALAAALQNIVVEDDEVAAAAI-----------EYLKAAKAGRATFLPLDKIRARAALAAALA 593
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 523 PRSTLGDLDTVAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAADMESLTRNIQIKEDLIKDLQMQ 602
Cdd:COG1196   594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 603 LVDPEDIPAMERLTQEVLLLREKVASVESQGQEISGNRRQQLLLMLEGLVDERSRLNEALQAERQLYSSLvkfhAHPESS 682
Cdd:COG1196   674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE----EEELLE 749
                         570       580       590
                  ....*....|....*....|....*....|.
gi 2056392211 683 ERDRTLQVELEGAQVLRSRLEEvLGRSLERL 713
Cdd:COG1196   750 EEALEELPEPPDLEELERELER-LEREIEAL 779
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
151-464 4.29e-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: 56.99  E-value: 4.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  151 QKERQLADAKQCVQFVEAAAHESEQQkeaswkhnqelRKALQQLQEELQNKSQQLRAWEAEKYNEI-----------RTQ 219
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKA-----------LAELRKELEELEEELEQLRKELEELSRQIsalrkdlarleAEV 742
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  220 EQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDkavaLERAIDEKFSALEEKEKELRQLRLA 299
Cdd:TIGR02168  743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKEELKALREALDELRAELTLLNEE 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  300 VRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQTSLHDRnk 379
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL-- 896
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  380 EDLSATLlcklgpgqsEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERN 459
Cdd:TIGR02168  897 EELSEEL---------RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDE 967

                   ....*
gi 2056392211  460 SELQA 464
Cdd:TIGR02168  968 EEARR 972
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
28-623 4.72e-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: 4.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211   28 LAELQEKIQQTEATNKILQEKLNEMSyelkcaqESSQKQDGTIQNLKETLKSRERETEELYqviegqndtMAKLREMlhQ 107
Cdd:pfam15921  262 LQQHQDRIEQLISEHEVEITGLTEKA-------SSARSQANSIQSQLEIIQEQARNQNSMY---------MRQLSDL--E 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  108 SQLGQLHSSEGTSPAQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQEL 187
Cdd:pfam15921  324 STVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  188 --------------RKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKT 253
Cdd:pfam15921  404 wdrdtgnsitidhlRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEE 483
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  254 LEANEMLLEKLRQRIHDKAVALEraidEKFSALEEKEKELRQLRLAVRERDHDLERLR---DVLSSNEATMQSMESLLRA 330
Cdd:pfam15921  484 LTAKKMTLESSERTVSDLTASLQ----EKERAIEATNAEITKLRSRVDLKLQELQHLKnegDHLRNVQTECEALKLQMAE 559
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  331 KGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQesiiQQLQTSLHDRNKEDLSATLLCKLGPGQSEIAEELCQRLQRKER 410
Cdd:pfam15921  560 KDKVIEILRQQIENMTQLVGQHGRTAGAMQVEK----AQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKV 635
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  411 MLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLvqALMERNSELQALRQYLGGRDSLMSQAPISNQQAEVTP 490
Cdd:pfam15921  636 KLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDY--EVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRN 713
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  491 TGRLGKQTDQGSMQIpsrddstSLTAKEDVSIPRSTLGDLDT-VAGLEKELSNAKEELELMAKKERESQMELSALQSMMA 569
Cdd:pfam15921  714 TLKSMEGSDGHAMKV-------AMGMQKQITAKRGQIDALQSkIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKN 786
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2056392211  570 VQEEELQVQAADMESLTRNIQIKEDLIKDLQMQLVDPEDIpaMERLTQEVLLLR 623
Cdd:pfam15921  787 KMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDI--IQRQEQESVRLK 838
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
149-341 7.19e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 7.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 149 VRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWE--AEKYNEIRTQEQNIQHL 226
Cdd:PRK02224  532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLEriRTLLAAIADAEDEIERL 611
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 227 NHSLSHKEQLLQEFRELLQYRDNSDKTLEA--NEMLLEKLRQRiHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERD 304
Cdd:PRK02224  612 REKREALAELNDERRERLAEKRERKRELEAefDEARIEEARED-KERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL 690
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2056392211 305 HDLERLRDVLSSNEATMQSMESLLRakglEVEQLSTT 341
