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Conserved domains on  [gi|1953036481|ref|XP_038433657|]
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keratin, type II cytoskeletal 7 [Canis lupus familiaris]

Protein Classification

type II keratin( domain architecture ID 12177255)

type II keratin is an intermediate filament-forming protein that provides mechanical support and fulfills a variety of additional functions in epithelial cells

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
90-402 2.38e-143

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 412.39  E-value: 2.38e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  90 EEREQIKTLNNRFASFIDKVRFLEQQNKLLETKWALLQEQRSARSSCLPSIFEAHIAGLRRHLEGLQTDGGRLEVELRNM 169
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 170 QDVLEDFKNKYEDEINRRTAAENEFVVLKKDVDAAYMSKVELEAKVEALNDEINFFKTLYETELAELQSQISDTSVVLSM 249
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 250 DNSRSLDLDGIIAEVKAQYEEMANRSRAETETMYQSKFETLQAQAGKHGDDLRNTRNEIAEMNRAIQRLQAEIDNIKNQR 329
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953036481 330 AKLEAAIAEAEERGELALKDAHAKQEELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESR 402
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
10-87 5.83e-11

Keratin type II head;


:

Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 60.82  E-value: 5.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  10 FSSRSAAFPG--RGLQVRLSSAR------------PGGFGSRSLLGLGASR---PRVAVRSASGGPGGAG---------- 62
Cdd:pfam16208   2 FSSCSAVVPSrsRRSYSSVSSSRrgggggggggggGGGFGSRSLYNLGGSKsisISVAGGGSRPGSGFGFgggggggfgg 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953036481  63 --------------------------------------------------IRQVTVNQSLLAPLRVDIDPAIQQV 87
Cdd:pfam16208  82 gfgggggggfgggggfgggfggggyggggfggggfggrggfggppcppggIQEVTVNQSLLQPLNLEIDPEIQRV 156
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
90-402 2.38e-143

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 412.39  E-value: 2.38e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  90 EEREQIKTLNNRFASFIDKVRFLEQQNKLLETKWALLQEQRSARSSCLPSIFEAHIAGLRRHLEGLQTDGGRLEVELRNM 169
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 170 QDVLEDFKNKYEDEINRRTAAENEFVVLKKDVDAAYMSKVELEAKVEALNDEINFFKTLYETELAELQSQISDTSVVLSM 249
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 250 DNSRSLDLDGIIAEVKAQYEEMANRSRAETETMYQSKFETLQAQAGKHGDDLRNTRNEIAEMNRAIQRLQAEIDNIKNQR 329
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953036481 330 AKLEAAIAEAEERGELALKDAHAKQEELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESR 402
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
10-87 5.83e-11

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 60.82  E-value: 5.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  10 FSSRSAAFPG--RGLQVRLSSAR------------PGGFGSRSLLGLGASR---PRVAVRSASGGPGGAG---------- 62
Cdd:pfam16208   2 FSSCSAVVPSrsRRSYSSVSSSRrgggggggggggGGGFGSRSLYNLGGSKsisISVAGGGSRPGSGFGFgggggggfgg 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953036481  63 --------------------------------------------------IRQVTVNQSLLAPLRVDIDPAIQQV 87
Cdd:pfam16208  82 gfgggggggfgggggfgggfggggyggggfggggfggrggfggppcppggIQEVTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 84-384 1.66e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 1.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481   84 IQQVRREEREQIKTLNNRFASFIDKVRFLEQQNKLLETKWALLQEQRSARSSCLPSIF------EAHIAGLRRHLEGLQT 157
Cdd:TIGR02168  717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEeelaeaEAEIEELEAQIEQLKE 796

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  158 DGGRLEVELRNMQDVLEDFKNKYEDEINRRTAAENEFVVLKKDVDAAYMSKVELEAKVEALNDEINffktLYETELAELQ 237
Cdd:TIGR02168  797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE----ELEELIEELE 872

