NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|348581109|ref|XP_003476320|]
View 

keratin, type II cytoskeletal 8 [Cavia porcellus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
92-403 1.49e-148

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 426.26  E-value: 1.49e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   92 QEKEQIKNLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSR-SNMDNMFESYINNLRRQLDTLGQEKLKLEAELGNM 170
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  171 QGMVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEEEIRELQSQISDTSVVLSM 250
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  251 DNSRSLDLDGIIAEVKAQYEEIANRSRAEAESMYQIKYEELQTLAGKHGDDLRRTKSEISEMNRSISRLQAEIEALKGQR 330
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 348581109  331 AALEAAIADAEQRGEMAIKDANAKLAQLESALQKAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEENR 403
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
65-89 3.68e-09

Keratin type II head;


:

Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 55.43  E-value: 3.68e-09
                          10        20
                  ....*....|....*....|....*
gi 348581109   65 ITAVQVNQSLLNPLNLEVDPNIQAV 89
Cdd:pfam16208 132 IQEVTVNQSLLQPLNLEIDPEIQRV 156
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
92-403 1.49e-148

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 426.26  E-value: 1.49e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   92 QEKEQIKNLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSR-SNMDNMFESYINNLRRQLDTLGQEKLKLEAELGNM 170
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  171 QGMVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEEEIRELQSQISDTSVVLSM 250
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  251 DNSRSLDLDGIIAEVKAQYEEIANRSRAEAESMYQIKYEELQTLAGKHGDDLRRTKSEISEMNRSISRLQAEIEALKGQR 330
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 348581109  331 AALEAAIADAEQRGEMAIKDANAKLAQLESALQKAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEENR 403
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 87-411 2.66e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 69.32  E-value: 2.66e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109    87 QAVRIQEKEQIKNLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQLDTLGQEKLKLEAE 166
Cdd:TIGR02168  669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   167 LGNMQGMVEDFKNKYEDEINKRTEMENEFVlikkdvdEAYMNKVELESRLEGLTDEINFLRqlyeEEIRELQSQISDTSV 246
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELA-------EAEAEIEELEAQIEQLKEELKALR----EALDELRAELTLLNE 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   247 VLSMDNSRSLDLDGIIAEVKAQYEEIANRSRAEAESMYQIK--YEELQTLAGKHGDDLRRTKSEISEMNRSISRLQAEIE 324
Cdd:TIGR02168  818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaeIEELEELIEELESELEALLNERASLEEALALLRSELE 897

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   325 ALKGQRAALEAAIADAEQrgemAIKDANAKLAQLESALQKAKQDMARQLR----EYQELMNVKLALDIEIATYRKLLEGE 400
Cdd:TIGR02168  898 ELSEELRELESKRSELRR----ELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEALENKIEDDEEEARRR 973

                          330
                   ....*....|.
gi 348581109   401 ENRLEAGMQNL 411
Cdd:TIGR02168  974 LKRLENKIKEL 984
Keratin_2_head pfam16208
Keratin type II head;
65-89 3.68e-09

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 55.43  E-value: 3.68e-09
                          10        20
                  ....*....|....*....|....*
gi 348581109   65 ITAVQVNQSLLNPLNLEVDPNIQAV 89
Cdd:pfam16208 132 IQEVTVNQSLLQPLNLEIDPEIQRV 156
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
94-398 7.07e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.07  E-value: 7.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  94 KEQIKNLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKtsrSNMDNMFESyINNLRRQLDTLGQEKLKLEAELGNMQGM 173
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEV---KELEELKEE-IEELEKELESLEGSKRKLEEKIRELEER 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 174 VEDFKNKYED------EINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGltdeinflrqlYEEEIRELQSQISDtsvv 247
Cdd:PRK03918 268 IEELKKEIEEleekvkELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR-----------LEEEINGIEERIKE---- 332

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 248 LSMDNSRSLDLDGIIAEVKAQYEEIA------NRSRAEAESMYQIK--------------YEELQTLAGKHGDDLRRTKS 307
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEELEerhelyEEAKAKKEELERLKkrltgltpeklekeLEELEKAKEEIEEEISKITA 412

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 308 EISEMNRSISRLQAEIEALKGQRAA--LEAAIADAEQRGEMaIKDANAKLAQLESALQKAKqDMARQLREYQELMNVKLA 385
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKEL-LEEYTAELKRIEKELKEIE-EKERKLRKELRELEKVLK 490

                        330
                 ....*....|...
gi 348581109 386 LDIEIATYRKLLE 398
Cdd:PRK03918 491 KESELIKLKELAE 503
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 145-411 1.09e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 145 YINNLRRQLDTLGQEKLKLEAELgnmqgmvEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEIN 224
Cdd:COG1196  233 KLRELEAELEELEAELEELEAEL-------EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 225 FLrqlyEEEIRELQSQISDTSVVLSMDNSRSLDLDGIIAEVKAQYEEIANRSRAEAESMYQI--KYEELQTLAGKHGDDL 302
Cdd:COG1196  306 RL----EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeeALLEAEAELAEAEEEL 381

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 303 RRTKSEISEMNRSISRLQAEIEALKGQRAALEAAIADAEQrgemAIKDANAKLAQLESALQKAKQDMARQLREYQELMNV 382
Cdd:COG1196  382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE----ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                        250       260
                 ....*....|....*....|....*....
gi 348581109 383 KLALDIEIATYRKLLEGEENRLEAGMQNL 411
Cdd:COG1196  458 EEALLELLAELLEEAALLEAALAELLEEL 486
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
92-403 1.49e-148

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 426.26  E-value: 1.49e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   92 QEKEQIKNLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSR-SNMDNMFESYINNLRRQLDTLGQEKLKLEAELGNM 170
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  171 QGMVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEEEIRELQSQISDTSVVLSM 250
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  251 DNSRSLDLDGIIAEVKAQYEEIANRSRAEAESMYQIKYEELQTLAGKHGDDLRRTKSEISEMNRSISRLQAEIEALKGQR 330
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 348581109  331 AALEAAIADAEQRGEMAIKDANAKLAQLESALQKAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEENR 403
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 87-411 2.66e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 69.32  E-value: 2.66e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109    87 QAVRIQEKEQIKNLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQLDTLGQEKLKLEAE 166
Cdd:TIGR02168  669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   167 LGNMQGMVEDFKNKYEDEINKRTEMENEFVlikkdvdEAYMNKVELESRLEGLTDEINFLRqlyeEEIRELQSQISDTSV 246
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELA-------EAEAEIEELEAQIEQLKEELKALR----EALDELRAELTLLNE 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   247 VLSMDNSRSLDLDGIIAEVKAQYEEIANRSRAEAESMYQIK--YEELQTLAGKHGDDLRRTKSEISEMNRSISRLQAEIE 324
Cdd:TIGR02168  818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaeIEELEELIEELESELEALLNERASLEEALALLRSELE 897

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   325 ALKGQRAALEAAIADAEQrgemAIKDANAKLAQLESALQKAKQDMARQLR----EYQELMNVKLALDIEIATYRKLLEGE 400
Cdd:TIGR02168  898 ELSEELRELESKRSELRR----ELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEALENKIEDDEEEARRR 973

                          330
                   ....*....|.
gi 348581109   401 ENRLEAGMQNL 411
Cdd:TIGR02168  974 LKRLENKIKEL 984
Keratin_2_head pfam16208
Keratin type II head;
65-89 3.68e-09

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 55.43  E-value: 3.68e-09
                          10        20
                  ....*....|....*....|....*
gi 348581109   65 ITAVQVNQSLLNPLNLEVDPNIQAV 89
Cdd:pfam16208 132 IQEVTVNQSLLQPLNLEIDPEIQRV 156
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
94-398 7.07e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.07  E-value: 7.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  94 KEQIKNLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKtsrSNMDNMFESyINNLRRQLDTLGQEKLKLEAELGNMQGM 173
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEV---KELEELKEE-IEELEKELESLEGSKRKLEEKIRELEER 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 174 VEDFKNKYED------EINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGltdeinflrqlYEEEIRELQSQISDtsvv 247
Cdd:PRK03918 268 IEELKKEIEEleekvkELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR-----------LEEEINGIEERIKE---- 332

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 248 LSMDNSRSLDLDGIIAEVKAQYEEIA------NRSRAEAESMYQIK--------------YEELQTLAGKHGDDLRRTKS 307
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEELEerhelyEEAKAKKEELERLKkrltgltpeklekeLEELEKAKEEIEEEISKITA 412

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 308 EISEMNRSISRLQAEIEALKGQRAA--LEAAIADAEQRGEMaIKDANAKLAQLESALQKAKqDMARQLREYQELMNVKLA 385
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKEL-LEEYTAELKRIEKELKEIE-EKERKLRKELRELEKVLK 490

                        330
                 ....*....|...
gi 348581109 386 LDIEIATYRKLLE 398
Cdd:PRK03918 491 KESELIKLKELAE 503
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 145-411 1.09e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 145 YINNLRRQLDTLGQEKLKLEAELgnmqgmvEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEIN 224
Cdd:COG1196  233 KLRELEAELEELEAELEELEAEL-------EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 225 FLrqlyEEEIRELQSQISDTSVVLSMDNSRSLDLDGIIAEVKAQYEEIANRSRAEAESMYQI--KYEELQTLAGKHGDDL 302
Cdd:COG1196  306 RL----EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeeALLEAEAELAEAEEEL 381

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 303 RRTKSEISEMNRSISRLQAEIEALKGQRAALEAAIADAEQrgemAIKDANAKLAQLESALQKAKQDMARQLREYQELMNV 382
Cdd:COG1196  382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE----ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                        250       260
                 ....*....|....*....|....*....
gi 348581109 383 KLALDIEIATYRKLLEGEENRLEAGMQNL 411
Cdd:COG1196  458 EEALLELLAELLEEAALLEAALAELLEEL 486
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 149-406 1.94e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 149 LRRQLDTLGQEK------LKLEAELGNMQGMV-----EDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLE 217
Cdd:COG1196  198 LERQLEPLERQAekaeryRELKEELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 218 GLTDEINFLRqlyeEEIRELQSQISDTSVVLSMDNSRSLDLDGIIAEVKAQYEEIANRSRAEAESMYQIKyEELQTLAGK 297
Cdd:COG1196  278 ELELELEEAQ----AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE-EELEEAEEE 352

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 298 hgddLRRTKSEISEMNRSISRLQAEIEALKGQRAALEAAIADAEQrgemAIKDANAKLAQLESALQKAKQDMARQLREYQ 377
Cdd:COG1196  353 ----LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR----AAAELAAQLEELEEAEEALLERLERLEEELE 424

                        250       260
                 ....*....|....*....|....*....
gi 348581109 378 ELMNVKLALDIEIATYRKLLEGEENRLEA 406
Cdd:COG1196  425 ELEEALAELEEEEEEEEEALEEAAEEEAE 453
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 112-413 2.39e-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: 53.52  E-value: 2.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   112 RFLEQQNKMLETKWSLLQQQKTSrsnmdnmFESYINNLRRQLDTLGQEKLKLEAELGNMQGMVEDFKNKyedeinkRTEM 191
Cdd:TIGR02168  214 RYKELKAELRELELALLVLRLEE-------LREELEELQEELKEAEEELEELTAELQELEEKLEELRLE-------VSEL 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   192 ENEFVLIKKDVDEAYMNKVELESRLegltdeinflrQLYEEEIRELQSQISDTSVVLSMDNSRSLDLDGIIAEVKAQYEE 271
Cdd:TIGR02168  280 EEEIEELQKELYALANEISRLEQQK-----------QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   272 IANRSRAEAESM--YQIKYEELQTLAGKHGDDLRRTKSEISEMNRSISRLQAEIEALKgqraaleaaiadaeqrgemaik 349
Cdd:TIGR02168  349 LKEELESLEAELeeLEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE---------------------- 406

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 348581109   350 danAKLAQLESALQKAKQDMARQLREYQElmNVKLALDIEIATYRKLLEGEENRLEAGMQNLSI 413
Cdd:TIGR02168  407 ---ARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEE 465
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 95-411 2.81e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.07  E-value: 2.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109    95 EQIKNLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYIN-------NLRRQLDTLGQEKLKLEAEL 167
Cdd:TIGR02169  681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEklkerleELEEDLSSLEQEIENVKSEL 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   168 GNMQGMVEDF---KNKYEDEINKRTEMENEfvlikkdvdeaymnkveleSRLEGLTDEINFLrqlyEEEIRELQSQISDT 244
Cdd:TIGR02169  761 KELEARIEELeedLHKLEEALNDLEARLSH-------------------SRIPEIQAELSKL----EEEVSRIEARLREI 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   245 SVVLSmdnsrSLDLDGIIAEVKAQYEEIANRSRAEAESMYQIKYEELQTLAGKHGDDLRRTKSEISEMNRSISRLQAEIE 324
Cdd:TIGR02169  818 EQKLN-----RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   325 ALKGQraalEAAIADAEQRGEMAIKDANAKLAQLESALQKAKQdmarQLREYQELMNVKLALDIEIATYRKLLEgEENRL 404
Cdd:TIGR02169  893 ELEAQ----LRELERKIEELEAQIEKKRKRLSELKAKLEALEE----ELSEIEDPKGEDEEIPEEELSLEDVQA-ELQRV 963


                   ....*..
gi 348581109   405 EAGMQNL 411
Cdd:TIGR02169  964 EEEIRAL 970
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
227-409 5.69e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 5.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  227 RQLYEEEIRELQSQISDtsvvlsmdnsrsldLDGIIAEVKAQYEEIANRSRA----EAESMYQIKYEELQ-TLAGKHG-- 299
Cdd:COG4913   612 LAALEAELAELEEELAE--------------AEERLEALEAELDALQERREAlqrlAEYSWDEIDVASAErEIAELEAel 677

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  300 DDLRRTKSEISEMNRSISRLQAEIEALKGQRAALEAAIADAEQRgemaIKDANAKLAQLESALQKAKQDMARQLRE---- 375
Cdd:COG4913   678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE----LEQAEEELDELQDRLEAAEDLARLELRAllee 753