Cdd:PRK02224  691 EELEELRERREALENRVEALEALYD----EAEELESM 723
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
24-212 4.83e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  24 SDSHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKL-- 101
Cdd:COG3883    14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERar 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 102 ---REMLHQSQLGQLHSSEGTSPAQQQVALLDLQSALfcSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKE 178
Cdd:COG3883    94 alyRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADA--DADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2056392211 179 ASWKHNQELRKALQQLQEELQNKSQQLRAWEAEK 212
Cdd:COG3883   172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
123-713 1.19e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 123 QQQVALLDLQSAlfcsQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEaswkhnqELRKALQQLQEELQNKS 202
Cdd:COG1196   226 EAELLLLKLREL----EAELEELEAELEELEAELEELEAELAELEAELEELRLELE-------ELELELEEAQAEEYELL 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 203 QQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEK 282
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 283 FSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKE 362
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 363 QESIIQQLQTSLHDRNKEDLSATLLCKLGPGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQ 442
Cdd:COG1196   455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEA 534
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 443 ESQAAAEklvqalmernSELQALRQYLGGRDSLMSQAPIsnqqaevtptgRLGKQTDQGSMQIPSRDDSTSLTAKEDVSI 522
Cdd:COG1196   535 AYEAALE----------AALAAALQNIVVEDDEVAAAAI-----------EYLKAAKAGRATFLPLDKIRARAALAAALA 593
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 523 PRSTLGDLDTVAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAADMESLTRNIQIKEDLIKDLQMQ 602
Cdd:COG1196   594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 603 LVDPEDIPAMERLTQEVLLLREKVASVESQGQEISGNRRQQLLLMLEGLVDERSRLNEALQAERQLYSSLvkfhAHPESS 682
Cdd:COG1196   674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE----EEELLE 749
                         570       580       590
                  ....*....|....*....|....*....|.
gi 2056392211 683 ERDRTLQVELEGAQVLRSRLEEvLGRSLERL 713
Cdd:COG1196   750 EEALEELPEPPDLEELERELER-LEREIEAL 779
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
151-464 4.29e-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: 56.99  E-value: 4.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  151 QKERQLADAKQCVQFVEAAAHESEQQkeaswkhnqelRKALQQLQEELQNKSQQLRAWEAEKYNEI-----------RTQ 219
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKA-----------LAELRKELEELEEELEQLRKELEELSRQIsalrkdlarleAEV 742
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  220 EQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDkavaLERAIDEKFSALEEKEKELRQLRLA 299
Cdd:TIGR02168  743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKEELKALREALDELRAELTLLNEE 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  300 VRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQTSLHDRnk 379
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL-- 896
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  380 EDLSATLlcklgpgqsEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERN 459
Cdd:TIGR02168  897 EELSEEL---------RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDE 967

                   ....*
gi 2056392211  460 SELQA 464
Cdd:TIGR02168  968 EEARR 972
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
28-717 5.88e-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: 56.60  E-value: 5.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211   28 LAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEElyqviegqndtmaklremlHQ 107
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQI-------------------LR 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  108 SQLGQLHssegTSPAQQQVALLDLQSALFCSQLEIQKLqrvvrqkERQLADAKQCVQFVEAAAHESEQQKEASWKHNQEL 187
Cdd:TIGR02168  309 ERLANLE----RQLEELEAQLEELESKLDELAEELAEL-------EEKLEELKEELESLEAELEELEAELEELESRLEEL 377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  188 RKALQQLQEELQNKSQQLRAWEAEkyneirtQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDktLEANEMLLEKLRQR 267
Cdd:TIGR02168  378 EEQLETLRSKVAQLELQIASLNNE-------IERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEE 448
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  268 IHDKAVALERAIdekfSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQW 347
Cdd:TIGR02168  449 LEELQEELERLE----EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV 524
