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Conserved domains on  [gi|984880688|ref|NP_001306166|]
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peripherin [Danio rerio]

Protein Classification

intermediate filament family protein( domain architecture ID 12057329)

intermediate filament family protein similar to desmin, a muscle-specific type III intermediate filament essential for proper muscular structure and function

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
72-385 1.40e-120

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 353.84  E-value: 1.40e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   72 NEKRELQELNDRFASFIEKVRYLEQQNSRLTQELGQFKEQQQGPSGRLGDLCQQEMRELRRQLELMGKDRDQMQVERDNL 151
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688  152 AEDVALLKQRLNEEMQKREEAENNLTLFRKDVDDATLARLELERKIESLMDEIEFLKKMHDEEIQDVQVSVQSQQMKMEv 231
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688  232 METSSRPDLTAALRDIRSQYESIASKNMQESEEWYKSKFADLTDSAKRNAEAMRQSKQDNNDLRRQIQAQNCDIEALKST 311
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 984880688  312 NEALLRQMREMEEQFTLEAGNYQDAVGRLEEEIRHLKEEMSRHLREYQDLLNVKMALDIEIATYRKLLEGEESR 385
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
 1-71 3.55e-17

Intermediate filament head (DNA binding) region; This family represents the N-terminal head region of intermediate filaments. Intermediate filament heads bind DNA. Vimentin heads are able to alter nuclear architecture and chromatin distribution, and the liberation of heads by HIV-1 protease liberates may play an important role in HIV-1 associated cytopathogenesis and carcinogenesis. Phosphorylation of the head region can affect filament stability. The head has been shown to interaction with the rod domain of the same protein.


:

Pssm-ID: 461414 [Multi-domain]  Cd Length: 83  Bit Score: 75.89  E-value: 3.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688    1 MSHYSYRTSHH------RSYGTPS----VSSRIGGRYTSSIPS----RPVdfRSRSSAPAPRLSYDKVDFSLAEAVNQEF 66
Cdd:pfam04732   1 YSSSSYRRMFGdssssrPSYSSSSgsrsVSSRSYSRSSSSSPSsssrRSS--RSSSRSSYPSLAADSLDFSLADALNQEF 78


                  ....*
gi 984880688   67 LATRS 71
Cdd:pfam04732  79 KATRT 83
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
72-385 1.40e-120

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 353.84  E-value: 1.40e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   72 NEKRELQELNDRFASFIEKVRYLEQQNSRLTQELGQFKEQQQGPSGRLGDLCQQEMRELRRQLELMGKDRDQMQVERDNL 151
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688  152 AEDVALLKQRLNEEMQKREEAENNLTLFRKDVDDATLARLELERKIESLMDEIEFLKKMHDEEIQDVQVSVQSQQMKMEv 231
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688  232 METSSRPDLTAALRDIRSQYESIASKNMQESEEWYKSKFADLTDSAKRNAEAMRQSKQDNNDLRRQIQAQNCDIEALKST 311
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 984880688  312 NEALLRQMREMEEQFTLEAGNYQDAVGRLEEEIRHLKEEMSRHLREYQDLLNVKMALDIEIATYRKLLEGEESR 385
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
 1-71 3.55e-17

Intermediate filament head (DNA binding) region; This family represents the N-terminal head region of intermediate filaments. Intermediate filament heads bind DNA. Vimentin heads are able to alter nuclear architecture and chromatin distribution, and the liberation of heads by HIV-1 protease liberates may play an important role in HIV-1 associated cytopathogenesis and carcinogenesis. Phosphorylation of the head region can affect filament stability. The head has been shown to interaction with the rod domain of the same protein.


Pssm-ID: 461414 [Multi-domain]  Cd Length: 83  Bit Score: 75.89  E-value: 3.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688    1 MSHYSYRTSHH------RSYGTPS----VSSRIGGRYTSSIPS----RPVdfRSRSSAPAPRLSYDKVDFSLAEAVNQEF 66
Cdd:pfam04732   1 YSSSSYRRMFGdssssrPSYSSSSgsrsVSSRSYSRSSSSSPSsssrRSS--RSSSRSSYPSLAADSLDFSLADALNQEF 78


                  ....*
gi 984880688   67 LATRS 71
Cdd:pfam04732  79 KATRT 83
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 74-386 4.87e-09

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: 58.53  E-value: 4.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688    74 KRELQELNDRFASFIEKVRYLEQQNSRLTQELGQFKEQqqgpsgrlGDLCQQEMRELRRQLELMGKDRDQMQVERDNLAE 153
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEE--------LEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   154 DVALLKQRLNEEMQKREEAEnnltlfrKDVDDATLARLELERKIESL-------MDEIEFLKKMHDE---EIQDVQVSVQ 223
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELE-------ERLEEAEEELAEAEAEIEELeaqieqlKEELKALREALDElraELTLLNEEAA 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   224 SQQMKMEVMETSSR------PDLTAALRDIRSQYESIAS--KNMQESEEWYKSKFADLTDSAKRNAEAMRQSKQDNNDLR 295
Cdd:TIGR02168  821 NLRERLESLERRIAaterrlEDLEEQIEELSEDIESLAAeiEELEELIEELESELEALLNERASLEEALALLRSELEELS 900

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   296 RQIQaqncDIEALKSTNEALLRQMREMEEQFTLEagnyqdaVGRLEEEIRHLKEEMSrhlREYQDLLNVKMALDIEIATY 375
Cdd:TIGR02168  901 EELR----ELESKRSELRRELEELREKLAQLELR-------LEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDD 966

                          330
                   ....*....|.
gi 984880688   376 RKLLEGEESRI 386
Cdd:TIGR02168  967 EEEARRRLKRL 977
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 124-353 1.61e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 53.23  E-value: 1.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 124 QQEMRELRRQLELMGKDRDQMQVERDNLAEDVALLKQRLNEEMQKREEAENNLTLFRKDVDdatlarlELERKIESLMDE 203
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 204 IEFLKKMHDEEIQDVQVSVQSQQMKMEVmetsSRPDLTAALRdiRSQYESIASKNMQESEEWYKSKFADLtdsaKRNAEA 283
Cdd:COG4942   99 LEAQKEELAELLRALYRLGRQPPLALLL----SPEDFLDAVR--RLQYLKYLAPARREQAEELRADLAEL----AALRAE 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 284 MRQSKQDNNDLRRQIQAQNCDIEALKSTNEALLRQMREMEEQFTLEAGNYQDAVGRLEEEIRHLKEEMSR 353
Cdd:COG4942  169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
F-BAR_FCHO1 cd07674
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; ...
 178-352 2.88e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH domain Only 1 (FCHO1) may be involved in clathrin-coated vesicle formation. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO2 and endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153358 [Multi-domain]  Cd Length: 261  Bit Score: 39.16  E-value: 2.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 178 LFRKDVDDATLARLELERKIESLMDEI----EFLKKMH---DEEIQDVQVSVQSQQMKMEVMETSSRPDLTAALRDIRSQ 250
Cdd:cd07674   64 VFRVSSDKLALCHLELMRKLNDLIKDInrygDEQVKIHkktKEEAIGTLEAVQSLQVQSQHLQKSRENYHSKCVEQERLR 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 251 YESIASKNMQESEEwykskfadltdSAKRNAEAMRQSKQDNNDLRRQIQAQNCD-IEALKSTNEALLRQMREMEEQFTLE 329
Cdd:cd07674  144 REGVPQKELEKAEL-----------KTKKAAESLRGSVEKYNRARGDFEQKMLEsAQKFQDIEETHLRHMKLLIKGYSHS 212

                        170       180
                 ....*....|....*....|...
gi 984880688 330 AGNYQDAVGRLEEEIRHLKEEMS 352
Cdd:cd07674  213 VEDTHVQIGQVHEEFKQNVENVG 235
PTZ00121 PTZ00121
MAEBL; Provisional
 60-349 5.45e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 5.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   60 EAVNQEFLATRSNEKRELQELNDRFASFIEKVRYLEQ--QNSRLTQELGQFKEQQQGPSGRLGdlcqqemrELRRQLELM 137
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKA--------EEAKKADEA 1539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688  138 GKDRDQMQVERDNLAEDVALLKQRLNEEMQKREEAENNLTLFRkdvddATLARLELERKIESLMDEIEFLKKMHDEEIQD 217
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK-----AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688  218 V-QVSVQSQQMKMEVMETSSRPDLTAALRDIRSQYESIasKNMQESEEWYKSKFADLTDSAKRNAEAMRQSKQDNNDLRR 296
Cdd:PTZ00121 1615 AeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 984880688  297 QIQAQNCD---IEALKSTNEALLRQMREMEEQFTLEAGNYQDAVGRLEEEIRHLKE 349
Cdd:PTZ00121 1693 ALKKEAEEakkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
72-385 1.40e-120

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 353.84  E-value: 1.40e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   72 NEKRELQELNDRFASFIEKVRYLEQQNSRLTQELGQFKEQQQGPSGRLGDLCQQEMRELRRQLELMGKDRDQMQVERDNL 151
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688  152 AEDVALLKQRLNEEMQKREEAENNLTLFRKDVDDATLARLELERKIESLMDEIEFLKKMHDEEIQDVQVSVQSQQMKMEv 231
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688  232 METSSRPDLTAALRDIRSQYESIASKNMQESEEWYKSKFADLTDSAKRNAEAMRQSKQDNNDLRRQIQAQNCDIEALKST 311
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 984880688  312 NEALLRQMREMEEQFTLEAGNYQDAVGRLEEEIRHLKEEMSRHLREYQDLLNVKMALDIEIATYRKLLEGEESR 385
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
 1-71 3.55e-17

Intermediate filament head (DNA binding) region; This family represents the N-terminal head region of intermediate filaments. Intermediate filament heads bind DNA. Vimentin heads are able to alter nuclear architecture and chromatin distribution, and the liberation of heads by HIV-1 protease liberates may play an important role in HIV-1 associated cytopathogenesis and carcinogenesis. Phosphorylation of the head region can affect filament stability. The head has been shown to interaction with the rod domain of the same protein.


Pssm-ID: 461414 [Multi-domain]  Cd Length: 83  Bit Score: 75.89  E-value: 3.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688    1 MSHYSYRTSHH------RSYGTPS----VSSRIGGRYTSSIPS----RPVdfRSRSSAPAPRLSYDKVDFSLAEAVNQEF 66
Cdd:pfam04732   1 YSSSSYRRMFGdssssrPSYSSSSgsrsVSSRSYSRSSSSSPSsssrRSS--RSSSRSSYPSLAADSLDFSLADALNQEF 78


                  ....*
gi 984880688   67 LATRS 71
Cdd:pfam04732  79 KATRT 83
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 74-386 4.87e-09

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: 58.53  E-value: 4.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688    74 KRELQELNDRFASFIEKVRYLEQQNSRLTQELGQFKEQqqgpsgrlGDLCQQEMRELRRQLELMGKDRDQMQVERDNLAE 153
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEE--------LEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   154 DVALLKQRLNEEMQKREEAEnnltlfrKDVDDATLARLELERKIESL-------MDEIEFLKKMHDE---EIQDVQVSVQ 223
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELE-------ERLEEAEEELAEAEAEIEELeaqieqlKEELKALREALDElraELTLLNEEAA 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   224 SQQMKMEVMETSSR------PDLTAALRDIRSQYESIAS--KNMQESEEWYKSKFADLTDSAKRNAEAMRQSKQDNNDLR 295
Cdd:TIGR02168  821 NLRERLESLERRIAaterrlEDLEEQIEELSEDIESLAAeiEELEELIEELESELEALLNERASLEEALALLRSELEELS 900

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   296 RQIQaqncDIEALKSTNEALLRQMREMEEQFTLEagnyqdaVGRLEEEIRHLKEEMSrhlREYQDLLNVKMALDIEIATY 375
Cdd:TIGR02168  901 EELR----ELESKRSELRRELEELREKLAQLELR-------LEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDD 966

                          330
                   ....*....|.
gi 984880688   376 RKLLEGEESRI 386
Cdd:TIGR02168  967 EEEARRRLKRL 977
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 124-353 1.61e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 53.23  E-value: 1.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 124 QQEMRELRRQLELMGKDRDQMQVERDNLAEDVALLKQRLNEEMQKREEAENNLTLFRKDVDdatlarlELERKIESLMDE 203
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 204 IEFLKKMHDEEIQDVQVSVQSQQMKMEVmetsSRPDLTAALRdiRSQYESIASKNMQESEEWYKSKFADLtdsaKRNAEA 283
Cdd:COG4942   99 LEAQKEELAELLRALYRLGRQPPLALLL----SPEDFLDAVR--RLQYLKYLAPARREQAEELRADLAEL----AALRAE 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 284 MRQSKQDNNDLRRQIQAQNCDIEALKSTNEALLRQMREMEEQFTLEAGNYQDAVGRLEEEIRHLKEEMSR 353
Cdd:COG4942  169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 51-315 1.65e-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: 53.91  E-value: 1.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688    51 YDKVDFSLAEAVNQEF-LATRSNEKRE-LQELNDRFASFIEKVRYLEQQNSRLTQELGQFKEQQQGPSGRLGDLCQQ--- 125
Cdd:TIGR02168  241 LEELQEELKEAEEELEeLTAELQELEEkLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQlee 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   126 ---EMRELRRQLELMGKDRDQMQVERDNLAEDVALLKQRLNEEMQKREEAENNLTLFRKDVDDATLARLELERKIESLMD 202
Cdd:TIGR02168  321 leaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   203 EIEFLkkmhDEEIQDVQVSVQSQQmkmEVMETSSRPDLTAALRDIRSQYESIasknmQESEEWYKSKFADLTDSAKRNAE 282
Cdd:TIGR02168  401 EIERL----EARLERLEDRRERLQ---QEIEELLKKLEEAELKELQAELEEL-----EEELEELQEELERLEEALEELRE 468

                          250       260       270
                   ....*....|....*....|....*....|...
gi 984880688   283 AMRQSKQDNNDLRRQIQAQNCDIEALKSTNEAL 315
Cdd:TIGR02168  469 ELEEAEQALDAAERELAQLQARLDSLERLQENL 501
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 64-375 1.79e-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: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688  64 QEFLATRSNEKRELQELNDRFASFIEKVRYLEQQNSRLTQELGQFKEQQQGPSGRLGDL------CQQEMRELRRQLELM 137
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELlaelarLEQDIARLEERRREL 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 138 GKDRDQMQVERDNLAEDVALLKQRLNEEMQKREEAENNLTLFRKDVDDATLARLELERKIESLMDEIEFLKKMHDEEIQD 217
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 218 VQVSVQSQQMKMEVMETSSRpdLTAALRDIRSQYESIASKNMQESEEWYKSKFADLTDSAKRNAEAMRQSKQDNNDLRRQ 297
Cdd:COG1196  395 AAELAAQLEELEEAEEALLE--RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 984880688 298 IQAQNCDIEALKSTNEALLRqmREMEEQFTLEAGNYQDAVGRLeeeirHLKEEMSRHLREYQDLLNVKMALDIEIATY 375
Cdd:COG1196  473 ALLEAALAELLEELAEAAAR--LLLLLEAEADYEGFLEGVKAA-----LLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 128-388 2.99e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.15  E-value: 2.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   128 RELRRQLELMGKDRDQMQVERDNLAEDVALLKQRLNEEMQKREEAENNLTLFRKDV-----DDATLARL--ELERKIESL 200
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIeqleqEEEKLKERleELEEDLSSL 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   201 MDEIEFLKKMHDE---EIQDVQVSVQSQQMKMEVMETSSRPDltaALRDIRSQYESIasknmqeseEWYKSKFADLTDSA 277
Cdd:TIGR02169  750 EQEIENVKSELKEleaRIEELEEDLHKLEEALNDLEARLSHS---RIPEIQAELSKL---------EEEVSRIEARLREI 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   278 KRNAEAMRQSKQDNNDLRRQIQAQNCDIEALKSTNEALLRQMREMEEQFTLEAGNYQDAVGRLEEEIRHLKEEMSRHLRE 357
Cdd:TIGR02169  818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897

                          250       260       270
                   ....*....|....*....|....*....|.
gi 984880688   358 YQDLLNVKMALDIEIATYRKLLEGEESRIAV 388
Cdd:TIGR02169  898 LRELERKIEELEAQIEKKRKRLSELKAKLEA 928
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 126-387 1.18e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 126 EMRELRRQLELMGKDRDQMQVERDNLAEDVALLKQRLNEEMQKREEAENNLTLFRKDVDDATLARLELERKIESLMDEIE 205
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 206 FLKKMHDEEIQDVQVSVQSQQMKMEVMETssrpdLTAALRDIRSQYESIASKNMQESEEwyksKFADLTDSAKRNAEAMR 285
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEE-----LEEELEEAEEELEEAEAELAEAEEA----LLEAEAELAEAEEELEE 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 286 QSKQDNNDLRRQIQAQNcDIEALKSTNEALLRQMREMEEQFTLEAGNYQDAVGRLEEEIRHLKEEMSRHLREYQDLLnvk 365
Cdd:COG1196  384 LAEELLEALRAAAELAA-QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE--- 459

                        250       260
                 ....*....|....*....|..
gi 984880688 366 mALDIEIATYRKLLEGEESRIA 387
Cdd:COG1196  460 -ALLELLAELLEEAALLEAALA 480
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 139-377 2.42e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 49.38  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 139 KDRDQMQVERDNLAEDVALLKQRLNEEMQKREEAENNLTLFRKDVDDATLARLELERKIESLMDEIEFLKKmhdeEIQDV 218
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK----EIAEL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 219 QVSVQSQQMKME----VMETSSRPDLTAALRDIRSQYESIASKNMqeseewykskFADLTDSAKRNAEAMRQSKQDNNDL 294
Cdd:COG4942   96 RAELEAQKEELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQY----------LKYLAPARREQAEELRADLAELAAL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 295 RRQIQAQNCDIEALKSTNEALLRQMREMEEQftleagnYQDAVGRLEEEIRHLKEEMSRHLREYQDLLNVKMALDIEIAT 374
Cdd:COG4942  166 RAELEAERAELEALLAELEEERAALEALKAE-------RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238


                 ...
gi 984880688 375 YRK 377
Cdd:COG4942  239 AAE 241
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 118-387 2.97e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 2.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 118 RLGDLcqqeMRELRRQLELMGKDRDQ------------------MQVERDNLAEDVALLKQRLNEEMQKREEAENNLTLF 179
Cdd:COG1196  190 RLEDI----LGELERQLEPLERQAEKaeryrelkeelkeleaelLLLKLRELEAELEELEAELEELEAELEELEAELAEL 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 180 RKDVDDATLARLELERKIESLMDEIEFLKKMHDEEIQDVQVSVQSQQmkmevmetssrpDLTAALRDIRSQYESIASKNM 259
Cdd:COG1196  266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR------------ELEERLEELEEELAELEEELE 333

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 260 QESEEwYKSKFADLTDSAKRNAEAMRQSKQDNNDLRRQIQAQNCDIEALKSTNEALLRQMREMEEQftleagnyQDAVGR 339
Cdd:COG1196  334 ELEEE-LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL--------AAQLEE 404

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 984880688 340 LEEEIRHLKEEMSRHLREYQDLLNVKMALDIEIATYRKLLEGEESRIA 387
Cdd:COG1196  405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 78-386 9.41e-06

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: 48.19  E-value: 9.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688    78 QELNDRFASFIEKVRYLEQQNSRLTQELGQFKEqqqgpsgrlgdLCQQEMRELRRQLELMGKDRDQMQVERDNLAEDVAL 157
Cdd:pfam15921  306 EQARNQNSMYMRQLSDLESTVSQLRSELREAKR-----------MYEDKIEELEKQLVLANSELTEARTERDQFSQESGN 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   158 LK---QRLNEEMQKRE-----EAENNLTLFRKDVDDATLA---RLELERKIESLMDEIEFLKKMHDEEIQDVQVSVQSQQ 226
Cdd:pfam15921  375 LDdqlQKLLADLHKREkelslEKEQNKRLWDRDTGNSITIdhlRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQ 454

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   227 MKMEVMETSSrpDLTAALRD----IRSQYESIASKNMQ-ESEEwykSKFADLTDSAKRNAEAMRQSKQDNNDLRRQIQAQ 301
Cdd:pfam15921  455 GKNESLEKVS--SLTAQLEStkemLRKVVEELTAKKMTlESSE---RTVSDLTASLQEKERAIEATNAEITKLRSRVDLK 529

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   302 NCDIEALKSTNEAlLRQMREMEEQFTLEAGNYQDAVGRLEEEIRHLKEEMSRHLREYQDLLNVKMALDIEIATYRklLEG 381
Cdd:pfam15921  530 LQELQHLKNEGDH-LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR--LEL 606


                   ....*
gi 984880688   382 EESRI 386
Cdd:pfam15921  607 QEFKI 611
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 71-204 1.85e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 1.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688    71 SNEKRELQELNDRFASFIEKVRYLEQQNSRLTQELGQFKEQQQGPSGRLGDLcQQEMRELRRQLELMGKDRDQMQVERDN 150
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL-EELIEELESELEALLNERASLEEALAL 891

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 984880688   151 LAEDVALLKQRLNEEMQKREEAENNLTLFRKDVDDATLARLELERKIESLMDEI 204
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 128-387 2.01e-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: 2.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   128 RELRRQLELMGKDRDQMQVERDNLAE----DVALLKQRLNEEMQKREEAENNLTLFRKDVDDATLARLELERKIESLMDE 203
Cdd:TIGR02169  194 DEKRQQLERLRREREKAERYQALLKEkreyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   204 IEFLKKMHDEEIQDVQVSVQSqqmKMEvmetssrpDLTAALRDIRSQyESIASKNMQESEEWYKSKFADLtDSAKRNAEA 283
Cdd:TIGR02169  274 LEELNKKIKDLGEEEQLRVKE---KIG--------ELEAEIASLERS-IAEKERELEDAEERLAKLEAEI-DKLLAEIEE 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   284 MRQSKQDNNDLRRQIQAQncdIEALKSTNEALLRQMREMEEqftlEAGNYQDAVGRLEEEIRHLKEEMSRHLREYQDLLN 363
Cdd:TIGR02169  341 LEREIEEERKRRDKLTEE---YAELKEELEDLRAELEEVDK----EFAETRDELKDYREKLEKLKREINELKRELDRLQE 413

                          250       260
                   ....*....|....*....|....
gi 984880688   364 VKMALDIEIATYRKLLEGEESRIA 387
Cdd:TIGR02169  414 ELQRLSEELADLNAAIAGIEAKIN 437
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
58-209 4.07e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 4.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   58 LAEAVNQEFLATRSNE-KRELQELNDRFASFIEKVRYLEQQNSRLTQELGQFKEQQQGPSGRLGDLCQQEMRELRRQLEL 136
Cdd:COG4913   277 LRAALRLWFAQRRLELlEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEE 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688  137 MGKDRDQMQ-------VERDNLAEDVALLKQRLNEEMQKREEAENNLtlfRKDVDDATLARLELERKIESLMDEIEFLKK 209
Cdd:COG4913   357 RERRRARLEallaalgLPLPASAEEFAALRAEAAALLEALEEELEAL---EEALAEAEAALRDLRRELRELEAEIASLER 433
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 126-405 6.01e-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: 45.44  E-value: 6.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   126 EMRELRRQLELMGKDRDQMQVERDNLAEDVALLKQRLNEEMQK-REEAENNLTLFRKDVDDATLARLELERKIESLMDEI 204
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   205 EFLkkmhDEEIQDVQVSVQSQQMKMEVMETSSRP-------------DLTAALRDIRSQYESIASKN---------MQES 262
Cdd:TIGR02169  318 EDA----EERLAKLEAEIDKLLAEIEELEREIEEerkrrdklteeyaELKEELEDLRAELEEVDKEFaetrdelkdYREK 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   263 EEWYKSKFADLTDSAKRNAEAMRQSKQDNNDLRRQIQAQNCDIEALKSTNEALLRQMREMEEqftlEAGNYQDAVGRLEE 342
Cdd:TIGR02169  394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW----KLEQLAADLSKYEQ 469

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 984880688   343 EIRHLKEEMSRHLREYQDLlnvKMALDIEIATYRKLLEGEESRIAVPIMKMPSMSGHSGDYGQ 405
Cdd:TIGR02169  470 ELYDLKEEYDRVEKELSKL---QRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQ 529
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 126-387 6.62e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 6.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   126 EMRELRRQLELMGKDRDQMQVERDNLAEDVALLKQRLNEEMQKREEAEnnltlfrKDVDDATLARLELERKIESLMDEIE 205
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE-------EEIEELQKELYALANEISRLEQQKQ 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   206 FLK-KMHDEEIQDVQVSVQSQQMKmevmetSSRPDLTAALRDIRSQYESIA--SKNMQESEEWYKSKFADLTDSAKRNAE 282
Cdd:TIGR02168  306 ILReRLANLERQLEELEAQLEELE------SKLDELAEELAELEEKLEELKeeLESLEAELEELEAELEELESRLEELEE 379

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   283 AMRQSKQDNNDLRRQIQAQNCDIEALKSTNEAL-LRQMREMEEQFTLEAGNYQDAVGRLEEEIRHLKEEMSRHLREYQDL 361
Cdd:TIGR02168  380 QLETLRSKVAQLELQIASLNNEIERLEARLERLeDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459

                          250       260
                   ....*....|....*....|....*.
gi 984880688   362 LNVKMALDIEIATYRKLLEGEESRIA 387
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELA 485
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
131-363 1.32e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688  131 RRQLELMGKDRDQMQVERDNLAEDVALLKQRLnEEMQKREEAENNLTLFRKDVDDAtlarLELERKIESLMDEIEFLKKM 210
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAEL-DALQERREALQRLAEYSWDEIDV----ASAEREIAELEAELERLDAS 683

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688  211 HD------EEIQDVQVSVQSQQMKMEVMET------SSRPDLTAALRDIRSQYESIASKNMQESEEWYKSKFADLTDSAK 278
Cdd:COG4913   684 SDdlaaleEQLEELEAELEELEEELDELKGeigrleKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688  279 RNAEAmrqskqdnNDLRRQIQAQNcdiEALKSTNEALLRQMREMEEQFTLEAGNYQDAVGRLEEEIRHLK----EEMSRH 354
Cdd:COG4913   764 ERELR--------ENLEERIDALR---ARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDrleeDGLPEY 832


                  ....*....
gi 984880688  355 LREYQDLLN 363
Cdd:COG4913   833 EERFKELLN 841
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 60-286 2.08e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 2.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688    60 EAVNQEFLATRSNEKRELQElndRFASFIEKVRYLEQQNSRLTQELGQFKEQQQGPSGRLGDLcQQEMRELRRQLELMGK 139
Cdd:TIGR02169  275 EELNKKIKDLGEEEQLRVKE---KIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL-LAEIEELEREIEEERK 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   140 DRDQMQVERDNLAEDVALLKQRLNEEMQKREEAENNLTLFRKDVDDATLARLELERKIESLMDEieflKKMHDEEIQDVQ 219
Cdd:TIGR02169  351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE----LQRLSEELADLN 426

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 984880688   220 VSVQSQQMKMEVMETsSRPDLTAALRDIRSQYESIASKNMQESEEWYKSKfADLTDSAKRNAEAMRQ 286
Cdd:TIGR02169  427 AAIAGIEAKINELEE-EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK-EEYDRVEKELSKLQRE 491
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
64-380 4.21e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 4.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688  64 QEFLATRSNEKRELQELNDRFASFIEKVRYLEQQNSRLTQELGQFKEQQQ-GPSGRLGDLCQQEMRELRRQLELM---GK 139
Cdd:COG4717   77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQlLPLYQELEALEAELAELPERLEELeerLE 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 140 DRDQMQVERDNLAEDVALLKQRLNEEMQK-REEAENNLTLFRKDVDDATLARLELERKIESLMDEIEFLKkmhdEEIQDV 218
Cdd:COG4717  157 ELRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE----EELEQL 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 219 QVSVQSQQMKMEVMETSSRPDLTAALRDIRSQYESIASKNMQESEEWY--KSKFADLTDSAKRNAEAMRQSKQDNNDLRR 296
Cdd:COG4717  233 ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFlvLGLLALLFLLLAREKASLGKEAEELQALPA 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 297 QIQAQNCDIEALKSTNEALLRQMREMEEQFTLEAGNYQDAVGRLEEEIRHLKEEmsRHLREYQDLLNVKMALDIEiaTYR 376
Cdd:COG4717  313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE--ELEQEIAALLAEAGVEDEE--ELR 388


                 ....
gi 984880688 377 KLLE 380
Cdd:COG4717  389 AALE 392
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 67-365 8.50e-04

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: 41.63  E-value: 8.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   67 LATRSNEKRELQELNDRFASFIEKVRYLEQQNSRLTQELGQFK---EQQQGPSGRLGDLCQ---QEMRELRRQLELMgkd 140
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEkiaEELKGKEQELIFLLQareKEIHDLEIQLTAI--- 462

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688  141 rdqmQVERDNLAEDVALLKQRLNEEMQKREEAENNLTLF----RKDVDDATLARLELERKIESLMDEieflKKMHDEEIQ 216
Cdd:pfam05483 463 ----KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLllenKELTQEASDMTLELKKHQEDIINC----KKQEERMLK 534

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688  217 DVQvsvqsqqmKMEVMETSSRPDLTAALRDIRSQYESIASKnMQESEEWYKSKFADLTDSAKRnaeaMRQSKQDNNDLRR 296
Cdd:pfam05483 535 QIE--------NLEEKEMNLRDELESVREEFIQKGDEVKCK-LDKSEENARSIEYEVLKKEKQ----MKILENKCNNLKK 601

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 984880688  297 QIQAQNCDIEALKSTNEALLRQMREMEEQFTLeagnYQDAVGRLEEEIRHLKEEMSRHLREYQDLLNVK 365
Cdd:pfam05483 602 QIENKNKNIEELHQENKALKKKGSAENKQLNA----YEIKVNKLELELASAKQKFEEIIDNYQKEIEDK 666
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 167-363 1.29e-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: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   167 QKREEAENNLTLFRKDVDDATLARLELERKIESLMDEIEFLKKMHD--EEIQDVQVSVQSQQMKMEV-----------ME 233
Cdd:TIGR02168  172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKElkAELRELELALLVLRLEELReeleelqeelkEA 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   234 TSSRPDLTAALRDIRSQYESIASK--NMQESEEWYKSKFADLT-DSAKRNAEAMRQSKQDNNdLRRQIQAQNCDIEALKS 310
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEvsELEEEIEELQKELYALAnEISRLEQQKQILRERLAN-LERQLEELEAQLEELES 330

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 984880688   311 TNEALLRQMREMEEQFTLEAGNYQDAVGRLEEEiRHLKEEMSRHLREYQDLLN 363
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEEL-EAELEELESRLEELEEQLE 382
F-BAR_FCHO1 cd07674
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; ...
 178-352 2.88e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH domain Only 1 (FCHO1) may be involved in clathrin-coated vesicle formation. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO2 and endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153358 [Multi-domain]  Cd Length: 261  Bit Score: 39.16  E-value: 2.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 178 LFRKDVDDATLARLELERKIESLMDEI----EFLKKMH---DEEIQDVQVSVQSQQMKMEVMETSSRPDLTAALRDIRSQ 250
Cdd:cd07674   64 VFRVSSDKLALCHLELMRKLNDLIKDInrygDEQVKIHkktKEEAIGTLEAVQSLQVQSQHLQKSRENYHSKCVEQERLR 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 251 YESIASKNMQESEEwykskfadltdSAKRNAEAMRQSKQDNNDLRRQIQAQNCD-IEALKSTNEALLRQMREMEEQFTLE 329
Cdd:cd07674  144 REGVPQKELEKAEL-----------KTKKAAESLRGSVEKYNRARGDFEQKMLEsAQKFQDIEETHLRHMKLLIKGYSHS 212

                        170       180
                 ....*....|....*....|...
gi 984880688 330 AGNYQDAVGRLEEEIRHLKEEMS 352
Cdd:cd07674  213 VEDTHVQIGQVHEEFKQNVENVG 235
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 72-213 3.11e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   72 NEKRELQELNDRFASFIEKVRYLEQQNSRLTQELGQFKEQQQGPSGRLGDLcQQEMRELRRQLELM--GKDRDQMQVERD 149
Cdd:TIGR04523 486 QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK-ESKISDLEDELNKDdfELKKENLEKEID 564

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 984880688  150 NLAEDVALLKQRLNEEMQKREEAENNLTLFRKDVDDATLARLELERKIESLMDEIEFLKKMHDE 213
Cdd:TIGR04523 565 EKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 68-284 5.38e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 5.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688  68 ATRSNEKRELQELNDRFASFIEKVRYLEQQNSRLTQELGQFKEQQQGPSGRLGDLcQQEMRELRRQLELMGKDRDQMQVE 147
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL-EQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688 148 rdnLAEDVALLKQRLNEEMQKREEAENNLTLFRKDVDDA----------TLARLELERKIESLMDEIEFLKKMHDEEIQD 217
Cdd:COG4942   99 ---LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAvrrlqylkylAPARREQAEELRADLAELAALRAELEAERAE 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 984880688 218 VQVSVQSQQMKMEVMET--SSRPDLTAALRDIRSQYESiASKNMQESEEWYKSKFADLTDSAKRNAEAM 284
Cdd:COG4942  176 LEALLAELEEERAALEAlkAERQKLLARLEKELAELAA-ELAELQQEAEELEALIARLEAEAAAAAERT 243
PTZ00121 PTZ00121
MAEBL; Provisional
 60-349 5.45e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 5.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688   60 EAVNQEFLATRSNEKRELQELNDRFASFIEKVRYLEQ--QNSRLTQELGQFKEQQQGPSGRLGdlcqqemrELRRQLELM 137
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKA--------EEAKKADEA 1539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688  138 GKDRDQMQVERDNLAEDVALLKQRLNEEMQKREEAENNLTLFRkdvddATLARLELERKIESLMDEIEFLKKMHDEEIQD 217
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK-----AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984880688  218 V-QVSVQSQQMKMEVMETSSRPDLTAALRDIRSQYESIasKNMQESEEWYKSKFADLTDSAKRNAEAMRQSKQDNNDLRR 296
Cdd:PTZ00121 1615 AeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 984880688  297 QIQAQNCD---IEALKSTNEALLRQMREMEEQFTLEAGNYQDAVGRLEEEIRHLKE 349
Cdd:PTZ00121 1693 ALKKEAEEakkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
 
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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