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Conserved domains on  [gi|40254675|ref|NP_694504|]
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lamin-B1 [Danio rerio]

Protein Classification

intermediate filament family protein( domain architecture ID 11755560)

intermediate filament family protein such as lamins, which are a major component of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Filament super family cl25641
Intermediate filament protein;
32-388 1.13e-89

Intermediate filament protein;


The actual alignment was detected with superfamily member pfam00038:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 279.50  E-value: 1.13e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    32 QEKEELQQLNDRLAAYIDTVRSLESENSVLQIQIREREDVRNRELTGLRTLYETELADARKALDDTARERARLQIELGKI 111
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   112 KSEQEQLQHTYAKKdadltssqnrlkdveallnakeaalntaVSERKTLENTLSDLqirvqelegglisaKKQLSDETLL 191
Cdd:pfam00038  81 RLAAEDFRQKYEDE----------------------------LNLRTSAENDLVGL--------------RKDLDEATLA 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   192 RVDLENRCQSLMEELEFRKNMFEEEIKDTRRRH--ETRLVEVDSGRQMEyefkLAQALTDMRQQHDEQVKLYKEEMEQTY 269
Cdd:pfam00038 119 RVDLEAKIESLKEELAFLKKNHEEEVRELQAQVsdTQVNVEMDAARKLD----LTSALAEIRAQYEEIAAKNREEAEEWY 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   270 VSKLENIRLSSEMNSSSASMAREELRESTLRVESLAGQLANLQKEARAWQDRINELEGALSHEKDLSRRLLAEKEREIAE 349
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQE 274

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 40254675   350 IRAKMQQQLDEYEQLLDVKLALDMEINAYRKLLEGEEER 388
Cdd:pfam00038 275 TRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 437-544 8.62e-20

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


:

Pssm-ID: 460003 [Multi-domain]  Cd Length: 108  Bit Score: 84.78  E-value: 8.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   437 ASATGNVSIDELDVDG-----KFIRLHNNSEQDQPMAGFQLTRTIGEvtaTYKFTAKYNLKAGQKVTIWASNAGIS---- 507
Cdd:pfam00932   1 SSATGDVVISEVVYDGsggndEFIELYNTGSKAVDLSGWKLQDASGG---TYTFPNGTTLAPGQTVVVWTGSGTNSatag 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 40254675   508 SNPPADLIWKNQpswgtgeNIKVALLSPAGEKVAVRS 544
Cdd:pfam00932  78 YWGPSNAVWNNG-------GDAVALYDANGELVDSVG 107
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
32-388 1.13e-89

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 279.50  E-value: 1.13e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    32 QEKEELQQLNDRLAAYIDTVRSLESENSVLQIQIREREDVRNRELTGLRTLYETELADARKALDDTARERARLQIELGKI 111
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   112 KSEQEQLQHTYAKKdadltssqnrlkdveallnakeaalntaVSERKTLENTLSDLqirvqelegglisaKKQLSDETLL 191
Cdd:pfam00038  81 RLAAEDFRQKYEDE----------------------------LNLRTSAENDLVGL--------------RKDLDEATLA 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   192 RVDLENRCQSLMEELEFRKNMFEEEIKDTRRRH--ETRLVEVDSGRQMEyefkLAQALTDMRQQHDEQVKLYKEEMEQTY 269
Cdd:pfam00038 119 RVDLEAKIESLKEELAFLKKNHEEEVRELQAQVsdTQVNVEMDAARKLD----LTSALAEIRAQYEEIAAKNREEAEEWY 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   270 VSKLENIRLSSEMNSSSASMAREELRESTLRVESLAGQLANLQKEARAWQDRINELEGALSHEKDLSRRLLAEKEREIAE 349
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQE 274

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 40254675   350 IRAKMQQQLDEYEQLLDVKLALDMEINAYRKLLEGEEER 388
Cdd:pfam00038 275 TRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 437-544 8.62e-20

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


Pssm-ID: 460003 [Multi-domain]  Cd Length: 108  Bit Score: 84.78  E-value: 8.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   437 ASATGNVSIDELDVDG-----KFIRLHNNSEQDQPMAGFQLTRTIGEvtaTYKFTAKYNLKAGQKVTIWASNAGIS---- 507
Cdd:pfam00932   1 SSATGDVVISEVVYDGsggndEFIELYNTGSKAVDLSGWKLQDASGG---TYTFPNGTTLAPGQTVVVWTGSGTNSatag 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 40254675   508 SNPPADLIWKNQpswgtgeNIKVALLSPAGEKVAVRS 544
Cdd:pfam00932  78 YWGPSNAVWNNG-------GDAVALYDANGELVDSVG 107
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 32-330 7.55e-13

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: 71.63  E-value: 7.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675     32 QEKEELQQLNDRLAAYIDTVRSLESENSVLQIQIREREDvRNRELtglrtlyETELADARKALDDTARERARLQIELGKI 111
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRL-EVSEL-------EEEIEELQKELYALANEISRLEQQKQIL 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    112 KSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIRVQELEGGLISAKKQLSDETLL 191
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    192 RVDLENRCQSLMEELEfrknMFEEEIKDTRRRHEtRLVEVDSGRQMEYEfKLAQALTDMRQQHDEQVKLYKEEMEQTYVS 271
Cdd:TIGR02168  388 VAQLELQIASLNNEIE----RLEARLERLEDRRE-RLQQEIEELLKKLE-EAELKELQAELEELEEELEELQEELERLEE 461

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40254675    272 KLENIRLSSEMNSSSASMAREELRESTLRVESLAGQLANLQKEARA------WQDRINELEGALS 330
Cdd:TIGR02168  462 ALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGvkallkNQSGLSGILGVLS 526
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 64-371 1.63e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.27  E-value: 1.63e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  64 QIREREDVRNRELTGLR-TLYETELADARKALDDTARERARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEAL 142
Cdd:COG1196 217 ELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675 143 LNAKEAALNTAVSERKTLENTLSDLQIRVQELEGGLISAKKQLSDETLLRVDLENRCQSLMEELEFRKNMFEEEIKDTRR 222
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675 223 RHETRLvevdsgrqmeyEFKLAQALTDMRQQHDEQVKLYKEEMEQTYVSKLENIRLSSEMNSSSASMAREELRESTLRVE 302
Cdd:COG1196 377 AEEELE-----------ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40254675 303 SLAGQLANLQKEARAWQDRINELEGALSHEKDLSRRLLAEKEREIAEIRAKMQQQLDEYEQLLDVKLAL 371
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
84-382 5.10e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 5.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   84 ETELADARKALDDTARERARLQIELGKIKSEQEQLQHTYAKkdadLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENT 163
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE----IEELEKELESLEGSKRKLEEKIRELEERIEELKKE 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  164 LSDLQIRVQELEGGLISAKKQLSDETLLR--VDLENRCQSLMEELEFRKNMFEEEIKD----TRRRHETRLVEVDSGRQM 237
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFYEeyLDELREIEKRLSRLEEEINGIEERIKEleekEERLEELKKKLKELEKRL 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  238 EYEFKLAQALTDMRQQHDEQVKLYKEEMEQTyVSKLENirlssemNSSSASMAREELREstlRVESLAGQLANLQKEARA 317
Cdd:PRK03918 355 EELEERHELYEEAKAKKEELERLKKRLTGLT-PEKLEK-------ELEELEKAKEEIEE---EISKITARIGELKKEIKE 423

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40254675  318 WQDRINELEGA----------LSHEKDLsrRLLAEKEREIAEIRAKMQQQLDEYEQLLDVKLALDMEINAYRKLL 382
Cdd:PRK03918 424 LKKAIEELKKAkgkcpvcgreLTEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI 496
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
32-388 1.13e-89

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 279.50  E-value: 1.13e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    32 QEKEELQQLNDRLAAYIDTVRSLESENSVLQIQIREREDVRNRELTGLRTLYETELADARKALDDTARERARLQIELGKI 111
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   112 KSEQEQLQHTYAKKdadltssqnrlkdveallnakeaalntaVSERKTLENTLSDLqirvqelegglisaKKQLSDETLL 191
Cdd:pfam00038  81 RLAAEDFRQKYEDE----------------------------LNLRTSAENDLVGL--------------RKDLDEATLA 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   192 RVDLENRCQSLMEELEFRKNMFEEEIKDTRRRH--ETRLVEVDSGRQMEyefkLAQALTDMRQQHDEQVKLYKEEMEQTY 269
Cdd:pfam00038 119 RVDLEAKIESLKEELAFLKKNHEEEVRELQAQVsdTQVNVEMDAARKLD----LTSALAEIRAQYEEIAAKNREEAEEWY 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   270 VSKLENIRLSSEMNSSSASMAREELRESTLRVESLAGQLANLQKEARAWQDRINELEGALSHEKDLSRRLLAEKEREIAE 349
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQE 274

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 40254675   350 IRAKMQQQLDEYEQLLDVKLALDMEINAYRKLLEGEEER 388
Cdd:pfam00038 275 TRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 437-544 8.62e-20

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


Pssm-ID: 460003 [Multi-domain]  Cd Length: 108  Bit Score: 84.78  E-value: 8.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   437 ASATGNVSIDELDVDG-----KFIRLHNNSEQDQPMAGFQLTRTIGEvtaTYKFTAKYNLKAGQKVTIWASNAGIS---- 507
Cdd:pfam00932   1 SSATGDVVISEVVYDGsggndEFIELYNTGSKAVDLSGWKLQDASGG---TYTFPNGTTLAPGQTVVVWTGSGTNSatag 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 40254675   508 SNPPADLIWKNQpswgtgeNIKVALLSPAGEKVAVRS 544
Cdd:pfam00932  78 YWGPSNAVWNNG-------GDAVALYDANGELVDSVG 107
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 32-330 7.55e-13

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: 71.63  E-value: 7.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675     32 QEKEELQQLNDRLAAYIDTVRSLESENSVLQIQIREREDvRNRELtglrtlyETELADARKALDDTARERARLQIELGKI 111
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRL-EVSEL-------EEEIEELQKELYALANEISRLEQQKQIL 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    112 KSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIRVQELEGGLISAKKQLSDETLL 191
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    192 RVDLENRCQSLMEELEfrknMFEEEIKDTRRRHEtRLVEVDSGRQMEYEfKLAQALTDMRQQHDEQVKLYKEEMEQTYVS 271
Cdd:TIGR02168  388 VAQLELQIASLNNEIE----RLEARLERLEDRRE-RLQQEIEELLKKLE-EAELKELQAELEELEEELEELQEELERLEE 461

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40254675    272 KLENIRLSSEMNSSSASMAREELRESTLRVESLAGQLANLQKEARA------WQDRINELEGALS 330
Cdd:TIGR02168  462 ALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGvkallkNQSGLSGILGVLS 526
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-390 1.29e-12

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: 70.86  E-value: 1.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675      7 TPAGQQSLSRGTSSTPLSPARISRLQEKEELQQLNDRLAAYIDTVRSLESENSVLQIQIREredvrnreltglrtlYETE 86
Cdd:TIGR02168  649 TLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEE---------------LEEE 713

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675     87 LADARKALDDTARERARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSD 166
Cdd:TIGR02168  714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    167 LQIRVQELEGGLISAKKQLSDETLLRVDLENRCQSLmeelEFRKNMFEEEIKDTRRRHETRlvevdSGRQMEYEFKLAQA 246
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLNEEAANLRERLESL----ERRIAATERRLEDLEEQIEEL-----SEDIESLAAEIEEL 864

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    247 LTDMRQQHDEQVKLYKEEMEQtyvsklenirlssemnsssaSMAREELREstlrveslagQLANLQKEARAWQDRINELE 326
Cdd:TIGR02168  865 EELIEELESELEALLNERASL--------------------EEALALLRS----------ELEELSEELRELESKRSELR 914

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40254675    327 galsHEKDLSRRLLAEKEREIAEIRAKMQQQLD----EYEQLLDVKLALDMEINAYRKLLEGEEERLK 390
Cdd:TIGR02168  915 ----RELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 64-371 1.63e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.27  E-value: 1.63e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  64 QIREREDVRNRELTGLR-TLYETELADARKALDDTARERARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEAL 142
Cdd:COG1196 217 ELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675 143 LNAKEAALNTAVSERKTLENTLSDLQIRVQELEGGLISAKKQLSDETLLRVDLENRCQSLMEELEFRKNMFEEEIKDTRR 222
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675 223 RHETRLvevdsgrqmeyEFKLAQALTDMRQQHDEQVKLYKEEMEQTYVSKLENIRLSSEMNSSSASMAREELRESTLRVE 302
Cdd:COG1196 377 AEEELE-----------ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40254675 303 SLAGQLANLQKEARAWQDRINELEGALSHEKDLSRRLLAEKEREIAEIRAKMQQQLDEYEQLLDVKLAL 371
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 84-389 7.76e-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: 52.37  E-value: 7.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675     84 ETE--LADARKALD---DTARERARlQIELGKIKSEQEQLQHTY--AKKDADLTSSQNRLKDVEALLNAKEAALNTAVSE 156
Cdd:TIGR02168  176 ETErkLERTRENLDrleDILNELER-QLKSLERQAEKAERYKELkaELRELELALLVLRLEELREELEELQEELKEAEEE 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    157 RKTLENTLSDLQIRVQELEggliSAKKQLSDETLLRVDLENRCQSLMEELEFRKNMFEEEIKDTRR---RHETRLVEVDS 233
Cdd:TIGR02168  255 LEELTAELQELEEKLEELR----LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERqleELEAQLEELES 330

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    234 GRQmEYEFKLAQ---ALTDMRQQHDEQVKLYKEEME--QTYVSKLENIRLSSEMNSSSASMAREELRESTLRVESLAGQL 308
Cdd:TIGR02168  331 KLD-ELAEELAEleeKLEELKEELESLEAELEELEAelEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    309 ANLQKEARAWQDRINELEGALS-HEKDLSRRLLAEKEREIAEIRA----------KMQQQLDEYEQLLDVKLALDMEINA 377
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEelerleealeELREELEEAEQALDAAERELAQLQA 489

                          330
                   ....*....|..
gi 40254675    378 YRKLLEGEEERL 389
Cdd:TIGR02168  490 RLDSLERLQENL 501
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 26-186 1.19e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 1.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675     26 ARISRLQEK-----EELQQLNDRLAAYIDTVRSLESENSVLQIQIRErEDVRNRELtglrtlyETELADARKALDDTARE 100
Cdd:TIGR02169  329 AEIDKLLAEieeleREIEEERKRRDKLTEEYAELKEELEDLRAELEE-VDKEFAET-------RDELKDYREKLEKLKRE 400

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    101 R-------ARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIRVQE 173
Cdd:TIGR02169  401 InelkrelDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480

                          170
                   ....*....|...
gi 40254675    174 LEGGLISAKKQLS 186
Cdd:TIGR02169  481 VEKELSKLQRELA 493
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 160-364 3.32e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.45  E-value: 3.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    160 LENTLSDLQIRVQELEGGLISAKKQLSDETLLRVDLENRCQSLMEELEfrknMFEEEIKDTRRRHETRLVEVDSGRQM-- 237
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE----KLKERLEELEEDLSSLEQEIENVKSElk 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    238 EYEFKLAQALTDMRQQHDEQVKLYKEEME---QTYVSKLENIRLSSEMNSSSASMAREELRESTLRVESLAGQLANLQKE 314
Cdd:TIGR02169  762 ELEARIEELEEDLHKLEEALNDLEARLSHsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 40254675    315 ARAWQDRINELEgalsHEKDLSRRLLAEKEREIAEIRAKMQQQLDEYEQL 364
Cdd:TIGR02169  842 RIDLKEQIKSIE----KEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 98-354 5.89e-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: 48.61  E-value: 5.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  98 ARERARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIRVQELEGG 177
Cdd:COG4942  19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675 178 LISAKKQLSDetLLRVDLENRCQSLMEElefrknmfeeeikdtrrrhetrLVEVDSGRQMEYEFKLAQALTDMRQQHDEQ 257
Cdd:COG4942  99 LEAQKEELAE--LLRALYRLGRQPPLAL----------------------LLSPEDFLDAVRRLQYLKYLAPARREQAEE 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675 258 VKLYKEEMEQTyVSKLENIRLSSEMNSSSASMAREELRESTLRVESLagqLANLQKEARAWQDRINELEGAlshEKDLsR 337
Cdd:COG4942 155 LRADLAELAAL-RAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQE---AEEL-E 226

                       250
                ....*....|....*..
gi 40254675 338 RLLAEKEREIAEIRAKM 354
Cdd:COG4942 227 ALIARLEAEAAAAAERT 243
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 66-362 8.50e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.91  E-value: 8.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675     66 RERED-VRNRELtgLRTLYETELADARKALDDTARERARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLN 144
Cdd:TIGR02169  205 REREKaERYQAL--LKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    145 AKEAalntavSERKTLENTLSDLQIRVQELEGGLISAKKQLSDETLLRVDLENRCQSLMEELEfrknMFEEEIKDTRRRH 224
Cdd:TIGR02169  283 DLGE------EEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE----ELEREIEEERKRR 352

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    225 ETRLVEVDSGRQ--MEYEFKLAQALTDMRQQHDEQVKlYKEEMEQtYVSKLENIRLSSEMNSSSASMAREELRESTLRVE 302
Cdd:TIGR02169  353 DKLTEEYAELKEelEDLRAELEEVDKEFAETRDELKD-YREKLEK-LKREINELKRELDRLQEELQRLSEELADLNAAIA 430

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40254675    303 SLAGQLANLQKEARAWQDRINELEGALSHEK----DLSRRLLAEKE--REIAEIRAKMQQQLDEYE 362
Cdd:TIGR02169  431 GIEAKINELEEEKEDKALEIKKQEWKLEQLAadlsKYEQELYDLKEeyDRVEKELSKLQRELAEAE 496
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
89-396 1.74e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   89 DARKALDDTARERARLQIELGKIKSEQEQLQhtyakkdADLTSSQNRLKDVEALLNAKEAALNTAvserkTLENTLSDLQ 168
Cdd:COG4913  607 DNRAKLAALEAELAELEEELAEAEERLEALE-------AELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELE 674

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  169 IRVQELE---GGLISAKKQLSDETLLRVDLENRCQSLMEE---LEFRKNMFEEEIKDTRRRHETRLVEVDSGRQMEYEFK 242
Cdd:COG4913  675 AELERLDassDDLAALEEQLEELEAELEELEEELDELKGEigrLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  243 LAQALTD-----MRQQHDEQVKLYKEEMEQTYvSKLENIRlssemnsssasmaREELRESTLRVESLAGQLANLQkEARA 317
Cdd:COG4913  755 FAAALGDavereLRENLEERIDALRARLNRAE-EELERAM-------------RAFNREWPAETADLDADLESLP-EYLA 819

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  318 WQDRINElEGALSHEKDLSRRLLAEKEREIAEIRAKMQQQLDEYEQLLDvklaldmEINAYRKLLE-GEEERLKLSPSPS 396
Cdd:COG4913  820 LLDRLEE-DGLPEYEERFKELLNENSIEFVADLLSKLRRAIREIKERID-------PLNDSLKRIPfGPGRYLRLEARPR 891
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 91-398 5.55e-05

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.50  E-value: 5.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675     91 RKALDDTARERARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIR 170
Cdd:pfam02463  172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    171 VQELEGGLISAKKQLSDETLLRVDLENRCQSLMEELEFRKNMFEEEIKDTRRRHETRLVevdsgrqmEYEFKLAQALTDM 250
Cdd:pfam02463  252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV--------DDEEKLKESEKEK 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    251 RqQHDEQVKLYKEEMEQTYVSKLENIRLSSEMNSSSASMAREELRESTLRVESLAGQLanLQKEARAWQDRINELEGALS 330
Cdd:pfam02463  324 K-KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK--LESERLSSAAKLKEEELELK 400

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40254675    331 HEKDLSRRLLAEKEREIAEIRAKMQQQLD----EYEQLLDVKLALDMEINAYRKLLEGEEERLKLSPSPSSR 398
Cdd:pfam02463  401 SEEEKEAQLLLELARQLEDLLKEEKKEELeileEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 35-272 9.20e-05

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: 45.55  E-value: 9.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675     35 EELQQLNDRLAAYIDTVRSLESENSVLQIQIREREDvRNRELTGLRTLYETELADarkaLDDTARERARLQIELGKIKSE 114
Cdd:pfam01576  138 EDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEE-KAKSLSKLKNKHEAMISD----LEERLKKEEKGRQELEKAKRK 212

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    115 QEQLQHTYAKKDADLtssQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIRVQELEGGLISAKKQLSDETLLRVD 194
Cdd:pfam01576  213 LEGESTDLQEQIAEL---QAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNK 289

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    195 LENRCQSLMEELEFRKNMFEEEIKDT------RRRHETRLVEVDsgRQMEYEFKLAQA-LTDMRQQHDEQVKLYKEEMEQ 267
Cdd:pfam01576  290 AEKQRRDLGEELEALKTELEDTLDTTaaqqelRSKREQEVTELK--KALEEETRSHEAqLQEMRQKHTQALEELTEQLEQ 367


                   ....*
gi 40254675    268 TYVSK 272
Cdd:pfam01576  368 AKRNK 372
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 123-380 1.01e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 1.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675 123 AKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIRVQELEGGLISAKKQLSDetllrvdLENRCQSL 202
Cdd:COG4942  23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-------LEKEIAEL 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675 203 MEELEFRKNMFEEEIKDTRRRHETRLVEV----DSGRQMEYEFKLAQALTDMRQQHdeqvklykeemeqtyvsklenirl 278
Cdd:COG4942  96 RAELEAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQ------------------------ 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675 279 ssemnsssasmaREELRESTLRVESLAGQLANLQKEARAWQDRINELEGALSHEKDLSRRLLAEKEREIAEIRAKMQQQL 358
Cdd:COG4942 152 ------------AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219

                       250       260
                ....*....|....*....|..
gi 40254675 359 DEYEQLLDVKLALDMEINAYRK 380
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAAE 241
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 31-390 1.65e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 44.83  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675     31 LQEKEELQQLNDRLAAYIDT-VRSLESENSVLQIQ---IREREDVRNRELTGLRTLYETELADARKALDD-TARERARLQ 105
Cdd:pfam12128  386 EQNNRDIAGIKDKLAKIREArDRQLAVAEDDLQALeseLREQLEAGKLEFNEEEYRLKSRLGELKLRLNQaTATPELLLQ 465

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    106 IE------------LGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLsdLQIRVQE 173
Cdd:pfam12128  466 LEnfderierareeQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTL--LHFLRKE 543

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    174 LEGGLISAKKQLSDETLLRVDLEnrcqslmeelefrKNMFEEEIKDTRRRHETRL----VEVDSGRQMEYEFK--LAQAL 247
Cdd:pfam12128  544 APDWEQSIGKVISPELLHRTDLD-------------PEVWDGSVGGELNLYGVKLdlkrIDVPEWAASEEELRerLDKAE 610

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    248 TDMRQQHDEQVKLyKEEMEQTYVsKLENIRLSSEMNSSSASMAREELRESTLRVESLAGQLANLQKEARAW-QDRINELE 326
Cdd:pfam12128  611 EALQSAREKQAAA-EEQLVQANG-ELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSaNERLNSLE 688

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40254675    327 GALSHEKDLSRRLLAEKEREIAEIRAKMQQQLDEYEQLLDVKLA-LDMEINAYRKLLEGEEERLK 390
Cdd:pfam12128  689 AQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLAlLKAAIAARRSGAKAELKALE 753
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 107-187 1.82e-04

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 43.95  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   107 ELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSER--------KTLENTLSDLQIRVQELEGGL 178
Cdd:TIGR04320 255 SLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELanaqaqalQTAQNNLATAQAALANAEARL 334


                  ....*....
gi 40254675   179 ISAKKQLSD 187
Cdd:TIGR04320 335 AKAKEALAN 343
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 20-226 2.93e-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: 43.60  E-value: 2.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  20 STPLSPARISRLQEKEELQQLNDRLAAYIDTVRSLESENSVLQIQIREREDvRNRELTGLRTLYETELADARKALDDTAR 99
Cdd:COG4942  12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-RIAALARRIRALEQELAALEAELAELEK 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675 100 ERARLQIELGKIKSE-QEQLQHTYAKKDAD----LTSSQN------RLKDVEALLNAKEAALNTAVSERKTLENTLSDLQ 168
Cdd:COG4942  91 EIAELRAELEAQKEElAELLRALYRLGRQPplalLLSPEDfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELE 170

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 40254675 169 IRVQELEggliSAKKQLSDETLLRVDLENRCQSLMEELEFRKNMFEEEIKDTRRRHET 226
Cdd:COG4942 171 AERAELE----ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
85-256 4.12e-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: 4.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   85 TELADARKALDDTARERARLQ-------------IELGKIKSEQEQLQHTYAKKDADLtsSQNRLKDVEALLNAKEAALN 151
Cdd:COG4913  235 DDLERAHEALEDAREQIELLEpirelaeryaaarERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELE 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  152 TAVSERKTLENTLSDLQIRVQELEGGLI-SAKKQLSDETLLRVDLENRCQSLME---ELEFRKNMFEEEIKDTRRRHETR 227
Cdd:COG4913  313 RLEARLDALREELDELEAQIRGNGGDRLeQLEREIERLERELEERERRRARLEAllaALGLPLPASAEEFAALRAEAAAL 392

                        170       180       190
                 ....*....|....*....|....*....|.
gi 40254675  228 LVEVDS--GRQMEYEFKLAQALTDMRQQHDE 256
Cdd:COG4913  393 LEALEEelEALEEALAEAEAALRDLRRELRE 423
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 11-326 5.05e-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: 43.13  E-value: 5.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675     11 QQSLSRGTSSTPLSPARISRLQEKEE------------LQQLNDRLAAYIDTVRSLESENSVLQIQIREREDVRN----- 73
Cdd:TIGR02169  708 SQELSDASRKIGEIEKEIEQLEQEEEklkerleeleedLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNdlear 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675     74 ------RELTGLRTLYETELADARKALDDTARERARLQIELG----KIKSEQEQLQHTYAKKD---ADLTSSQNRLKDVE 140
Cdd:TIGR02169  788 lshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEylekEIQELQEQRIDLKEQIKsieKEIENLNGKKEELE 867

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    141 ALLNAKEAALNTAVS-------ERKTLENTLSDLQIRVQELEGGLISAKKQLSdetllrvDLENRCQSLMEELefrknmf 213
Cdd:TIGR02169  868 EELEELEAALRDLESrlgdlkkERDELEAQLRELERKIEELEAQIEKKRKRLS-------ELKAKLEALEEEL------- 933

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    214 eEEIKDTRRRHETrlvevDSGRQMEYefklaqaltdmrqqhdEQVKLYKEEMEQTyVSKLENIRLSsemnsssasmAREE 293
Cdd:TIGR02169  934 -SEIEDPKGEDEE-----IPEEELSL----------------EDVQAELQRVEEE-IRALEPVNML----------AIQE 980

                          330       340       350
                   ....*....|....*....|....*....|...
gi 40254675    294 LRESTLRVESLAGQLANLQKEARAWQDRINELE 326
Cdd:TIGR02169  981 YEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
84-382 5.10e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 5.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   84 ETELADARKALDDTARERARLQIELGKIKSEQEQLQHTYAKkdadLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENT 163
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE----IEELEKELESLEGSKRKLEEKIRELEERIEELKKE 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  164 LSDLQIRVQELEGGLISAKKQLSDETLLR--VDLENRCQSLMEELEFRKNMFEEEIKD----TRRRHETRLVEVDSGRQM 237
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFYEeyLDELREIEKRLSRLEEEINGIEERIKEleekEERLEELKKKLKELEKRL 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  238 EYEFKLAQALTDMRQQHDEQVKLYKEEMEQTyVSKLENirlssemNSSSASMAREELREstlRVESLAGQLANLQKEARA 317
Cdd:PRK03918 355 EELEERHELYEEAKAKKEELERLKKRLTGLT-PEKLEK-------ELEELEKAKEEIEE---EISKITARIGELKKEIKE 423

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40254675  318 WQDRINELEGA----------LSHEKDLsrRLLAEKEREIAEIRAKMQQQLDEYEQLLDVKLALDMEINAYRKLL 382
Cdd:PRK03918 424 LKKAIEELKKAkgkcpvcgreLTEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI 496
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
29-390 6.05e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 6.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   29 SRLQEKEELQQLNDRLAAYIDTVRSLESENsvlqiqIREREDVRNReltglrtlyeteLADARKALDDTARERARLQIEL 108
Cdd:PRK02224 241 EVLEEHEERREELETLEAEIEDLRETIAET------EREREELAEE------------VRDLRERLEELEEERDDLLAEA 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  109 GKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIRVQELEGGLISAKKQLSDE 188
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDR 382

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  189 TLLRVDLENRCQSLMEELEF----------RKNMFEEEIKDTRRRHETRLVE-------VDSGRQMEYEFK--------- 242
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDapvdlgnaedFLEELREERDELREREAELEATlrtarerVEEAEALLEAGKcpecgqpve 462

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  243 ---LAQALTDMRQQHDE------QVKLYKEEMEQTY---------VSKLENIRLSSEMNSSSASMAREELRESTLRVESL 304
Cdd:PRK02224 463 gspHVETIEEDRERVEEleaeleDLEEEVEEVEERLeraedlveaEDRIERLEERREDLEELIAERRETIEEKRERAEEL 542

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  305 AGQLANLQKEARAWQDRINELEGAlshekdlsrrllAEKERE-IAEIRAKMQQQLDEYEQLLDVKLALDmEINAYRKLLE 383
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEE------------AEEAREeVAELNSKLAELKERIESLERIRTLLA-AIADAEDEIE 609


                 ....*..
gi 40254675  384 GEEERLK 390
Cdd:PRK02224 610 RLREKRE 616
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 19-366 6.19e-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: 42.80  E-value: 6.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675     19 SSTPLSPARISRLQEKEELQQLNDRLAAYIDTVRSLESENSVlqiqirerEDVRNRELTGLRTLYETELADARKALDDTA 98
Cdd:pfam15921  354 ANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSL--------EKEQNKRLWDRDTGNSITIDHLRRELDDRN 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675     99 RERARLQIELGKIKSE-----QEQLQHTYAKKD---------ADLTSSQNRLKDVEALLNAKEAALNTAvserktlENTL 164
Cdd:pfam15921  426 MEVQRLEALLKAMKSEcqgqmERQMAAIQGKNEslekvssltAQLESTKEMLRKVVEELTAKKMTLESS-------ERTV 498

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    165 SDLQIRVQELEGGLISAKKQLSdETLLRVDLEnrcqslMEELEFRKNMfEEEIKDTRRRHET-RLVEVDSGRQMEYEFKL 243
Cdd:pfam15921  499 SDLTASLQEKERAIEATNAEIT-KLRSRVDLK------LQELQHLKNE-GDHLRNVQTECEAlKLQMAEKDKVIEILRQQ 570

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    244 AQALTDMRQQHD--------EQVKLYKEEMEQtyvsKLENIRLSSEMNSSSASMAREELRESTLRVESLagQLANLQKEA 315
Cdd:pfam15921  571 IENMTQLVGQHGrtagamqvEKAQLEKEINDR----RLELQEFKILKDKKDAKIRELEARVSDLELEKV--KLVNAGSER 644

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40254675    316 -RAWQD-------RINELE------GALSHEKDLSRRLLAEKEREIAEIRAKMQQQLDEYEQLLD 366
Cdd:pfam15921  645 lRAVKDikqerdqLLNEVKtsrnelNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELE 709
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
32-369 7.62e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 7.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   32 QEKEELQQLNDRLAAYIDTVRSLESENSVLQIQIRE--------REDVRNRELTglRTLYETELADARKALDDTARERAR 103
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAEleseleeaREAVEDRREE--IEELEEEIEELRERFGDAPVDLGN 409

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  104 LQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIRVQELEGGLISAKK 183
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEE 489

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  184 QLSdetllrvDLENRCQSLME--ELEFRKNMFEEEIKDTRRRHETRLVEVDSGR-QMEYEFKLAQAL-TDMRQQHDEQVK 259
Cdd:PRK02224 490 EVE-------EVEERLERAEDlvEAEDRIERLEERREDLEELIAERRETIEEKReRAEELRERAAELeAEAEEKREAAAE 562

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  260 LYKE-EMEQTYVSKLENirlssemnsssasmAREELRESTLRVESLAGQLANLQkEARAWQDRINELEGALSHEKDLSRR 338
Cdd:PRK02224 563 AEEEaEEAREEVAELNS--------------KLAELKERIESLERIRTLLAAIA-DAEDEIERLREKREALAELNDERRE 627

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 40254675  339 LLAEKEREIAEIRAKMQ-----------QQLDEYEQLLDVKL 369
Cdd:PRK02224 628 RLAEKRERKRELEAEFDearieearedkERAEEYLEQVEEKL 669
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 13-362 1.16e-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: 42.03  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675     13 SLSRGTSSTPLSPARISRLQEK-----EELQQLNDRLaayiDTVRSLESENSVLQIQIREREDVRNRELTGLRTLYETEL 87
Cdd:pfam15921  504 SLQEKERAIEATNAEITKLRSRvdlklQELQHLKNEG----DHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVG 579

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675     88 ADARKAlDDTARERARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVE----ALLNAKEAALNTAVSERKTLENT 163
Cdd:pfam15921  580 QHGRTA-GAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekvKLVNAGSERLRAVKDIKQERDQL 658

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    164 LSDLQIRVQELegglisakKQLSDE-TLLRVDLENRCqslmEELEFRKNMFEEEIKDTRR-----RHETRLVEVDSGRQM 237
Cdd:pfam15921  659 LNEVKTSRNEL--------NSLSEDyEVLKRNFRNKS----EEMETTTNKLKMQLKSAQSeleqtRNTLKSMEGSDGHAM 726

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    238 EYEFKLAQALTDMRQQHDE-QVKLYKEEMEQTYVSKLENIrlssemNSSSASMAREELRESTLRVESLAGQLANLQKEAR 316
Cdd:pfam15921  727 KVAMGMQKQITAKRGQIDAlQSKIQFLEEAMTNANKEKHF------LKEEKNKLSQELSTVATEKNKMAGELEVLRSQER 800

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 40254675    317 AWQDRINELEGALshekDLSRRLLAE-----KEREIAEIRAKMQQQLDEYE 362
Cdd:pfam15921  801 RLKEKVANMEVAL----DKASLQFAEcqdiiQRQEQESVRLKLQHTLDVKE 847
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
26-175 1.60e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 1.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  26 ARISRLQEKEELQQLNDRLAAYIDTVRSLeSENSVLQiQIREREDVRNRELTGLRTLYETELADARKALDDTARERARLQ 105
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPEL-LQSPVIQ-QLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ 308

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675 106 IELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIRVQELE 175
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
26-207 1.71e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   26 ARISRLQEkeELQQLNDRLAAYIDTVRSLESENSVLQIQIREREDVRNRELTGLRTLY-ETELA---DARKALDDTARER 101
Cdd:COG4913  610 AKLAALEA--ELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASaEREIAeleAELERLDASSDDL 687

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  102 ARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIRVQELEGGLISA 181
Cdd:COG4913  688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767

                        170       180
                 ....*....|....*....|....*.
gi 40254675  182 KKQLSDEtllRVDLENRCQSLMEELE 207
Cdd:COG4913  768 RENLEER---IDALRARLNRAEEELE 790
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-383 1.83e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   33 EKEELQQLNDRLAAYIDTVRSLESENSVLQIQIREREDVRNRELTGLRtlyetELADARKALDDTaRERARLQIELGKIK 112
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE-----ELEEKVKELKEL-KEKAEEYIKLSEFY 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  113 SEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIRVQELE------GGLISAKKQLS 186
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEeakakkEELERLKKRLT 382

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  187 DETLLRVDLEnrcqslMEELEFRKNMFEEEIKDTRRRHETRLVEVDSGRQMEYEFKLAQALTDM-RQQHDEQvklYKEEM 265
Cdd:PRK03918 383 GLTPEKLEKE------LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVcGRELTEE---HRKEL 453

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  266 EQTYVSKLENIRLSSEMNSSSASMAREELRE---------STLRVESLAGQLANLQ---------------KEARAWQDR 321
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRElekvlkkesELIKLKELAEQLKELEeklkkynleelekkaEEYEKLKEK 533

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40254675  322 INELEGALSH-EKDLSR--------RLLAEKEREIAEIRAKMQQQLDE--YEQLLDVKLALDMEINAYRKLLE 383
Cdd:PRK03918 534 LIKLKGEIKSlKKELEKleelkkklAELEKKLDELEEELAELLKELEElgFESVEELEERLKELEPFYNEYLE 606
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
35-361 2.29e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  35 EELQQLNDRLAAYIDTVRSLESENSV---LQIQIREREDVRNRELTGLRTLYETELADARKALDDTARERARLQIELGKI 111
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEElreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675 112 KSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEA-ALNTAVSERKTLENTLSDLQIRVQELEGGLISA--------- 181
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALEERLKEArLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVlgllallfl 291

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675 182 ----KKQLSDETLLRVDLENRCQSLMEE--------LEFRKNMFEEEIKDTRRRHETRLVEVDSGRQMEYEFKLAQALTD 249
Cdd:COG4717 292 llarEKASLGKEAEELQALPALEELEEEeleellaaLGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE 371

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675 250 MRQ--------------QHDEQVKLYKEEMEQtyVSKLENiRLSSEMNSSSASMAREELRESTLRVESLAGQLANLQKEA 315
Cdd:COG4717 372 IAAllaeagvedeeelrAALEQAEEYQELKEE--LEELEE-QLEELLGELEELLEALDEEELEEELEELEEELEELEEEL 448

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 40254675 316 RAWQDRINELEGALshEKDLSRRLLAEKEREIAEIRAKMQQQLDEY 361
Cdd:COG4717 449 EELREELAELEAEL--EQLEEDGELAELLQELEELKAELRELAEEW 492
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 86-185 3.42e-03

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 40.10  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    86 ELADARKALDDTARERARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEA-LLNAKEAALNTAVSERKTLENTL 164
Cdd:TIGR04320 255 SLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAqALQTAQNNLATAQAALANAEARL 334

                          90       100
                  ....*....|....*....|.
gi 40254675   165 SDLQIRVQELEGGLISAKKQL 185
Cdd:TIGR04320 335 AKAKEALANLNADLAKKQAAL 355
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 34-211 3.55e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 3.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  34 KEELQQLNDRLAAYIDTVRSLESENSVLQIQIRE---REDVRNRELTGLRTLYETELADARKALD----------DTARE 100
Cdd:COG4942  54 LKQLAALERRIAALARRIRALEQELAALEAELAElekEIAELRAELEAQKEELAELLRALYRLGRqpplalllspEDFLD 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675 101 RARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLkdvEALLNAKEAALNTAVSERKTLENTLSDLQIRVQELEGGLIS 180
Cdd:COG4942 134 AVRRLQYLKYLAPARREQAEELRADLAELAALRAEL---EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210

                       170       180       190
                ....*....|....*....|....*....|.
gi 40254675 181 AKKQLSDETLLRVDLENRCQSLMEELEFRKN 211
Cdd:COG4942 211 LAAELAELQQEAEELEALIARLEAEAAAAAE 241
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 34-390 4.46e-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: 4.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    34 KEELQQLNDRLAAYIDTVRSLESE----NSVLQIQIREREDVRNREltglrTLYETELADARKALDDTARERARLQIELG 109
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKKEKEleklNNKYNDLKKQKEELENEL-----NLLEKEKLNIQKNIDKIKNKLLKLELLLS 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   110 KIKSeQEQLQHTYAKKDADLTSSQNRLKD-----------VEALLNAKEAALNTAVSERKTLENTLSDLQIRVQEleggl 178
Cdd:TIGR04523 205 NLKK-KIQKNKSLESQISELKKQNNQLKDniekkqqeineKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ----- 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   179 isAKKQLSdetllrvDLENRCQSLMEELEFRKNMFEE----EIKDTRRRHETRLVEVDSgrqmeyefKLAQALTDMRQQH 254
Cdd:TIGR04523 279 --NNKKIK-------ELEKQLNQLKSEISDLNNQKEQdwnkELKSELKNQEKKLEEIQN--------QISQNNKIISQLN 341

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   255 DEQVKLYKEEMEqtyvSKLENIRLssemnsssasmaREELRESTLRVESLAGQLANLQKEARAWQDRINELEGALSHEKD 334
Cdd:TIGR04523 342 EQISQLKKELTN----SESENSEK------------QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK 405

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40254675   335 LSRRL----------LAEKEREIAEIRAKMQQQLDEYEQLLDVKLALDMEINAYRKLLEGEEERLK 390
Cdd:TIGR04523 406 LNQQKdeqikklqqeKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLK 471
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 81-252 4.46e-03

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: 39.33  E-value: 4.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    81 TLYETELADARKALDDTARERARLQIELgkikSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALntavserKTL 160
Cdd:pfam00529  54 TDYQAALDSAEAQLAKAQAQVARLQAEL----DRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQL-------AQA 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675   161 ENTLSDLQIRVQElegGLISAKKQLSDETLLRVDLENRCQSLMEELEFRKNmFEEEIKDTRRRHETRLVEVDSGRQmEYE 240
Cdd:pfam00529 123 QIDLARRRVLAPI---GGISRESLVTAGALVAQAQANLLATVAQLDQIYVQ-ITQSAAENQAEVRSELSGAQLQIA-EAE 197

                         170
                  ....*....|..
gi 40254675   241 FKLAQALTDMRQ 252
Cdd:pfam00529 198 AELKLAKLDLER 209
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
256-399 8.96e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 8.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675  256 EQVKLYKEEMEQTYVSKLENIRLSSEMNSSSASmAREELRESTLRVESLAGQLANLQKE-------ARAWQDRINELEGA 328
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINEISSELPELRE-ELEKLEKEVKELEELKEEIEELEKEleslegsKRKLEEKIRELEER 267

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40254675  329 LShEKDLSRRLLAEKEREIAEIRAKMQQQL---DEYEQLLDVKLALDMEINAYRKLLEGEEERLKLSPSPSSRV 399
Cdd:PRK03918 268 IE-ELKKEIEELEEKVKELKELKEKAEEYIklsEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 35-389 9.77e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.00  E-value: 9.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675     35 EELQQLNDRLAAYIDTVRSLESENSVLQIQIREREDVRNRELTGLRTLyETELADARKALDDTARERARLQIELGKIKSE 114
Cdd:pfam01576  363 EQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKL-EGQLQELQARLSESERQRAELAEKLSKLQSE 441

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    115 QEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNtavserktlENTLSDLQI--RVQELEGGLISAKKQLSDETLLR 192
Cdd:pfam01576  442 LESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ---------EETRQKLNLstRLRQLEDERNSLQEQLEEEEEAK 512

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    193 VDLENRCQSLMEELEFRKNMFEEEIKDTRRRHETRLvevdsgrqmeyefKLAQALTDMRQQHDEQVKLYkEEMEQTyvsk 272
Cdd:pfam01576  513 RNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKK-------------RLQRELEALTQQLEEKAAAY-DKLEKT---- 574

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254675    273 leNIRLssemnsssasmaREELRESTLRVESLAGQLANLQKEARawqdrinELEGALSHEKDLSRRLLAEKEREIAEIRA 352
Cdd:pfam01576  575 --KNRL------------QQELDDLLVDLDHQRQLVSNLEKKQK-------KFDQMLAEEKAISARYAEERDRAEAEARE 633

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 40254675    353 KMQQQLDEYEQLLDVKLALDmEINAYRKLLEGEEERL 389
Cdd:pfam01576  634 KETRALSLARALEEALEAKE-ELERTNKQLRAEMEDL 669
 
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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