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Conserved domains on  [gi|334184688|ref|NP_001189677|]
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myosin heavy chain-like protein [Arabidopsis thaliana]

Protein Classification

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

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 543-756 2.18e-08

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 57.08  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 543 EAVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQV 622
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 623 ERQETEIQDKIEALSVVS-----------------ARELEKVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSET 685
Cdd:COG4942  100 EAQKEELAELLRALYRLGrqpplalllspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334184688 686 KAEKETLKKQLVsldlvvppQLIKGFDILEGLIAEKTQKTNSRLKNMQSQLSDLSHQINEVKGKASTYKQR 756
Cdd:COG4942  180 LAELEEERAALE--------ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 368-700 7.89e-07

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 7.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   368 ERGSFSFVGKDKELGALKKKIPFVISKLDKILMEDEKFVSEGKNDAGLKRQLDSLLLENRQLKDSLSD-----------A 436
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlarleaeveqL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   437 AEKMSQLSQAEADHQELIRKLETDVEDSRNEASIYEDVYGcFVTEFVGQIKCTKQETDLEHSMLREAYELLLEDLARKEA 516
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE-ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   517 RKSKEDFE-DSCVKSVMMEECCSVIYKEAVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKEKENLVQ 595
Cdd:TIGR02168  825 RLESLERRiAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   596 TAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEALSVVSARELE----KVKGYETKISSLREELELARESLKEM 671
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeaeaLENKIEDDEEEARRRLKRLENKIKEL 984

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 334184688   672 K-------DEKRKTEEKLSETKAEKETLKKQLVSLD 700
Cdd:TIGR02168  985 GpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLE 1020
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 543-756 2.18e-08

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: 57.08  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 543 EAVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQV 622
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 623 ERQETEIQDKIEALSVVS-----------------ARELEKVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSET 685
Cdd:COG4942  100 EAQKEELAELLRALYRLGrqpplalllspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334184688 686 KAEKETLKKQLVsldlvvppQLIKGFDILEGLIAEKTQKTNSRLKNMQSQLSDLSHQINEVKGKASTYKQR 756
Cdd:COG4942  180 LAELEEERAALE--------ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 418-699 2.52e-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: 57.76  E-value: 2.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   418 QLDSLLLENRQLKDSLSDAAEKMSQLSQAEADHQELIRKLETDVEDSR-------NEASIYEDVYGCFVTE---FVGQIK 487
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRlevseleEEIEELQKELYALANEisrLEQQKQ 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   488 CTKQETDLEHSMLREAYELLLEDLARKEarKSKEDFEDSCVKSVMMEECCSVIyKEAVKEAHKKIVELNLHVTEKEgtlr 567
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLD--ELAEELAELEEKLEELKEELESL-EAELEELEAELEELESRLEELE---- 378

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   568 semVDKERLKEEIHRLgclvkekenlvqtaENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEALSVVSAREL-EK 646
Cdd:TIGR02168  379 ---EQLETLRSKVAQL--------------ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELqAE 441

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 334184688   647 VKGYETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSL 699
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 368-700 7.89e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 7.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   368 ERGSFSFVGKDKELGALKKKIPFVISKLDKILMEDEKFVSEGKNDAGLKRQLDSLLLENRQLKDSLSD-----------A 436
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlarleaeveqL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   437 AEKMSQLSQAEADHQELIRKLETDVEDSRNEASIYEDVYGcFVTEFVGQIKCTKQETDLEHSMLREAYELLLEDLARKEA 516
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE-ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   517 RKSKEDFE-DSCVKSVMMEECCSVIYKEAVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKEKENLVQ 595
Cdd:TIGR02168  825 RLESLERRiAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   596 TAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEALSVVSARELE----KVKGYETKISSLREELELARESLKEM 671
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeaeaLENKIEDDEEEARRRLKRLENKIKEL 984

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 334184688   672 K-------DEKRKTEEKLSETKAEKETLKKQLVSLD 700
Cdd:TIGR02168  985 GpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLE 1020
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
543-788 2.00e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.50  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 543 EAVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLqsqv 622
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL---- 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 623 ERQETEIQDKIEALSVVSARELEKVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSLDLV 702
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 703 V---PPQLIKGFDILEgLIAEKTQKTNSRLKNMQSQLSDLSHQINEVK-----GKASTYKQRLEKKCCVCELCPYPYLVE 774
Cdd:PRK02224 400 FgdaPVDLGNAEDFLE-ELREERDELREREAELEATLRTARERVEEAEalleaGKCPECGQPVEGSPHVETIEEDRERVE 478

                        250
                 ....*....|....
gi 334184688 775 ELTVEtLLDLLEKI 788
Cdd:PRK02224 479 ELEAE-LEDLEEEV 491
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 509-702 2.90e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 47.79  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688  509 EDLARKEARKSKEDFEDSCVKSVMMEECCSVIY---KEAVKEAHKKIVELNLH--------------------VTEKEGT 565
Cdd:pfam05483 466 EEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLlenKELTQEASDMTLELKKHqediinckkqeermlkqienLEEKEMN 545

