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Conserved domains on  [gi|17533053|ref|NP_495137|]
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Intermediate filament protein ifb-1 [Caenorhabditis elegans]

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;
50-401 1.24e-54

Intermediate filament protein;


The actual alignment was detected with superfamily member pfam00038:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 187.05  E-value: 1.24e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    50 EKKTLQGLNDRLGNYIDRVKKLEEQNRKLVADLDELRGKWGKDTSEIKIKYSESLSTARKDIDDAARRKAEVDVKVARHR 129
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053   130 DDLAEYRSRYEDIQQRRESdrekisqwtnaiadAQSEVEMLRArfkqltdeekrvtadnsriweelqkarsDLDDETIGR 209
Cdd:pfam00038  82 LAAEDFRQKYEDELNLRTS--------------AENDLVGLRK----------------------------DLDEATLAR 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053   210 IDFQNQVQTLMEELEFLRRVHEQEVKELQALLA--QAPADTREFFKNELALAIRDIKDEYDIIAKQGKQDMESWYKLKVS 287
Cdd:pfam00038 120 VDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdtQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLE 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053   288 EVQGSANRANMESTYQRDEVKRMRDNIGDLRGKLGDLENKNSLLEKEVQNLNYQLTDDQRQYEAALNDRDATLRRMREEC 367
Cdd:pfam00038 200 ELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEM 279

                         330       340       350
                  ....*....|....*....|....*....|....
gi 17533053   368 QTLVAELQALLDTKQMLDAEIAIYRKMLEGEETR 401
Cdd:pfam00038 280 ARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 442-551 3.30e-13

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: 65.91  E-value: 3.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053   442 SAKGNVTISECDPNG-----KFIKLENShRNKDENVGEHKIRRKLDGrreiVYSIPANVVIKPGKNLTIYArdqGGINNP 516
Cdd:pfam00932   2 SATGDVVISEVVYDGsggndEFIELYNT-GSKAVDLSGWKLQDASGG----TYTFPNGTTLAPGQTVVVWT---GSGTNS 73

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 17533053   517 PESLVFDGENTWGIGANVVTSLVNKDGEERATHTQ 551
Cdd:pfam00932  74 ATAGYWGPSNAVWNNGGDAVALYDANGELVDSVGY 108
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
50-401 1.24e-54

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 187.05  E-value: 1.24e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    50 EKKTLQGLNDRLGNYIDRVKKLEEQNRKLVADLDELRGKWGKDTSEIKIKYSESLSTARKDIDDAARRKAEVDVKVARHR 129
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053   130 DDLAEYRSRYEDIQQRRESdrekisqwtnaiadAQSEVEMLRArfkqltdeekrvtadnsriweelqkarsDLDDETIGR 209
Cdd:pfam00038  82 LAAEDFRQKYEDELNLRTS--------------AENDLVGLRK----------------------------DLDEATLAR 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053   210 IDFQNQVQTLMEELEFLRRVHEQEVKELQALLA--QAPADTREFFKNELALAIRDIKDEYDIIAKQGKQDMESWYKLKVS 287
Cdd:pfam00038 120 VDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdtQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLE 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053   288 EVQGSANRANMESTYQRDEVKRMRDNIGDLRGKLGDLENKNSLLEKEVQNLNYQLTDDQRQYEAALNDRDATLRRMREEC 367
Cdd:pfam00038 200 ELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEM 279

                         330       340       350
                  ....*....|....*....|....*....|....
gi 17533053   368 QTLVAELQALLDTKQMLDAEIAIYRKMLEGEETR 401
Cdd:pfam00038 280 ARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 442-551 3.30e-13

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: 65.91  E-value: 3.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053   442 SAKGNVTISECDPNG-----KFIKLENShRNKDENVGEHKIRRKLDGrreiVYSIPANVVIKPGKNLTIYArdqGGINNP 516
Cdd:pfam00932   2 SATGDVVISEVVYDGsggndEFIELYNT-GSKAVDLSGWKLQDASGG----TYTFPNGTTLAPGQTVVVWT---GSGTNS 73

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 17533053   517 PESLVFDGENTWGIGANVVTSLVNKDGEERATHTQ 551
Cdd:pfam00932  74 ATAGYWGPSNAVWNNGGDAVALYDANGELVDSVGY 108
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 59-403 2.18e-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: 63.54  E-value: 2.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053     59 DRLGNYIDRVKKLEEQNRKLVADLDELRGKW---GKDTSEIK--IKYSESLSTARKDIDDAARRKAEVDVKVARHRDDLA 133
Cdd:TIGR02168  629 DDLDNALELAKKLRPGYRIVTLDGDLVRPGGvitGGSAKTNSsiLERRREIEELEEKIEELEEKIAELEKALAELRKELE 708

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    134 EYRSRYEDIQQRRESDREKISQWTNAIADAQSEVEMLRARFKQLTDEEKRVTADNSRIWEELQKARSDLDDETIGRIDFQ 213
Cdd:TIGR02168  709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    214 NQVQTLMEELEFLRRVHEQEVKELQALlaQAPADTREFFKNELALAIRDIKDEYDIIAKQGKQDMESWYKLKVSEVQGSA 293
Cdd:TIGR02168  789 AQIEQLKEELKALREALDELRAELTLL--NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    294 NRANMESTYQRDEVKRM---------RDNIGDLRGKLGDLENKNSLLEKEVQNLNYQLTDDQRQYEAALNDRDATLRRMR 364
Cdd:TIGR02168  867 LIEELESELEALLNERAsleealallRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 17533053    365 EECQTLVAELQALLDTKQMLDAEIAIYRKMLEGEETRVG 403
Cdd:TIGR02168  947 EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELG 985
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 57-411 1.87e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 1.87e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  57 LNDRLGNYIDRVKKLEEQ------NRKLVADLDELRGKWgkdtseikikyseslstARKDIDDAARRKAEVDVKVARHRD 130
Cdd:COG1196 191 LEDILGELERQLEPLERQaekaerYRELKEELKELEAEL-----------------LLLKLRELEAELEELEAELEELEA 253

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 131 DLAEYRSRYEDIQQRRESDREKISQWTNAIADAQSEVEMLRARFKQLTDEEKRVTADNSRIWEELQKARSDLDDETIGRI 210
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 211 DFQNQVQTLMEELEflrrVHEQEVKELQALLAQApADTREFFKNELALAIRDIKDEYDIIAKQGKQdmeswyklkVSEVQ 290
Cdd:COG1196 334 ELEEELEELEEELE----EAEEELEEAEAELAEA-EEALLEAEAELAEAEEELEELAEELLEALRA---------AAELA 399

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 291 GSANRANMESTYQRDEVKRMRDNIGDLRGKLGDLENKNSLLEKEVQNLNYQLTDDQRQYEAALNDRDATLRRmREECQTL 370
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE-AALLEAA 478

                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 17533053 371 VAELQALLDTKQMLDAEIAIYRKMLEGEETRVGLTQMVEQA 411
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
40-370 6.56e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 6.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053   40 AKSFLEATDKEKKTLQGlndRLGNYIDRVKKLEEQNRKLVADLDELRGKWGKDTSEikikysesLSTARKDIDDAARRKA 119
Cdd:PRK02224 382 RREEIEELEEEIEELRE---RFGDAPVDLGNAEDFLEELREERDELREREAELEAT--------LRTARERVEEAEALLE 450

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  120 E-------VDVKVARHRDDLAEYRSRYEDIQQRRESDREKISQWTNAI------ADAQSEVEMLRARFKQLTD--EEKRV 184
Cdd:PRK02224 451 AgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLeraedlVEAEDRIERLEERREDLEEliAERRE 530

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  185 TADNSRI-WEELQKARSDLDDETIGRidfQNQVQTLMEELEFLRrvheQEVKELQALLAQApADTREFFKN--ELALAIR 261
Cdd:PRK02224 531 TIEEKRErAEELRERAAELEAEAEEK---REAAAEAEEEAEEAR----EEVAELNSKLAEL-KERIESLERirTLLAAIA 602

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  262 DIKDEYDIIAKQGKQ----DMESWYKLK-----VSEVQGSANRANMESTYQRDE-----VKRMRDNIGDLRGKLGDLENK 327
Cdd:PRK02224 603 DAEDEIERLREKREAlaelNDERRERLAekrerKRELEAEFDEARIEEAREDKEraeeyLEQVEEKLDELREERDDLQAE 682

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 17533053  328 NSLLEKEVQNLnyqltDDQRQYEAALNDRDATLRRMREECQTL 370
Cdd:PRK02224 683 IGAVENELEEL-----EELRERREALENRVEALEALYDEAEEL 720
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
50-401 1.24e-54

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 187.05  E-value: 1.24e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    50 EKKTLQGLNDRLGNYIDRVKKLEEQNRKLVADLDELRGKWGKDTSEIKIKYSESLSTARKDIDDAARRKAEVDVKVARHR 129
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053   130 DDLAEYRSRYEDIQQRRESdrekisqwtnaiadAQSEVEMLRArfkqltdeekrvtadnsriweelqkarsDLDDETIGR 209
Cdd:pfam00038  82 LAAEDFRQKYEDELNLRTS--------------AENDLVGLRK----------------------------DLDEATLAR 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053   210 IDFQNQVQTLMEELEFLRRVHEQEVKELQALLA--QAPADTREFFKNELALAIRDIKDEYDIIAKQGKQDMESWYKLKVS 287
Cdd:pfam00038 120 VDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdtQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLE 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053   288 EVQGSANRANMESTYQRDEVKRMRDNIGDLRGKLGDLENKNSLLEKEVQNLNYQLTDDQRQYEAALNDRDATLRRMREEC 367
Cdd:pfam00038 200 ELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEM 279

                         330       340       350
                  ....*....|....*....|....*....|....
gi 17533053   368 QTLVAELQALLDTKQMLDAEIAIYRKMLEGEETR 401
Cdd:pfam00038 280 ARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 442-551 3.30e-13

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: 65.91  E-value: 3.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053   442 SAKGNVTISECDPNG-----KFIKLENShRNKDENVGEHKIRRKLDGrreiVYSIPANVVIKPGKNLTIYArdqGGINNP 516
Cdd:pfam00932   2 SATGDVVISEVVYDGsggndEFIELYNT-GSKAVDLSGWKLQDASGG----TYTFPNGTTLAPGQTVVVWT---GSGTNS 73

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 17533053   517 PESLVFDGENTWGIGANVVTSLVNKDGEERATHTQ 551
Cdd:pfam00932  74 ATAGYWGPSNAVWNNGGDAVALYDANGELVDSVGY 108
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 59-403 2.18e-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: 63.54  E-value: 2.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053     59 DRLGNYIDRVKKLEEQNRKLVADLDELRGKW---GKDTSEIK--IKYSESLSTARKDIDDAARRKAEVDVKVARHRDDLA 133
Cdd:TIGR02168  629 DDLDNALELAKKLRPGYRIVTLDGDLVRPGGvitGGSAKTNSsiLERRREIEELEEKIEELEEKIAELEKALAELRKELE 708

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    134 EYRSRYEDIQQRRESDREKISQWTNAIADAQSEVEMLRARFKQLTDEEKRVTADNSRIWEELQKARSDLDDETIGRIDFQ 213
Cdd:TIGR02168  709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    214 NQVQTLMEELEFLRRVHEQEVKELQALlaQAPADTREFFKNELALAIRDIKDEYDIIAKQGKQDMESWYKLKVSEVQGSA 293
Cdd:TIGR02168  789 AQIEQLKEELKALREALDELRAELTLL--NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    294 NRANMESTYQRDEVKRM---------RDNIGDLRGKLGDLENKNSLLEKEVQNLNYQLTDDQRQYEAALNDRDATLRRMR 364
Cdd:TIGR02168  867 LIEELESELEALLNERAsleealallRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 17533053    365 EECQTLVAELQALLDTKQMLDAEIAIYRKMLEGEETRVG 403
Cdd:TIGR02168  947 EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELG 985
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 67-400 1.12e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 1.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053     67 RVKKLEEQNRK------LVADLDEL-RGKWGKDTSEIKIKYSESLST---ARKDIDDAARRKAEVDVKVARHRDDLAEYR 136
Cdd:TIGR02168  201 QLKSLERQAEKaerykeLKAELRELeLALLVLRLEELREELEELQEElkeAEEELEELTAELQELEEKLEELRLEVSELE 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    137 SRYEDIQQRRESdrekisqWTNAIADAQSEVEMLRARFKQLTDEEKRVTadnsriwEELQKARSDLDDEtigridfQNQV 216
Cdd:TIGR02168  281 EEIEELQKELYA-------LANEISRLEQQKQILRERLANLERQLEELE-------AQLEELESKLDEL-------AEEL 339

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    217 QTLMEELEFLRRVHEQEVKELQALLAQAPadtreffknELALAIRDIKDEYDIIAKqgkqdmeswyklKVSEVQGSANRA 296
Cdd:TIGR02168  340 AELEEKLEELKEELESLEAELEELEAELE---------ELESRLEELEEQLETLRS------------KVAQLELQIASL 398

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    297 NMESTYQRDEVKRMRDNIGDLRGKLGDLENKNSLLE-KEVQNLNYQLTDDQRQYEAALNDRDATLRRMREECQTLVAELQ 375
Cdd:TIGR02168  399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478

                          330       340
                   ....*....|....*....|....*
gi 17533053    376 ALLDTKQMLDAEIAIYRKMLEGEET 400
Cdd:TIGR02168  479 AAERELAQLQARLDSLERLQENLEG 503
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 44-324 1.79e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.30  E-value: 1.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053     44 LEATDKEKKTLQGLNDRLGNYIDRVKKLEEQNRK----LVADLDELRGKWGKDTSE----IKIKYSE---SLSTARKDID 112
Cdd:TIGR02169  232 KEALERQKEAIERQLASLEEELEKLTEEISELEKrleeIEQLLEELNKKIKDLGEEeqlrVKEKIGEleaEIASLERSIA 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    113 DAARRKAEVDVKVARHRDDLAEYRSRYEDIQQRRESDREKISQWTNAIADAQSEVEMLRARFKQLTDEEKRVTADNSRIW 192
Cdd:TIGR02169  312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    193 EELQKARSDLDDETIGRIDFQNQVQTLMEELEFLR---RVHEQEVKELQALLAQAPADTREFFKNELALA---------I 260
Cdd:TIGR02169  392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNaaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAadlskyeqeL 471

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17533053    261 RDIKDEYDIIAKQGKQdmeswYKLKVSEVQGSANRANMESTYQRDEVKRMRDNIGDLRGKLGDL 324
Cdd:TIGR02169  472 YDLKEEYDRVEKELSK-----LQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 57-411 1.87e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 1.87e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  57 LNDRLGNYIDRVKKLEEQ------NRKLVADLDELRGKWgkdtseikikyseslstARKDIDDAARRKAEVDVKVARHRD 130
Cdd:COG1196 191 LEDILGELERQLEPLERQaekaerYRELKEELKELEAEL-----------------LLLKLRELEAELEELEAELEELEA 253

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 131 DLAEYRSRYEDIQQRRESDREKISQWTNAIADAQSEVEMLRARFKQLTDEEKRVTADNSRIWEELQKARSDLDDETIGRI 210
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 211 DFQNQVQTLMEELEflrrVHEQEVKELQALLAQApADTREFFKNELALAIRDIKDEYDIIAKQGKQdmeswyklkVSEVQ 290
Cdd:COG1196 334 ELEEELEELEEELE----EAEEELEEAEAELAEA-EEALLEAEAELAEAEEELEELAEELLEALRA---------AAELA 399

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 291 GSANRANMESTYQRDEVKRMRDNIGDLRGKLGDLENKNSLLEKEVQNLNYQLTDDQRQYEAALNDRDATLRRmREECQTL 370
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE-AALLEAA 478

                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 17533053 371 VAELQALLDTKQMLDAEIAIYRKMLEGEETRVGLTQMVEQA 411
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 157-402 2.16e-07

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: 53.23  E-value: 2.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 157 TNAIADAQSEVEMLRARFKQLTDEEKRVTADNSRIWEELQKARSDLDDETIGRIDFQNQVQTLMEELEFLrrvhEQEVKE 236
Cdd:COG4942  19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL----EKEIAE 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 237 LQALLAQApadtreffKNELALAIRdikdeydIIAKQGKQDmeswyKLKVSEVQGSANRANMESTYQRDEVKRMRDNIGD 316
Cdd:COG4942  95 LRAELEAQ--------KEELAELLR-------ALYRLGRQP-----PLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 317 LRGKLGDLENKNSLLEKEVQNLNYQLTD---DQRQYEAALNDRDATLRRMREECQTLVAELQALLDTKQMLDAEIAIYRK 393
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAEleeERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234


                ....*....
gi 17533053 394 MLEGEETRV 402
Cdd:COG4942 235 EAAAAAERT 243
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 166-398 4.20e-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: 49.68  E-value: 4.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    166 EVEMLRARFKQLTDEEKRVTADNSRIWEELQKARSDLDDETIGRIDFQNQVQTLMEELEFLRRVHEQEVKELQALlaqap 245
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL----- 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    246 ADTREFFKNELALAIRDIKDEYDIIAKQGKQDMESWYKLKVSEVQGSANranmESTYQRDEVKRMRDNIGDLRGKLGDLE 325
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQA----ELSKLEEEVSRIEARLREIEQKLNRLT 825

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17533053    326 NKNSLLEKEVQNLnyqltddqRQYEAALNDRDATLRRMREECQTLVAELQALLDTKQMLDAEIAIYRKMLEGE 398
Cdd:TIGR02169  826 LEKEYLEKEIQEL--------QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 51-377 1.27e-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: 48.13  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053     51 KKTLQGLNDRLGNYIDRVKKLEEQNRKLVADLDELRGKWGKDTSEIKiKYSESLSTARKDIDDAARRKAEVDVKVARHRD 130
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQLSKELTELEAEIEELEERLEEAEE 775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    131 DLAEYRSRYEDIQQRRESDREKISQWTNAIADAQSEVEMLRARFKQLTDEEKRVTADNSRIWEELQkarsDLDDETIGRI 210
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE----DLEEQIEELS 851

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    211 DFQNQVQTLMEELEFLRRVHEQEVKELQALlaqapadtreffKNELALAIRDIKDEYDIIAKQGKQDmeswyklkvsevq 290
Cdd:TIGR02168  852 EDIESLAAEIEELEELIEELESELEALLNE------------RASLEEALALLRSELEELSEELREL------------- 906

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    291 gsanranmestyqRDEVKRMRDNIGDLRGKLGDLENKNSLLEKEVQNLNYQLTDD-QRQYEAAL---NDRDATLRRMREE 366
Cdd:TIGR02168  907 -------------ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEaleNKIEDDEEEARRR 973

                          330
                   ....*....|.
gi 17533053    367 CQTLVAELQAL 377
Cdd:TIGR02168  974 LKRLENKIKEL 984
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 124-389 1.91e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.76  E-value: 1.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    124 KVARHRDDLAEYRSRYEDIQQRRESDREKISQWTNAIADAQSEVEMLRARFKQLTDEE---KRVTADNSRIWEELQKARS 200
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEeklKERLEELEEDLSSLEQEIE 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    201 DLDDE---TIGRIDFQ----NQVQTLMEELEflRRVHEQEVKELQALLAQAPADTREFFKN----ELALAIRDIKDEYDI 269
Cdd:TIGR02169  755 NVKSElkeLEARIEELeedlHKLEEALNDLE--ARLSHSRIPEIQAELSKLEEEVSRIEARlreiEQKLNRLTLEKEYLE 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    270 IAKQGKQDMESWYKLKVSEVQGSANRANMESTYQRDEVKRMRDNIGDLRGKLGDLEnknslleKEVQNLNYQLtddqRQY 349
Cdd:TIGR02169  833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK-------KERDELEAQL----REL 901

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 17533053    350 EAALNDRDATLRRMREECQTLVAELQALLDTKQMLDAEIA 389
Cdd:TIGR02169  902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 49-348 9.96e-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: 9.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053     49 KEKKTLQ----GLNDRLGNYIDRVK---KLEEQNRKLVADLDELRGKWGK---DTSEIKIKYSESLSTARKDIDDAARRK 118
Cdd:pfam01576  152 KERKLLEerisEFTSNLAEEEEKAKslsKLKNKHEAMISDLEERLKKEEKgrqELEKAKRKLEGESTDLQEQIAELQAQI 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    119 AEVDVKVARHRDDLAEYRSRYEDIQQRRESDREKISQWTNAIADAQSEVEMLRArfkqltdEEKRVTADNSRIWEELQKA 198
Cdd:pfam01576  232 AELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERA-------ARNKAEKQRRDLGEELEAL 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    199 RSDLDDeTIGRIDFQNQVQTLME-------------------ELEFLRRVHEQEVKELQALLAQAPADTREFFKNELALA 259
Cdd:pfam01576  305 KTELED-TLDTTAAQQELRSKREqevtelkkaleeetrsheaQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALE 383

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    260 --IRDIKDEYDIIAkQGKQDMESWYK---LKVSEVQGSANRANMESTYQRDEVKRMRDNIGDLRGKLGDLENKNSLLEKE 334
Cdd:pfam01576  384 seNAELQAELRTLQ-QAKQDSEHKRKkleGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKD 462

                          330
                   ....*....|....
gi 17533053    335 VQNLNYQLTDDQRQ 348
Cdd:pfam01576  463 VSSLESQLQDTQEL 476
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
34-366 1.08e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  34 ALSANAAKSFLEATDKEKKTLQGLNDRLGNYIDRVKKLEEQNRKLVADLDELRGKWGKDTSEIKIKYSESLSTARKDIDD 113
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 114 AARRKAEVDVKVARHRDDLAEYRSRYEDI--QQRRESDREKISQWTNAIADA---------------------------- 163
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLenELEAAALEERLKEARLLLLIAaallallglggsllsliltiagvlflvl 283

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 164 -------------QSEVEMLRARFKQLTDEEKRVTADNSRIWEELQKARSDLDDETIGRIDFQNQVQTLMEELEFLRRVH 230
Cdd:COG4717 284 gllallflllareKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 231 EQEV--KELQALLAQAPADTREFF---------KNELALAIRDIKDEYDIIAKQGKQDMESWYKlkvSEVQGSANRANME 299
Cdd:COG4717 364 QLEEleQEIAALLAEAGVEDEEELraaleqaeeYQELKEELEELEEQLEELLGELEELLEALDE---EELEEELEELEEE 440

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17533053 300 STYQRDEVKRMRDNIGDLRGKLGDLENKNSL--LEKEVQNLNYQLTDDQRQYeAALNDRDATLRRMREE 366
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQLEEDGELaeLLQELEELKAELRELAEEW-AALKLALELLEEAREE 508
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
113-262 1.38e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  113 DAARRKAEVDVKVARHRDDLAEYRSRYEDIQQRRESDREKISQWTN--AIADAQSEVEMLRARFKQLTDEEKRVTADNSR 190
Cdd:COG4913  607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDASSDD 686

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17533053  191 I------WEELQKARSDLDDEtigRIDFQNQVQTLMEELEFLRRVHEQEVKELQALLAQAPADTREFFKNELALAIRD 262
Cdd:COG4913  687 LaaleeqLEELEAELEELEEE---LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD 761
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 102-275 4.81e-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: 41.83  E-value: 4.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 102 ESLSTARKDIDDAARRKAEVDVKVARHRDDLAEYRSRYEDIQQRRESDREKISQWTNA--IADAQSEVEMLRARFKQLTD 179
Cdd:COG1579  31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeYEALQKEIESLKRRISDLED 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 180 EEKrvtadnsRIWEELQKARSDLDDEtigridfQNQVQTLMEELEFLRRVHEQEVKELQALLAQAPADtreffKNELALA 259
Cdd:COG1579 111 EIL-------ELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELEELEAE-----REELAAK 171

                       170
                ....*....|....*..
gi 17533053 260 I-RDIKDEYDIIAKQGK 275
Cdd:COG1579 172 IpPELLALYERIRKRKN 188
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 116-273 5.37e-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: 41.83  E-value: 5.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 116 RRKAEVDVKVARHRDDLAEYRSRYEDIQQRRESDREKISQWTNAIADAQSEVEMLRARFKQltDEEKRVTADNSRIWEEL 195
Cdd:COG1579  17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK--YEEQLGNVRNNKEYEAL 94

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17533053 196 QKARSDLDDEtigRIDFQNQVQTLMEELEFLrrvhEQEVKELQALLAQApADTREFFKNELALAIRDIKDEYDIIAKQ 273
Cdd:COG1579  95 QKEIESLKRR---ISDLEDEILELMERIEEL----EEELAELEAELAEL-EAELEEKKAELDEELAELEAELEELEAE 164
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
66-270 5.81e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 5.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053   66 DRVKKLEEQNRKLVADLDELrgkwgkdtseikikyseslstaRKDIDDAARRKAEVDVKVARHRDDLAEYRSRYEDIQQR 145
Cdd:COG4913  685 DDLAALEEQLEELEAELEEL----------------------EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  146 resdrekISQWTNAIADAQSEVEMLRARFKQ----LTDEEKRVTADNSRIWEELQKAR-----------SDLDDETIGRI 210
Cdd:COG4913  743 -------ARLELRALLEERFAAALGDAVERElrenLEERIDALRARLNRAEEELERAMrafnrewpaetADLDADLESLP 815

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  211 DFQNQVQTLMEEleflrRVHEQEVKELQALLAQAPADtREFFKNELALAIRDIKDEYDII 270
Cdd:COG4913  816 EYLALLDRLEED-----GLPEYEERFKELLNENSIEF-VADLLSKLRRAIREIKERIDPL 869
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
40-370 6.56e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 6.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053   40 AKSFLEATDKEKKTLQGlndRLGNYIDRVKKLEEQNRKLVADLDELRGKWGKDTSEikikysesLSTARKDIDDAARRKA 119
Cdd:PRK02224 382 RREEIEELEEEIEELRE---RFGDAPVDLGNAEDFLEELREERDELREREAELEAT--------LRTARERVEEAEALLE 450

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  120 E-------VDVKVARHRDDLAEYRSRYEDIQQRRESDREKISQWTNAI------ADAQSEVEMLRARFKQLTD--EEKRV 184
Cdd:PRK02224 451 AgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLeraedlVEAEDRIERLEERREDLEEliAERRE 530

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  185 TADNSRI-WEELQKARSDLDDETIGRidfQNQVQTLMEELEFLRrvheQEVKELQALLAQApADTREFFKN--ELALAIR 261
Cdd:PRK02224 531 TIEEKRErAEELRERAAELEAEAEEK---REAAAEAEEEAEEAR----EEVAELNSKLAEL-KERIESLERirTLLAAIA 602

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  262 DIKDEYDIIAKQGKQ----DMESWYKLK-----VSEVQGSANRANMESTYQRDE-----VKRMRDNIGDLRGKLGDLENK 327
Cdd:PRK02224 603 DAEDEIERLREKREAlaelNDERRERLAekrerKRELEAEFDEARIEEAREDKEraeeyLEQVEEKLDELREERDDLQAE 682

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 17533053  328 NSLLEKEVQNLnyqltDDQRQYEAALNDRDATLRRMREECQTL 370
Cdd:PRK02224 683 IGAVENELEEL-----EELRERREALENRVEALEALYDEAEEL 720
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
103-379 1.16e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  103 SLSTARKDIDDAARRKAEVDVKVARHRDDLAEYRSRYEDIQQRRESDREKISQWTNAIADAQSEVEMLRARFKQLTDEEK 182
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  183 RVTADNSRIWEELqkARSDLDDETIgridfQNQVQTLMEELEFLRRVHEQEVKELQALLAQAPAdtreffkneLALAIRD 262
Cdd:PRK02224 290 ELEEERDDLLAEA--GLDDADAEAV-----EARREELEDRDEELRDRLEECRVAAQAHNEEAES---------LREDADD 353

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  263 IKDEYDiiakqgkqdmeswyklkvsEVQGSANRANMESTYQRDEVKRMRDNIGDLRGKLGDLENKNSLLEKEVQNLNYQL 342
Cdd:PRK02224 354 LEERAE-------------------ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 17533053  343 tDDQRQYEAALNDRDATLRRMREECQTLVAELQALLD 379
Cdd:PRK02224 415 -EELREERDELREREAELEATLRTARERVEEAEALLE 450
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
51-202 1.16e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053   51 KKTLQGLNDRLGNYIDRVKKLEEQNRKLVADLDELRGKWGKDTSEIKIKYSESLSTARKDIDDAARRKAEVDVKVAR--- 127
Cdd:COG4913  294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAlgl 373

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17533053  128 ----HRDDLAEYRSRYEDIQQRRESDREKISQwtnAIADAQSEVEMLRARFKQLTDEEKRVTADNSRIWEELQKARSDL 202
Cdd:COG4913  374 plpaSAEEFAALRAEAAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
108-396 1.18e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  108 RKDIDDAARRkaevdvkVARHRDDLAEYRSRYEDIQQRRESdREKISQWTNAIADAQSEVEMLRARFKQLTDEEKRvtad 187
Cdd:COG4913  220 EPDTFEAADA-------LVEHFDDLERAHEALEDAREQIEL-LEPIRELAERYAAARERLAELEYLRAALRLWFAQ---- 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  188 nsRIWEELQKARSDLDDEtigridfQNQVQTLMEELEFLRRVHEQEVKELQALLAQAPADTREffknELALAIRDIKDEY 267
Cdd:COG4913  288 --RRLELLEAELEELRAE-------LARLEAELERLEARLDALREELDELEAQIRGNGGDRLE----QLEREIERLEREL 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  268 DIIAKqgkqdmeswyklKVSEVQGSANRANMESTYQRDEVKRMRDNIGDLRGklgdlenknsllekevqnlnyQLTDDQR 347
Cdd:COG4913  355 EERER------------RRARLEALLAALGLPLPASAEEFAALRAEAAALLE---------------------ALEEELE 401

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 17533053  348 QYEAALNDRDATLRRMREECQTLVAELQALLDTKQMLDAEIAIYRKMLE 396
Cdd:COG4913  402 ALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
PTZ00121 PTZ00121
MAEBL; Provisional
 69-338 1.29e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    69 KKLEEQNRKLVADLDELRGKWGKDTSEIKIKySESLSTA---RKDIDDAARRKAEVDVKVARHRDDLAEYRSRYEDIQQR 145
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-AEELKKAeeeKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053   146 RESDREKISQWTNAIADAQSEVEMLR--ARFKQLTDEEKRVTADNSRIWEELQKARSDLD-----------------DET 206
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDEKKAAEALKkeAEEAKKAEELKKKEAEEKKKAEELKKAEEENKikaeeakkeaeedkkkaEEA 1749

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053   207 IGRIDFQNQVQTLMEELEflrRVHEQEVKELQALLAQAPADTREFFKNELALAIRDIKDEYDIIAKQGKQD---MESWYK 283
Cdd:PTZ00121 1750 KKDEEEKKKIAHLKKEEE---KKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGnlvINDSKE 1826

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17533053   284 LKVSEVQGSANRANMESTyQRDEVKRMRDNIGDLRGKLGdleNKNSLLEKEVQNL 338
Cdd:PTZ00121 1827 MEDSAIKEVADSKNMQLE-EADAFEKHKFNKNNENGEDG---NKEADFNKEKDLK 1877
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
43-246 1.39e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  43 FLEATDKEKKTLQGLNDRLG-NYIDRVKKLEEQNRKLVADLDELRGKwgkdtSEIKIKYSESLSTARKDIDDAARRKAEV 121
Cdd:COG4717  47 LLERLEKEADELFKPQGRKPeLNLKELKELEEELKEAEEKEEEYAEL-----QEELEELEEELEELEAELEELREELEKL 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 122 DVKVARH---------RDDLAEYRSRYEDIQQR---RESDREKISQWTNAIADAQSEVEMLRARFKQLTDEEKRVTADNs 189
Cdd:COG4717 122 EKLLQLLplyqelealEAELAELPERLEELEERleeLRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE- 200

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17533053 190 riWEELQKARSDLDDEtigRIDFQNQVQTLMEELEFLRRVHE-----QEVKELQALLAQAPA 246
Cdd:COG4717 201 --LEELQQRLAELEEE---LEEAQEELEELEEELEQLENELEaaaleERLKEARLLLLIAAA 257
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 57-420 1.57e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.57  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053     57 LNDRLGNYIDRVKKLEEQNRKLVADLDELRGKWGKDTSEIKIKyseslstaRKDIDDAARRKAEVDVKVARHRDDLAEYR 136
Cdd:TIGR00606  700 LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLK--------EKEIPELRNKLQKVNRDIQRLKNDIEEQE 771

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    137 SRYEDIQQRRESDRekisqwtnaiaDAQSEVEMLRARFKQLTDEEKRV--------TADNSRIWEELQKARSDLDDEtig 208
Cdd:TIGR00606  772 TLLGTIMPEEESAK-----------VCLTDVTIMERFQMELKDVERKIaqqaaklqGSDLDRTVQQVNQEKQEKQHE--- 837

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    209 ridfqnqVQTLMEELEFLRRVHEQEVKELQALLAQ------------APADTREFFKNELALAIRDIKDEYDIIAKQGKQ 276
Cdd:TIGR00606  838 -------LDTVVSKIELNRKLIQDQQEQIQHLKSKtnelkseklqigTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ 910

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    277 D--MESWYKLKVSEVQGSANRANMESTYQRDEVKRMRDNIGDLRGKLGDLENK------NSLLEKE--VQNLNYQLTDDQ 346
Cdd:TIGR00606  911 DspLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiqdgkdDYLKQKEteLNTVNAQLEECE 990

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17533053    347 RQYEAALNDrdatLRRMREECQTLVAELQALLD--TKQMLDAEIAIYRKMLEGEETRVGLTQMVEQAVKTHSLQQQ 420
Cdd:TIGR00606  991 KHQEKINED----MRLMRQDIDTQKIQERWLQDnlTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEEN 1062
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 41-379 1.89e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 41.10  E-value: 1.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  41 KSFLEATDKEKKTLQGLNDRLGNYIDRVKKLEEQN---RKLVADLDELRGKWGKDTSEIKIKYSESLSTARKDIDDAARR 117
Cdd:COG5185 218 ESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSdklEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEK 297

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 118 KAEV--DVKVARHRDDLAEYRSRYEDIQQRRESDREKISQWTNAIADAQSEVEMLRARFKQLTDEEKRVTADN--SRIWE 193
Cdd:COG5185 298 IAEYtkSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVelSKSSE 377

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 194 ELQKARSDLD-----DETIGRiDFQNQVQTLMEELEFLRRVHEQEVKELQALLAQAPADTREfFKNELALAIRDIKDEYD 268
Cdd:COG5185 378 ELDSFKDTIEstkesLDEIPQ-NQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEE-VSKLLNELISELNKVMR 455

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 269 IIAKQGKQDMESWYKLKVSEVQGSANRANmestyqrDEVKRMRDNIGDLRGKLGDLENKnslLEKEVQNLNYQLTDDQRQ 348
Cdd:COG5185 456 EADEESQSRLEEAYDEINRSVRSKKEDLN-------EELTQIESRVSTLKATLEKLRAK---LERQLEGVRSKLDQVAES 525

                       330       340       350
                ....*....|....*....|....*....|.
gi 17533053 349 YEAALNDRDATLRRMREECQTLVAELQALLD 379
Cdd:COG5185 526 LKDFMRARGYAHILALENLIPASELIQASNA 556
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 59-326 2.12e-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: 41.19  E-value: 2.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053     59 DRLGNYIDRVKKLE---EQNRKLVADLDELRGKWGKDTSEIKIKYSE-----SLSTARKDIDDAARRKAEVDVKVARHRD 130
Cdd:TIGR01612 1486 NELKEHIDKSKGCKdeaDKNAKAIEKNKELFEQYKKDVTELLNKYSAlaiknKFAKTKKDSEIIIKEIKDAHKKFILEAE 1565

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    131 DLAEYRSRYEDIQQRRESDREKISQWTNAIADAQSEVEMLRARFKQLTDEEKRVTaDNSRIWEELQKARSDL-----DDE 205
Cdd:TIGR01612 1566 KSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKIN-DCLKETESIEKKISSFsidsqDTE 1644

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    206 TIGRIDFQNQVQTLMEELEFLRRVHEQEVKELQAL---LAQAPADTREFFKNELALAIRDIKDeydiIAKQGKQDMESWY 282
Cdd:TIGR01612 1645 LKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELdseIEKIEIDVDQHKKNYEIGIIEKIKE----IAIANKEEIESIK 1720

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 17533053    283 KL---KVSEVQGSANRANMESTYQRDEVKRMRDNIGDLRGKLGDLEN 326
Cdd:TIGR01612 1721 ELiepTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYN 1767
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 38-247 2.57e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 39.59  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    38 NAAKSFLEATDKEKKTLQGLNDRLGNYIDRVKKLEEQnrklvadLDELRGKwgKDTSEIKIKYSESLSTARKDIDDAARR 117
Cdd:pfam12795  23 QQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQE-------LAALQAK--AEAAPKEILASLSLEELEQRLLQTSAQ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053   118 KAEVDVKVARHRDDLAEYRSRYEDIQQRRESDREKISQWTNAIADAQSEVEMLR-ARFKQLTDEEKRVTADNSRIWEELQ 196
Cdd:pfam12795  94 LQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSeAQRWALQAELAALKAQIDMLEQELL 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17533053   197 ---------KARSDLDDETIGRIDfqNQVQTLMEELEFLRRV-HEQEVKELQALLAQAPAD 247
Cdd:pfam12795 174 snnnrqdllKARRDLLTLRIQRLE--QQLQALQELLNEKRLQeAEQAVAQTEQLAEEAAGD 232
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
39-421 4.75e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 4.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  39 AAKSFLEATDKEKKTLQGLNDRLGNYIDRVKKLEEQNRKLVADLDELR---------GKWGKDTSEIKIKYS--ESLSTA 107
Cdd:COG4717  75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPErlEELEER 154

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 108 RKDIDDAARRKAEVDVKVARHRDDLAEY--------RSRYEDIQQRRESDREKISQWTNAIADAQSEVEMLRARFKQLTD 179
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELleqlslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 180 eEKRVTADNSRIWEELQKAR--------SDLDDETIGRIDF----------------------QNQVQTLMEELEFLRRV 229
Cdd:COG4717 235 -ELEAAALEERLKEARLLLLiaaallalLGLGGSLLSLILTiagvlflvlgllallflllareKASLGKEAEELQALPAL 313

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 230 HEQEVKELQALLAQ--APADTREFFKNELALAIRDIKDEYDIIAKQGKQDMESWYKLKVSEVQGSANRANMESTYQRDEV 307
Cdd:COG4717 314 EELEEEELEELLAAlgLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQ 393

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053 308 KRMRDNIGDLRGKL-GDLENKNSLLEKEVQNLNY-QLTDDQRQYEAALNDRDATLRRMREECQTLVAELQALL--DTKQM 383
Cdd:COG4717 394 AEEYQELKEELEELeEQLEELLGELEELLEALDEeELEEELEELEEELEELEEELEELREELAELEAELEQLEedGELAE 473

                       410       420       430
                ....*....|....*....|....*....|....*...
gi 17533053 384 LDAEIAIYRKMLEGEETRVGLTQMVEQAVKTHSLQQQE 421
Cdd:COG4717 474 LLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 36-401 6.57e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.57  E-value: 6.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053     36 SANAAKSFLEATDKEKKTLQGLNDRLGNYIDRVKKLEEQNRKLVADLDELRGKWGKDTSEIKikyseSLSTARKDIDdaA 115
Cdd:TIGR00618  216 TYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEA-----VLEETQERIN--R 288

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    116 RRKAEvdvKVARHRDDLAEYRSRYEDIQQR---RESDREKISQWTNAIADAQSEVEMLRARFKQLTDEEKRVtadnsRIW 192
Cdd:TIGR00618  289 ARKAA---PLAAHIKAVTQIEQQAQRIHTElqsKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHI-----RDA 360

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    193 EELQKARSDLDDETIGRIDFQNQVQTLMEELEFLRRVHEQEVKELQALLAQAPADTREFfkneLALAIRDIKDEYDIIAK 272
Cdd:TIGR00618  361 HEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF----RDLQGQLAHAKKQQELQ 436

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053    273 QGKQDMESWYKLKVSEVQGSANRANMESTYQRDEVKRMRDNIGDLRGKLGDLENKNSLLEKEVQNLNYQLTDDQRQYEAA 352
Cdd:TIGR00618  437 QRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPA 516

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 17533053    353 LNDRD---ATLRRMREECQTLVAELQALLDTKQMLDAEIAiYRKMLEGEETR 401
Cdd:TIGR00618  517 RQDIDnpgPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK-QRASLKEQMQE 567
46 PHA02562
endonuclease subunit; Provisional
 141-391 7.46e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.23  E-value: 7.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  141 DIQQRRESDREKISQwtNAIADAQSEVEMLRARFKQLTDEEKRVTADNSRIWEELQKARSDLDDETIGRIDFQNQVQTLM 220
Cdd:PHA02562 198 KTYNKNIEEQRKKNG--ENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQ 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  221 EELEFLRRVHE-----QEVKELQALLAqapadtreffknelalairDIKDEYDIIAKQGKQDMEswyklKVSEVQGSANR 295
Cdd:PHA02562 276 KVIKMYEKGGVcptctQQISEGPDRIT-------------------KIKDKLKELQHSLEKLDT-----AIDELEEIMDE 331

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  296 ANMESTYQRDevkrMRDNIGDLRGKLGDLENKNSLLEKEVQNLNYQLTDDQrqyeaalndrdatlrrmrEECQTLVAELQ 375
Cdd:PHA02562 332 FNEQSKKLLE----LKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNA------------------EELAKLQDELD 389

                        250
                 ....*....|....*.
gi 17533053  376 ALLDTKQMLDAEIAIY 391
Cdd:PHA02562 390 KIVKTKSELVKEKYHR 405
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
41-400 9.26e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 9.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053   41 KSFLEATDKEKKTLQGLNDRLGNYIDRVKKLEEQNRKLVADLDELRgkwgkdtseikikyseslstarkdiddaaRRKAE 120
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLE-----------------------------KEVKE 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  121 VDvkvaRHRDDLAEYRSRYEDIQQRRESDREKISQWTNAIADAQSEVEMLRARFKQLTDEEKRVTAdnsriWEELQKARS 200
Cdd:PRK03918 233 LE----ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEE-----YIKLSEFYE 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  201 DLDDEtigridfqnqvqtlMEELEFLRRVHEQEVKELQALLAQAPADTREffKNELALAIRDIKDEYDIIAK------QG 274
Cdd:PRK03918 304 EYLDE--------------LREIEKRLSRLEEEINGIEERIKELEEKEER--LEELKKKLKELEKRLEELEErhelyeEA 367

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17533053  275 KQDMESWYKLKVSEVQGSANRANMESTYQRDEVKRMRDNIGDLRGKLGDLENKNSLLEKEVQNL----------NYQLTD 344
Cdd:PRK03918 368 KAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcGRELTE 447

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17533053  345 DQRqyEAALNDRDATLRRMREECQTLVAELQALLDTKQMLDAEIAIYRKMLEGEET 400
Cdd:PRK03918 448 EHR--KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKEL 501
 
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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