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  238 SQisdtsvvlsmdnsrsldLDGIIAEVKAQYEEMANRSRAETETMyqSKFETLQAQAGKHGDDLRNTRNEIAEMNRAIQR 317
Cdd:TIGR02168  873 SE-----------------LEALLNERASLEEALALLRSELEELS--EELRELESKRSELRRELEELREKLAQLELRLEG 933

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953036481  318 LQAEIDNIKNQRAkleaaiaeaeERGELALKDAHAKQEELEAALQRAKQDMARQLREYQELMNVKLA 384
Cdd:TIGR02168  934 LEVRIDNLQERLS----------EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 149-404 1.11e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 149 RRHLEgLQTDGGRLEVELRNMQdvLEDFKNKYEDEINRRTAAENEFVVLKKDVDAAYMSKVELEAKVEALNDEINffktL 228
Cdd:COG1196   213 ERYRE-LKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE----E 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 229 YETELAELQSQISDTSVVLSMDNSRSLDLDGIIAEVKAQYEEMANRSRAETETMyqskfETLQAQAGKHGDDLRNTRNEI 308
Cdd:COG1196   286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL-----EELEEELEEAEEELEEAEAEL 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 309 AEMNRAIQRLQAEIDNIKNQRAKLEAAIAEAeergELALKDAHAKQEELEAALQRAKQDMARQLREYQELMNVKLALDIE 388
Cdd:COG1196   361 AEAEEALLEAEAELAEAEEELEELAEELLEA----LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436

                         250
                  ....*....|....*.
gi 1953036481 389 IATYRKLLEGEESRLA 404
Cdd:COG1196   437 EEEEEEALEEAAEEEA 452
46 PHA02562
endonuclease subunit; Provisional
 107-332 1.34e-06

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 50.78  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 107 DKVRFLEQQNKLLETKWALLQEQrsarssclpsifeahIAGLRRHLEGLQTDGGRLEVELRNMQDVLEDFKNKYEDEINR 186
Cdd:PHA02562  174 DKIRELNQQIQTLDMKIDHIQQQ---------------IKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEE 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 187 RTAAENEFVVLKKDVDAAY----MSKVELEAKVEALNDEINFFKTlyETELAELQSQISDTSVVLSMDNSRSLDLDGIIA 262
Cdd:PHA02562  239 LTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEK--GGVCPTCTQQISEGPDRITKIKDKLKELQHSLE 316

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 263 EVKAQYEEMAnrSRAETETMYQSKFETLQAQAGKHGDDLRNTRNEIAEMNRAIQRLQAEIDNIKNQRAKL 332
Cdd:PHA02562  317 KLDTAIDELE--EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKL 384
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
90-402 2.38e-143

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 412.39  E-value: 2.38e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  90 EEREQIKTLNNRFASFIDKVRFLEQQNKLLETKWALLQEQRSARSSCLPSIFEAHIAGLRRHLEGLQTDGGRLEVELRNM 169
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 170 QDVLEDFKNKYEDEINRRTAAENEFVVLKKDVDAAYMSKVELEAKVEALNDEINFFKTLYETELAELQSQISDTSVVLSM 249
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 250 DNSRSLDLDGIIAEVKAQYEEMANRSRAETETMYQSKFETLQAQAGKHGDDLRNTRNEIAEMNRAIQRLQAEIDNIKNQR 329
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953036481 330 AKLEAAIAEAEERGELALKDAHAKQEELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESR 402
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
10-87 5.83e-11

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 60.82  E-value: 5.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  10 FSSRSAAFPG--RGLQVRLSSAR------------PGGFGSRSLLGLGASR---PRVAVRSASGGPGGAG---------- 62
Cdd:pfam16208   2 FSSCSAVVPSrsRRSYSSVSSSRrgggggggggggGGGFGSRSLYNLGGSKsisISVAGGGSRPGSGFGFgggggggfgg 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953036481  63 --------------------------------------------------IRQVTVNQSLLAPLRVDIDPAIQQV 87
Cdd:pfam16208  82 gfgggggggfgggggfgggfggggyggggfggggfggrggfggppcppggIQEVTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 84-384 1.66e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 1.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481   84 IQQVRREEREQIKTLNNRFASFIDKVRFLEQQNKLLETKWALLQEQRSARSSCLPSIF------EAHIAGLRRHLEGLQT 157
Cdd:TIGR02168  717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEeelaeaEAEIEELEAQIEQLKE 796