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688  566 LRSEMVD-KERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQET---EIQDKIEALSVVSA 641
Cdd:pfam05483 546 LRDELESvREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKnieELHQENKALKKKGS 625

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334184688  642 RELEKVKGYETKISSLREELELARESLKEMKDEKRKTEE--KLSETKAEKETLKKQLVSLDLV 702
Cdd:pfam05483 626 AENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEdkKISEEKLLEEVEKAKAIADEAV 688
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 415-635 1.63e-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: 44.75  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 415 LKRQLDSLLLENRQLKDSLSDAAEKMSQLSQAEADHQELIRKLETDVEDSRNEASIYEDVYGcfvtefvgqikctkqetd 494
Cdd:COG4942   46 LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA------------------ 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 495 lehSMLREAYelLLEDLARKEARKSKEDFEDScVKSVMMEECCSVIYKEAVKEAHKKIVELNLHVTEKEGTLRSEMVDKE 574
Cdd:COG4942  108 ---ELLRALY--RLGRQPPLALLLSPEDFLDA-VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334184688 575 RLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEA 635
Cdd:COG4942  182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 377-696 1.47e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.47  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   377 KDKELGALKKKIPFVISKLDKILMEDEKFVSEGKNdagLKRQLDSLLLENR-QLKDSLSDAAEKMSQLSQAEADHQELIR 455
Cdd:pfam01576  174 KAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEK---AKRKLEGESTDLQeQIAELQAQIAELRAQLAKKEEELQAALA 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   456 KLETDVEDSRN--------EASIYEdVYGCFVTEFVGQIKCTKQETDL--EHSMLREAYELLLEDLARKEARKSKEDFED 525
Cdd:pfam01576  251 RLEEETAQKNNalkkirelEAQISE-LQEDLESERAARNKAEKQRRDLgeELEALKTELEDTLDTTAAQQELRSKREQEV 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   526 SCVKSVMMEEccSVIYKEAVKEAHKK----IVELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKekenLVQTAENNL 601
Cdd:pfam01576  330 TELKKALEEE--TRSHEAQLQEMRQKhtqaLEELTEQLEQAKRNKANLEKAKQALESENAELQAELR----TLQQAKQDS 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   602 ATERKKIEVVSQQINDLQSQVERQETEIQDKIEALSVvsarELEKVKGY----ETK-------ISSLREELELARESLKE 670
Cdd:pfam01576  404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQS----ELESVSSLlneaEGKniklskdVSSLESQLQDTQELLQE 479

                          330       340
                   ....*....|....*....|....*.
gi 334184688   671 MKDEKRKTEEKLSETKAEKETLKKQL 696
Cdd:pfam01576  480 ETRQKLNLSTRLRQLEDERNSLQEQL 505
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 543-756 2.18e-08

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: 57.08  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 543 EAVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQV 622
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 623 ERQETEIQDKIEALSVVS-----------------ARELEKVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSET 685
Cdd:COG4942  100 EAQKEELAELLRALYRLGrqpplalllspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334184688 686 KAEKETLKKQLVsldlvvppQLIKGFDILEGLIAEKTQKTNSRLKNMQSQLSDLSHQINEVKGKASTYKQR 756
Cdd:COG4942  180 LAELEEERAALE--------ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 418-699 2.52e-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: 57.76  E-value: 2.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   418 QLDSLLLENRQLKDSLSDAAEKMSQLSQAEADHQELIRKLETDVEDSR-------NEASIYEDVYGCFVTE---FVGQIK 487
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRlevseleEEIEELQKELYALANEisrLEQQKQ 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   488 CTKQETDLEHSMLREAYELLLEDLARKEarKSKEDFEDSCVKSVMMEECCSVIyKEAVKEAHKKIVELNLHVTEKEgtlr 567
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLD--ELAEELAELEEKLEELKEELESL-EAELEELEAELEELESRLEELE---- 378

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   568 semVDKERLKEEIHRLgclvkekenlvqtaENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEALSVVSAREL-EK 646
Cdd:TIGR02168  379 ---EQLETLRSKVAQL--------------ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELqAE 441

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 334184688   647 VKGYETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSL 699
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 414-734 7.35e-08

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: 56.23  E-value: 7.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   414 GLKRQLDSLLLENRQLKDSLSDAAEKMS----QLSQAEADHQELIRKLETDVEDsrneasiyedvygcfVTEFVGQIKCT 489
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRLDELSQELSdasrKIGEIEKEIEQLEQEEEKLKER---------------LEELEEDLSSL 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   490 KQETDLEHSMLREayelLLEDLARKEARKSK-----EDFEDSCVKSVMMEeccSVIYKEAVKEAHKKIVELnlhVTEKEG 564
Cdd:TIGR02169  750 EQEIENVKSELKE----LEARIEELEEDLHKleealNDLEARLSHSRIPE---IQAELSKLEEEVSRIEAR---LREIEQ 819