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  348 LKEEMETKfSRWQKEQESIIQQLQTSLHDRNKEDlsatllcklgpgQSEIAEELCQ-RLQRKERMLQDLLSDRNKQVLEH 426
Cdd:TIGR02168  525 LSELISVD-EGYEAAIEAALGGRLQAVVVENLNA------------AKKAIAFLKQnELGRVTFLPLDSIKGTEIQGNDR 591
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  427 EM--EIQGLLQSVSTREqESQAAAEKLVQALMERNSELQALRQYLGGRDSLMSQAPISNQQAE-VTPTGRLGKQTDQGSM 503
Cdd:TIGR02168  592 EIlkNIEGFLGVAKDLV-KFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDlVRPGGVITGGSAKTNS 670
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  504 QIPSRdDSTSLTAKEDVSIPRSTLGDLDT-VAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAADM 582
Cdd:TIGR02168  671 SILER-RREIEELEEKIEELEEKIAELEKaLAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  583 ESLTRNIQIKEDLIKDLQMQLvdpedipamERLTQEVLLLREKVASVESQGQEISgNRRQQLLLMLEGLVDERSRLNEAL 662
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERL---------EEAEEELAEAEAEIEELEAQIEQLK-EELKALREALDELRAELTLLNEEA 819
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2056392211  663 QAERQLYSSLVKFHAhpESSERDRTLQVELEGAQVLRSRLEEVLGRSLERLNRLE 717
Cdd:TIGR02168  820 ANLRERLESLERRIA--ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
186-454 1.42e-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: 55.07  E-value: 1.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  186 ELRKALQQLQEE---------LQNKSQQLRAWEaeKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDnsdKTLEA 256
Cdd:TIGR02169  195 EKRQQLERLRRErekaeryqaLLKEKREYEGYE--LLKEKEALERQKEAIERQLASLEEELEKLTEEISELE---KRLEE 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  257 NEMLLEKLRQRIHDKAVALERAIDEKfsaLEEKEKELRQLRLAVRERDHDLERLrdvlssnEATMQSMESLLRAKGLEVE 336
Cdd:TIGR02169  270 IEQLLEELNKKIKDLGEEEQLRVKEK---IGELEAEIASLERSIAEKERELEDA-------EERLAKLEAEIDKLLAEIE 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  337 QLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQtSLHDRNKE--DLSATLLCKLGPGQSEIAEelcqrLQRKERMLQD 414
Cdd:TIGR02169  340 ELEREIEEERKRRDKLTEEYAELKEELEDLRAELE-EVDKEFAEtrDELKDYREKLEKLKREINE-----LKRELDRLQE 413
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2056392211  415 LLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQA 454
Cdd:TIGR02169  414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
15-467 1.26e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  15 ETTITQQSVSDSHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQ 94
Cdd:COG1196   256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  95 NDTMAKLREMLHQSQLGQLHSSEgtSPAQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESE 174
Cdd:COG1196   336 EEELEELEEELEEAEEELEEAEA--ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 175 QQKEASWKHNQELRKALQQLQEELQNKSQQLR---AWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQ---YRD 248
Cdd:COG1196   414 ERLERLEEELEELEEALAELEEEEEEEEEALEeaaEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAeaaARL 493
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 249 NSDKTLEANEM--------LLEKLRQRIHDKAVALERAIDEKFSALEEkEKELRQLRLAVRERDHDLERLRDVLSSNEAT 320
Cdd:COG1196   494 LLLLEAEADYEgflegvkaALLLAGLRGLAGAVAVLIGVEAAYEAALE-AALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 321 MQSMESLLRAKGLEVEQLSTTCQNLQW----LKEEMETKFSRWQKEQESIIQQLQTSLHDRNKEDLSATL----LCKLGP 392
Cdd:COG1196   573 RATFLPLDKIRARAALAAALARGAIGAavdlVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLagrlREVTLE 652
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2056392211 393 GQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNSELQALRQ 467
Cdd:COG1196   653 GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
26-311 1.73e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 1.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211   26 SHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREML 105
Cdd:TIGR02169  695 SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL 774
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  106 H--QSQLGQLHSSEGTSPAQQQVALL---------------DLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEA 168
Cdd:TIGR02169  775 HklEEALNDLEARLSHSRIPEIQAELskleeevsriearlrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  169 AAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAekynEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRD 248
Cdd:TIGR02169  855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA----QLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  249 NSDKTLE----------ANEMLLEKLRQRIHDKAVALE-------RAIDE------KFSALEEKEKELRQLRLAVRERDH 305
Cdd:TIGR02169  931 EELSEIEdpkgedeeipEEELSLEDVQAELQRVEEEIRalepvnmLAIQEyeevlkRLDELKEKRAKLEEERKAILERIE 1010

                   ....*.