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 348581109  376 -YQELM------NVKLALDIEIATYRKLLEGEENRLEAGMQ 409
Cdd:COG4913   754 rFAAALgdaverELRENLEERIDALRARLNRAEEELERAMR 794
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 146-395 2.74e-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: 46.30  E-value: 2.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 146 INNLRRQLDTLGQEKLKLEAELGNMQGMVEDFK---NKYEDEINKRTEMENEfvlIKKDVDEAYMNKVELESRLEGLTDE 222
Cdd:COG4942   22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLkqlAALERRIAALARRIRA---LEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 223 INFLRQLYEEEIRELQ--SQISDTSVVLSMDNSRSldldgiiAEVKAQYEEIANRSRAEaesmyqikyeelqtlagkHGD 300
Cdd:COG4942   99 LEAQKEELAELLRALYrlGRQPPLALLLSPEDFLD-------AVRRLQYLKYLAPARRE------------------QAE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 301 DLRRTKSEISEMNRSISRLQAEIEALKGQRAALeaaiadaEQRGEMAIKDANAKLAQLESALQKAKQDMARQLREYQELM 380
Cdd:COG4942  154 ELRADLAELAALRAELEAERAELEALLAELEEE-------RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226

                        250
                 ....*....|....*
gi 348581109 381 NVKLALDIEIATYRK 395
Cdd:COG4942  227 ALIARLEAEAAAAAE 241
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 142-404 2.75e-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: 46.98  E-value: 2.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   142 FESYINNLRRQLDTLGQEKLKLEaelgnmqgmvedfknKYeDEINKRTEmENEFVLIKKDVDEAYMNKVELESRLEGLTD 221
Cdd:TIGR02169  189 LDLIIDEKRQQLERLRREREKAE---------------RY-QALLKEKR-EYEGYELLKEKEALERQKEAIERQLASLEE 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   222 EINFLrqlyEEEIRELQSQISDTSVVLSMDNSRSLDL-DGIIAEVKAQYEEIANrSRAEAESMYQIKYEELQTLAGKhgd 300
Cdd:TIGR02169  252 ELEKL----TEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEA-EIASLERSIAEKERELEDAEER--- 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   301 dLRRTKSEISEMNRSISRLQAEIEALKGQRAALEAAIADAEQ-----RGEMAIKDANA-----KLAQLESALQKAKQDMA 370
Cdd:TIGR02169  324 -LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEeledlRAELEEVDKEFaetrdELKDYREKLEKLKREIN 402

                          250       260       270
                   ....*....|....*....|....*....|....
gi 348581109   371 RQLREYQELMNVKLALDIEIATYRKLLEGEENRL 404
Cdd:TIGR02169  403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 94-416 3.72e-05

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: 46.17  E-value: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   94 KEQIKNLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQLDTLGQEKLKLEAELGNMQGM 173
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  174 VEDFKnKYEDEINkrtEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEEEIRELQSQISDtsvvLSMDNS 253
Cdd:TIGR04523 210 IQKNK-SLESQIS---ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE----LEQNNK 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  254 RSLDLDGIIAEVKAQYEEIANRsrAEAESMYQIKyEELQtlagKHGDDLRRTKSEISEMNRSISRLQAEIEALKGQRAAL 333
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQ--KEQDWNKELK-SELK----NQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNS 354

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  334 EAAIADAE------------------------QRGEMAIKDANAKL-------AQLESALQKAKQDMARQLREYQELMNV 382
Cdd:TIGR04523 355 ESENSEKQreleekqneieklkkenqsykqeiKNLESQINDLESKIqnqeklnQQKDEQIKKLQQEKELLEKEIERLKET 434

                         330       340       350
                  ....*....|....*....|....*....|....
gi 348581109  383 KLALDIEIatyrKLLEGEENRLEAGMQNLSIHTK 416
Cdd:TIGR04523 435 IIKNNSEI----KDLTNQDSVKELIIKNLDNTRE 464
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 143-375 3.80e-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: 45.91  E-value: 3.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 143 ESYINNLRRQLDTLGQEKLKLEAELGNMQGMVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDE 222
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 223 I-NFLRQLYeeeireLQSQISDTSVVLSMDNSRSldldgiiAEVKAQYEEIANRSRAEAESMYQIKYEELQTLAgkhgDD 301
Cdd:COG4942  106 LaELLRALY------RLGRQPPLALLLSPEDFLD-------AVRRLQYLKYLAPARREQAEELRADLAELAALR----AE 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 348581109 302 LRRTKSEISEMNRSISRLQAEIEALKGQRAALEAAIADAEQRGEMAIKDANAKLAQLESALQKAKQDMARQLRE 375
Cdd:COG4942  169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
PRK09039 PRK09039
peptidoglycan -binding protein;
231-375 4.78e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 45.34  E-value: 4.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 231 EEEIRELQSQISDTSVVLSMDNSRSLDLDGIIAEVKAQYEEI-ANRSRAEA-ESMYQIKYEELQTLAGKHGDDLRRTKSE 308
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAeAERSRLQAlLAELAGAGAAAEGRAGELAQELDSEKQV 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 348581109 309 ISEMNRSISRLQAEIEALKGQRAALEAAIADAEQRGemaiKDANAKLA----QLESALQKAKQDMAR-------QLRE 375
Cdd:PRK09039 132 SARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIAdlgrRLNVALAQRVQELNRyrseffgRLRE 205
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 86-316 1.01e-04

