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Conserved domains on  [gi|30686193|ref|NP_181020|]
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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 3.23e-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: 56.70  E-value: 3.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 543 EAVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQV 622
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 623 ERQETEIQDKIEALSVVS-----------------ARELEKVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSET 685
Cdd:COG4942 100 EAQKEELAELLRALYRLGrqpplalllspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30686193 686 KAEKETLKKQLVsldlvvppQLIKGFDILEGLIAEKTQKTNSRLKNMQSQLSDLSHQINEVKGKASTYKQR 756
Cdd:COG4942 180 LAELEEERAALE--------ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 380-695 1.87e-04

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.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 1.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    380 ELGALKKKIPFVISKLDKILME-DEKF--VSEGKNDAG-LKRQLDSLLLENRQLKDSLSDAAEKMSQLSQAEADHQELIR 455
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRlDELSqeLSDASRKIGeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    456 KLETDVEDSRNEASIYE----DVYGCFVTEFVGQIKCTKQETDLEHSMLREAYELLLEDLARKEARKSKEDfEDSCVKSV 531
Cdd:TIGR02169  762 ELEARIEELEEDLHKLEealnDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE-KEIQELQE 840

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    532 MMEECCSVI--YKEAVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEIHRLgclvKEKENLVQTAENNLATERKKIE 609
Cdd:TIGR02169  841 QRIDLKEQIksIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL----EAQLRELERKIEELEAQIEKKR 916

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    610 VVSQQINDLQSQVERQETEIQDKIEALSVVSAREL------EKVKGYETKISSLR-------EELELARESLKEMKDEKR 676
Cdd:TIGR02169  917 KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELsledvqAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRA 996

                          330       340
                   ....*....|....*....|..
gi 30686193    677 KTEEK---LSETKAEKETLKKQ 695
Cdd:TIGR02169  997 KLEEErkaILERIEEYEKKKRE 1018
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 543-756 3.23e-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: 56.70  E-value: 3.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 543 EAVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQV 622
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 623 ERQETEIQDKIEALSVVS-----------------ARELEKVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSET 685
Cdd:COG4942 100 EAQKEELAELLRALYRLGrqpplalllspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30686193 686 KAEKETLKKQLVsldlvvppQLIKGFDILEGLIAEKTQKTNSRLKNMQSQLSDLSHQINEVKGKASTYKQR 756
Cdd:COG4942 180 LAELEEERAALE--------ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 541-821 5.02e-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: 5.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    541 YKEAVKEAHKKIVELNLHVTEKEgtlrsemvdKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQS 620
Cdd:TIGR02168  218 LKAELRELELALLVLRLEELREE---------LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    621 QVERQETEIQDK---IEALSVVSARELEKVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLV 697
Cdd:TIGR02168  289 ELYALANEISRLeqqKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    698 SLDLVVpPQLIKGFDILEGLIAEKTQK---TNSRLKNMQSQLSDLSHQINE------------VKGKASTYKQRLEKKCC 762
Cdd:TIGR02168  369 ELESRL-EELEEQLETLRSKVAQLELQiasLNNEIERLEARLERLEDRRERlqqeieellkklEEAELKELQAELEELEE 447

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 30686193    763 DLKKAEAEVDLLGDEVETLLDLLEKIYIALDHYSPILKHYPGIIEILRLVRRELSGESK 821
Cdd:TIGR02168  448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 496-794 1.60e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.58  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    496 EHSMLREAyellLEDLARKEArKSKEDFEDSCVKSVMMEECCSVIYKEAVKEAHKKIVELNLHVTEKEGTL---RSEMVD 572
Cdd:pfam15921  121 EMQMERDA----MADIRRRES-QSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLqeiRSILVD 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    573 KERLKeeihrlGCLVKEKENLVQTAENNLATERKK--------IEVVSQQINDLQSQVERQETEIQDKIEALSVVSAREL 644
Cdd:pfam15921  196 FEEAS------GKKIYEHDSMSTMHFRSLGSAISKilreldteISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRI 269

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    645 EK-VKGYETKISSLREELELARESLKEMKDEKRKTEEklsETKAEKETLKKQLVSLDLVVPpQLIKGFDILEGLIAEKTQ 723
Cdd:pfam15921  270 EQlISEHEVEITGLTEKASSARSQANSIQSQLEIIQE---QARNQNSMYMRQLSDLESTVS-QLRSELREAKRMYEDKIE 345

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30686193    724 KTNSRLKNMQSQLSDLSHQINEVKGKASTYKQRLEKKCCDLKKAEAEVDLLGDEVETLLDLLEKIYIALDH 794
Cdd:pfam15921  346 ELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDH 416
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
543-786 5.91e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 5.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193  543 EAVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLqsqv 622
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL---- 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193  623 ERQETEIQDKIEALSVVSARELEKVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSLDLV 702
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193  703 V---PPQLIKGFDILEgLIAEKTQKTNSRLKNMQSQLSDLSHQINEVK-----GKAST----------------YKQRLE 758
Cdd:PRK02224 400 FgdaPVDLGNAEDFLE-ELREERDELREREAELEATLRTARERVEEAEalleaGKCPEcgqpvegsphvetieeDRERVE 478