gi 2056392211  306 DLERLR 311
Cdd:TIGR02169 1011 EYEKKK 1016
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
28-242 1.99e-05

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: 47.45  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  28 LAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLhQ 107
Cdd:COG4942    29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL-A 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 108 SQLGQLHSSEGTSPAQQQVALLDLQSALFCSQLeIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQEL 187
Cdd:COG4942   108 ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2056392211 188 RKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRE 242
Cdd:COG4942   187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
43-666 7.61e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 7.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211   43 KILQEKLNEMSYELKCAQEssQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLHQSQLGQLHSSEGTSpa 122
Cdd:TIGR02169  214 QALLKEKREYEGYELLKEK--EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-- 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  123 qqqvalLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKS 202
Cdd:TIGR02169  290 ------LRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  203 QQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDkavaLERAIDEK 282
Cdd:TIGR02169  364 EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG----IEAKINEL 439
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  283 FSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLqwlkEEMETKFSRWQKE 362
Cdd:TIGR02169  440 EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS----EERVRGGRAVEEV 515
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  363 QESIIQQLQTSLHDRNKEDLSATLLCKLGPG---------QSEIAEELCQRLQRKE--RM----LQDLLSDRNKQVLEHE 427
Cdd:TIGR02169  516 LKASIQGVHGTVAQLGSVGERYATAIEVAAGnrlnnvvveDDAVAKEAIELLKRRKagRAtflpLNKMRDERRDLSILSE 595
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  428 MEIQGLLQSVSTREQESQAAAEKLVQALMERNSeLQALRQYLGG------------RDSLMSQAPISNQQAEVTPTgRLG 495
Cdd:TIGR02169  596 DGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVED-IEAARRLMGKyrmvtlegelfeKSGAMTGGSRAPRGGILFSR-SEP 673
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  496 KQTDQGSMQIPSRDDSTSLTAKEDVSIPRSTLGDLDTVAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEEL 575
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  576 QVQAADMESLTRNIQIKEDLIKDLQMQLVDPEDIPAMER---LTQEVLLLREKVASVESQGQEISG--NRRQQLLLMLEG 650
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeIQAELSKLEEEVSRIEARLREIEQklNRLTLEKEYLEK 833
                          650
                   ....*....|....*.
gi 2056392211  651 LVDERSRLNEALQAER 666
Cdd:TIGR02169  834 EIQELQEQRIDLKEQI 849
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
70-371 1.43e-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: 45.43  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211   70 IQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLHQSQLGQLHSSEGTSPAQQQVALLDLQSALFCSQLEIQKLQRVV 149
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  150 RQKERQLADAKQCVQFVEAAAHESEQQK-----EASWKHNQELRKALQQLQEELQN---KSQQLRAWEAEKYNEIRTQEQ 221
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEEleaqiEQLKEELKALREALDELRAELTLlneEAANLRERLESLERRIAATER 838
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  222 NIQHLNHSLSHKEQLLQEFR-ELLQYRDNSDKTLEANEMLLEKLRQrihdkavaLERAIDEKFSALEEKEKELRQLRLAV 300
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAaEIEELEELIEELESELEALLNERAS--------LEEALALLRSELEELSEELRELESKR 910
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392211  301 RERDHDLERLRDVLSSNEATMQSMES-LLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQ 371
Cdd:TIGR02168  911 SELRRELEELREKLAQLELRLEGLEVrIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
118-325 1.92e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.37  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 118 GTSPAQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEE 197
Cdd:COG4942    12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 198 LQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALER 277
Cdd:COG4942    92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2056392211 278 AIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSME 325
Cdd:COG4942   172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
139-427 2.15e-04

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: 44.67  E-value: 2.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  139 QLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWE-AEKYNEIR 217
Cdd:TIGR02169  722 EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELS 801
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  218 TQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLr 297