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   565 TLRSEMVDKERLKEEIhrlgclvKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEALsvvsarel 644
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEI-------QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL-------- 884

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   645 ekvKGYETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSLDLVVP-PQLIKGFDILEGLIAEKTQ 723
Cdd:TIGR02169  885 ---GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGeDEEIPEEELSLEDVQAELQ 961

                          330
                   ....*....|.
gi 334184688   724 KTNSRLKNMQS 734
Cdd:TIGR02169  962 RVEEEIRALEP 972
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 439-701 8.96e-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: 56.22  E-value: 8.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   439 KMSQLSQAEADHQELIRKLETDVEDSRNEASIYEDVygcfvtefVGQIKCTKQETDLEHSMLREAYELLLEDLARKEARK 518
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEE--------LEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   519 SKEDFEDSCVKSVMMEECCSVI-YKEAVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKEKENLVQTA 597
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEeAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   598 ENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEALsvvsARELEKVKGYETKISSLREELELARESLKEMKDEKRK 677
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI----EELESELEALLNERASLEEALALLRSELEELSEELRE 905

                          250       260
                   ....*....|....*....|....
gi 334184688   678 TEEKLSETKAEKETLKKQLVSLDL 701
Cdd:TIGR02168  906 LESKRSELRRELEELREKLAQLEL 929
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
590-693 6.55e-07

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 50.98  E-value: 6.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 590 KENLVQtAENNLA---TERKKIEvvsQQINDLQSQVErqetEIQDKIEaLSVVSARE------LEKVKGYETKISSLREE 660
Cdd:COG1842   36 EEDLVE-ARQALAqviANQKRLE---RQLEELEAEAE----KWEEKAR-LALEKGREdlareaLERKAELEAQAEALEAQ 106

                         90       100       110
                 ....*....|....*....|....*....|...
gi 334184688 661 LELARESLKEMKDEKRKTEEKLSETKAEKETLK 693
Cdd:COG1842  107 LAQLEEQVEKLKEALRQLESKLEELKAKKDTLK 139
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 368-700 7.89e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 7.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   368 ERGSFSFVGKDKELGALKKKIPFVISKLDKILMEDEKFVSEGKNDAGLKRQLDSLLLENRQLKDSLSD-----------A 436
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlarleaeveqL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   437 AEKMSQLSQAEADHQELIRKLETDVEDSRNEASIYEDVYGcFVTEFVGQIKCTKQETDLEHSMLREAYELLLEDLARKEA 516
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE-ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   517 RKSKEDFE-DSCVKSVMMEECCSVIYKEAVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKEKENLVQ 595
Cdd:TIGR02168  825 RLESLERRiAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   596 TAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEALSVVSARELE----KVKGYETKISSLREELELARESLKEM 671
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeaeaLENKIEDDEEEARRRLKRLENKIKEL 984

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 334184688   672 K-------DEKRKTEEKLSETKAEKETLKKQLVSLD 700
Cdd:TIGR02168  985 GpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLE 1020
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 572-759 2.08e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 2.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   572 DKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQETEiqdkIEALSVVSARELEKVKGYE 651
Cdd:TIGR02168  685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE----VEQLEERIAQLSKELTELE 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   652 TKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSLDLVVPPQLIKGFDILEGLIAEKTQK--TNSRL 729
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIaaTERRL 840

                          170       180       190
                   ....*....|....*....|....*....|
gi 334184688   730 KNMQSQLSDLSHQINEVKGKASTYKQRLEK 759
Cdd:TIGR02168  841 EDLEEQIEELSEDIESLAAEIEELEELIEE 870
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 541-821 3.00e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 3.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   541 YKEAVKEAHKKIVELNLHVTEKEgtlrsemvdKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQS 620
Cdd:TIGR02168  218 LKAELRELELALLVLRLEELREE---------LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   621 QVERQETEIQDK---IEALSVVSARELEKVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLV 697
Cdd:TIGR02168  289 ELYALANEISRLeqqKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   698 SLDLVVpPQLIKGFDILEGLIAEKTQK---TNSRLKNMQSQLSDLSHQIN---EVKGKASTYKQRLEKKCCVCELCPYPY 771
Cdd:TIGR02168  369 ELESRL-EELEEQLETLRSKVAQLELQiasLNNEIERLEARLERLEDRRErlqQEIEELLKKLEEAELKELQAELEELEE 447

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 334184688   772 LVEELT---------VETLLDLLEKIYIALDHYSPILKHYPGIIEILRLVRRELSGESK 821
Cdd:TIGR02168  448 ELEELQeelerleeaLEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 413-703 1.12e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 413 AGLKRQLDSLLLENRQLKDSLSDAAEKMSQLSQAEADHQELIRKLETDVEDSRNEASIYEDvygcfvtefvgqikcTKQE 492
Cdd:COG1196  256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE---------------RLEE 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 493 TDLEHSMLREAYELLLEDLARKEARKSKEDFEDSCVKSVMMEEccSVIYKEAVKEAHKKIVELNLHVTEKEGTLRSEMVD 572
Cdd:COG1196  321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA--EEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 573 KERLKEEIHRLGCLVKEKENLvQTAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEALSVVSARELEKVKGYET 652
Cdd:COG1196  399 AAQLEELEEAEEALLERLERL-EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334184688 653 KISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSLDLVV 703
Cdd:COG1196  478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 490-760 1.24e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 490 KQETDLEHSMLREAYELLLEDLARKEARKSKEDfEDSCVKSVMMEECcsviyKEAVKEAHKKIVELNLHVTEKEGTLRSE 569
Cdd:COG1196  220 EELKELEAELLLLKLRELEAELEELEAELEELE-AELEELEAELAEL-----EAELEELRLELEELELELEEAQAEEYEL 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 570 MVDKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEALSVVSARELEKVKG 649
Cdd:COG1196  294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 650 YETKISSLREELELARESLKEMKDEKRK---TEEKLSETKAEKETLKKQLVSLDlvvppQLIKGFDILEGLIAEKTQKTN 726
Cdd:COG1196  374 LAEAEEELEELAEELLEALRAAAELAAQleeLEEAEEALLERLERLEEELEELE-----EALAELEEEEEEEEEALEEAA 448

                        250       260       270
                 ....*....|....*....|....*....|....
gi 334184688 727 SRLKNMQSQLSDLSHQINEVKGKASTYKQRLEKK 760
Cdd:COG1196  449 EEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 561-696 1.99e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.90  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 561 EKEGTLRSEMVDKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQETEIQ---------- 630
Cdd:COG3883   20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralyrsg 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 631 -------------------DKIEALSVVSARELEKVKGYET---KISSLREELELARESLKEMKDEKRKTEEKLSETKAE 688
Cdd:COG3883  100 gsvsyldvllgsesfsdflDRLSALSKIADADADLLEELKAdkaELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179


                 ....*...
gi 334184688 689 KETLKKQL 696
Cdd:COG3883  180 QEALLAQL 187
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
543-788 2.00e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.50  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 543 EAVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLqsqv 622
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL---- 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 623 ERQETEIQDKIEALSVVSARELEKVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSLDLV 702
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 703 V---PPQLIKGFDILEgLIAEKTQKTNSRLKNMQSQLSDLSHQINEVK-----GKASTYKQRLEKKCCVCELCPYPYLVE 774
Cdd:PRK02224 400 FgdaPVDLGNAEDFLE-ELREERDELREREAELEATLRTARERVEEAEalleaGKCPECGQPVEGSPHVETIEEDRERVE 478

                        250
                 ....*....|....
gi 334184688 775 ELTVEtLLDLLEKI 788
Cdd:PRK02224 479 ELEAE-LEDLEEEV 491
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
566-759 2.89e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688  566 LRSEMVDKERLKEEIHRLgclVKEKENLVQtAENNLATERKKIEVVsQQINDLQSQVERQETEIqDKIEALsvVSARELE 645
Cdd:COG4913   213 VREYMLEEPDTFEAADAL---VEHFDDLER-AHEALEDAREQIELL-EPIRELAERYAAARERL-AELEYL--RAALRLW 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688  646 KVkgyETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSLDLvvppqlikgfdilegliaektqkt 725
Cdd:COG4913   285 FA---QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG------------------------ 337

                         170       180       190
                  ....*....|....*....|....*....|....
gi 334184688  726 nSRLKNMQSQLSDLSHQINEVKGKASTYKQRLEK 759
Cdd:COG4913   338 -DRLEQLEREIERLERELEERERRRARLEALLAA 370
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 509-702 2.90e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 47.79  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688  509 EDLARKEARKSKEDFEDSCVKSVMMEECCSVIY---KEAVKEAHKKIVELNLH--------------------VTEKEGT 565
Cdd:pfam05483 466 EEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLlenKELTQEASDMTLELKKHqediinckkqeermlkqienLEEKEMN 545

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688  566 LRSEMVD-KERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQET---EIQDKIEALSVVSA 641
Cdd:pfam05483 546 LRDELESvREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKnieELHQENKALKKKGS 625

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334184688  642 RELEKVKGYETKISSLREELELARESLKEMKDEKRKTEE--KLSETKAEKETLKKQLVSLDLV 702
Cdd:pfam05483 626 AENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEdkKISEEKLLEEVEKAKAIADEAV 688
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 572-760 7.49e-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: 46.60  E-value: 7.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   572 DKERLKEEIHRLGCLVKEKENLVQtaennlatERKKIEVVSQQINDLQSQVERQETEIQDKIEALSVVSARELEKVKGYE 651
Cdd:TIGR02169  672 EPAELQRLRERLEGLKRELSSLQS--------ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   652 TKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKqlvSLDLVVPPQLIKGFDIL-------EGLIAEKTQK 724
Cdd:TIGR02169  744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA---RLSHSRIPEIQAELSKLeeevsriEARLREIEQK 820

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 334184688   725 TNSRL----------KNMQSQLSDLSHQINEVKGKASTYKQRLEKK 760
Cdd:TIGR02169  821 LNRLTlekeylekeiQELQEQRIDLKEQIKSIEKEIENLNGKKEEL 866
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
595-745 8.17e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.16  E-value: 8.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 595 QTAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEalsvvsarelekvkgyETKISSLREELELARESLKEMKDE 674
Cdd:COG3206  164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQ----------------KNGLVDLSEEAKLLLQQLSELESQ 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 675 KRKTEEKLSETKAEKETLKKQLVSLDLVVP--------PQLIKGFDILEGLIAEKTQK---TNSRLKNMQSQLSDLSHQI 743
Cdd:COG3206  228 LAEARAELAEAEARLAALRAQLGSGPDALPellqspviQQLRAQLAELEAELAELSARytpNHPDVIALRAQIAALRAQL 307


                 ..
gi 334184688 744 NE 745
Cdd:COG3206  308 QQ 309
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 380-695 9.10e-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: 9.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   380 ELGALKKKIPFVISKLDKILME-DEKF--VSEGKNDAG-LKRQLDSLLLENRQLKDSLSDAAEKMSQLSQAEADHQELIR 455
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRlDELSqeLSDASRKIGeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   456 KLETDVEDSRNEASIYE----DVYGCFVTEFVGQIKCTKQETDLEHSMLREAYELLLEDLARKEARKSKEDfEDSCVKSV 531
Cdd:TIGR02169  762 ELEARIEELEEDLHKLEealnDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE-KEIQELQE 840

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   532 MMEECCSVI--YKEAVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEIHRLgclvKEKENLVQTAENNLATERKKIE 609
Cdd:TIGR02169  841 QRIDLKEQIksIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL----EAQLRELERKIEELEAQIEKKR 916

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   610 VVSQQINDLQSQVERQETEIQDKIEALSVVSAREL------EKVKGYETKISSLR-------EELELARESLKEMKDEKR 676
Cdd:TIGR02169  917 KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELsledvqAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRA 996

                          330       340
                   ....*....|....*....|..
gi 334184688   677 KTEEK---LSETKAEKETLKKQ 695
Cdd:TIGR02169  997 KLEEErkaILERIEEYEKKKRE 1018
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 587-755 1.44e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.21  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 587 VKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQETEI---QDKIEALSVVSARELEKVKG-----YET------ 652
Cdd:COG3883   25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIdklQAEIAEAEAEIEERREELGEraralYRSggsvsy 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 653 ---------------KISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSLDLVVppqlikgfDILEGL 717
Cdd:COG3883  105 ldvllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK--------AELEAQ 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 334184688 718 IAEKT---QKTNSRLKNMQSQLSDLSHQINEVKGKASTYKQ 755
Cdd:COG3883  177 QAEQEallAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 415-635 1.63e-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: 44.75  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 415 LKRQLDSLLLENRQLKDSLSDAAEKMSQLSQAEADHQELIRKLETDVEDSRNEASIYEDVYGcfvtefvgqikctkqetd 494
Cdd:COG4942   46 LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA------------------ 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 495 lehSMLREAYelLLEDLARKEARKSKEDFEDScVKSVMMEECCSVIYKEAVKEAHKKIVELNLHVTEKEGTLRSEMVDKE 574
Cdd:COG4942  108 ---ELLRALY--RLGRQPPLALLLSPEDFLDA-VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334184688 575 RLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEA 635
Cdd:COG4942  182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
560-756 3.96e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 3.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688  560 TEKEGTLRSEMvdkERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQInDLQsQVERQETEIQDKIEALSVV 639
Cdd:COG4913   609 RAKLAALEAEL---AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-DVA-SAEREIAELEAELERLDAS 683

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688  640 SA--RELEKvkgyetKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSLDLVVPPQLIKGFD----- 712
Cdd:COG4913   684 SDdlAALEE------QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerfaa 757

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 334184688  713 -ILEGLIAEKTQKTNSRLKNMQSQLSDLSHQINEvkgKASTYKQR 756
Cdd:COG4913   758 aLGDAVERELRENLEERIDALRARLNRAEEELER---AMRAFNRE 799
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
 487-696 4.19e-04

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.


Pssm-ID: 464838 [Multi-domain]  Cd Length: 384  Bit Score: 43.51  E-value: 4.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688  487 KCTKQETDLEHSMLReAYELLLEDLARKEARKSKedfedscvkSVMMEECCSViyKEAVKEAHKKIVEL--NLHVTEKEG 564
Cdd:pfam15742  77 MCSSLTAEWKHCQQK-IRELELEVLKQAQSIKSQ---------NSLQEKLAQE--KSRVADAEEKILELqqKLEHAHKVC 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688  565 TLRSEMVDKERLKEEIHRLgclvkeKENLVQTaENNLATERKKIEVVSQQINDLQSQVerqeTEIQDKIEALSVVSAREL 644
Cdd:pfam15742 145 LTDTCILEKKQLEERIKEA------SENEAKL-KQQYQEEQQKRKLLDQNVNELQQQV----RSLQDKEAQLEMTNSQQQ 213

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 334184688  645 EKVKGYETKISSLREELELARESLKEmkdeKRKTEEKLSETKAEKETLKKQL 696
Cdd:pfam15742 214 LRIQQQEAQLKQLENEKRKSDEHLKS----NQELSEKLSSLQQEKEALQEEL 261
PRK12704 PRK12704
phosphodiesterase; Provisional
 540-684 6.70e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 6.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 540 IYKEAVKEAHKKIVELNLHVTEKEGTLRSEMvDKERL--KEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQIND 617
Cdd:PRK12704  43 ILEEAKKEAEAIKKEALLEAKEEIHKLRNEF-EKELRerRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQ 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334184688 618 LQSQVERQETEIQDKIEALsvvsARELEKVKGY---ETK---ISSLREELELARESL-KEMKDEKRKTEEKLSE 684
Cdd:PRK12704 122 KQQELEKKEEELEELIEEQ----LQELERISGLtaeEAKeilLEKVEEEARHEAAVLiKEIEEEAKEEADKKAK 191
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
377-760 7.61e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 7.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 377 KDKELGALKKKIPFVISKLDKILMEDEKFVSEGKNDAGLKRQLDSLLLENRQLKDSLSDAAEKMSQLSQAEADHQELIRK 456
Cdd:PRK03918 198 KEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 457 LETDVEDSrNEASIYEDVYGCFVtEFVGQIKCTKQETDLEHSMLRE---AYELLLEDLARKEARKSKedfedscvksvmm 533
Cdd:PRK03918 278 LEEKVKEL-KELKEKAEEYIKLS-EFYEEYLDELREIEKRLSRLEEeinGIEERIKELEEKEERLEE------------- 342

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 534 eeccsviYKEAVKEAHKKIVELNLHVTEKEgTLRSEMVDKERLKEeihRLGCLVKEK-ENLVQTAENNLATERKKIEVVS 612
Cdd:PRK03918 343 -------LKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKK---RLTGLTPEKlEKELEELEKAKEEIEEEISKIT 411

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 613 QQINDLQSQVERQETEIQDKIEALSV--VSARELEK------VKGYETKISSLREELELARESLKEMKDEKRKTEEKLS- 683
Cdd:PRK03918 412 ARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKk 491

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 684 --------ETKAEKETLKKQLVSLDLVVPPQLIKGFDILEGLIAE------KTQKTNSRLKNMQSQLSDLSHQINEVKGK 749
Cdd:PRK03918 492 eseliklkELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKlkgeikSLKKELEKLEELKKKLAELEKKLDELEEE 571

                        410
                 ....*....|.
gi 334184688 750 ASTYKQRLEKK 760
Cdd:PRK03918 572 LAELLKELEEL 582
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
565-699 7.86e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 7.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 565 TLRSEMVDKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEALSVVSarel 644
Cdd:COG4372   32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ---- 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334184688 645 EKVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSL 699
Cdd:COG4372  108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 377-696 1.47e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.47  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   377 KDKELGALKKKIPFVISKLDKILMEDEKFVSEGKNdagLKRQLDSLLLENR-QLKDSLSDAAEKMSQLSQAEADHQELIR 455
Cdd:pfam01576  174 KAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEK---AKRKLEGESTDLQeQIAELQAQIAELRAQLAKKEEELQAALA 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   456 KLETDVEDSRN--------EASIYEdVYGCFVTEFVGQIKCTKQETDL--EHSMLREAYELLLEDLARKEARKSKEDFED 525
Cdd:pfam01576  251 RLEEETAQKNNalkkirelEAQISE-LQEDLESERAARNKAEKQRRDLgeELEALKTELEDTLDTTAAQQELRSKREQEV 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   526 SCVKSVMMEEccSVIYKEAVKEAHKK----IVELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKekenLVQTAENNL 601
Cdd:pfam01576  330 TELKKALEEE--TRSHEAQLQEMRQKhtqaLEELTEQLEQAKRNKANLEKAKQALESENAELQAELR----TLQQAKQDS 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   602 ATERKKIEVVSQQINDLQSQVERQETEIQDKIEALSVvsarELEKVKGY----ETK-------ISSLREELELARESLKE 670
Cdd:pfam01576  404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQS----ELESVSSLlneaEGKniklskdVSSLESQLQDTQELLQE 479

                          330       340
                   ....*....|....*....|....*.
gi 334184688   671 MKDEKRKTEEKLSETKAEKETLKKQL 696
Cdd:pfam01576  480 ETRQKLNLSTRLRQLEDERNSLQEQL 505
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 596-760 1.65e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 596 TAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEALSVVSArELEKVkgyETKISSLREELELARESLKEMKDEk 675
Cdd:COG3883   13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA-ELEAL---QAEIDKLQAEIAEAEAEIEERREE- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 676 rkteeklsetkaeketLKKQLVS----------LDLVV----PPQLIKGFDILEgLIAEKTQKTNSRLKNMQSQLSDLSH 741
Cdd:COG3883   88 ----------------LGERARAlyrsggsvsyLDVLLgsesFSDFLDRLSALS-KIADADADLLEELKADKAELEAKKA 150