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: 45.04  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109    86 IQAVRIQEKEQIKNLNNK---FASFIDKVRFLEQQNKMLE--TKWSLLQQQK----------TSRSNMDNMFESYINNLR 150
Cdd:TIGR01612  598 INKLKLELKEKIKNISDKneyIKKAIDLKKIIENNNAYIDelAKISPYQVPEhlknkdkiysTIKSELSKIYEDDIDALY 677

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   151 RQLDTLGQEKLKLEAElgnMQGMVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNK-----VELESRLEG-LTDEIN 224
Cdd:TIGR01612  678 NELSSIVKENAIDNTE---DKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNElldiiVEIKKHIHGeINKDLN 754

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   225 FLRQLYEEEIRELQSQISDtsvvLSMDNSRSLDLDGIIAEVKAQYEE---IANRSRAEAESMYQIKYEELQTLAGKHgDD 301
Cdd:TIGR01612  755 KILEDFKNKEKELSNKIND----YAKEKDELNKYKSKISEIKNHYNDqinIDNIKDEDAKQNYDKSKEYIKTISIKE-DE 829

                          250
                   ....*....|....*
gi 348581109   302 LRRTKSEISEMNRSI 316
Cdd:TIGR01612  830 IFKIINEMKFMKDDF 844
46 PHA02562
endonuclease subunit; Provisional
 109-330 3.06e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.08  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 109 DKVRFLEQQNKMLETKWSLLQQQKtsrsnmdNMFESYINNLRRQLDTLGQEKlkleaelgnmQGMVEDFKNKYED---EI 185
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQI-------KTYNKNIEEQRKKNGENIARK----------QNKYDELVEEAKTikaEI 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 186 NKRTEMENEFVLIKKDVDEAY----MNKVELESRLEGLTDEINFLRQlyEEEIRELQSQISDTSVVLSmdnsrslDLDGI 261
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEK--GGVCPTCTQQISEGPDRIT-------KIKDK 307

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 348581109 262 IAEVKAQYEEIANRSRAEAESMyqIKYEELQTLAGKHGDDLRRTKSEISEMNRSISRLQAEIEALKGQR 330
Cdd:PHA02562 308 LKELQHSLEKLDTAIDELEEIM--DEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEF 374
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 92-385 3.25e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 3.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109    92 QEKEQIKNLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQLDTLGQEKLKLEAELGNMQ 171
Cdd:TIGR02168  730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   172 GMVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLrqlyEEEIRELQSQisdtsvvlsmd 251
Cdd:TIGR02168  810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL----EELIEELESE----------- 874

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   252 nsrsldldgiIAEVKAQYEEIaNRSRAEAESMYQIKYEELQTLAGKHG---DDLRRTKSEISEMNRSISRLQAEIEALKG 328
Cdd:TIGR02168  875 ----------LEALLNERASL-EEALALLRSELEELSEELRELESKRSelrRELEELREKLAQLELRLEGLEVRIDNLQE 943

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 348581109   329 QRAAleaaiadaeqRGEMAIKDANAKLAQLESALQKAKQDMARQLREYQELMNVKLA 385
Cdd:TIGR02168  944 RLSE----------EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
140-375 3.73e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 140 NMFESYINNLRRQLDTLGQEKLKLEAELGNMQGMVEDfknkYEDeinKRTEMENefvlIKKDVDEAYMNKVELESRLEGL 219
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREQARETRDEADEVLEE----HEE---RREELET----LEAEIEDLRETIAETEREREEL 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 220 TDEINFLRqlyeEEIRELQSQISDTSVVLSMDNSRSLDLDGIIAEVKAQYEEI----------ANRSRAEAESM------ 283
Cdd:PRK02224 278 AEEVRDLR----ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELrdrleecrvaAQAHNEEAESLredadd 353

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 284 YQIKYEELQTLAGKHGDDLRRTKSEISEMNRSISRLQAEIEALKGQRAALEAAIADAEQRGEMAIK---DANAKLAQLES 360
Cdd:PRK02224 354 LEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREerdELREREAELEA 433

                        250
                 ....*....|....*..
gi 348581109 361 ALQKAKQDM--ARQLRE 375
Cdd:PRK02224 434 TLRTARERVeeAEALLE 450
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 92-411 5.31e-04

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: 42.70  E-value: 5.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   92 QEKEQIKNLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQLDTLGQEKLKLEAELGNMQ 171
Cdd:TIGR04523  51 NKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLE 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  172 GMVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEIN--------------------FLRQLYE 231
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLniqknidkiknkllklelllSNLKKKI 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  232 EEIRELQSQISD----TSVVLSMDNSRSLDLDGIIAEVKAQYEEIANRSRAEAESMYQIKYEELQtlagkhgddLRRTKS 307
Cdd:TIGR04523 211 QKNKSLESQISElkkqNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE---------LEQNNK 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  308 EISEMNRSISRLQAEIEALKGQRAALEAAIADAE-QRGEMAIKDANAKLAQLESALQKAKQDMARQLREYQELMNVKLAL 386
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQKEQDWNKELKSElKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK 361

                         330       340
                  ....*....|....*....|....*
gi 348581109  387 DIEIATYRKLLEGEENRLEAGMQNL 411
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEI 386
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 122-419 5.48e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.80  E-value: 5.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   122 ETKWSLLQQQKTSRSNMDNMFESYINNLRRQLDTLGQEKLKLEAELGNM----QGMVE------DFKNKYEDEINKRT-E 190
Cdd:pfam15921  390 EKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMksecQGQMErqmaaiQGKNESLEKVSSLTaQ 469

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   191 MENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLR------QLYEEEIRELQSQISDTSVVLSMDNSRSLDLDGIIAE 264
Cdd:pfam15921  470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQekeraiEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTE 549

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   265 VKAQYEEIANRSRAEAESMYQIkyEELQTLAGKHGDDLRRTKSEISEMNRSISRLQAEIEALKgqraaleaaiaDAEQRG 344
Cdd:pfam15921  550 CEALKLQMAEKDKVIEILRQQI--ENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFK-----------ILKDKK 616

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 348581109   345 EMAIKDANAKLAQLESALQKAKQDMARQLREYQELMNVKLALDIEIATYRKLLEG---EENRLEAGMQNLSIHTKTTS 419
Cdd:pfam15921  617 DAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSlseDYEVLKRNFRNKSEEMETTT 694
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 211-406 5.64e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 5.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 211 ELESRLEGLTdeinflRQ--------LYEEEIRELQSQISdtsvVLSMD--NSRSLDLDGIIAEVKAQYEEI-ANRSRAE 279
Cdd:COG1196  197 ELERQLEPLE------RQaekaeryrELKEELKELEAELL----LLKLRelEAELEELEAELEELEAELEELeAELAELE 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 280 AE-SMYQIKYEELQTLAGKHGDDLRRTKSEISEMNRSISRLQAEIEALKGQRAALEAAIADAEQRG-------------- 344
Cdd:COG1196  267 AElEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELeeleeeleeleeel 346

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 348581109 345 ---EMAIKDANAKLAQLESALQKAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEENRLEA 406
Cdd:COG1196  347 eeaEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 152-406 8.94e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.03  E-value: 8.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   152 QLDTLGQE-KLKLEAELGNMQGMVEDFKNKYEDEINKRTE-----------MENEFVLIK---KDVDEAYMNKV-ELESR 215
Cdd:pfam15921  246 QLEALKSEsQNKIELLLQQHQDRIEQLISEHEVEITGLTEkassarsqansIQSQLEIIQeqaRNQNSMYMRQLsDLEST 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   216 LEGLTDEINFLRQLYEEEIRELQSQISDTSVVLS---------MDNSRSLD--LDGIIAEVKAQYEEIAnRSRAEAESMY 284
Cdd:pfam15921  326 VSQLRSELREAKRMYEDKIEELEKQLVLANSELTearterdqfSQESGNLDdqLQKLLADLHKREKELS-LEKEQNKRLW 404

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   285 QIKYEELQTLagkhgDDLRRtksEISEMNRSISRLQAEIEALKGQRAALEAAIADAEQRGEMAIKDANAKLAQLESAlqk 364
Cdd:pfam15921  405 DRDTGNSITI-----DHLRR---ELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLEST--- 473

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 348581109   365 akQDMARQLREyqELMNVKLALDIEIATYRKL---LEGEENRLEA 406
Cdd:pfam15921  474 --KEMLRKVVE--ELTAKKMTLESSERTVSDLtasLQEKERAIEA 514
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 91-327 9.07e-04

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: 41.93  E-value: 9.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   91 IQEKE-QIKNLNNKFASFIDKVRFLEQQNKMLETKwslLQQQKTSRSNMDNmfesyinnlrrQLDTLGQEKLKLEAELGN 169
Cdd:TIGR04523 365 LEEKQnEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQEKLNQQKDE-----------QIKKLQQEKELLEKEIER 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  170 MQGMVEDFKNKYEDEINKRTEMENEFVLIKKDVDeaymnkvELESRLEGLTDEINFLRQLYEEEIRELQSQISDtsvvLS 249
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE-------SLETQLKVLSRSINKIKQNLEQKQKELKSKEKE----LK 499

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  250 MDNSRSLDLDGIIAEVKAQYEEIANRSRAEAESMYQIKYE--ELQTLAGKHGDDLRRT--KSEISEMNRSISRLQAEIEA 325
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKisDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKS 579


                  ..
gi 348581109  326 LK 327
Cdd:TIGR04523 580 LK 581
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
150-404 9.10e-04

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: 9.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  150 RRQLDTLGQEKLKLEAELGNMQGMVEDFKNKYEDEINKRtemenefvlikkdvdeaymnkvELESRLEGLTDEINFLRQL 229
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERR----------------------EALQRLAEYSWDEIDVASA 666