                        250       260
                 ....*....|....*....|....*...
gi 30686193  759 KKCCDLKKAEAEVDLLGDEVETLLDLLE 786
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLERAEDLVE 506
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 380-695 1.87e-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: 45.06  E-value: 1.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    380 ELGALKKKIPFVISKLDKILME-DEKF--VSEGKNDAG-LKRQLDSLLLENRQLKDSLSDAAEKMSQLSQAEADHQELIR 455
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRlDELSqeLSDASRKIGeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    456 KLETDVEDSRNEASIYE----DVYGCFVTEFVGQIKCTKQETDLEHSMLREAYELLLEDLARKEARKSKEDfEDSCVKSV 531
Cdd:TIGR02169  762 ELEARIEELEEDLHKLEealnDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE-KEIQELQE 840

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    532 MMEECCSVI--YKEAVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEIHRLgclvKEKENLVQTAENNLATERKKIE 609
Cdd:TIGR02169  841 QRIDLKEQIksIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL----EAQLRELERKIEELEAQIEKKR 916

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    610 VVSQQINDLQSQVERQETEIQDKIEALSVVSAREL------EKVKGYETKISSLR-------EELELARESLKEMKDEKR 676
Cdd:TIGR02169  917 KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELsledvqAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRA 996

                          330       340
                   ....*....|....*....|..
gi 30686193    677 KTEEK---LSETKAEKETLKKQ 695
Cdd:TIGR02169  997 KLEEErkaILERIEEYEKKKRE 1018
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 415-635 2.43e-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: 2.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 415 LKRQLDSLLLENRQLKDSLSDAAEKMSQLSQAEADHQELIRKLETDVEDSRNEASIYEDVYGcfvtefvgqikctkqetd 494
Cdd:COG4942  46 LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA------------------ 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 495 lehSMLREAYelLLEDLARKEARKSKEDFEDScVKSVMMEECCSVIYKEAVKEAHKKIVELNLHVTEKEGTLRSEMVDKE 574
Cdd:COG4942 108 ---ELLRALY--RLGRQPPLALLLSPEDFLDA-VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30686193 575 RLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEA 635
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 543-756 3.23e-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: 56.70  E-value: 3.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 543 EAVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQV 622
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 623 ERQETEIQDKIEALSVVS-----------------ARELEKVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSET 685
Cdd:COG4942 100 EAQKEELAELLRALYRLGrqpplalllspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30686193 686 KAEKETLKKQLVsldlvvppQLIKGFDILEGLIAEKTQKTNSRLKNMQSQLSDLSHQINEVKGKASTYKQR 756
Cdd:COG4942 180 LAELEEERAALE--------ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 541-821 5.02e-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: 5.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    541 YKEAVKEAHKKIVELNLHVTEKEgtlrsemvdKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQS 620
Cdd:TIGR02168  218 LKAELRELELALLVLRLEELREE---------LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    621 QVERQETEIQDK---IEALSVVSARELEKVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLV 697
Cdd:TIGR02168  289 ELYALANEISRLeqqKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    698 SLDLVVpPQLIKGFDILEGLIAEKTQK---TNSRLKNMQSQLSDLSHQINE------------VKGKASTYKQRLEKKCC 762
Cdd:TIGR02168  369 ELESRL-EELEEQLETLRSKVAQLELQiasLNNEIERLEARLERLEDRRERlqqeieellkklEEAELKELQAELEELEE 447

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 30686193    763 DLKKAEAEVDLLGDEVETLLDLLEKIYIALDHYSPILKHYPGIIEILRLVRRELSGESK 821
Cdd:TIGR02168  448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 418-699 5.29e-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: 5.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    418 QLDSLLLENRQLKDSLSDAAEKMSQLSQAEADHQELIRKLETDVEDSR-------NEASIYEDVYGCFVTE---FVGQIK 487
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRlevseleEEIEELQKELYALANEisrLEQQKQ 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    488 CTKQETDLEHSMLREAYELLLEDLARKEarKSKEDFEDSCVKSVMMEECCSVIyKEAVKEAHKKIVELNLHVTEKEgtlr 567
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLD--ELAEELAELEEKLEELKEELESL-EAELEELEAELEELESRLEELE---- 378

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    568 semVDKERLKEEIHRLgclvkekenlvqtaENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEALSVVSAREL-EK 646
Cdd:TIGR02168  379 ---EQLETLRSKVAQL--------------ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELqAE 441

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 30686193    647 VKGYETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSL 699
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 572-787 1.04e-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: 55.83  E-value: 1.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    572 DKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQETEiqdkIEALSVVSARELEKVKGYE 651
Cdd:TIGR02168  685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE----VEQLEERIAQLSKELTELE 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    652 TKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSLDLVVPPQLIKGFDILEGLIAEKTQK--TNSRL 729
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIaaTERRL 840

