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Conserved domains on  [gi|15238455|ref|NP_196137|]
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myosin heavy chain, striated protein [Arabidopsis thaliana]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000095)

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
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 159-401 1.08e-10

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: 63.92  E-value: 1.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    159 RDIAIETERKRVLEVQRQVVDLETELSDLSFKFEHLVNEHEVSRDCLDVSFSEISKLREMLcdcqQNFSIEKTKLVDQIK 238
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL----ARLEAEVEQLEERIA 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    239 HSEAEKMEMQRKEVELQAEISALKTDLATRGEHIEALNKDFDKHKLRYDMLMAEKDGVCAEVDNLKAEMRSRDIQIQQME 318
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    319 EQLNQLVYKQTELVSESGNAKNTVEELKAVVK-------ELEIEVELQSKAKKTVEELRAtvwEMEKHAELQRNAISQGE 391
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEeleelieELESELEALLNERASLEEALA---LLRSELEELSEELRELE 907

                          250
                   ....*....|
gi 15238455    392 EEKREAIRQL 401
Cdd:TIGR02168  908 SKRSELRREL 917
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 159-401 1.08e-10

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: 63.92  E-value: 1.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    159 RDIAIETERKRVLEVQRQVVDLETELSDLSFKFEHLVNEHEVSRDCLDVSFSEISKLREMLcdcqQNFSIEKTKLVDQIK 238
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL----ARLEAEVEQLEERIA 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    239 HSEAEKMEMQRKEVELQAEISALKTDLATRGEHIEALNKDFDKHKLRYDMLMAEKDGVCAEVDNLKAEMRSRDIQIQQME 318
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    319 EQLNQLVYKQTELVSESGNAKNTVEELKAVVK-------ELEIEVELQSKAKKTVEELRAtvwEMEKHAELQRNAISQGE 391
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEeleelieELESELEALLNERASLEEALA---LLRSELEELSEELRELE 907

                          250
                   ....*....|
gi 15238455    392 EEKREAIRQL 401
Cdd:TIGR02168  908 SKRSELRREL 917
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 145-401 6.36e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 6.36e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 145 LRGEREIAQGEIAIRdiAIETERKRVLEVQRQVVDLETELSDLSFKFEHLVNEHEVSRDCLDVSFSEISKLREMLcdcqQ 224
Cdd:COG1196 218 LKEELKELEAELLLL--KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE----Y 291

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 225 NFSIEKTKLVDQIKHSEAEKMEMQRKEVELQAEISALKTDLATRGEHIEALNKDFDKhklrydmLMAEKDGVCAEVDNLK 304
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-------AEEELEEAEAELAEAE 364

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 305 AEMRSRDIQIQQMEEQLNQLVYKQTELVSESGNAKNTVEELKAVVKELEIEVELQSKAKKTVEELRATVWEMEKHAELQR 384
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444

                       250
                ....*....|....*..
gi 15238455 385 NAISQGEEEKREAIRQL 401
Cdd:COG1196 445 EEAAEEEAELEEEEEAL 461
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
157-371 3.26e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 3.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455  157 AIRDIAIETERKRVLEVQRQVVDLETELSDLSFKFEHL-----------------VNEHEVSRDCLDVSFSEISKLREML 219
Cdd:PRK02224 188 SLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYeeqreqaretrdeadevLEEHEERREELETLEAEIEDLRETI 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455  220 CDCQQnfsiEKTKLVDQIKHS----------------------------EAEKMEMQRKEVELQAEISALKTDLATRGEH 271
Cdd:PRK02224 268 AETER----EREELAEEVRDLrerleeleeerddllaeaglddadaeavEARREELEDRDEELRDRLEECRVAAQAHNEE 343

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455  272 IEALNKDFDKHKLRYDMLMAEKDGVCAEVDNLKAEMRSRDIQIQQMEEQLNQLVYKQTELVSESGNAKNTVEEL-----K 346
Cdd:PRK02224 344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELreerdE 423

                        250       260
                 ....*....|....*....|....*
gi 15238455  347 AVVKELEIEVELQSkAKKTVEELRA 371
Cdd:PRK02224 424 LREREAELEATLRT-ARERVEEAEA 447
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 254-401 8.44e-04

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 41.25  E-value: 8.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455   254 LQAEISALKTDLATRGEHIEALNKDFDkhklRYDMLMAEKDGVCAEVDN-------LKAEMRSRDIQIQQMEEQLNQLVY 326
Cdd:pfam00529  56 YQAALDSAEAQLAKAQAQVARLQAELD----RLQALESELAISRQDYDGataqlraAQAAVKAAQAQLAQAQIDLARRRV 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15238455   327 kqteLVSESGNAKNTVEELKAVVKELEIEVElqsKAKKTVEELRATVWEMEKH-AELQRNAISQGEEEKREAIRQL 401
Cdd:pfam00529 132 ----LAPIGGISRESLVTAGALVAQAQANLL---ATVAQLDQIYVQITQSAAEnQAEVRSELSGAQLQIAEAEAEL 200
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 159-401 1.08e-10

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: 63.92  E-value: 1.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    159 RDIAIETERKRVLEVQRQVVDLETELSDLSFKFEHLVNEHEVSRDCLDVSFSEISKLREMLcdcqQNFSIEKTKLVDQIK 238
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL----ARLEAEVEQLEERIA 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    239 HSEAEKMEMQRKEVELQAEISALKTDLATRGEHIEALNKDFDKHKLRYDMLMAEKDGVCAEVDNLKAEMRSRDIQIQQME 318
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    319 EQLNQLVYKQTELVSESGNAKNTVEELKAVVK-------ELEIEVELQSKAKKTVEELRAtvwEMEKHAELQRNAISQGE 391
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEeleelieELESELEALLNERASLEEALA---LLRSELEELSEELRELE 907

                          250
                   ....*....|
gi 15238455    392 EEKREAIRQL 401
Cdd:TIGR02168  908 SKRSELRREL 917
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 166-425 1.04e-09

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: 60.85  E-value: 1.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    166 ERKRVLEVQRQVVDLETELSDLSFKFEHLVNEHEVSRDCLDV---SFSEISKLREMLCDCQQNFSIEKTKLVDQIKHSEA 242
Cdd:TIGR02169  672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDasrKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    243 EKMEMQRKEVELQAEISALKTDLATRGEHIEALNKDFDKHKLRYdmlmaekdgVCAEVDNLKAEMRSRDIQIQQMEEQLN 322
Cdd:TIGR02169  752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPE---------IQAELSKLEEEVSRIEARLREIEQKLN 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    323 QLVYKQTELVSESGNAKNTVEELKAVVKELEIEVE-LQSKAKKT---VEELRATVWEMEK-HAELQR---NAISQGEEEK 394
Cdd:TIGR02169  823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnLNGKKEELeeeLEELEAALRDLESrLGDLKKerdELEAQLRELE 902

                          250       260       270
                   ....*....|....*....|....*....|.
gi 15238455    395 REaIRQLCFSLDHYKSGYKQLLWYLSGNNQQ 425
Cdd:TIGR02169  903 RK-IEELEAQIEKKRKRLSELKAKLEALEEE 932
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 145-401 6.36e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 6.36e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 145 LRGEREIAQGEIAIRdiAIETERKRVLEVQRQVVDLETELSDLSFKFEHLVNEHEVSRDCLDVSFSEISKLREMLcdcqQ 224
Cdd:COG1196 218 LKEELKELEAELLLL--KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE----Y 291

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 225 NFSIEKTKLVDQIKHSEAEKMEMQRKEVELQAEISALKTDLATRGEHIEALNKDFDKhklrydmLMAEKDGVCAEVDNLK 304
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-------AEEELEEAEAELAEAE 364

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 305 AEMRSRDIQIQQMEEQLNQLVYKQTELVSESGNAKNTVEELKAVVKELEIEVELQSKAKKTVEELRATVWEMEKHAELQR 384
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444

                       250
                ....*....|....*..
gi 15238455 385 NAISQGEEEKREAIRQL 401
Cdd:COG1196 445 EEAAEEEAELEEEEEAL 461
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 100-395 1.86e-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: 56.61  E-value: 1.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    100 ELMKKYVQCEEELRTTSLKLQEFEQEIEKLKETEkkesvvlfgEYLRGEREIAQGEIAIRDIAIETERKRVLEVQRQVVD 179
Cdd:TIGR02169  706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL---------EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    180 LETELSDLsfkfEHLVNEHEV--SRDCLDVSFSEISKLREMLCDCQQNFS---IEKTKLVDQIKHSEAEKMEMQRKEVEL 254
Cdd:TIGR02169  777 LEEALNDL----EARLSHSRIpeIQAELSKLEEEVSRIEARLREIEQKLNrltLEKEYLEKEIQELQEQRIDLKEQIKSI 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    255 QAEISALKTDlatrgehIEALNKDFDKHKLRYDMLMAEKDGVCAEVDNLKAEMRSRDIQIQQMEEQLNQLVYKQTELVSE 334
Cdd:TIGR02169  853 EKEIENLNGK-------KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15238455    335 SGNAKNTVEELKAVVKELEIEVELQSKAKKTVEELRATVWEMEKHAELQRNAISQGEEEKR 395
Cdd:TIGR02169  926 LEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLK 986
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 89-397 3.36e-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: 55.84  E-value: 3.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455     89 DLSPEKQ-MSYEELMKKYVQCEEELRTTSLKLQEFEQEIEKLKETEKKEsvvlfgeylrgEREIAQGEIAIRDIAIETER 167
Cdd:TIGR02169  215 ALLKEKReYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISEL-----------EKRLEEIEQLLEELNKKIKD 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    168 K---RVLEVQRQVVDLETELSDLSFKFEHLVNEHEVSRDCLDVSFSEISKLR---EMLCDCQQNFSIEKTKLVDQIKHSE 241
Cdd:TIGR02169  284 LgeeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLaeiEELEREIEEERKRRDKLTEEYAELK 363

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    242 AEKMEMQRKEVELQAEISALKTDLATRGEHIEALNKDFDKHKLRYDMLMAEKDGVCAEVDNLKAEMRSRDIQIQQMEEQL 321
Cdd:TIGR02169  364 EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15238455    322 NQlvyKQTELVSESGNAKNTVEELKAVVKELEievELQSKAKKTVEELRATVWEMEKhAELQRNAISQGEEEKREA 397
Cdd:TIGR02169  444 ED---KALEIKKQEWKLEQLAADLSKYEQELY---DLKEEYDRVEKELSKLQRELAE-AEAQARASEERVRGGRAV 512
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 101-415 3.97e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 3.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    101 LMKKYVQCEEELRTTSLKLQEFEQeieklketekkesvvlfgeylrgEREIAQGEIAIRDIAIETERKRVLEVQRQVVDL 180
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEE-----------------------ELEELTAELQELEEKLEELRLEVSELEEEIEEL 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    181 ETELSDLSfkfehlvnehevsrdcldvsfSEISKLREMLcdcqQNFSIEKTKLVDQIKHSEAEKMEMQRKEVELQAEISA 260
Cdd:TIGR02168  287 QKELYALA---------------------NEISRLEQQK----QILRERLANLERQLEELEAQLEELESKLDELAEELAE 341

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    261 LKTDLATRGEHIEALNKDFDKHKLRYDMLMAEKDGVCAEVDNLKAEMRSRDIQIQQMEEQLNQLVYKQTELVSESGNAKN 340
Cdd:TIGR02168  342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15238455    341 TVEELkavvkeleiEVELQSKAKKTVEELRATVWEMEKHAELQRNAISQGEEEKREAIRQLCFSLDHYKSGYKQL 415
Cdd:TIGR02168  422 EIEEL---------LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 148-401 2.60e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 2.60e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 148 EREIAQGEIAIRDIAIETERKRVLEVQRQVVDLETELSDLSFKFEHLVNEHEVSRDCLDVSFSEISKLREmlcdcQQNFS 227
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ-----DIARL 307

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 228 IEKTK-LVDQIKHSEAEKMEMQRKEVELQAEISALKTDLATRGEHIEALNKDFDKHKLRYDMLMAEKDGVCAEVDNLKAE 306
Cdd:COG1196 308 EERRReLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 307 MRSRDIQIQQMEEQLNQLVYKQTELVSESGNAKNTVEELKAVVKELEIEVELQSKAKKTVEELRATVWEMEKHAELQRNA 386
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467

                       250
                ....*....|....*
gi 15238455 387 ISQGEEEKREAIRQL 401
Cdd:COG1196 468 LLEEAALLEAALAEL 482
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 211-401 1.38e-06

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: 50.15  E-value: 1.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 211 EISKLREMLCDCQQnfsiEKTKLVDQIKHSEAEKMEMQRKEVELQAEISALKTDLATRGEHIEALNKDFDKHKLRYDMLM 290
Cdd:COG4942  35 EIAELEKELAALKK----EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 291 --AEKDGvcaEVDNLKAEMRSRDIQ------------IQQMEEQLNQLVYKQTELVSESGNAKNTVEELKAVVKELEIEV 356
Cdd:COG4942 111 raLYRLG---RQPPLALLLSPEDFLdavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEER 187

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15238455 357 ELQSKAKKTVEELRATVWEMEKHAELQRNAISQGEEEKREAIRQL 401
Cdd:COG4942 188 AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 93-394 1.29e-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: 47.74  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455     93 EKQMSYEELMKKYVQCEEELRTTSLKLQEFEQEIEKLKETEKKesvvLFGEYLRGEREIA--QGEIAIRDIAIETERKRV 170
Cdd:TIGR02168  730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE----AEEELAEAEAEIEelEAQIEQLKEELKALREAL 805

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    171 LEVQRQVVDLETELSDLSFKFEHLVNEHEVSRDCLDVSFSEISKLREmlcdcqqnfsiektklvdQIKHSEAEKMEMQRK 250
Cdd:TIGR02168  806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE------------------DIESLAAEIEELEEL 867

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    251 EVELQAEISALKTDLATRGEHIEALNKDFDKhklrydmLMAEKDGVCAEVDNLKAEMRSRDIQIQQMEEQLNQLvykqte 330
Cdd:TIGR02168  868 IEELESELEALLNERASLEEALALLRSELEE-------LSEELRELESKRSELRRELEELREKLAQLELRLEGL------ 934

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15238455    331 lvseSGNAKNTVEELKAVVK-ELEIEVELQSKAKKTVEELRATVWEMEKhaELQR------NAISQGEEEK 394
Cdd:TIGR02168  935 ----EVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLEN--KIKElgpvnlAAIEEYEELK 999
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 235-401 2.96e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.98  E-value: 2.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 235 DQIKHSEAEKMEMQRKEVELQAEISALKTDLATRGEHIEALNKDFDKHKlrydmlmaekdgvcAEVDNLKAEMRSRDIQI 314
Cdd:COG3883  16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ--------------AEIDKLQAEIAEAEAEI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 315 QQMEEQLNQLV---YKQ----------------TELVSE-------SGNAKNTVEELKAVVKELEievELQSKAKKTVEE 368
Cdd:COG3883  82 EERREELGERAralYRSggsvsyldvllgsesfSDFLDRlsalskiADADADLLEELKADKAELE---AKKAELEAKLAE 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15238455 369 LRATVWEME-KHAEL------QRNAISQGEEEKREAIRQL 401
Cdd:COG3883 159 LEALKAELEaAKAELeaqqaeQEALLAQLSAEEAAAEAQL 198
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
225-386 7.79e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.01  E-value: 7.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 225 NFSIEKTKLVDQIKHSEAEKMEMQRKEVELQAEISALKTDLATRGEHIEALNKDFDKHKLRYDMLMAEkdgvcAEVDNLK 304
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELE-----AELAELS 283

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 305 AEMRSRDIQIQQMEEQLNQL-VYKQTELVSESGNAKNTVEELKAVVKELEIEVELQSKAKKTVEELRAtvwemeKHAELQ 383
Cdd:COG3206 284 ARYTPNHPDVIALRAQIAALrAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEA------ELRRLE 357


                ...
gi 15238455 384 RNA 386
Cdd:COG3206 358 REV 360
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
248-401 2.26e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 2.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455  248 QRKEVELQAEISALKTDLATRGEHIEALNKDFDKHKlrydmlmaekdgvcAEVDNLKAEMRSRD-IQIQQMEEQLNQLVY 326
Cdd:COG4913  287 QRRLELLEAELEELRAELARLEAELERLEARLDALR--------------EELDELEAQIRGNGgDRLEQLEREIERLER 352

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15238455  327 KQTELVSESGNAKNTVEELKAVVKELEIE-VELQSKAKKTVEELRATVWEMEKHAELQRNAISQGEEEKREAIRQL 401
Cdd:COG4913  353 ELEERERRRARLEALLAALGLPLPASAEEfAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
157-371 3.26e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 3.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455  157 AIRDIAIETERKRVLEVQRQVVDLETELSDLSFKFEHL-----------------VNEHEVSRDCLDVSFSEISKLREML 219
Cdd:PRK02224 188 SLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYeeqreqaretrdeadevLEEHEERREELETLEAEIEDLRETI 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455  220 CDCQQnfsiEKTKLVDQIKHS----------------------------EAEKMEMQRKEVELQAEISALKTDLATRGEH 271
Cdd:PRK02224 268 AETER----EREELAEEVRDLrerleeleeerddllaeaglddadaeavEARREELEDRDEELRDRLEECRVAAQAHNEE 343

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455  272 IEALNKDFDKHKLRYDMLMAEKDGVCAEVDNLKAEMRSRDIQIQQMEEQLNQLVYKQTELVSESGNAKNTVEEL-----K 346
Cdd:PRK02224 344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELreerdE 423

                        250       260
                 ....*....|....*....|....*
gi 15238455  347 AVVKELEIEVELQSkAKKTVEELRA 371
Cdd:PRK02224 424 LREREAELEATLRT-ARERVEEAEA 447
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 229-371 4.34e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 4.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 229 EKTKLVDQIKHSEAEKMEMQRKEVELQAEISALKTDLATRGEHIEALNKDFDKHKLRYDMLMAEKdgvcaEVDNLKAEMR 308
Cdd:COG1579  25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-----EYEALQKEIE 99

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15238455 309 SRDIQIQQMEEQLNQLVYKQTELVSESGNAKNTVEELKAVVKELEIEVELQ-SKAKKTVEELRA 371
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEElAELEAELEELEA 163
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 93-401 4.43e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 4.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455     93 EKQMSYEELMKKYVQCEEELRTTSLKLQEFEQeieklketekkesvvlfgeylrgereiaqgeiairdiAIETERKRVLE 172
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEELRLEVSELEE-------------------------------------EIEELQKELYA 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    173 VQRQVVDLETELSDLSFKFEHLVNEHEVSRDCLDVSFSEISKLREmlcdcqqnfsiEKTKLVDQIKHSEAEKMEMQRKEV 252
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE-----------ELAELEEKLEELKEELESLEAELE 361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    253 ELQAEISALKTDLATRGEHIEALNKDFDKhklrydmlmaekdgvcaevdnLKAEMRSRDIQIQQMEEQLNQLVYKQTELV 332
Cdd:TIGR02168  362 ELEAELEELESRLEELEEQLETLRSKVAQ---------------------LELQIASLNNEIERLEARLERLEDRRERLQ 420

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15238455    333 SEsgNAKNTVEELKAVVKELEIEVElqsKAKKTVEELRATVWEMEKHAELQRNAISQGEEEKREAIRQL 401
Cdd:TIGR02168  421 QE--IEELLKKLEEAELKELQAELE---ELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 145-341 4.99e-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: 42.06  E-value: 4.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 145 LRGEREIAQGEIAIRDIAIETERKRVLEVQRQVVDLETELSDLSFKFEHLVNEHEVSRDCLDVSFSEISKL----REMLC 220
Cdd:COG4942  46 LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqpPLALL 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 221 DCQQNF--SIEKTKLVDQIKHSEAEKMEMQRKEvelQAEISALKTDLATRGEHIEALNKDFDKHKLRYDMLMAEKDGVCA 298
Cdd:COG4942 126 LSPEDFldAVRRLQYLKYLAPARREQAEELRAD---LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA 202

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15238455 299 EVDNLKAEMRSRDIQIQQMEEQLNQLVYKQTELVSESGNAKNT 341
Cdd:COG4942 203 RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 264-401 6.07e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 6.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 264 DLATRGEHIEALNKDFDKHKLRYDMLMAEKDGVCAEVDNLKAEMRSRDIQIQQMEEQLNQLVYKQTELVSESGNAKNTvE 343
Cdd:COG1579  11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-K 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15238455 344 ELKAVVKELEIEVELQSKAKKTVEELRATVWEMEKHAELQRNAISQGEEEKREAIRQL 401
Cdd:COG1579  90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
235-396 7.99e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 7.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 235 DQIKHSEAEKMEMQRKEVELQAEISALKTdLATRGEHIEALNKDFDKHKLRYDMLMAEKDgVCAEVDNLKAEMRSRDIQI 314
Cdd:COG4717  71 KELKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEAELEELREELEKLEKLLQLLP-LYQELEALEAELAELPERL 148

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 315 QQMEEQLNQLVYKQTELVSESGNAKNTVEELKAVVKELEIEVELQ-SKAKKTVEELRATVWEMEKHAELQRNAISQGEEE 393
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228


                ...
gi 15238455 394 KRE 396
Cdd:COG4717 229 LEQ 231
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 254-401 8.44e-04

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 41.25  E-value: 8.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455   254 LQAEISALKTDLATRGEHIEALNKDFDkhklRYDMLMAEKDGVCAEVDN-------LKAEMRSRDIQIQQMEEQLNQLVY 326
Cdd:pfam00529  56 YQAALDSAEAQLAKAQAQVARLQAELD----RLQALESELAISRQDYDGataqlraAQAAVKAAQAQLAQAQIDLARRRV 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15238455   327 kqteLVSESGNAKNTVEELKAVVKELEIEVElqsKAKKTVEELRATVWEMEKH-AELQRNAISQGEEEKREAIRQL 401
Cdd:pfam00529 132 ----LAPIGGISRESLVTAGALVAQAQANLL---ATVAQLDQIYVQITQSAAEnQAEVRSELSGAQLQIAEAEAEL 200
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 145-353 1.52e-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: 41.20  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    145 LRGEREIAQGEIAIRDIAIETERKRVLEVQRQVVDLETELSDL--------------SFKFEHLVNEHEVSRDCLDVSFS 210
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALaneisrleqqkqilRERLANLERQLEELEAQLEELES 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    211 EISKLREMLCDCQQNF---SIEKTKLVDQIKHSEAEKMEMQRKEVELQAEISALKTDLATRGEHIEALNK---------- 277
Cdd:TIGR02168  331 KLDELAEELAELEEKLeelKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNeierlearle 410

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    278 -----------------------DFDKHKLRYDMLMAEKDGVCAEVDNLKAEMRSRDIQI-------QQMEEQLNQLVYK 327
Cdd:TIGR02168  411 rledrrerlqqeieellkkleeaELKELQAELEELEEELEELQEELERLEEALEELREELeeaeqalDAAERELAQLQAR 490

                          250       260
                   ....*....|....*....|....*.
gi 15238455    328 QTELVSESGNAKNTVEELKAVVKELE 353
Cdd:TIGR02168  491 LDSLERLQENLEGFSEGVKALLKNQS 516
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 210-389 1.90e-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: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    210 SEISKLREMLCDCQQNFSIEKTKLVDQIKHSEAEKMEMQRKEVELQAEISALKTDLATRGEHIEALNKDFDKHKLRYDML 289
Cdd:pfam15921  324 STVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    290 MAEKDGVCAEVDNLKAEMRSRDIQIQ---------------QMEEQLNQLVYKQTEL---VSESGNAKNTVEELKAVVKE 351
Cdd:pfam15921  404 WDRDTGNSITIDHLRRELDDRNMEVQrleallkamksecqgQMERQMAAIQGKNESLekvSSLTAQLESTKEMLRKVVEE 483

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 15238455    352 LEIEVELQSKAKKTVEELRATVWEMEKHAELQRNAISQ 389
Cdd:pfam15921  484 LTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITK 521
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
110-398 2.31e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455  110 EELRTTSLKLQEFEQEIEKLKEtekkesvvlfgeylrgereiaqgeiairDIAiETERKR------VLEVQRQVVDLETE 183
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRE----------------------------TIA-ETEREReelaeeVRDLRERLEELEEE 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455  184 LSDLSFKFEHLVNEHEVSRDCLDVSFSEISKLREMLCDC---QQNFSIEKTKLVDQIKHSEAEKMEMQRKEVELQAEISA 260
Cdd:PRK02224 295 RDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECrvaAQAHNEEAESLREDADDLEERAEELREEAAELESELEE 374

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455  261 LKTDLATRGEHIEALNK--------------DFDKHKLRYDMLMAEKDGVCAEVDNLKAEMRSRDIQIQQMEEQLN---- 322
Cdd:PRK02224 375 AREAVEDRREEIEELEEeieelrerfgdapvDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkc 454

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455  323 ----QLVyKQTELVSESGNAKNTVEELKAVVKELEIEVELQSKAKKTVEELRATVWEMEKHAElQRNAISQGEEEKREAI 398
Cdd:PRK02224 455 pecgQPV-EGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEE-RREDLEELIAERRETI 532
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 216-401 3.03e-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: 40.10  E-value: 3.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    216 REMLCDCQQNFSIEK-TKLVDQIKHSEaekmEMQRKEVE-LQAE----------ISALKTDLATRGEHIEALNKDFDKHK 283
Cdd:pfam15921  448 RQMAAIQGKNESLEKvSSLTAQLESTK----EMLRKVVEeLTAKkmtlessertVSDLTASLQEKERAIEATNAEITKLR 523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    284 LRYDMLMAEKD----------GVCAEVDNLKAEMRSRDIQIQQMEEQLNQLvykqTELVSESGNAKNTVEELKAvvkELE 353
Cdd:pfam15921  524 SRVDLKLQELQhlknegdhlrNVQTECEALKLQMAEKDKVIEILRQQIENM----TQLVGQHGRTAGAMQVEKA---QLE 596

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 15238455    354 IEVE-----------LQSKAKKTVEELRATVWEMekhaELQRNAISQGEEEKREAIRQL 401
Cdd:pfam15921  597 KEINdrrlelqefkiLKDKKDAKIRELEARVSDL----ELEKVKLVNAGSERLRAVKDI 651
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
235-413 3.13e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 3.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455  235 DQIKHSEAEKMEMQRKEVELQAEISALKTDLATRGEHIEALNK---------DFDKHKLRYDMLMAEKDGV---CAEVDN 302
Cdd:COG4913  610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLdasSDDLAA 689

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455  303 LKAEMRSRDIQIQQMEEQLNQLVYKQTELVSESGNAKNTVEELKAVVKELEIEVELQSKAkkTVEELRATVWEMEKHAEL 382
Cdd:COG4913  690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LLEERFAAALGDAVEREL 767

                        170       180       190
                 ....*....|....*....|....*....|....
gi 15238455  383 QRN---AISQGEEEKREAIRQLCFSLDHYKSGYK 413
Cdd:COG4913  768 RENleeRIDALRARLNRAEEELERAMRAFNREWP 801
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
93-385 3.98e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 3.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455   93 EKQMSYEELMKKYVQCEEELRTTSLKLQEFEQEIEKLKETEKKESVVL-----FGEYLRGEREIAQGEIAIRDIAIETER 167
Cdd:PRK02224 360 ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLgnaedFLEELREERDELREREAELEATLRTAR 439

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455  168 KRVLEVQR----------------------------QVVDLETELSDLSFKFEHLVNEHEVSRDCLDVSfSEISKLREML 219
Cdd:PRK02224 440 ERVEEAEAlleagkcpecgqpvegsphvetieedreRVEELEAELEDLEEEVEEVEERLERAEDLVEAE-DRIERLEERR 518

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455  220 CDCQQNFS-----IEKTKLVDQIKHSEAEKMEMQRKEVELQA------------EISALKTDLATRGEHIEALNK----- 277
Cdd:PRK02224 519 EDLEELIAerretIEEKRERAEELRERAAELEAEAEEKREAAaeaeeeaeeareEVAELNSKLAELKERIESLERirtll 598

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455  278 ------------------------DFDKHKL-----RYDMLMAEKDGvcAEVDNLKAEMRSRDIQIQQMEEQLNQLVYKQ 328
Cdd:PRK02224 599 aaiadaedeierlrekrealaelnDERRERLaekreRKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREER 676

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15238455  329 TELVSESGNAKNTVEELKAVVKELEiEVELQSKAKKTV----EELRATVweMEKHAEL-QRN 385
Cdd:PRK02224 677 DDLQAEIGAVENELEELEELRERRE-ALENRVEALEALydeaEELESMY--GDLRAELrQRN 735
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
229-401 4.54e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 4.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 229 EKTKLVDQIKHSEAEKMEMQRKEVELQAEISALKTDLATRGEHIEALNKDFDKHKLRYDMLMAEKDGVCAEVDNLKAEMR 308
Cdd:COG4372  46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455 309 SRDIQIQQMEEQLNQLVYKQTELVSESGNAKNTVEELKAVVKELEIEV------ELQSKAKKTVEELRATVWEMEKHAEL 382
Cdd:COG4372 126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELqalseaEAEQALDELLKEANRNAEKEEELAEA 205

                       170
                ....*....|....*....
gi 15238455 383 QRNAISQGEEEKREAIRQL 401
Cdd:COG4372 206 EKLIESLPRELAEELLEAK 224
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 147-293 5.19e-03

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


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 39.26  E-value: 5.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    147 GEREIAQGEIAIRDIAIETERKRVLEVQRQVVDLETELSDLSFKFEHLVNEHEVSRDCLDVSFSEISKLREMLCDCQQNF 226
Cdd:TIGR01612 1565 EKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDTE 1644

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15238455    227 SIEKTKLVDQIKhSEAEKMEMQRKEVELQaeisalKTDLATRGEHIEALNKDFDKHKLRYDMLMAEK 293
Cdd:TIGR01612 1645 LKENGDNLNSLQ-EFLESLKDQKKNIEDK------KKELDELDSEIEKIEIDVDQHKKNYEIGIIEK 1704
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 166-334 7.19e-03

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


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 38.88  E-value: 7.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    166 ERKRVLEVQRQVVDLETELSDLSFKFEHLVNEhevsrdcLDVSFSEISKLREMLCDCQQNFSIEKTKLVDQIKhSEAEKM 245
Cdd:TIGR01612 1985 ENQQLYEKIQASNELKDTLSDLKYKKEKILND-------VKLLLHKFDELNKLSCDSQNYDTILELSKQDKIK-EKIDNY 2056

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238455    246 EMQRKEVELQAEISALKTDLATRGEHIEALNKDFDKHKLRYDMLMAEKDGVCAEVDNLKAEMRSRDIQIQQMEEQL---N 322
Cdd:TIGR01612 2057 EKEKEKFGIDFDVKAMEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEKDNIIQSKKKLKELTEAFNTEIKIIEDKIiekN 2136

                          170
                   ....*....|..
gi 15238455    323 QLVYKQTELVSE 334
Cdd:TIGR01612 2137 DLIDKLIEMRKE 2148
 
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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