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  158 DGGRLEVELRNMQDVLEDFKNKYEDEINRRTAAENEFVVLKKDVDAAYMSKVELEAKVEALNDEINffktLYETELAELQ 237
Cdd:TIGR02168  797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE----ELEELIEELE 872

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  238 SQisdtsvvlsmdnsrsldLDGIIAEVKAQYEEMANRSRAETETMyqSKFETLQAQAGKHGDDLRNTRNEIAEMNRAIQR 317
Cdd:TIGR02168  873 SE-----------------LEALLNERASLEEALALLRSELEELS--EELRELESKRSELRRELEELREKLAQLELRLEG 933

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953036481  318 LQAEIDNIKNQRAkleaaiaeaeERGELALKDAHAKQEELEAALQRAKQDMARQLREYQELMNVKLA 384
Cdd:TIGR02168  934 LEVRIDNLQERLS----------EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 85-406 3.56e-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: 52.75  E-value: 3.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481   85 QQVRREEREQIKTLNNRFASFIDKVRFLEQQNKLLETKWALLQEQRSARSSCLPSIfEAHIAGLRRHLEGLQTDGGRLEV 164
Cdd:TIGR02168  669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL-SRQISALRKDLARLEAEVEQLEE 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  165 ELRNMQDVLEDFKNKYEDEINRRTAAENEFVVLKKDvdaaymsKVELEAKVEALNDEINffktLYETELAELQSQISDTS 244
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELK----ALREALDELRAELTLLN 816

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  245 VVLSMDNSRSLDLDGIIAEVKAQYEEMANRSRAETETMyqskfETLQAqagkhgddlrntrnEIAEMNRAIQRLQAEIDN 324
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI-----ESLAA--------------EIEELEELIEELESELEA 877

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  325 IKNQRAKLEAAIAEAeergELALKDAHAKQEELEAALQRAKQDMaRQLREYQELMNVKLA-LDIEIATYRKLLEGEESRL 403
Cdd:TIGR02168  878 LLNERASLEEALALL----RSELEELSEELRELESKRSELRREL-EELREKLAQLELRLEgLEVRIDNLQERLSEEYSLT 952


                   ...
gi 1953036481  404 AGD 406
Cdd:TIGR02168  953 LEE 955
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 149-404 1.11e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 149 RRHLEgLQTDGGRLEVELRNMQdvLEDFKNKYEDEINRRTAAENEFVVLKKDVDAAYMSKVELEAKVEALNDEINffktL 228
Cdd:COG1196   213 ERYRE-LKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE----E 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 229 YETELAELQSQISDTSVVLSMDNSRSLDLDGIIAEVKAQYEEMANRSRAETETMyqskfETLQAQAGKHGDDLRNTRNEI 308
Cdd:COG1196   286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL-----EELEEELEEAEEELEEAEAEL 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 309 AEMNRAIQRLQAEIDNIKNQRAKLEAAIAEAeergELALKDAHAKQEELEAALQRAKQDMARQLREYQELMNVKLALDIE 388
Cdd:COG1196   361 AEAEEALLEAEAELAEAEEELEELAEELLEA----LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436

                         250
                  ....*....|....*.
gi 1953036481 389 IATYRKLLEGEESRLA 404
Cdd:COG1196   437 EEEEEEALEEAAEEEA 452
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 117-410 1.16e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 117 KLLETKWALLQEQRSARssclpsifEAHIAGLRRHLEGLQTDGGRLEVELRNMQDVLEDFKNKYEDEINRRTAAENEFVV 196
Cdd:COG1196   235 RELEAELEELEAELEEL--------EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 197 LKKDVDAAYMSKVELEAKVEALNDEINffktLYETELAELQSQISDTSVVLSMDNSRSLDLDGIIAEVKAQYEEmanrSR 276
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELE----ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE----AE 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 277 AETETMYQSKFETLQAQAGKHgDDLRNTRNEIAEMNRAIQRLQAEIDNIKNQRAKLEAAIAEAEERGELALKDAHAKQEE 356
Cdd:COG1196   379 EELEELAEELLEALRAAAELA-AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953036481 357 LEAALQRAKQDmARQLREYQELMNVKLALDIEIATYRKLLEGEESRLAGDGVGA 410
Cdd:COG1196   458 EEALLELLAEL-LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
46 PHA02562
endonuclease subunit; Provisional
 107-332 1.34e-06

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 50.78  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 107 DKVRFLEQQNKLLETKWALLQEQrsarssclpsifeahIAGLRRHLEGLQTDGGRLEVELRNMQDVLEDFKNKYEDEINR 186
Cdd:PHA02562  174 DKIRELNQQIQTLDMKIDHIQQQ---------------IKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEE 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 187 RTAAENEFVVLKKDVDAAY----MSKVELEAKVEALNDEINFFKTlyETELAELQSQISDTSVVLSMDNSRSLDLDGIIA 262
Cdd:PHA02562  239 LTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEK--GGVCPTCTQQISEGPDRITKIKDKLKELQHSLE 316

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 263 EVKAQYEEMAnrSRAETETMYQSKFETLQAQAGKHGDDLRNTRNEIAEMNRAIQRLQAEIDNIKNQRAKL 332
Cdd:PHA02562  317 KLDTAIDELE--EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKL 384
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 253-404 4.94e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 4.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  253 RSLDLDGIIAEVKAQYEEMANRSraETETMYQSKFETLQAQAGKHGDDLRNTRNEIAEMNRAIQRLQAEIDNIKNQRAKL 332
Cdd:TIGR02168  223 RELELALLVLRLEELREELEELQ--EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953036481  333 EAAIAEAEERGELA---LKDAHAKQEELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLA 404
Cdd:TIGR02168  301 EQQKQILRERLANLerqLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 88-379 6.89e-06

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 48.35  E-value: 6.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  88 RREEREQIKTLNNRFASFIDKVRFLEQQNKLLETKWALLQEQRSArsscLPSIFEAHIAGLRRHLEGLQTDGGRL---EV 164
Cdd:pfam07888  75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDA----LLAQRAAHEARIRELEEDIKTLTQRVlerET 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 165 ELRNMQDVLEDFKN-KYEDEINRRT------AAENEFVVLKKDVDAAYMSKVELEAKVEALNDEINFFKTL------YET 231
Cdd:pfam07888 151 ELERMKERAKKAGAqRKEEEAERKQlqaklqQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKlttahrKEA 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 232 ELAELQSQISDTSVVLSMDNSRSLDLDGIIAEVKAQyeemanRSRAETEtMYQSKFETLQ----------------AQAG 295
Cdd:pfam07888 231 ENEALLEELRSLQERLNASERKVEGLGEELSSMAAQ------RDRTQAE-LHQARLQAAQltlqladaslalregrARWA 303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 296 KHGDDLRNT----RNEIAEMNRAIQRLQAEIDNIKNQRAKLEAAIAEAEERGELALKDAHAKQEELEAALQRAKQDMARQ 371
Cdd:pfam07888 304 QERETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQL 383


                  ....*...
gi 1953036481 372 LREYQELM 379
Cdd:pfam07888 384 QAEKQELL 391
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 110-403 8.76e-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: 45.05  E-value: 8.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  110 RFLEQQNKLLETKWALL----QEQRSARSSclpsiFEAHIAGLRRHLEGLQTDGGRLEVELrnmqDVLEDFKNKYEDEIN 185
Cdd:TIGR02168  214 RYKELKAELRELELALLvlrlEELREELEE-----LQEELKEAEEELEELTAELQELEEKL----EELRLEVSELEEEIE 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  186 RRTAAENEFVVLKKDVDaayMSKVELEAKVEALNDEInffkTLYETELAELQSQISDTSVVLSMDNSRSLDLDGIIAEVK 265
Cdd:TIGR02168  285 ELQKELYALANEISRLE---QQKQILRERLANLERQL----EELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  266 AQYEEmANRSRAETETMYQSKFETLQAQAGK---HGDDLRNTRNEIAEMNRAIQRLQAEIDNIKNQRAKLEAAIAEAEE- 341
Cdd:TIGR02168  358 AELEE-LEAELEELESRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELk 436

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953036481  342 --RGELALKDahAKQEELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRL 403
Cdd:TIGR02168  437 elQAELEELE--EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 161-374 9.62e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.37  E-value: 9.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 161 RLEVELRNMQDVLEDFKNKYEDEINRRTAAENEFVVLKKDVDAAYMSKVELEAKVEALNDEINffktLYETELAELQSQI 240
Cdd:COG4942    31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA----ELRAELEAQKEEL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 241 SDTSVVLSMdNSRSLDLDGII-------AEVKAQYEEMANRSRAETETMYQSKFETLQAQAgkhgDDLRNTRNEIAEMNR 313
Cdd:COG4942   107 AELLRALYR-LGRQPPLALLLspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALR----AELEAERAELEALLA 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953036481 314 AIQRLQAEIDNIKNQRAKLEAAIAEAEERGELALKDAHAKQEELEAALQRAKQDMARQLRE 374
Cdd:COG4942   182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
PRK01156 PRK01156
chromosome segregation protein; Provisional
 77-400 4.14e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.97  E-value: 4.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  77 RVDIDPAIQQVRREE-REQIKTLNNRFASFIDKVRFLEQQNKLLETKWALLqEQRSARSSCLPSIFEAHIAGLRRH---- 151
Cdd:PRK01156  399 IQEIDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEML-NGQSVCPVCGTTLGEEKSNHIINHynek 477

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 152 LEGLQTDGGRLEVELRNMQDVLEDFKNKYE----DEINRRTAAENEFVVLKKDVDAAYMSKVELEAKVEALNDEINFFKT 227
Cdd:PRK01156  478 KSRLEEKIREIEIEVKDIDEKIVDLKKRKEylesEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKS 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 228 LyetELAELQSQisDTSVVLSMDNSRSLDLDGIIA---EVKAQYEEMANRSRaETETMYQSKFETLQAQAGKHGDDLRNT 304
Cdd:PRK01156  558 L---KLEDLDSK--RTSWLNALAVISLIDIETNRSrsnEIKKQLNDLESRLQ-EIEIGFPDDKSYIDKSIREIENEANNL 631

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 305 R---NEIAEMNRAIQRLQAEIDNIKNQRAKLEAAIAEAEERGELALkDAHAKQEELEAALQRAKQDMARQLREYQELMNV 381
Cdd:PRK01156  632 NnkyNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIN-DIEDNLKKSRKALDDAKANRARLESTIEILRTR 710

                         330
                  ....*....|....*....
gi 1953036481 382 KLALDIEIATYRKLLEGEE 400
Cdd:PRK01156  711 INELSDRINDINETLESMK 729
PRK09039 PRK09039
peptidoglycan -binding protein;
230-374 5.09e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.26  E-value: 5.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 230 ETELAELQSQISDTSVVLSMDNSRSLDLDGIIAEVKAQYEEM-ANRSRAETETMYQSKFET-LQAQAGKHGDDLRNTRNE 307
Cdd:PRK09039   52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAeAERSRLQALLAELAGAGAaAEGRAGELAQELDSEKQV 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953036481 308 IAEMNRAIQRLQAEIDNIKNQRAKLEAAIAEAEERGELALKDAHAKQEELEAALQRAKQDMAR-------QLRE 374
Cdd:PRK09039  132 SARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALAQRVQELNRyrseffgRLRE 205
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 145-404 1.05e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  145 IAGLRRHLEGLQTDGGRLEVELRNMQDVLEDFKNKYEDEINRRTAAENEFVVLKKDVDAAYMSKVELEAKVEALNDEINF 224
Cdd:TIGR02169  655 MTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  225 FKTlyetELAELQSQISDTSVVLSMDNSRSLDLDGIIAEVKAQYEEmanrsraetetmYQSKFETLQAQAGKHGddlrnt 304
Cdd:TIGR02169  735 LKE----RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK------------LEEALNDLEARLSHSR------ 792

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  305 rneiaemnraIQRLQAEIDNIKNQRAKLEaaiaeaeergelalkdahAKQEELEAALQRAKQDMARQLREYQELMNVKLA 384
Cdd:TIGR02169  793 ----------IPEIQAELSKLEEEVSRIE------------------ARLREIEQKLNRLTLEKEYLEKEIQELQEQRID 844

                          250       260
                   ....*....|....*....|
gi 1953036481  385 LDIEIATYRKLLEGEESRLA 404
Cdd:TIGR02169  845 LKEQIKSIEKEIENLNGKKE 864
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 83-386 1.09e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.64  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481   83 AIQQVRREEREQIKTLNNRFASFIDKVRFL--EQQNKLletkwALLQEQRSARSSCLPSIFEAHIAGLRRHLEGLQTDGG 160
Cdd:pfam15921  221 AISKILRELDTEISYLKGRIFPVEDQLEALksESQNKI-----ELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQAN 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  161 RLEVELRNMQDvledfknkyedeinrrtAAENEfvvlkkdvDAAYMSKV-ELEAKVEALNDEINFFKTLYETELAELQSQ 239
Cdd:pfam15921  296 SIQSQLEIIQE-----------------QARNQ--------NSMYMRQLsDLESTVSQLRSELREAKRMYEDKIEELEKQ 350

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  240 ISDTSVVLSMDNSRSLDLDGIIAEVKAQYEE-MANRSRAETE-TMYQSKFETLQAQAGKHGDDLRNTRNEIAEMNRAIQR 317
Cdd:pfam15921  351 LVLANSELTEARTERDQFSQESGNLDDQLQKlLADLHKREKElSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQR 430

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  318 LQAEIDNIKNQ-RAKLEAAIAEAEERGElalkdAHAKQEELEAALQRAKQdMARQLREyqELMNVKLALD 386
Cdd:pfam15921  431 LEALLKAMKSEcQGQMERQMAAIQGKNE-----SLEKVSSLTAQLESTKE-MLRKVVE--ELTAKKMTLE 492
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
93-400 1.40e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  93 EQIKTLNNRFASFIDKVRFLEQQNKLLETKWALLqeqrSARSSCLPSIFEAhIAGLRRHLEGLQTDGGRLEVELRNMQDV 172
Cdd:PRK03918  193 ELIKEKEKELEEVLREINEISSELPELREELEKL----EKEVKELEELKEE-IEELEKELESLEGSKRKLEEKIRELEER 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 173 LEDFKNKYED-EINRRTAAEnefvvLKKDVDaAYMSKVELEAKVEALNDEINFFKTLYETELAELQSQISDtsvvLSMDN 251
Cdd:PRK03918  268 IEELKKEIEElEEKVKELKE-----LKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE----LEEKE 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 252 SRSLDLDGIIAEVKAQYEEMANRSRaETETMYQSKFETLQAQAGKHGDDLRNTRNEIAEMNRAIQRLQAEIDNIKNQRAK 331
Cdd:PRK03918  338 ERLEELKKKLKELEKRLEELEERHE-LYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953036481 332 LEAAIAEAEERGElALKDAHAK---------QEELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEE 400
Cdd:PRK03918  417 LKKEIKELKKAIE-ELKKAKGKcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES 493
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 78-331 2.68e-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: 40.42  E-value: 2.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481   78 VDIDPAIQQVRREEREQIKTLNNRFASFIDKVRFLEQQNKLLETKWALLQEQRSARSSCLPSI-----FEAHIAGLRRHL 152
Cdd:TIGR00606  818 SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLqrrqqFEEQLVELSTEV 897

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  153 EGLQTDGGRLEVELRNMQDVLEDFKNKYEDEINRRTA----AENEFVVLKKDVDAAYMSKVELEAKVEALNDEinfFKTL 228
Cdd:TIGR00606  898 QSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETsnkkAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDD---YLKQ 974

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  229 YETELAELQSQISDTSVVLSMDNSrslDLDGIIAEVKAQYEEMANRSRAETETMYQSKFETLQAQAGKHGDDLRNTRneI 308
Cdd:TIGR00606  975 KETELNTVNAQLEECEKHQEKINE---DMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQ--V 1049

                          250       260
                   ....*....|....*....|...
gi 1953036481  309 AEMNRAIQRLQAEIDNIKNQRAK 331
Cdd:TIGR00606 1050 LQMKQEHQKLEENIDLIKRNHVL 1072
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 107-393 3.07e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 3.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  107 DKVRFLEQQNKLLETKWALLQEQRSARSSCLPSIFE-AHIAGLRRHLEGLQTDGGRLEVELRNMQDVLEDFKNKYEDEIN 185
Cdd:TIGR02169  637 GKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEpAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR 716

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  186 RRTAAENEFVVLKKDVDAAYMSKVELEAKVEALNDEInffkTLYETELAELQSQISdtsvvlsmdnsrslDLDGIIAEVK 265
Cdd:TIGR02169  717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI----ENVKSELKELEARIE--------------ELEEDLHKLE 778

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  266 AQYEEMANRSRaetetmyQSKFETLQAQAGKHGDDLRNTRNEIAEMNRAIQR-------LQAEIDNIKNQRAKLEAAIAE 338
Cdd:TIGR02169  779 EALNDLEARLS-------HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRltlekeyLEKEIQELQEQRIDLKEQIKS 851

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953036481  339 AEERGELALKDAHAKQEELE-------------AALQRAKQDMARQLREYQELMNvKLALDIEIATYR 393
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEeleaalrdlesrlGDLKKERDELEAQLRELERKIE-ELEAQIEKKRKR 918
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
230-403 4.26e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 4.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  230 ETELAELQSQISDtsvvlsmdnsrsldLDGIIAEVKAQYEEMANRSRA----ETETMYQSKFETLQAQAGKHGD---DLR 302
Cdd:COG4913    616 EAELAELEEELAE--------------AEERLEALEAELDALQERREAlqrlAEYSWDEIDVASAEREIAELEAeleRLD 681

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  303 NTRNEIAEMNRAIQRLQAEIDNIKNQRAKLEAAIAEAEERGELALKDAHAKQEELEAALQRAKQDMARQLRE-YQELM-- 379
Cdd:COG4913    682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErFAAALgd 761

                          170       180
                   ....*....|....*....|....*...
gi 1953036481  380 ----NVKLALDIEIATYRKLLEGEESRL 403
Cdd:COG4913    762 averELRENLEERIDALRARLNRAEEEL 789
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 84-332 6.03e-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: 39.23  E-value: 6.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  84 IQQVRREEREQIKTLNNRFASFIDKVRFLEQQNKLLETKwalLQEQrsarssclpsifEAHIAGLRRHLEGLQTDGGRLE 163
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQ------------EKLNQQKDEQIKKLQQEKELLE 425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 164 VELRNmqdvLEDFKNKYEDEINRrtaAENEFVVLKKDVDAAYMSKVELEAKVEALNDEINFFKTLYETELAELQSQISDt 243
Cdd:TIGR04523 426 KEIER----LKETIIKNNSEIKD---LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE- 497

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 244 svvLSMDNSRSLDLDGIIAEVKAQYEEMANRSRAETETMYQSKFETLQAQAGKHGDDLRNTRN----EIAEMNRAIQRLQ 319
Cdd:TIGR04523 498 ---LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlekEIDEKNKEIEELK 574

                         250
                  ....*....|...
gi 1953036481 320 AEIDNIKNQRAKL 332
Cdd:TIGR04523 575 QTQKSLKKKQEEK 587
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 300-376 6.31e-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: 38.59  E-value: 6.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 300 DLRNTRNEIAEMNRAIQRLQAEIDNIKNQRAKLEAAIAEAEER----------GELALKDAHAKQEELEAALQRAKQDMA 369
Cdd:COG4942    28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraleqelaaLEAELAELEKEIAELRAELEAQKEELA 107


                  ....*..
gi 1953036481 370 RQLREYQ 376
Cdd:COG4942   108 ELLRALY 114
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 190-410 6.98e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 6.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 190 AENEFVVLKKDVDAAYMSKVELEAKVEALNDEINFFKTLY---ETELAELQSQISDTSVvlsmdnsrslDLDGIIAEVKA 266
Cdd:COG3883    14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYnelQAELEALQAEIDKLQA----------EIAEAEAEIEE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 267 QYEEMANRSRAETETMYQSKFETLQAQAGKHGDDLRN--TRNEIAEMNRAI----QRLQAEIDNIKNQRAKLEAAIAEAE 340
Cdd:COG3883    84 RREELGERARALYRSGGSVSYLDVLLGSESFSDFLDRlsALSKIADADADLleelKADKAELEAKKAELEAKLAELEALK 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481 341 ERGELALKDAHAKQEELEAALQRAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEESRLAGDGVGA 410
Cdd:COG3883   164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 84-406 7.90e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 38.95  E-value: 7.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481   84 IQQVRREEREQIKTLNNRFASFIDKVRFLEQQNKLLETKWALLQEQRSARSSCLPSIfeAHIAGLRRHLEGLQTDGGRLE 163
Cdd:pfam15921  477 LRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQEL--QHLKNEGDHLRNVQTECEALK 554

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  164 VELRNMQDVLEDFKNKYEDEI-----NRRTAAenefvvlkkdvdAAYMSKVELEAKVEALNDEINFFKTLYE---TELAE 235
Cdd:pfam15921  555 LQMAEKDKVIEILRQQIENMTqlvgqHGRTAG------------AMQVEKAQLEKEINDRRLELQEFKILKDkkdAKIRE 622

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  236 LQSQISDTSV-VLSMDNSRSLDLDGIiAEVKAQYEEMANR---SRAETETMYQsKFETLQaqagkhgddlRNTRNEIAEM 311
Cdd:pfam15921  623 LEARVSDLELeKVKLVNAGSERLRAV-KDIKQERDQLLNEvktSRNELNSLSE-DYEVLK----------RNFRNKSEEM 690

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  312 NRAIQRLQAEIDNIKNQRAKLEAAIAEAEERGELALKDAHAKQEE----------LEAALQRAKQDMARQLREYQELMNV 381
Cdd:pfam15921  691 ETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQitakrgqidaLQSKIQFLEEAMTNANKEKHFLKEE 770

                          330       340
                   ....*....|....*....|....*
gi 1953036481  382 KLALDIEIATyrklLEGEESRLAGD 406
Cdd:pfam15921  771 KNKLSQELST----VATEKNKMAGE 791
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 83-328 9.05e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.51  E-value: 9.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481   83 AIQQVRREEREQIKTLNNRFASFIDKVRFLEQQNKLLETKWALLQEQRSARssclpsifEAHIAGLRRHLEGLQTDGGRL 162
Cdd:TIGR02169  802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI--------EKEIENLNGKKEELEEELEEL 873

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  163 EVELRNMQDVLEDFKNKYEDEINRRTAAENEFVVLKKDVDAAYMSKVELEAKVEALNDEInffkTLYETELAELQSQISD 242
Cdd:TIGR02169  874 EAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL----SEIEDPKGEDEEIPEE 949

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953036481  243 TsvvlsmdnsrsLDLDGIIAEVKAQYEEMAN----RSRAETEtmYQSKFETLqaqagkhgDDLRNTRNEIAEMNRAIQRL 318
Cdd:TIGR02169  950 E-----------LSLEDVQAELQRVEEEIRAlepvNMLAIQE--YEEVLKRL--------DELKEKRAKLEEERKAILER 1008

                          250
                   ....*....|
gi 1953036481  319 QAEIDNIKNQ 328
Cdd:TIGR02169 1009 IEEYEKKKRE 1018
 
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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