                        170
                 ....*....|....*....
gi 334184688 742 QINEVKGKASTYKQRLEKK 760
Cdd:COG3883  151 ELEAKLAELEALKAELEAA 169
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 554-699 1.88e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.80  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688  554 ELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVE--RQETEIQD 631
Cdd:pfam07888  42 ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEelSEEKDALL 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334184688  632 KIEALSVVSARELE--------KVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSL 699
Cdd:pfam07888 122 AQRAAHEARIRELEediktltqRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 547-760 2.37e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   547 EAHKKIVELNLHVTEK-EGTLRSEMVDKERLKEEIHRLGCLVKEKENLVQTAENnlatERKKIEVvsqQINDLQSQVERQ 625
Cdd:TIGR02169  269 EIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE----RLAKLEA---EIDKLLAEIEEL 341

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   626 ETEIQDKIEALSVVSARELEKVKGYETkissLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSLDLVVPP 705
Cdd:TIGR02169  342 EREIEEERKRRDKLTEEYAELKEELED----LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 334184688   706 QLIKGFDI---LEGLIAEKTQkTNSRLKNMQSQLSDLSHQINEVKGKASTYKQRLEKK 760
Cdd:TIGR02169  418 LSEELADLnaaIAGIEAKINE-LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
568-700 3.06e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.00  E-value: 3.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 568 SEMVDKERLKEEihrlgclvKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEalsvvsarelekv 647
Cdd:COG2433  383 EELIEKELPEEE--------PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDE------------- 441

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 334184688 648 kgyetKISSLREELELAReslKEMKDEKRKTEEkLSETKAEKETLKKQLVSLD 700
Cdd:COG2433  442 -----RIERLERELSEAR---SEERREIRKDRE-ISRLDREIERLERELEEER 485
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
497-695 3.24e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 3.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 497 HSMLREAYELLLEDLARKEARKSKEDFEDSCVKSVMMEECCSVI--YKEAVKEAHKKIVELNlHVTEKEGTLRSEMVDKE 574
Cdd:COG4717   44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEeeYAELQEELEELEEELE-ELEAELEELREELEKLE 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 575 RLKEEIHRLGCLVKEKENLVQTAE--NNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEALSVVSARELEKVKgyeT 652
Cdd:COG4717  123 KLLQLLPLYQELEALEAELAELPErlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA---E 199

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 334184688 653 KISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQ 695
Cdd:COG4717  200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 429-738 4.11e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.87  E-value: 4.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   429 LKDSLSDAAEKMSQLsQAEADHQELIRKLETDV-EDSRNEA--SIYEdvygcfvtefVGQIKCTKQE----TDLEHSMLR 501
Cdd:pfam15921  108 LRQSVIDLQTKLQEM-QMERDAMADIRRRESQSqEDLRNQLqnTVHE----------LEAAKCLKEDmledSNTQIEQLR 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   502 EAyeLLLEDLARKEARKSKEDFEDSCVKSVMMEECCSVIYKEAVKEAHKKIV-ELNLHVTEKEG----------TLRSEM 570
Cdd:pfam15921  177 KM--MLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILrELDTEISYLKGrifpvedqleALKSES 254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   571 VDKERLKEEIHRlgclvKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERqeteIQDKIEALSVVSARELEKVkgy 650
Cdd:pfam15921  255 QNKIELLLQQHQ-----DRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEI----IQEQARNQNSMYMRQLSDL--- 322

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   651 ETKISSLREELELARESLKEMKDEKRK----TEEKLSETKAEKETLKKQLVSLDlvvppqlikgfDILEGLIAE--KTQK 724
Cdd:pfam15921  323 ESTVSQLRSELREAKRMYEDKIEELEKqlvlANSELTEARTERDQFSQESGNLD-----------DQLQKLLADlhKREK 391

                          330
                   ....*....|....
gi 334184688   725 TNSRLKNMQSQLSD 738
Cdd:pfam15921  392 ELSLEKEQNKRLWD 405
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 605-759 5.32e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 5.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   605 RKKIEVVSQQINDLQSQVERQETEIQDKIEALSvvsaRELEKVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSE 684
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELE----ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   685 TKAEKETLKKQLVSLDLvvppQLIKGFDILEGLIAEKTQ------KTNSRLKNMQSQLSDLSHQINEVKGKASTYKQRLE 758
Cdd:TIGR02168  752 LSKELTELEAEIEELEE----RLEEAEEELAEAEAEIEEleaqieQLKEELKALREALDELRAELTLLNEEAANLRERLE 827


                   .
gi 334184688   759 K 759
Cdd:TIGR02168  828 S 828
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 384-758 5.87e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.49  E-value: 5.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   384 LKKKIPFVISKLDKILMEDEKFVSEGKNdagLKRQLDSLLLENRQLKDSLSDAAEKMSQLSQAEADHQELIRKLETDVED 463
Cdd:pfam15921  347 LEKQLVLANSELTEARTERDQFSQESGN---LDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDD 423