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 30686193    730 KNMQSQLSDLSHQINEVKGKASTYKQRLEKKCCDLKKAEAEVDLLGDEVETLLDLLEK 787
Cdd:TIGR02168  841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 439-701 1.48e-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: 55.45  E-value: 1.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    439 KMSQLSQAEADHQELIRKLETDVEDSRNEASIYEDVygcfvtefVGQIKCTKQETDLEHSMLREAYELLLEDLARKEARK 518
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEE--------LEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    519 SKEDFEDSCVKSVMMEECCSVI-YKEAVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKEKENLVQTA 597
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEeAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    598 ENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEALsvvsARELEKVKGYETKISSLREELELARESLKEMKDEKRK 677
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI----EELESELEALLNERASLEEALALLRSELEELSEELRE 905

                          250       260
                   ....*....|....*....|....
gi 30686193    678 TEEKLSETKAEKETLKKQLVSLDL 701
Cdd:TIGR02168  906 LESKRSELRRELEELREKLAQLEL 929
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 414-734 1.73e-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: 1.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    414 GLKRQLDSLLLENRQLKDSLSDAAEKMS----QLSQAEADHQELIRKLETDVEDsrneasiyedvygcfVTEFVGQIKCT 489
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRLDELSQELSdasrKIGEIEKEIEQLEQEEEKLKER---------------LEELEEDLSSL 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    490 KQETDLEHSMLREayelLLEDLARKEARKSK-----EDFEDSCVKSVMMEeccSVIYKEAVKEAHKKIVELnlhVTEKEG 564
Cdd:TIGR02169  750 EQEIENVKSELKE----LEARIEELEEDLHKleealNDLEARLSHSRIPE---IQAELSKLEEEVSRIEAR---LREIEQ 819

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    565 TLRSEMVDKERLKEEIhrlgclvKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEALsvvsarel 644
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEI-------QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL-------- 884

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    645 ekvKGYETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSLDLVVP-PQLIKGFDILEGLIAEKTQ 723
Cdd:TIGR02169  885 ---GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGeDEEIPEEELSLEDVQAELQ 961

                          330
                   ....*....|.
gi 30686193    724 KTNSRLKNMQS 734
Cdd:TIGR02169  962 RVEEEIRALEP 972
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 572-781 5.42e-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: 53.53  E-value: 5.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    572 DKERLKEEIHRLGCLVKEKENLVQtaennlatERKKIEVVSQQINDLQSQVERQETEIQDKIEALSVVSARELEKVKGYE 651
Cdd:TIGR02169  672 EPAELQRLRERLEGLKRELSSLQS--------ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    652 TKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKqlvSLDLVVPPQLIKGFDIL-------EGLIAEKTQK 724
Cdd:TIGR02169  744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA---RLSHSRIPEIQAELSKLeeevsriEARLREIEQK 820

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30686193    725 TNSRL----------KNMQSQLSDLSHQINEVKGKASTYKQRLEKKCCDLKKAEAEVDLLGDEVETL 781
Cdd:TIGR02169  821 LNRLTlekeylekeiQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
587-696 1.64e-06

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 49.82  E-value: 1.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 587 VKEKENLVQTAENNLA---TERKKIEvvsQQINDLQSQVErqetEIQDKIEaLSVVSARE------LEKVKGYETKISSL 657
Cdd:COG1842  32 IRDMEEDLVEARQALAqviANQKRLE---RQLEELEAEAE----KWEEKAR-LALEKGREdlareaLERKAELEAQAEAL 103

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 30686193 658 REELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQL 696
Cdd:COG1842 104 EAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARA 142
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 496-794 1.60e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.58  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    496 EHSMLREAyellLEDLARKEArKSKEDFEDSCVKSVMMEECCSVIYKEAVKEAHKKIVELNLHVTEKEGTL---RSEMVD 572
Cdd:pfam15921  121 EMQMERDA----MADIRRRES-QSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLqeiRSILVD 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    573 KERLKeeihrlGCLVKEKENLVQTAENNLATERKK--------IEVVSQQINDLQSQVERQETEIQDKIEALSVVSAREL 644
Cdd:pfam15921  196 FEEAS------GKKIYEHDSMSTMHFRSLGSAISKilreldteISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRI 269

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    645 EK-VKGYETKISSLREELELARESLKEMKDEKRKTEEklsETKAEKETLKKQLVSLDLVVPpQLIKGFDILEGLIAEKTQ 723
Cdd:pfam15921  270 EQlISEHEVEITGLTEKASSARSQANSIQSQLEIIQE---QARNQNSMYMRQLSDLESTVS-QLRSELREAKRMYEDKIE 345

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30686193    724 KTNSRLKNMQSQLSDLSHQINEVKGKASTYKQRLEKKCCDLKKAEAEVDLLGDEVETLLDLLEKIYIALDH 794
Cdd:pfam15921  346 ELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDH 416
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 413-703 1.82e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 1.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 413 AGLKRQLDSLLLENRQLKDSLSDAAEKMSQLSQAEADHQELIRKLETDVEDSRNEASIYEDvygcfvtefvgqikcTKQE 492
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE---------------RLEE 320

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 493 TDLEHSMLREAYELLLEDLARKEARKSKEDFEDSCVKSVMMEEccSVIYKEAVKEAHKKIVELNLHVTEKEGTLRSEMVD 572
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA--EEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 573 KERLKEEIHRLGCLVKEKENLvQTAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEALSVVSARELEKVKGYET 652
Cdd:COG1196 399 AAQLEELEEAEEALLERLERL-EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 30686193 653 KISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSLDLVV 703
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 490-760 2.08e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 2.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 490 KQETDLEHSMLREAYELLLEDLARKEARKSKEDfEDSCVKSVMMEECcsviyKEAVKEAHKKIVELNLHVTEKEGTLRSE 569
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELE-AELEELEAELAEL-----EAELEELRLELEELELELEEAQAEEYEL 293

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 570 MVDKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEALSVVSARELEKVKG 649
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 650 YETKISSLREELELARESLKEMKDEKRK---TEEKLSETKAEKETLKKQLVSLDlvvppQLIKGFDILEGLIAEKTQKTN 726
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQleeLEEAEEALLERLERLEEELEELE-----EALAELEEEEEEEEEALEEAA 448

                       250       260       270
                ....*....|....*....|....*....|....
gi 30686193 727 SRLKNMQSQLSDLSHQINEVKGKASTYKQRLEKK 760
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 561-696 4.29e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 4.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 561 EKEGTLRSEMVDKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQETEIQ---------- 630
Cdd:COG3883  20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralyrsg 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 631 -------------------DKIEALSVVSARELEKVKGYET---KISSLREELELARESLKEMKDEKRKTEEKLSETKAE 688
Cdd:COG3883 100 gsvsyldvllgsesfsdflDRLSALSKIADADADLLEELKAdkaELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179


                ....*...
gi 30686193 689 KETLKKQL 696
Cdd:COG3883 180 QEALLAQL 187
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
566-759 4.77e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 4.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193  566 LRSEMVDKERLKEEIHRLgclVKEKENLVQtAENNLATERKKIEVVsQQINDLQSQVERQETEIqDKIEALsvVSARELE 645
Cdd:COG4913  213 VREYMLEEPDTFEAADAL---VEHFDDLER-AHEALEDAREQIELL-EPIRELAERYAAARERL-AELEYL--RAALRLW 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193  646 KVkgyETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSLDlvvppqlikgfdilegliaektqkt 725
Cdd:COG4913  285 FA---QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG------------------------- 336

                        170       180       190
                 ....*....|....*....|....*....|....
gi 30686193  726 NSRLKNMQSQLSDLSHQINEVKGKASTYKQRLEK 759
Cdd:COG4913  337 GDRLEQLEREIERLERELEERERRRARLEALLAA 370
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 605-788 5.16e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 5.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    605 RKKIEVVSQQINDLQSQVERQETEIQDKIEALSvvsaRELEKVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSE 684
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELE----ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    685 TKAEKETLKKQLVSLDLvvppQLIKGFDILEGLIAEKtQKTNSRLKNMQSQLSDLSHQINEVKGKASTYKQRLEKKCCDL 764
Cdd:TIGR02168  752 LSKELTELEAEIEELEE----RLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826

                          170       180
                   ....*....|....*....|....
gi 30686193    765 KKAEAEVDLLGDEVETLLDLLEKI 788
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEEL 850
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 509-702 5.50e-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: 47.02  E-value: 5.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193   509 EDLARKEARKSKEDFEDSCVKSVMMEECCSVIY---KEAVKEAHKKIVELNLH--------------------VTEKEGT 565
Cdd:pfam05483 466 EEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLlenKELTQEASDMTLELKKHqediinckkqeermlkqienLEEKEMN 545

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193   566 LRSEMVD-KERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQET---EIQDKIEALSVVSA 641
Cdd:pfam05483 546 LRDELESvREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKnieELHQENKALKKKGS 625

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30686193   642 RELEKVKGYETKISSLREELELARESLKEMKDEKRKTEE--KLSETKAEKETLKKQLVSLDLV 702
Cdd:pfam05483 626 AENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEdkKISEEKLLEEVEKAKAIADEAV 688
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
543-786 5.91e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 5.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193  543 EAVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLqsqv 622
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL---- 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193  623 ERQETEIQDKIEALSVVSARELEKVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSLDLV 702
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193  703 V---PPQLIKGFDILEgLIAEKTQKTNSRLKNMQSQLSDLSHQINEVK-----GKAST----------------YKQRLE 758
Cdd:PRK02224 400 FgdaPVDLGNAEDFLE-ELREERDELREREAELEATLRTARERVEEAEalleaGKCPEcgqpvegsphvetieeDRERVE 478

                        250       260
                 ....*....|....*....|....*...
gi 30686193  759 KKCCDLKKAEAEVDLLGDEVETLLDLLE 786
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLERAEDLVE 506
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
595-788 6.54e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.55  E-value: 6.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 595 QTAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEalsvvsarelekvkgyETKISSLREELELARESLKEMKDE 674
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQ----------------KNGLVDLSEEAKLLLQQLSELESQ 227

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 675 KRKTEEKLSETKAEKETLKKQLVSLDLVVP--------PQLIKGFDILEGLIAEKTQK---TNSRLKNMQSQLSDLSHQI 743
Cdd:COG3206 228 LAEARAELAEAEARLAALRAQLGSGPDALPellqspviQQLRAQLAELEAELAELSARytpNHPDVIALRAQIAALRAQL 307

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 30686193 744 NEVKGKAstykqrlekkccdLKKAEAEVDLLGDEVETLLDLLEKI 788
Cdd:COG3206 308 QQEAQRI-------------LASLEAELEALQAREASLQAQLAQL 339
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 547-778 1.17e-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: 45.83  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    547 EAHKKIVELNLHVTEK-EGTLRSEMVDKERLKEEIHRLGCLVKEKENLVQTAENnlatERKKIEVvsqQINDLQSQVERQ 625
Cdd:TIGR02169  269 EIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE----RLAKLEA---EIDKLLAEIEEL 341

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    626 ETEIQDKIEALSVVSARELEKVKGYETkissLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSLDLVVPP 705
Cdd:TIGR02169  342 EREIEEERKRRDKLTEEYAELKEELED----LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    706 QLIKGFDI---LEGLIAEKTQ-------------KTNSRLKNMQSQLSDLSHQINEVKGKASTYKQRLEKKCCDLKKAEA 769
Cdd:TIGR02169  418 LSEELADLnaaIAGIEAKINEleeekedkaleikKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA 497


                   ....*....
gi 30686193    770 EVDLLGDEV 778
Cdd:TIGR02169  498 QARASEERV 506
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 587-779 1.43e-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: 1.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 587 VKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQETEI---QDKIEALSVVSARELEKVKG-----YET------ 652
Cdd:COG3883  25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIdklQAEIAEAEAEIEERREELGEraralYRSggsvsy 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 653 ---------------KISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSLDlvvppqlikgfdilegl 717
Cdd:COG3883 105 ldvllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE----------------- 167

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30686193 718 iaektqktnSRLKNMQSQLSDLSHQINEVKGKASTYKQRLEKKCCDLKKAEAEVDLLGDEVE 779
Cdd:COG3883 168 ---------AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 427-771 1.64e-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: 45.49  E-value: 1.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    427 RQLKDSLSDAAEKMSQLSQAEADHQELIRKLETDVEDSRNEASiyedvygcfvtefvgQIKCTKQETDLEHSMLREAYEL 506
Cdd:pfam15921  317 RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELT---------------EARTERDQFSQESGNLDDQLQK 381

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    507 LLEDLARKEARKSKEdfedscvksvmmeeccsviykeavKEAHKKIVELNLHVTEKEGTLRSEMVDKERlkeEIHRLGCL 586
Cdd:pfam15921  382 LLADLHKREKELSLE------------------------KEQNKRLWDRDTGNSITIDHLRRELDDRNM---EVQRLEAL 434

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    587 VKEKENLVQ-TAENNLATERKKIEVVsQQINDLQSQVERQETEIQDKIEALS----------------VVSARELEK-VK 648
Cdd:pfam15921  435 LKAMKSECQgQMERQMAAIQGKNESL-EKVSSLTAQLESTKEMLRKVVEELTakkmtlessertvsdlTASLQEKERaIE 513

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    649 GYETKISSLREELELARESLKEMKDEkrktEEKLSETKAEKETLKKQLVSLDLVVppqlikgfDILEGLIAEKTQKTNSR 728
Cdd:pfam15921  514 ATNAEITKLRSRVDLKLQELQHLKNE----GDHLRNVQTECEALKLQMAEKDKVI--------EILRQQIENMTQLVGQH 581

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 30686193    729 LKN---MQSQLSDLSHQINEVKGKASTYKQRLEKKCCDLKKAEAEV 771
Cdd:pfam15921  582 GRTagaMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARV 627
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 380-695 1.87e-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: 45.06  E-value: 1.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    380 ELGALKKKIPFVISKLDKILME-DEKF--VSEGKNDAG-LKRQLDSLLLENRQLKDSLSDAAEKMSQLSQAEADHQELIR 455
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRlDELSqeLSDASRKIGeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    456 KLETDVEDSRNEASIYE----DVYGCFVTEFVGQIKCTKQETDLEHSMLREAYELLLEDLARKEARKSKEDfEDSCVKSV 531
Cdd:TIGR02169  762 ELEARIEELEEDLHKLEealnDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE-KEIQELQE 840

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    532 MMEECCSVI--YKEAVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEIHRLgclvKEKENLVQTAENNLATERKKIE 609
Cdd:TIGR02169  841 QRIDLKEQIksIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL----EAQLRELERKIEELEAQIEKKR 916

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    610 VVSQQINDLQSQVERQETEIQDKIEALSVVSAREL------EKVKGYETKISSLR-------EELELARESLKEMKDEKR 676
Cdd:TIGR02169  917 KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELsledvqAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRA 996

                          330       340
                   ....*....|....*....|..
gi 30686193    677 KTEEK---LSETKAEKETLKKQ 695
Cdd:TIGR02169  997 KLEEErkaILERIEEYEKKKRE 1018
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 645-793 2.20e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 2.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 645 EKVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLvsldlvvppqlikgfDILEGLIAEKTQK 724
Cdd:COG3883  23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---------------AEAEAEIEERREE 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 725 TNSRLKNMQSQLSDLS--------------------------------HQINEVKGKASTYKQRLEKKCCDLKKAEAEVD 772
Cdd:COG3883  88 LGERARALYRSGGSVSyldvllgsesfsdfldrlsalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELE 167

                       170       180
                ....*....|....*....|.
gi 30686193 773 LLGDEVETLLDLLEKIYIALD 793
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLS 188
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 415-635 2.43e-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: 2.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 415 LKRQLDSLLLENRQLKDSLSDAAEKMSQLSQAEADHQELIRKLETDVEDSRNEASIYEDVYGcfvtefvgqikctkqetd 494
Cdd:COG4942  46 LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA------------------ 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 495 lehSMLREAYelLLEDLARKEARKSKEDFEDScVKSVMMEECCSVIYKEAVKEAHKKIVELNLHVTEKEGTLRSEMVDKE 574
Cdd:COG4942 108 ---ELLRALY--RLGRQPPLALLLSPEDFLDA-VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30686193 575 RLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEA 635
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 596-788 4.12e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 4.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 596 TAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEALSVVSArELEKVkgyETKISSLREELELARESLKEMKDEk 675
Cdd:COG3883  13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA-ELEAL---QAEIDKLQAEIAEAEAEIEERREE- 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 676 rkteeklsetkaeketLKKQLVS----------LDLVV----PPQLIKGFDILEgLIAEKTQKTNSRLKNMQSQLSDLSH 741
Cdd:COG3883  88 ----------------LGERARAlyrsggsvsyLDVLLgsesFSDFLDRLSALS-KIADADADLLEELKADKAELEAKKA 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 30686193 742 QINEVKGKASTYKQRLEKKCCDLKK----AEAEVDLLGDEVETLLDLLEKI 788
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAqqaeQEALLAQLSAEEAAAEAQLAEL 201
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
543-788 4.45e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 4.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193  543 EAVKEAHKKIVELNLHVTEKEGTLRSEMVDKER-LKEEIHRLGCLVKEKENLvqtaENNLATERKKIEVVSQQINDLQSQ 621
Cdd:PRK03918 503 EQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIkLKGEIKSLKKELEKLEEL----KKKLAELEKKLDELEEELAELLKE 578

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193  622 VERQETEIQDKIEAlsvvSARELEKVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSLDL 701
Cdd:PRK03918 579 LEELGFESVEELEE----RLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193  702 VVPPQLIKGfdileglIAEKTQKTNSRLKNMQSQLSDLSHQINEVKGKASTYKQRLEKkccdLKKAEAEVDLLGDEVETL 781
Cdd:PRK03918 655 KYSEEEYEE-------LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE----REKAKKELEKLEKALERV 723


                 ....*..
gi 30686193  782 LDLLEKI 788
Cdd:PRK03918 724 EELREKV 730
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 377-794 4.76e-04

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: 44.01  E-value: 4.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    377 KDKELGALKKKIPFVISKLDKILMEDEKFVSEGKNdagLKRQLDSLLLENR-QLKDSLSDAAEKMSQLSQAEADHQELIR 455
Cdd:pfam01576  174 KAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEK---AKRKLEGESTDLQeQIAELQAQIAELRAQLAKKEEELQAALA 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    456 KLETDVEDSRN--------EASIYEdVYGCFVTEFVGQIKCTKQETDL--EHSMLREAYELLLEDLARKEARKSKEDFED 525
Cdd:pfam01576  251 RLEEETAQKNNalkkirelEAQISE-LQEDLESERAARNKAEKQRRDLgeELEALKTELEDTLDTTAAQQELRSKREQEV 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    526 SCVKSVMMEEccSVIYKEAVKEAHKK----IVELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKekenLVQTAENNL 601
Cdd:pfam01576  330 TELKKALEEE--TRSHEAQLQEMRQKhtqaLEELTEQLEQAKRNKANLEKAKQALESENAELQAELR----TLQQAKQDS 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    602 ATERKKIEVVSQQINDLQSQVERQETEIQDKIEALSVvsarELEKVKGY----ETK-------ISSLREELELARESLKE 670
Cdd:pfam01576  404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQS----ELESVSSLlneaEGKniklskdVSSLESQLQDTQELLQE 479

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    671 MKDEKRKTEEKLSETKAEKETLKKQLVSLdlvvppqlikgfdilegliAEKTQKTNSRLKNMQSQLSDLSHQINEVKGKA 750
Cdd:pfam01576  480 ETRQKLNLSTRLRQLEDERNSLQEQLEEE-------------------EEAKRNVERQLSTLQAQLSDMKKKLEEDAGTL 540

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 30686193    751 ST-------YKQRLEKKCCDLKKAEAEVDLLGDEVETLLDLLEKIYIALDH 794
Cdd:pfam01576  541 EAleegkkrLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDH 591
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
503-818 4.80e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 4.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193  503 AYELLLEdlARKEARKSKEDFEDSCVKSVMMEECCSVIYKE--AVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEI 580
Cdd:PRK03918 163 AYKNLGE--VIKEIKRRIERLEKFIKRTENIEELIKEKEKEleEVLREINEISSELPELREELEKLEKEVKELEELKEEI 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193  581 HRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQEtEIQDKIEALSVVSA------RELEKVKGYETKI 654
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEfyeeylDELREIEKRLSRL 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193  655 SSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSLDLV-----------------VPPQLIKGFDILEGL 717
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAkakkeelerlkkrltglTPEKLEKELEELEKA 399

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193  718 ---IAEKTQKTNSRLKNMQSQLSDLSHQINEVKGKAST------------YKQRLEKKCCDLKKAEAEVDLLGDEVETLL 782
Cdd:PRK03918 400 keeIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLR 479

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 30686193  783 DLLEKIYIALDHYSPILKHYPgIIEILRLVRRELSG 818
Cdd:PRK03918 480 KELRELEKVLKKESELIKLKE-LAEQLKELEEKLKK 514
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
574-756 6.54e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 6.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193  574 ERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQInDLQsQVERQETEIQDKIEALSVVSA--RELEKvkgye 651
Cdd:COG4913  620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-DVA-SAEREIAELEAELERLDASSDdlAALEE----- 692

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193  652 tKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSLDLVVPPQLIKGFD------ILEGLIAEKTQKT 725
Cdd:COG4913  693 -QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerfaaaLGDAVERELRENL 771

                        170       180       190
                 ....*....|....*....|....*....|.
gi 30686193  726 NSRLKNMQSQLSDLSHQINEvkgKASTYKQR 756
Cdd:COG4913  772 EERIDALRARLNRAEEELER---AMRAFNRE 799
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
 487-696 7.18e-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: 42.74  E-value: 7.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193   487 KCTKQETDLEHSMLReAYELLLEDLARKEARKSKedfedscvkSVMMEECCSViyKEAVKEAHKKIVEL--NLHVTEKEG 564
Cdd:pfam15742  77 MCSSLTAEWKHCQQK-IRELELEVLKQAQSIKSQ---------NSLQEKLAQE--KSRVADAEEKILELqqKLEHAHKVC 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193   565 TLRSEMVDKERLKEEIHRLgclvkeKENLVQTaENNLATERKKIEVVSQQINDLQSQVerqeTEIQDKIEALSVVSAREL 644
Cdd:pfam15742 145 LTDTCILEKKQLEERIKEA------SENEAKL-KQQYQEEQQKRKLLDQNVNELQQQV----RSLQDKEAQLEMTNSQQQ 213

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 30686193   645 EKVKGYETKISSLREELELARESLKEmkdeKRKTEEKLSETKAEKETLKKQL 696
Cdd:pfam15742 214 LRIQQQEAQLKQLENEKRKSDEHLKS----NQELSEKLSSLQQEKEALQEEL 261
PRK12704 PRK12704
phosphodiesterase; Provisional
 540-684 9.21e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 9.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193  540 IYKEAVKEAHKKIVELNLHVTEKEGTLRSEMvDKERL--KEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQIND 617
Cdd:PRK12704  43 ILEEAKKEAEAIKKEALLEAKEEIHKLRNEF-EKELRerRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQ 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30686193  618 LQSQVERQETEIQDKIEALsvvsARELEKVKGY---ETK---ISSLREELELARESL-KEMKDEKRKTEEKLSE 684
Cdd:PRK12704 122 KQQELEKKEEELEELIEEQ----LQELERISGLtaeEAKeilLEKVEEEARHEAAVLiKEIEEEAKEEADKKAK 191
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 616-787 9.87e-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: 42.44  E-value: 9.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 616 NDLQSQVERQETEIQDKIEALSVVSARELEKVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQ 695
Cdd:COG4942  19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 696 LV--------------------SLDLVVPPQLIKGFDILEGLIAEKTQKTNSRLKNMQSQLSDLshqiNEVKGKASTYKQ 755
Cdd:COG4942  99 LEaqkeelaellralyrlgrqpPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL----AALRAELEAERA 174

                       170       180       190
                ....*....|....*....|....*....|..
gi 30686193 756 RLEKKCCDLKKAEAEVDLLGDEVETLLDLLEK 787
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEK 206
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
565-699 2.29e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 2.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 565 TLRSEMVDKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEALSVVSarel 644
Cdd:COG4372  32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ---- 107

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 30686193 645 EKVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSL 699
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 554-699 2.63e-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: 41.03  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193   554 ELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVE--RQETEIQD 631
Cdd:pfam07888  42 ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEelSEEKDALL 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30686193   632 KIEALSVVSARELE--------KVKGYETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSL 699
Cdd:pfam07888 122 AQRAAHEARIRELEediktltqRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 384-772 2.64e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.64  E-value: 2.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    384 LKKKIPFVISKLDKILMEDEKFVSEGKNdagLKRQLDSLLLENRQLKDSLSDAAEKMSQLSQAEADHQELIRKLETDVED 463
Cdd:pfam15921  347 LEKQLVLANSELTEARTERDQFSQESGN---LDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDD 423

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    464 SRNEASIYEDVYGCFVTEFVGQIKCTKQETDLEHSMLREAYELLLEDLARKEA-RKSKEDFEdscVKSVMMEECCSVI-- 540
Cdd:pfam15921  424 RNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMlRKVVEELT---AKKMTLESSERTVsd 500

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    541 YKEAVKEAHKKIVELNLHVTEKEGTLRSEMVDKERLKEEIHRLGCLVKEKENL-VQTAENNlaterKKIEVVSQQINDLQ 619
Cdd:pfam15921  501 LTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALkLQMAEKD-----KVIEILRQQIENMT 575

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193    620 SQVERQEteiqdkiealSVVSARELEKVKgyetkissLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVSL 699
Cdd:pfam15921  576 QLVGQHG----------RTAGAMQVEKAQ--------LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL 637

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30686193    700 DLVVPPQLIKGFDILEgliaEKTQKTNsRLKNMQSQLSDLSHQINEVKGKASTYKQRLE----KKCCDLKKAEAEVD 772
Cdd:pfam15921  638 VNAGSERLRAVKDIKQ----ERDQLLN-EVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtttnKLKMQLKSAQSELE 709
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
568-700 4.09e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.61  E-value: 4.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 568 SEMVDKERLKEEihrlgclvKEKENLVQTAENNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEalsvvsarelekv 647
Cdd:COG2433 383 EELIEKELPEEE--------PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDE------------- 441

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 30686193 648 kgyetKISSLREELELAReslKEMKDEKRKTEEkLSETKAEKETLKKQLVSLD 700
Cdd:COG2433 442 -----RIERLERELSEAR---SEERREIRKDRE-ISRLDREIERLERELEEER 485
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 597-788 4.62e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 4.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 597 AENNLATERKKIEVVSQQINDLQSQVERQE--TEIQDKIEALsvvsareleKVKGYETKISSLREELELARESLKEMKDE 674
Cdd:COG1196 184 TEENLERLEDILGELERQLEPLERQAEKAEryRELKEELKEL---------EAELLLLKLRELEAELEELEAELEELEAE 254

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 675 KRKTEEKLSETKAEKETLKKQLVSLDLVVPpQLIKGFDILEGLIAEKTQKTNS---RLKNMQSQLSDLSHQINEVKGKAS 751
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELE-EAQAEEYELLAELARLEQDIARleeRRRELEERLEELEEELAELEEELE 333

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 30686193 752 TYKQRLEKKCCDLKKAEAEVDLLGDEVETLLDLLEKI 788
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
497-695 5.46e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 5.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 497 HSMLREAYELLLEDLARKEARKSKEDFEDSCVKSVMMEECCSVI--YKEAVKEAHKKIVELNlHVTEKEGTLRSEMVDKE 574
Cdd:COG4717  44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEeeYAELQEELEELEEELE-ELEAELEELREELEKLE 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193 575 RLKEEIHRLGCLVKEKENLVQTAE--NNLATERKKIEVVSQQINDLQSQVERQETEIQDKIEALSVVSARELEKVKgyeT 652
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPErlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA---E 199

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 30686193 653 KISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQ 695
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 545-781 7.59e-03

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: 40.00  E-value: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193   545 VKEAHKKIVELNLHVTEkegtLRSEMVDKERLKEE--IHRLGCLVKEKENLVQTAENNLATERKKIEVVSQQINDLQSQV 622
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQ----LKSEISDLNNQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEL 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193   623 ERQETEIQDKIEALSvVSARELEKVK----GYETKISSLREELELARESLKEMKDEKRKTEEKLSETKAEKETLKKQLVS 698
Cdd:TIGR04523 352 TNSESENSEKQRELE-EKQNEIEKLKkenqSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193   699 LDlvvpPQLIKGFDILEGLIAEKTQK------TNSRLKNMQSQLSDLSHQINEVKGKASTYKQRLEKKCCDLKKAEAEVD 772
Cdd:TIGR04523 431 LK----ETIIKNNSEIKDLTNQDSVKeliiknLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506


                  ....*....
gi 30686193   773 LLGDEVETL 781
Cdd:TIGR04523 507 ELEEKVKDL 515
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 490-758 9.03e-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: 9.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193   490 KQETDLEHSMLREAYELLLEDLARKEARKSKEDFEDSCVKSVMMEEccSVIYKEAVKEAHKKIVELNlHVTEKEGTLRSE 569
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQ--AAIYAEQERMAMERERELE-RIRQEERKRELE 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193   570 MVDKERLKEEIHRLGCLVK---EKENLVQTAENNLATERK-------KIEVVSQQINDLQSQVERQETEIQDKIEALSVV 639
Cdd:pfam17380 364 RIRQEEIAMEISRMRELERlqmERQQKNERVRQELEAARKvkileeeRQRKIQQQKVEMEQIRAEQEEARQREVRRLEEE 443

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686193   640 SARELEKVKGYETKISSLREELELARESLKEMKDEKRKTEEKlsetKAEKETLKKQLVSLDLVVPPQLI----------- 708
Cdd:pfam17380 444 RAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD----RKRAEEQRRKILEKELEERKQAMieeerkrklle 519

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 30686193   709 KGFDILEGLIAEKTQKTNSRLKNMQSQLSDLSHQINEVKGKASTYKQRLE 758
Cdd:pfam17380 520 KEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE 569
 
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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