Cdd:TIGR02169  802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL- 880
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  298 lavRERDHDLERLRDvlssneatmqSMESLLRAKGLEVEQLSTTCQNLQWLKEEmetkfsrwQKEQESIIQQLQTSLHDR 377
Cdd:TIGR02169  881 ---ESRLGDLKKERD----------ELEAQLRELERKIEELEAQIEKKRKRLSE--------LKAKLEALEEELSEIEDP 939
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2056392211  378 NKEDLSAtllcklgPGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHE 427
Cdd:TIGR02169  940 KGEDEEI-------PEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYE 982
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
7-372 2.19e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.63  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211   7 KQQKLNSHETTITQQSVSDSH-LAELQEKIQQTEATNKILQEKLNEMS-YELKCAQESSQKQDGTIQNLKETLKSRERET 84
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKiKKQLSEKQKELEQNNKKIKELEKQLNqLKSEISDLNNQKEQDWNKELKSELKNQEKKL 323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  85 EELY-------QVIEGQNDTMAKLREMLHQSQLGQLHSSEGTSPAQQQVALLDLQSALFcsQLEIQKLQRVVRQKERQLA 157
Cdd:TIGR04523 324 EEIQnqisqnnKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY--KQEIKNLESQINDLESKIQ 401
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 158 DAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQlrawEAEKYNEIRTQEQNIQHLNHSLshkEQLL 237
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ----DSVKELIIKNLDNTRESLETQL---KVLS 474
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 238 QEFRELLQYRDNSDKTLEANEMLLEKLRQRIHD---KAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVL 314
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKELKKLNEEKKEleeKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL 554
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392211 315 SSNEatmqsMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQT 372
Cdd:TIGR04523 555 KKEN-----LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE 607
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
24-664 2.45e-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: 44.66  E-value: 2.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211   24 SDSHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLRE 103
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  104 ML--HQSQLGQLhSSEGTSPAQQQVALLDLQSALFCSQLE--IQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEA 179
Cdd:TIGR02168  394 QIasLNNEIERL-EARLERLEDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEELREELEE 472
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  180 SWKHNQELR----------KALQQLQEELQNKSQQLRAWEAEKyneiRTQEQNIQHLNHSLSHKEQLLQEFRELLQYR-- 247
Cdd:TIGR02168  473 AEQALDAAErelaqlqarlDSLERLQENLEGFSEGVKALLKNQ----SGLSGILGVLSELISVDEGYEAAIEAALGGRlq 548
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  248 ----DNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLA--VRERDHDLERLRDVLSSNEATM 321
Cdd:TIGR02168  549 avvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAkdLVKFDPKLRKALSYLLGGVLVV 628
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  322 QSMES--------------------LLRAKGLEVEQLSTTCQNLQWLKEEMEtKFSRWQKEQESIIQQLQTSLHDRNKEd 381
Cdd:TIGR02168  629 DDLDNalelakklrpgyrivtldgdLVRPGGVITGGSAKTNSSILERRREIE-ELEEKIEELEEKIAELEKALAELRKE- 706
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  382 lsatllcklgpgQSEIAEELCQRLQRKERMLQDlLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNSE 461
Cdd:TIGR02168  707 ------------LEELEEELEQLRKELEELSRQ-ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  462 LQALRQYLGGRDSLMSQAP------------ISNQQAEVTPTGRLGKQTDQGSMQIPSRDDSTSLTAKEDVSIPRSTLGD 529
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEqlkeelkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  530 LdtvAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAADMESLTRNIQIKEDLIKDLQMQLVDPEDi 609
Cdd:TIGR02168  854 I---ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL- 929
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2056392211  610 pAMERLTQEVLLLREKVASVESQGQEISGNRRQQLLLMLEGLVDERSRLNEALQA 664
Cdd:TIGR02168  930 -RLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
138-314 2.64e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 2.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  138 SQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEEL-QNKSQQLRAWEAekynEI 216
Cdd:COG4913    272 AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLER----EI 347
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  217 RTQEQNIQHLNHSLSHKEQLLQEF--------RELLQYRDNSDKTLEAnemlLEKLRQRIHDKAVALERAIDEKFSALEE 288
Cdd:COG4913    348 ERLERELEERERRRARLEALLAALglplpasaEEFAALRAEAAALLEA----LEEELEALEEALAEAEAALRDLRRELRE 423
                          170       180
                   ....*....|....*....|....*.
gi 2056392211  289 KEKELRQLRLAVRERDHDLERLRDVL 314
Cdd:COG4913    424 LEAEIASLERRKSNIPARLLALRDAL 449
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
28-623 4.72e-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: 4.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211   28 LAELQEKIQQTEATNKILQEKLNEMSyelkcaqESSQKQDGTIQNLKETLKSRERETEELYqviegqndtMAKLREMlhQ 107
Cdd:pfam15921  262 LQQHQDRIEQLISEHEVEITGLTEKA-------SSARSQANSIQSQLEIIQEQARNQNSMY---------MRQLSDL--E 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  108 SQLGQLHSSEGTSPAQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQEL 187
Cdd:pfam15921  324 STVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  188 --------------RKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKT 253
Cdd:pfam15921  404 wdrdtgnsitidhlRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEE 483
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  254 LEANEMLLEKLRQRIHDKAVALEraidEKFSALEEKEKELRQLRLAVRERDHDLERLR---DVLSSNEATMQSMESLLRA 330
Cdd:pfam15921  484 LTAKKMTLESSERTVSDLTASLQ----EKERAIEATNAEITKLRSRVDLKLQELQHLKnegDHLRNVQTECEALKLQMAE 559
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  331 KGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQesiiQQLQTSLHDRNKEDLSATLLCKLGPGQSEIAEELCQRLQRKER 410
Cdd:pfam15921  560 KDKVIEILRQQIENMTQLVGQHGRTAGAMQVEK----AQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKV 635
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  411 MLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLvqALMERNSELQALRQYLGGRDSLMSQAPISNQQAEVTP 490
Cdd:pfam15921  636 KLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDY--EVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRN 713
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  491 TGRLGKQTDQGSMQIpsrddstSLTAKEDVSIPRSTLGDLDT-VAGLEKELSNAKEELELMAKKERESQMELSALQSMMA 569
Cdd:pfam15921  714 TLKSMEGSDGHAMKV-------AMGMQKQITAKRGQIDALQSkIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKN 786
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2056392211  570 VQEEELQVQAADMESLTRNIQIKEDLIKDLQMQLVDPEDIpaMERLTQEVLLLR 623
Cdd:pfam15921  787 KMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDI--IQRQEQESVRLK 838
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
122-334 6.46e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 6.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 122 AQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNK 201
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 202 SQQLRAWEAEKY--------------NEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQR 267
Cdd:COG4942   103 KEELAELLRALYrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392211 268 IHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLE 334
Cdd:COG4942   183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
149-341 7.19e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 7.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 149 VRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWE--AEKYNEIRTQEQNIQHL 226
Cdd:PRK02224  532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLEriRTLLAAIADAEDEIERL 611
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 227 NHSLSHKEQLLQEFRELLQYRDNSDKTLEA--NEMLLEKLRQRiHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERD 304
Cdd:PRK02224  612 REKREALAELNDERRERLAEKRERKRELEAefDEARIEEARED-KERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL 690
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2056392211 305 HDLERLRDVLSSNEATMQSMESLLRakglEVEQLSTT 341
Cdd:PRK02224  691 EELEELRERREALENRVEALEALYD----EAEELESM 723
PRK11281 PRK11281
mechanosensitive channel MscK;
4-286 3.32e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 41.05  E-value: 3.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211    4 ELLKQQKLNSHETTITQQSVSDShlAELQEKIQQTEATNKILQEKLNEMSYELKCAQESsqkqdgtIQNLKETLKSRERE 83
Cdd:PRK11281    46 DALNKQKLLEAEDKLVQQDLEQT--LALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAE-------LEALKDDNDEETRE 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211   84 TEElyqviegqNDTMAKLREMLHQ--SQLGQLHSSEGTSPAQ---QQVALLDLQSALFCSQLEIQKL------------- 145
Cdd:PRK11281   117 TLS--------TLSLRQLESRLAQtlDQLQNAQNDLAEYNSQlvsLQTQPERAQAALYANSQRLQQIrnllkggkvggka 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  146 ----QRVVRQKERQLADAKQCVQFVEAAAHE------SEQQKEASWKHNQeLRKALQQLQEELQNKsqqlRAWEAEK-YN 214
Cdd:PRK11281   189 lrpsQRVLLQAEQALLNAQNDLQRKSLEGNTqlqdllQKQRDYLTARIQR-LEHQLQLLQEAINSK----RLTLSEKtVQ 263
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392211  215 EIRTQEQNIQHLNHSLSHKEqlLQEFRELLQYRDNSdkTLEANEMLLEKLRQR-IHDKAVALERAIDEKFSAL 286
Cdd:PRK11281   264 EAQSQDEAARIQANPLVAQE--LEINLQLSQRLLKA--TEKLNTLTQQNLRVKnWLDRLTQSERNIKEQISVL 332
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
27-329 4.69e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.34  E-value: 4.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211   27 HLAELQEKIQQTEATNKILQEKLNEMSYEL-KCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDtmakLREML 105
Cdd:TIGR00618  557 QRASLKEQMQEIQQSFSILTQCDNRSKEDIpNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDL----QDVRL 632
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  106 HQSQLGQLHSSEGTSPAQQQVALL---DLQSALFCSQLEIQKLQRVVRQ------KERQLADAKQCVQFVEAAAHESEQQ 176
Cdd:TIGR00618  633 HLQQCSQELALKLTALHALQLTLTqerVREHALSIRVLPKELLASRQLAlqkmqsEKEQLTYWKEMLAQCQTLLRELETH 712
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  177 KEASWKHNQELRKALQQLQEELQNK----SQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDK 252
Cdd:TIGR00618  713 IEEYDREFNEIENASSSLGSDLAARedalNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNR 792
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392211  253 TLEANEMLLEKLRQRIHDKAVALEraiDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLR 329
Cdd:TIGR00618  793 LREEDTHLLKTLEAEIGQEIPSDE---DILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQ 866
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
182-463 4.76e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 40.34  E-value: 4.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  182 KHNQELRKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQ---------------------HLNHSLSHKEQLLQEF 240
Cdd:pfam02463  166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKaleyyqlkekleleeeyllylDYLKLNEERIDLLQEL 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  241 RELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEAT 320
Cdd:pfam02463  246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  321 MQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQTSLHDRNKEDLSATLLCKLGPGQSEIAEE 400
Cdd:pfam02463  326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392211  401 LCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNSELQ 463
Cdd:pfam02463  406 EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELK 468
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
24-212 4.83e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211  24 SDSHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKL-- 101
Cdd:COG3883    14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERar 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 102 ---REMLHQSQLGQLHSSEGTSPAQQQVALLDLQSALfcSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKE 178
Cdd:COG3883    94 alyRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADA--DADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2056392211 179 ASWKHNQELRKALQQLQEELQNKSQQLRAWEAEK 212
Cdd:COG3883   172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
145-364 9.13e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 39.34  E-value: 9.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 145 LQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRaweaEKYNEIRTQEQNIQ 224
Cdd:pfam05557  11 LSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALR----EQAELNRLKKKYLE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 225 HLNHSLSHKEQLL-----------QEFRELLQYRDNSDKTLEANEMLLEKLRQRiHDKAVALERAIDEKFSALEEKEKEL 293
Cdd:pfam05557  87 ALNKKLNEKESQLadarevisclkNELSELRRQIQRAELELQSTNSELEELQER-LDLLKAKASEAEQLRQNLEKQQSSL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392211 294 RQLRLAVRERDHDLERLRD------VLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEE---METKFSRWQKEQE 364
Cdd:pfam05557 166 AEAEQRIKELEFEIQSQEQdseivkNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEvedLKRKLEREEKYRE 245
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH