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Conserved domains on  [gi|1952735413|ref|XP_038316070|]
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keratin, type II cytoskeletal 1b isoform X3 [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;
175-488 1.88e-119

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 356.15  E-value: 1.88e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 175 QEREQIMVLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVNTSTRTNnLEPVLENYISELRRQVDFLNAEQMRQNTDVKN 254
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSR-LYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 255 MQDVVEDYKSKYEEEINRRANTENDFVVLKKDVDAAYMSKVDLESKVNVLFGEINFLKYLFETELSQMQTHISDTNVILS 334
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 335 MDNNRFLDLDSIIDAVRTQYELIAQKSKDEAEALYQTKYQELQVSAGRHGDELKNSKLEITELNRTIQRLQAEISSVRKQ 414
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952735413 415 IEQMHVAISDAEERGEQALQDARQKLGDLEDALHQAKEELARLLRDYQALLGAKLSLDVEIATYRKLLEGEESR 488
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
61-172 1.30e-23

Keratin type II head;


:

Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 97.42  E-value: 1.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  61 SHARGFGSRSLYNLGGNKSISISLVG---RSASGFCQGGGAGGKFGGGGRSFGGGGFGGGG-------YGGGGFGGGGFG 130
Cdd:pfam16208  35 GGGGGFGSRSLYNLGGSKSISISVAGggsRPGSGFGFGGGGGGGFGGGFGGGGGGGFGGGGgfgggfgGGGYGGGGFGGG 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1952735413 131 GSSFGLGGFGPSCPPGGIQEVTINQSLLEPLHLEVDPEIQRV 172
Cdd:pfam16208 115 GFGGRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
175-488 1.88e-119

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 356.15  E-value: 1.88e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 175 QEREQIMVLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVNTSTRTNnLEPVLENYISELRRQVDFLNAEQMRQNTDVKN 254
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSR-LYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 255 MQDVVEDYKSKYEEEINRRANTENDFVVLKKDVDAAYMSKVDLESKVNVLFGEINFLKYLFETELSQMQTHISDTNVILS 334
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 335 MDNNRFLDLDSIIDAVRTQYELIAQKSKDEAEALYQTKYQELQVSAGRHGDELKNSKLEITELNRTIQRLQAEISSVRKQ 414
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952735413 415 IEQMHVAISDAEERGEQALQDARQKLGDLEDALHQAKEELARLLRDYQALLGAKLSLDVEIATYRKLLEGEESR 488
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
61-172 1.30e-23

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 97.42  E-value: 1.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  61 SHARGFGSRSLYNLGGNKSISISLVG---RSASGFCQGGGAGGKFGGGGRSFGGGGFGGGG-------YGGGGFGGGGFG 130
Cdd:pfam16208  35 GGGGGFGSRSLYNLGGSKSISISVAGggsRPGSGFGFGGGGGGGFGGGFGGGGGGGFGGGGgfgggfgGGGYGGGGFGGG 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1952735413 131 GSSFGLGGFGPSCPPGGIQEVTINQSLLEPLHLEVDPEIQRV 172
Cdd:pfam16208 115 GFGGRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 174-494 3.00e-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: 50.44  E-value: 3.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  174 TQEREQ-IMVLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVNTSTRTnnLEPVLENYISELRRQVDFLNAEQMRQNTDV 252
Cdd:TIGR02168  672 ILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK--ELEELSRQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  253 KNMQDVVEDYKSKYEEEINRRANTENDFVVLKKDvdaaymsKVDLESKVNVLFGEINflkyLFETELSQMQTHISDTNVI 332
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELK----ALREALDELRAELTLLNEE 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  333 LSMDNNRFLDLDSIIDAVRTQYELIAQKSKDEAEALYQTKYQ--ELQVSAGRHGDELKNSKLEITELNRTIQRLQAEISS 410
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEieELEELIEELESELEALLNERASLEEALALLRSELEE 898

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  411 VRKQIEQMHVAISDAeergEQALQDARQKLGDLEDALHQAKEELARLLR----DYQALLGAKLSLDVEIATYRKLLEGEE 486
Cdd:TIGR02168  899 LSEELRELESKRSEL----RRELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEALENKIEDDEEEARRRL 974


                   ....*...
gi 1952735413  487 SRMSGELQ 494
Cdd:TIGR02168  975 KRLENKIK 982
PRK09039 PRK09039
peptidoglycan -binding protein;
316-456 1.11e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 47.65  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 316 ETELSQMQTHISDTNVILSMDNNRFLDLDSIIDAVRTQYElIAQKSKDEAEALYQTKYQELQVSAGRHGD---ELKNSKL 392
Cdd:PRK09039   52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLS-AAEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952735413 393 EITELNRTIQRLQAEISSVRKQIEQMHVAISDAEERGEQalQDAR-QKLG-DLEDALHQAKEELAR 456
Cdd:PRK09039  131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRE--SQAKiADLGrRLNVALAQRVQELNR 194
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
343-480 1.47e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  343 LDSIIDAVRTQYELIAQKsKDEAEALY---QTKYQELQVS-AGRHGDELKNSKLEITELNRTIQRLQAEISSVRKQIEQM 418
Cdd:COG4913    293 LEAELEELRAELARLEAE-LERLEARLdalREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL 371

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952735413  419 HVAISDAEERGEQALQDARQKLGDLEDALHQAKEELARLLRDYQALLGAKLSLDVEIATYRK 480
Cdd:COG4913    372 GLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
175-488 1.88e-119

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 356.15  E-value: 1.88e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 175 QEREQIMVLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVNTSTRTNnLEPVLENYISELRRQVDFLNAEQMRQNTDVKN 254
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSR-LYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 255 MQDVVEDYKSKYEEEINRRANTENDFVVLKKDVDAAYMSKVDLESKVNVLFGEINFLKYLFETELSQMQTHISDTNVILS 334
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 335 MDNNRFLDLDSIIDAVRTQYELIAQKSKDEAEALYQTKYQELQVSAGRHGDELKNSKLEITELNRTIQRLQAEISSVRKQ 414
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952735413 415 IEQMHVAISDAEERGEQALQDARQKLGDLEDALHQAKEELARLLRDYQALLGAKLSLDVEIATYRKLLEGEESR 488
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
61-172 1.30e-23

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 97.42  E-value: 1.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  61 SHARGFGSRSLYNLGGNKSISISLVG---RSASGFCQGGGAGGKFGGGGRSFGGGGFGGGG-------YGGGGFGGGGFG 130
Cdd:pfam16208  35 GGGGGFGSRSLYNLGGSKSISISVAGggsRPGSGFGFGGGGGGGFGGGFGGGGGGGFGGGGgfgggfgGGGYGGGGFGGG 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1952735413 131 GSSFGLGGFGPSCPPGGIQEVTINQSLLEPLHLEVDPEIQRV 172
Cdd:pfam16208 115 GFGGRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 174-494 3.00e-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: 50.44  E-value: 3.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  174 TQEREQ-IMVLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVNTSTRTnnLEPVLENYISELRRQVDFLNAEQMRQNTDV 252
Cdd:TIGR02168  672 ILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK--ELEELSRQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  253 KNMQDVVEDYKSKYEEEINRRANTENDFVVLKKDvdaaymsKVDLESKVNVLFGEINflkyLFETELSQMQTHISDTNVI 332
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELK----ALREALDELRAELTLLNEE 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  333 LSMDNNRFLDLDSIIDAVRTQYELIAQKSKDEAEALYQTKYQ--ELQVSAGRHGDELKNSKLEITELNRTIQRLQAEISS 410
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEieELEELIEELESELEALLNERASLEEALALLRSELEE 898

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  411 VRKQIEQMHVAISDAeergEQALQDARQKLGDLEDALHQAKEELARLLR----DYQALLGAKLSLDVEIATYRKLLEGEE 486
Cdd:TIGR02168  899 LSEELRELESKRSEL----RRELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEALENKIEDDEEEARRRL 974


                   ....*...
gi 1952735413  487 SRMSGELQ 494
Cdd:TIGR02168  975 KRLENKIK 982
PRK09039 PRK09039
peptidoglycan -binding protein;
316-456 1.11e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 47.65  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 316 ETELSQMQTHISDTNVILSMDNNRFLDLDSIIDAVRTQYElIAQKSKDEAEALYQTKYQELQVSAGRHGD---ELKNSKL 392
Cdd:PRK09039   52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLS-AAEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952735413 393 EITELNRTIQRLQAEISSVRKQIEQMHVAISDAEERGEQalQDAR-QKLG-DLEDALHQAKEELAR 456
Cdd:PRK09039  131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRE--SQAKiADLGrRLNVALAQRVQELNR 194
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
343-480 1.47e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  343 LDSIIDAVRTQYELIAQKsKDEAEALY---QTKYQELQVS-AGRHGDELKNSKLEITELNRTIQRLQAEISSVRKQIEQM 418
Cdd:COG4913    293 LEAELEELRAELARLEAE-LERLEARLdalREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL 371

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952735413  419 HVAISDAEERGEQALQDARQKLGDLEDALHQAKEELARLLRDYQALLGAKLSLDVEIATYRK 480
Cdd:COG4913    372 GLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
ElaB COG4575
Membrane-anchored ribosome-binding protein ElaB, inhibits growth in stationary phase, YqjD ...
 389-461 2.11e-05

Membrane-anchored ribosome-binding protein ElaB, inhibits growth in stationary phase, YqjD/DUF883 family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 443632 [Multi-domain]  Cd Length: 108  Bit Score: 43.78  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 389 NSKLEITELNRTIQRLQAEISSVRKQIEQM--------HVAISDAEERGEQALQDARQKLGDLEDALHQAKEELARLLRD 460
Cdd:COG4575     2 ANTKTTTSVEDSKEDLEADLKALVDDLEELlkstaddaGEKAAELREKAEAALDEARERLSEAEDAAVERAREAADAADD 81


                  .
gi 1952735413 461 Y 461
Cdd:COG4575    82 Y 82
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 386-467 2.94e-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: 46.68  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 386 ELKNSKLEITELNRTIQRLQAEISSVRKQIEQMHVAISDAEER---GEQALQDARQKLGDLEDALHQAKEELARLLRDYQ 462
Cdd:COG4942    28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELA 107


                  ....*
gi 1952735413 463 ALLGA 467
Cdd:COG4942   108 ELLRA 112
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 355-494 3.54e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 3.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 355 ELIAQKSKDEAE-ALYQTKYQELQVSAGRHGDELKNSKLEITELNRTIQRLQAEISSVRKQIEQMHVAISDAEERGEQA- 432
Cdd:COG1196   236 ELEAELEELEAElEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELe 315

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952735413 433 --LQDARQKLGDLEDALHQAKEELARLLRDYQALLGAKLSLDVEIATYRKLLEGEESRMSGELQ 494
Cdd:COG1196   316 erLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 148-494 5.91e-05

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: 46.26  E-value: 5.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  148 IQEVTINQSLLEPLHLEVDPEIQRVKTQEReQIMVLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVNTSTRTNNLEPVL 227
Cdd:pfam15921  481 VEELTAKKMTLESSERTVSDLTASLQEKER-AIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAE 559

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  228 ENYISE-LRRQVDFLNAEQMRQNTDVKNMQdvVEdyKSKYEEEINRRANTENDFVVLKKDVDAAYMskvDLESKVNVLFG 306
Cdd:pfam15921  560 KDKVIEiLRQQIENMTQLVGQHGRTAGAMQ--VE--KAQLEKEINDRRLELQEFKILKDKKDAKIR---ELEARVSDLEL 632

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  307 EINFLKYLFETELSQMQTHISDTNVILSMDNNRFLDLDSIIDavrtQYELIAQKskdeaealYQTKYQELQVSAGRHGDE 386
Cdd:pfam15921  633 EKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSE----DYEVLKRN--------FRNKSEEMETTTNKLKMQ 700

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  387 LKNSKLEITELNRTIQRLQAEISSVRKQIEQMHVAISdaEERGE-QALQdarQKLGDLEDALHQAKEElARLLRDYQALL 465
Cdd:pfam15921  701 LKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQIT--AKRGQiDALQ---SKIQFLEEAMTNANKE-KHFLKEEKNKL 774

                          330       340
                   ....*....|....*....|....*....
gi 1952735413  466 GAKLSldvEIATyrkllegEESRMSGELQ 494
Cdd:pfam15921  775 SQELS---TVAT-------EKNKMAGELE 793
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 355-494 1.57e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 355 ELIAQKSKDEAE-ALYQTKYQELQVSAGRHGDELKNSKLEITELNRTIQRLQAEISSVRKQIEQMHVAISDAEERGEQA- 432
Cdd:COG1196   257 ELEAELAELEAElEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELe 336

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952735413 433 ---------LQDARQKLGDLEDALHQAKEELARLLRDYQALLGAKLSLDVEIATYRKLLEGEESRMSGELQ 494
Cdd:COG1196   337 eeleeleeeLEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
342-489 3.44e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 3.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  342 DLDSIIDAVRTQ---YELIAQKSKDEAEALY-QTKYQELQvsagRHGDELKNSKLEITELNRTIQRLQAEISSVRKQIEQ 417
Cdd:COG4913    635 ALEAELDALQERreaLQRLAEYSWDEIDVASaEREIAELE----AELERLDASSDDLAALEEQLEELEAELEELEEELDE 710

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952735413  418 MHVAISDAEERGEQALQDARQKLGDLEDALHQAKEEL-ARLLRDYQALLGAKL------SLDVEIATYRKLLEGEESRM 489
Cdd:COG4913    711 LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELrALLEERFAAALGDAVerelreNLEERIDALRARLNRAEEEL 789
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
354-464 6.55e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 6.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 354 YELIAQKSK-DEAEALYQTKYQELQVSAGRHGDELKNSKLEitELNRTIQRLQAEISSVRKQIEQMHVAISDAEERGEQA 432
Cdd:COG4717   388 RAALEQAEEyQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQL 465

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1952735413 433 LQDARqkLGDLEDALHQAKEELARLLRDYQAL 464
Cdd:COG4717   466 EEDGE--LAELLQELEELKAELRELAEEWAAL 495
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 158-466 1.05e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  158 LEPLHLEVDP--EIQRVKTQERE-QIMVLNNKFASFIDKVRFLEQQNQVLQtkwellQQVNTSTRTNNlepVLENYISEL 234
Cdd:TIGR02168  202 LKSLERQAEKaeRYKELKAELRElELALLVLRLEELREELEELQEELKEAE------EELEELTAELQ---ELEEKLEEL 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  235 RRQVDFLNAEQMRQNTDVKNMQDVVEDYKSKYEEEINRRANTENDFVVLKKDVDAAYMSKVDLESKVNVLFGEINFLKYL 314
Cdd:TIGR02168  273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  315 FETELSQMQThisdTNVILSMDNNRFLDLDsiiDAVRTQYELIAQKSKDEAEALYQTKYQELQVSagRHGDELKNSKLEI 394
Cdd:TIGR02168  353 LESLEAELEE----LEAELEELESRLEELE---EQLETLRSKVAQLELQIASLNNEIERLEARLE--RLEDRRERLQQEI 423

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  395 TELNRTIQR-----LQAEISSVRKQIEQMHVAISDAEERGE---QALQDARQKLGDLEDALHQAKEELARLLRDYQALLG 466
Cdd:TIGR02168  424 EELLKKLEEaelkeLQAELEELEEELEELQEELERLEEALEelrEELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
294-489 1.05e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 294 KVDLESKVNVLFGE--------INFLKYLFETELSQMQTHI-SDTNVILSMDNNRFLDLDSIIDAVRTQYELIAQKSKDE 364
Cdd:COG4717    18 TIEFSPGLNVIYGPneagkstlLAFIRAMLLERLEKEADELfKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 365 AEALYQTKYQELQVSAGRHGDELKNSKLEITELNRTIQRLQAEISSVRKQIEQM---HVAISDAEERGEQALQDARQKLG 441
Cdd:COG4717    98 EELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELeerLEELRELEEELEELEAELAELQE 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1952735413 442 DLEDALHQ----AKEELARLLRDYQALLGAKLSLDVEIATYRKLLEGEESRM 489
Cdd:COG4717   178 ELEELLEQlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 354-490 1.62e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 354 YELIAQKSKDEAE-ALYQTKYQELQvsagrhgDELKNSKLEITELNRTIQRLQAEISSVRKQIEqmhvAISDAEERGEQA 432
Cdd:COG1196   291 YELLAELARLEQDiARLEERRRELE-------ERLEELEEELAELEEELEELEEELEELEEELE----EAEEELEEAEAE 359

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952735413 433 LQDARQKLGDLEDALHQAKEELARLLRDYQALLGAKLSLDVEIATYRKLLEGEESRMS 490
Cdd:COG1196   360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
314-494 1.90e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 314 LFETELSQMQTHISDTNVILSMDNNRfldLDSIIDAVRTQYELIAQKSKDEAEALYQTKYQELQVsagrhgdELKNSKLE 393
Cdd:COG3206   216 LLLQQLSELESQLAEARAELAEAEAR---LAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEA-------ELAELSAR 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 394 ITELNRTIQRLQAEISSVRKQIEQmhvAISDAEERGEQALQDARQKLGDLEDALHQAKEELARLLRDYQALLGAKLSLDV 473
Cdd:COG3206   286 YTPNHPDVIALRAQIAALRAQLQQ---EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV 362

                         170       180
                  ....*....|....*....|..
gi 1952735413 474 EIATYRKLLEG-EESRMSGELQ 494
Cdd:COG3206   363 ARELYESLLQRlEEARLAEALT 384
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
341-483 2.05e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  341 LDLDSI---IDAVRTQYELIaQKSKDEAEALYQtKYQELQVSAGRHGDELKNSKLEITELNRTIQRLQAEISSVRKQIEQ 417
Cdd:COG4913    661 IDVASAereIAELEAELERL-DASSDDLAALEE-QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  418 M-----HVAISDAEERGEQALQDARQK---------LGDLEDALHQAKEELARLLRDYQALLGAKLS-LDVEIAT---YR 479
Cdd:COG4913    739 AedlarLELRALLEERFAAALGDAVERelrenleerIDALRARLNRAEEELERAMRAFNREWPAETAdLDADLESlpeYL 818


                   ....
gi 1952735413  480 KLLE 483
Cdd:COG4913    819 ALLD 822
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 343-464 2.22e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  343 LDSIIDAVRTQYE-LIAQKSKDEAEALYQTKYQELQ--VSAGR---HGDELKNSKLEITELNRTIQRLQAEISSVRKQIE 416
Cdd:TIGR02168  191 LEDILNELERQLKsLERQAEKAERYKELKAELRELElaLLVLRleeLREELEELQEELKEAEEELEELTAELQELEEKLE 270

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952735413  417 QMHVAISDAEERGEQA---LQDARQKLGDLEDALHQAKEELARLLRDYQAL 464
Cdd:TIGR02168  271 ELRLEVSELEEEIEELqkeLYALANEISRLEQQKQILRERLANLERQLEEL 321
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 343-488 2.92e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 343 LDSIIDAVRTQYE-LIAQKSKdeAEalyqtKYQELQvsagrhgDELKNSK-----LEITELNRTIQRLQAEISSVRKQIE 416
Cdd:COG1196   191 LEDILGELERQLEpLERQAEK--AE-----RYRELK-------EELKELEaelllLKLRELEAELEELEAELEELEAELE 256

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952735413 417 QMHVAISDAEERgeqaLQDARQKLGDLEDALHQAKEELARLLRDYQALLGAKLSLDVEIATYRKLLEGEESR 488
Cdd:COG1196   257 ELEAELAELEAE----LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
46 PHA02562
endonuclease subunit; Provisional
 192-442 3.82e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.00  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 192 DKVRFLEQQNQVLQTKWELL-QQVNTStrtnnlepvlENYISELRRQvdflnaeqmrQNTDVKNMQDVVEDYKSK---YE 267
Cdd:PHA02562  174 DKIRELNQQIQTLDMKIDHIqQQIKTY----------NKNIEEQRKK----------NGENIARKQNKYDELVEEaktIK 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 268 EEINRRANTENDFVVLKKDVDAAY----MSKVDLESKVNVLFGEINFLKYLFETElSQMQThISDTNVILSmdnnrflDL 343
Cdd:PHA02562  234 AEIEELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEKGGVCP-TCTQQ-ISEGPDRIT-------KI 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 344 DSIIDAVRTQYELIAQKSKDEAEALYQtkYQELQVSAgrhgDELKNsklEITELNRTIQRLQAEISSVRKQIEQMHVAIS 423
Cdd:PHA02562  305 KDKLKELQHSLEKLDTAIDELEEIMDE--FNEQSKKL----LELKN---KISTNKQSLITLVDKAKKVKAAIEELQAEFV 375

                         250
                  ....*....|....*....
gi 1952735413 424 DAEERGEQaLQDARQKLGD 442
Cdd:PHA02562  376 DNAEELAK-LQDELDKIVK 393
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 233-489 4.31e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 4.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  233 ELRRQVDFLNAEQMRQNTDVKNMQDVVEDYKSKYEEEINRRANTENDFVVLKKDVDAAYMSKVDLESKVNVLfgeinflk 312
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL-------- 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  313 ylfETELSQMQTHISDTNVILSMDNNRFLDLDSIIDAVRTQYELIaQKSKDEAEALYQTKYQELQVSAGRhgdeLKNSKL 392
Cdd:TIGR02168  308 ---RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL-KEELESLEAELEELEAELEELESR----LEELEE 379

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  393 EITELNRTIQRLQAEISSVRKQIEQMHVAISDAEERGEQALQDARQKLGDLEDA--------LHQAKEELARLLRDYQAL 464
Cdd:TIGR02168  380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAelkelqaeLEELEEELEELQEELERL 459

                          250       260
                   ....*....|....*....|....*
gi 1952735413  465 LGAKLSLDVEIATYRKLLEGEESRM 489
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAEREL 484
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 231-453 5.76e-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: 39.67  E-value: 5.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  231 ISELRRQVDFLNAEQMRQN-------TDVKNMQDVVEDYKSKYEEEINRRANTENDFVVLKKDVDAAYMSkvDLESKVNV 303
Cdd:TIGR02169  718 IGEIEKEIEQLEQEEEKLKerleeleEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRIPE 795

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  304 LFGEINFLkylfETELSQMQTHISDTNVIL-SMDNNRFLDLDSIIDAVRTQYELIAQKSKDEAE-ALYQTKYQELQVSAG 381
Cdd:TIGR02169  796 IQAELSKL----EEEVSRIEARLREIEQKLnRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEiENLNGKKEELEEELE 871

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  382 RH-------GDELKNskleiteLNRTIQRLQAEISSVRKQIEQMHVAISDAEERGEQ---ALQDARQKLGDLEDALHQAK 451
Cdd:TIGR02169  872 ELeaalrdlESRLGD-------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSElkaKLEALEEELSEIEDPKGEDE 944


                   ..
gi 1952735413  452 EE 453
Cdd:TIGR02169  945 EI 946
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 228-456 6.13e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 6.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 228 ENYISELRRQVDFLNAEQMRQNTDVKNMQDVVEDYKSKYEEEINRRANTENDFVVLKKDVDAAymsKVDLESKVNVLfge 307
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREEL--- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 308 INFLKYLFETELSqmqthISDTNVILSMDN-----NRFLDLDSIIDAVRTQYELI--AQKSKDEAEALYQTKYQELQVSA 380
Cdd:COG3883    89 GERARALYRSGGS-----VSYLDVLLGSESfsdflDRLSALSKIADADADLLEELkaDKAELEAKKAELEAKLAELEALK 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952735413 381 GRHGDELKNSKLEITELNRTIQRLQAEISSVRKQIEQMHVAISDAEERGEQALQDARQKLGDLEDALHQAKEELAR 456
Cdd:COG3883   164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 208-457 6.89e-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: 39.67  E-value: 6.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  208 WELLQQVNTstrtnnlepvLENYISELRRQVDFLNAEQmrQNTDVKnMQDVVEDYKSKYE--EEINRRAN--TENDFVVL 283
Cdd:TIGR02169  226 YELLKEKEA----------LERQKEAIERQLASLEEEL--EKLTEE-ISELEKRLEEIEQllEELNKKIKdlGEEEQLRV 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  284 KKDVDaaymskvDLESKVNVLFGEINFLkylfETELSQMQTHISDTNVILSMDNNRFLDLDSIIDAV---RTQYELIAQK 360
Cdd:TIGR02169  293 KEKIG-------ELEAEIASLERSIAEK----ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEErkrRDKLTEEYAE 361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  361 SKDEAEALYQtKYQELQVSAGRHGDELKNSKLEITELN-------RTIQRLQAEISSVRKQIEQMHVAISDAEER----- 428
Cdd:TIGR02169  362 LKEELEDLRA-ELEEVDKEFAETRDELKDYREKLEKLKreinelkRELDRLQEELQRLSEELADLNAAIAGIEAKinele 440

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1952735413  429 ------------GEQALQDARQKLGDLEDALHQAKEELARL 457
Cdd:TIGR02169  441 eekedkaleikkQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 385-461 7.63e-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: 39.28  E-value: 7.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413  385 DELKNSKLEITELNRTIQRLQAEISSVRKQIEQMHV---AISDAEERGEQALQDARQKLGDLEDALHQAKEELARLLRDY 461
Cdd:TIGR02169  709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdlsSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL 788
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 227-494 8.71e-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: 8.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 227 LENYISELRRQVDFLNAEQMRQNTDVKNMQDVVEDYKSKYEEEINRRANTENDFVVLKKDvdaaymsKVDLESKVNVLFG 306
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE-------KLNIQKNIDKIKN 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 307 EINFLKYL-------------FETELSQMQTHISDTNVILSMDNNRFLDLDSIIDAVRTQYELIAQKSKDEAEALyQTKY 373
Cdd:TIGR04523 195 KLLKLELLlsnlkkkiqknksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL-SEKQ 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952735413 374 QELQvsagrhgdelkNSKLEITELNRTIQRLQAEISSVRKQIEQ-MHVAISDAEERGEQALQDARQKLGDLEDALHQAKE 452
Cdd:TIGR04523 274 KELE-----------QNNKKIKELEKQLNQLKSEISDLNNQKEQdWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNE 342

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1952735413 453 ELARLLRDYQALLGAKLSLDVEIATYRKLLEGEESRMSGELQ 494
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQ 384
DUF6594 pfam20237
Family of unknown function (DUF6594); This entry represents a group of uncharacterized ...
 397-465 9.66e-03

Family of unknown function (DUF6594); This entry represents a group of uncharacterized proteins that contain a set of C-terminal transmembrane helices. The family may be related to pfam10267.


Pssm-ID: 466388  Cd Length: 233  Bit Score: 38.11  E-value: 9.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952735413 397 LN-RTIQRLQAEISSVRKQIEQMhvaisDAEERGEQALQDARQKLGDLEDALHQAK-EELARLLRDYQALL 465
Cdd:pfam20237  23 LNaRNLLHLQDELAELEEELDEL-----DDEESRDLSLGDDPRSRNSWDELSERRElLEIRKKLKEYDALL 88
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 395-463 9.91e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 36.91  E-value: 9.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952735413 395 TELNRTIQRLQAEISSVRKQIEQMHVAISDAEER---GEQALQDARQKLGDLEDALHQAKEELARLLRDYQA 463
Cdd:pfam11559  55 ESLNETIRTLEAEIERLQSKIERLKTQLEDLERElalLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQ 126
 
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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