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   464 SRNEASIYEDVYGCFVTEFVGQIKCTKQETDLEHSMLREAYELLLEDLARKEA-RKSKEDFEdscVKSVMMEECCSVI-- 540
Cdd:pfam15921  424 RNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMlRKVVEELT---AKKMTLESSERTVsd 500

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   541 YKEAVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKEKENL-VQTAENNlaterKKIEVVSQQINDLQ 619
Cdd:pfam15921  501 LTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALkLQMAEKD-----KVIEILRQQIENMT 575

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688   620 SQVERQEteiqdkiealSVVSARELEKVKgyetkissLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSL 699
Cdd:pfam15921  576 QLVGQHG----------RTAGAMQVEKAQ--------LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL 637

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 334184688   700 DLVVPPQLIKGFDILEgliaEKTQKTNsRLKNMQSQLSDLSHQINEVKGKASTYKQRLE 758
Cdd:pfam15921  638 VNAGSERLRAVKDIKQ----ERDQLLN-EVKTSRNELNSLSEDYEVLKRNFRNKSEEME 691
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 616-696 6.23e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 6.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688 616 NDLQSQVERQETEIQDKIEALSVVSARELEKVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQ 695
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98


                 .
gi 334184688 696 L 696
Cdd:COG4942   99 L 99
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 586-696 7.75e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 38.51  E-value: 7.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688  586 LVKEKENLVQTAENNLATERKkievvsqqINDLQSQVERQETEIQDKIEALSVVSARE-LEKVKGYETKISSLREELELA 664
Cdd:pfam04012  38 LVKARQALAQTIARQKQLERR--------LEQQTEQAKKLEEKAQAALTKGNEELAREaLAEKKSLEKQAEALETQLAQQ 109

                          90       100       110
                  ....*....|....*....|....*....|..
gi 334184688  665 RESLKEMKDEKRKTEEKLSETKAEKETLKKQL 696
Cdd:pfam04012 110 RSAVEQLRKQLAALETKIQQLKAKKNLLKARL 141
PTZ00121 PTZ00121
MAEBL; Provisional
 500-695 8.25e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 8.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688  500 LREAYELLLEDLARK--EARKSKEDFEDSCVKSvmmeeccsviykEAVKEAHKKIVELNLHVTEKEGTLRSEMVDKErlK 577
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKaeEAKKAEEDKNMALRKA------------EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA--E 1616

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688  578 EEIHRLGCLVKEKEnlvqtaennlatERKKIEVVSQQINDLQSQVER-QETEIQDKIEALSVVSARELEKVKGYETKISs 656
Cdd:PTZ00121 1617 EAKIKAEELKKAEE------------EKKKVEQLKKKEAEEKKKAEElKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA- 1683

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 334184688  657 lREELELARESLKEMKDEKRKTEE---KLSETKAEKETLKKQ 695
Cdd:PTZ00121 1684 -EEDEKKAAEALKKEAEEAKKAEElkkKEAEEKKKAEELKKA 1724
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 490-758 9.18e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.72  E-value: 9.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688  490 KQETDLEHSMLREAYELLLEDLARKEARKSKEDFEDSCVKSVMMEEccSVIYKEAVKEAHKKIVELNlHVTEKEGTLRSE 569
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQ--AAIYAEQERMAMERERELE-RIRQEERKRELE 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688  570 MVDKERLKEEIHRLGCLVK---EKENLVQTAENNLATERK-------KIEVVSQQINDLQSQVERQETEIQDKIEALSVV 639
Cdd:pfam17380 364 RIRQEEIAMEISRMRELERlqmERQQKNERVRQELEAARKvkileeeRQRKIQQQKVEMEQIRAEQEEARQREVRRLEEE 443

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688  640 SARELEKVKGYETKISSLREELELARESLKEMKDEKRKTEEKlsetKAEKETLKKQLVSLDLVVPPQLI----------- 708
Cdd:pfam17380 444 RAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD----RKRAEEQRRKILEKELEERKQAMieeerkrklle 519

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 334184688  709 KGFDILEGLIAEKTQKTNSRLKNMQSQLSDLSHQINEVKGKASTYKQRLE 758
Cdd:pfam17380 520 KEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE 569
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 580-690 9.86e-03

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 37.29  E-value: 9.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184688  580 IHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEAlsVVSARELEKVKGY--------- 650
Cdd:TIGR02473   1 EFRLQKLLDLREKEEEQAKLELAKAQAEFERLETQLQQLIKYREEYEQQALEKVGA--GTSALELSNYQRFirqldqriq 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 334184688  651 --ETKISSLREELELARESLKEMKdEKRKTEEKLSETKAEKE 690
Cdd:TIGR02473  79 qqQQELALLQQEVEAKRERLLEAR-RELKALEKLKEKKQKEY 119
 
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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