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  230 yEEEIRELQSQIsdtsvvlsmdnsRSLDL-DGIIAEVKAQYEEiANRSRAEAESmyqiKYEELQTLAGKHGDDLRRTKSE 308
Cdd:COG4913   667 -EREIAELEAEL------------ERLDAsSDDLAALEEQLEE-LEAELEELEE----ELDELKGEIGRLEKELEQAEEE 728

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  309 ISEMNRSISRLQAEIEALKGQRAALEAAIADAEQRGEMAIKDANAKLAQLESALQKAKQDMARQLREYQEL-MNVKLALD 387
Cdd:COG4913   729 LDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREwPAETADLD 808

                         250       260
                  ....*....|....*....|.
gi 348581109  388 IEIAT---YRKLLEG-EENRL 404
Cdd:COG4913   809 ADLESlpeYLALLDRlEEDGL 829
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 143-372 1.88e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 143 ESYINNLRRQLDTLGQEKLKLEAELGNMQGMVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAymnkvelESRLEGLTDE 222
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-------EAEIEERREE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 223 I-NFLRQLYEEeirelQSQISDTSVVLSMDN-----SRSLDLD-------GIIAEVKAQYEEIANrsraeAESMYQIKYE 289
Cdd:COG3883   88 LgERARALYRS-----GGSVSYLDVLLGSESfsdflDRLSALSkiadadaDLLEELKADKAELEA-----KKAELEAKLA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 290 ELQTLAGKHGDDLRRTKSEISEMNRSISRLQAEIEALKGQRAALEAAIADAEQRGEMAIKDANAKLAQLESALQKAKQDM 369
Cdd:COG3883  158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237


                 ...
gi 348581109 370 ARQ 372
Cdd:COG3883  238 AAA 240
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 146-281 1.92e-03

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: 39.91  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 146 INNLRRQLDTLGQEKLKLEAELGNMQGMVEDFKNKYEDEINKRTEMENEF--VLIKKDVDEAYMNKVELESRLEGLTDEI 223
Cdd:COG1579   19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIeeVEARIKKYEEQLGNVRNNKEYEALQKEI 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 348581109 224 NFL---RQLYEEEIRELQSQISDTSVVLSMDNSRSLDLDGIIAEVKAQYEEIANRSRAEAE 281
Cdd:COG1579   99 ESLkrrISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
212-413 1.95e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 212 LESRLEGLTDEinfLRQLyEEEIRELQSQ--ISDTSVVLSMDNSRSLDLDGIIAEVKAQYEEIANRsRAEAESMYQIKYE 289
Cdd:COG3206  180 LEEQLPELRKE---LEEA-EAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR-LAALRAQLGSGPD 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 290 ELQTLAGkhGDDLRRTKSEISEMNRSISRLQA-------EIEALKGQRAALEAAIADAEQRG----EMAIKDANAKLAQL 358
Cdd:COG3206  255 ALPELLQ--SPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRIlaslEAELEALQAREASL 332

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 348581109 359 ESALQKAKQDMARQLREYQELMNVKLALDIEIATYRKLLEG-EENRLEAGMQNLSI 413
Cdd:COG3206  333 QAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRlEEARLAEALTVGNV 388
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 114-405 2.16e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.48  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  114 LEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQLDTLGQEKLKLEAELGNMQGMVEdFKNkyedeiNKRTEMEN 193
Cdd:pfam05483 337 MEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTK-FKN------NKEVELEE 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  194 EFVLIKKDVDEAYMNKV--ELESRLEGLTDEINFLRQLYEEEIRELQSQISDTSV------------------------- 246
Cdd:pfam05483 410 LKKILAEDEKLLDEKKQfeKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTseehylkevedlktelekeklknie 489

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  247 ------VLSMDNSR-SLDLDGIIAEVKAQYEEIANRSRAEAESMYQIkyEELQTLAGKHGDDLRRTKSEISEMNRSI--- 316
Cdd:pfam05483 490 ltahcdKLLLENKElTQEASDMTLELKKHQEDIINCKKQEERMLKQI--ENLEEKEMNLRDELESVREEFIQKGDEVkck 567

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  317 ------SRLQAEIEALKGQRAALEAAIADAEQRGEMAIKDAN-AKLAQLESALQKAKQDMARQLREYQELMNvKLALDIE 389
Cdd:pfam05483 568 ldkseeNARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNiEELHQENKALKKKGSAENKQLNAYEIKVN-KLELELA 646

                         330       340
                  ....*....|....*....|....*....
gi 348581109  390 ---------IATYRKLLE----GEENRLE 405
Cdd:pfam05483 647 sakqkfeeiIDNYQKEIEdkkiSEEKLLE 675
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 86-330 2.24e-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: 40.82  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109    86 IQAVRIQEKEQIKNLNNKFASfidKVRFLEQQNKMLETKWS--LLQQQKTSRSnmdnmFESYINNLRRQLDTLGQEKLKL 163
Cdd:TIGR02169  249 LEEELEKLTEEISELEKRLEE---IEQLLEELNKKIKDLGEeeQLRVKEKIGE-----LEAEIASLERSIAEKERELEDA 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   164 EAELgnmqgmvedfkNKYEDEINK-RTEMENefvlIKKDVDEAYMNKVELESRLEGLTDEINFLRQ-------------- 228
Cdd:TIGR02169  321 EERL-----------AKLEAEIDKlLAEIEE----LEREIEEERKRRDKLTEEYAELKEELEDLRAeleevdkefaetrd 385

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   229 ---LYEEEIRELQSQISDTSVVLSMDNSRSLDLDGIIAEVKAQYEEIANRSRAEAESMYQIKYE------ELQTLA---G 296
Cdd:TIGR02169  386 elkDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEikkqewKLEQLAadlS 465

                          250       260       270
                   ....*....|....*....|....*....|....
gi 348581109   297 KHGDDLRRTKSEISEMNRSISRLQAEIEALKGQR 330
Cdd:TIGR02169  466 KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
46 PHA02562
endonuclease subunit; Provisional
 234-412 2.53e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 234 IRELQSQISDTSVvlsmdnsrslDLDGIIAEVKAQ--YEEIANRSRAEAESMYQIKYEELQTLAGKHGDDLRRTKSEISE 311
Cdd:PHA02562 176 IRELNQQIQTLDM----------KIDHIQQQIKTYnkNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLN 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 312 MNR-------SISRLQAEIEALKGQRAALEAAIADAEQRGE-----MAIKDANAKLAQLES----------ALQKAKQDM 369
Cdd:PHA02562 246 LVMdiedpsaALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVcptctQQISEGPDRITKIKDklkelqhsleKLDTAIDEL 325

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 348581109 370 ARQLREYQELMNVKLALDIEIATYRKLLEGEEN---RLEAGMQNLS 412
Cdd:PHA02562 326 EEIMDEFNEQSKKLLELKNKISTNKQSLITLVDkakKVKAAIEELQ 371
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 67-383 3.38e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.10  E-value: 3.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109    67 AVQVNQSLLNPLNLEVDPNIQAVR--IQEKEQIKNLNNKFASF----IDKVRFLEQQNKMLETKWSLLQQQKTSRSNM-- 138
Cdd:pfam15921  511 AIEATNAEITKLRSRVDLKLQELQhlKNEGDHLRNVQTECEALklqmAEKDKVIEILRQQIENMTQLVGQHGRTAGAMqv 590

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   139 -DNMFESYINNLRRQLDTLGQEKLKLEAELGNMQGMVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLE 217
Cdd:pfam15921  591 eKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELN 670

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   218 GLTDEINFLRQLYEEEIREL--------------QSQISDTSVVL-SMDNSrslDLDGIIAEVKAQYEEIANRSRAEA-E 281
Cdd:pfam15921  671 SLSEDYEVLKRNFRNKSEEMetttnklkmqlksaQSELEQTRNTLkSMEGS---DGHAMKVAMGMQKQITAKRGQIDAlQ 747

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109   282 SMYQIkYEELQTLAGKHGDDLRRTKSEISEMNRSIS----RLQAEIEALKGQRAALEAAIADAeqrgEMAIKDANAKLAQ 357
Cdd:pfam15921  748 SKIQF-LEEAMTNANKEKHFLKEEKNKLSQELSTVAteknKMAGELEVLRSQERRLKEKVANM----EVALDKASLQFAE 822

                          330       340
                   ....*....|....*....|....*.
gi 348581109   358 LESALQKAKQDMARqlREYQELMNVK 383
Cdd:pfam15921  823 CQDIIQRQEQESVR--LKLQHTLDVK 846
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
94-379 4.81e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 4.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109  94 KEQIKNLNNKFASFIDKVRFLEQQNKMLETKwsLLQQQKTSRsnMDNMFESyINNLRRQLDTLGQEKL--------KLEA 165
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKV--LKKESELIK--LKELAEQ-LKELEEKLKKYNLEELekkaeeyeKLKE 532

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 166 ELGNMQGMVEDFKnkyeDEINKRTEMENEFVLIKKDVDEAYMNKVELESRL--------EGLTDEINFLRQLYEEEIrEL 237
Cdd:PRK03918 533 KLIKLKGEIKSLK----KELEKLEELKKKLAELEKKLDELEEELAELLKELeelgfesvEELEERLKELEPFYNEYL-EL 607

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348581109 238 QSQISDTSVVLSMDNSRSLDLDGI---IAEVKAQYEEIANRsraeaesmyqikYEELQTLAGKhgDDLRRTKSEISEMNR 314
Cdd:PRK03918 608 KDAEKELEREEKELKKLEEELDKAfeeLAETEKRLEELRKE------------LEELEKKYSE--EEYEELREEYLELSR 673

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 348581109 315 SISRLQAEIEALKGQRAALEAAIADAEQRGEmAIKDANAKLAQLESALQKAkQDMARQLREYQEL 379
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERV-EELREKVKKYKAL 736
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH