NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|261245089|ref|NP_083710|]
View 

lebercilin isoform a [Mus musculus]

Protein Classification

Lebercilin domain-containing protein( domain architecture ID 12174059)

Lebercilin domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 103-295 1.23e-67

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


:

Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 213.23  E-value: 1.23e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089  103 VTKRVLSARLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQ 182
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089  183 EKERATEKRVKETEGELFRTKFSLQKLKKISEARHLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQLLA 262
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 261245089  263 ERKRAFEAYDENKVLQKELQRLHHKLKEKEKEL 295
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
 
Name Accession Description Interval E-value
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 103-295 1.23e-67

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 213.23  E-value: 1.23e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089  103 VTKRVLSARLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQ 182
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089  183 EKERATEKRVKETEGELFRTKFSLQKLKKISEARHLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQLLA 262
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 261245089  263 ERKRAFEAYDENKVLQKELQRLHHKLKEKEKEL 295
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 107-319 8.12e-11

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: 63.24  E-value: 8.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 107 VLSARLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKER 186
Cdd:COG4942   14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 187 ATEKRVKETEGELFRTKFSLQKLKKISEARHLPERDDLAKKLVSAEL---KLDDTERKIKELSKNLELSTNSfQRQLLAE 263
Cdd:COG4942   94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYlkyLAPARREQAEELRADLAELAAL-RAELEAE 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 261245089 264 RKRAFEAYDENKVLQKELQRLhhkLKEKEKELdikniyaNRLPKSSPKKEKEIERK 319
Cdd:COG4942  173 RAELEALLAELEEERAALEAL---KAERQKLL-------ARLEKELAELAAELAEL 218
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 112-296 9.93e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.29  E-value: 9.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089   112 LLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHR-------HNNEITALKERLRKSQEK 184
Cdd:TIGR02168  231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkelyaLANEISRLEQQKQILRER 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089   185 ERATEKRVKETEGELFRTKFSLQKLKKISEARHlPERDDLAKKLVSAELKLDdterKIKELSKNLELSTNSFQRQLLAER 264
Cdd:TIGR02168  311 LANLERQLEELEAQLEELESKLDELAEELAELE-EKLEELKEELESLEAELE----ELEAELEELESRLEELEEQLETLR 385

                          170       180       190
                   ....*....|....*....|....*....|..
gi 261245089   265 KRAFEAYDENKVLQKELQRLHHKLKEKEKELD 296
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRE 417
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 111-301 2.04e-07

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 53.01  E-value: 2.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 111 RLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEK---------ALNKFEDAENEISQLIhrhnNEITALKERLRKS 181
Cdd:PRK05771  44 RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVksleelikdVEEELEKIEKEIKELE----EEISELENEIKEL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 182 QEKERATE--KRVKETEGELFRTKFSLQKLKKISE--ARHLPERDDLAKKLVSAELKLDDT------ERKIKELSKnlEL 251
Cdd:PRK05771 120 EQEIERLEpwGNFDLDLSLLLGFKYVSVFVGTVPEdkLEELKLESDVENVEYISTDKGYVYvvvvvlKELSDEVEE--EL 197

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 261245089 252 STNSFQRQLLAERKRAFEAY----DENKVLQKELQRLHHKLKEKEKEL--DIKNIY 301
Cdd:PRK05771 198 KKLGFERLELEEEGTPSELIreikEELEEIEKERESLLEELKELAKKYleELLALY 253
 
Name Accession Description Interval E-value
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 103-295 1.23e-67

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 213.23  E-value: 1.23e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089  103 VTKRVLSARLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQ 182
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089  183 EKERATEKRVKETEGELFRTKFSLQKLKKISEARHLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQLLA 262
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 261245089  263 ERKRAFEAYDENKVLQKELQRLHHKLKEKEKEL 295
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 107-319 8.12e-11

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: 63.24  E-value: 8.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 107 VLSARLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKER 186
Cdd:COG4942   14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 187 ATEKRVKETEGELFRTKFSLQKLKKISEARHLPERDDLAKKLVSAEL---KLDDTERKIKELSKNLELSTNSfQRQLLAE 263
Cdd:COG4942   94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYlkyLAPARREQAEELRADLAELAAL-RAELEAE 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 261245089 264 RKRAFEAYDENKVLQKELQRLhhkLKEKEKELdikniyaNRLPKSSPKKEKEIERK 319
Cdd:COG4942  173 RAELEALLAELEEERAALEAL---KAERQKLL-------ARLEKELAELAAELAEL 218
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 112-296 9.93e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.29  E-value: 9.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089   112 LLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHR-------HNNEITALKERLRKSQEK 184
Cdd:TIGR02168  231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkelyaLANEISRLEQQKQILRER 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089   185 ERATEKRVKETEGELFRTKFSLQKLKKISEARHlPERDDLAKKLVSAELKLDdterKIKELSKNLELSTNSFQRQLLAER 264
Cdd:TIGR02168  311 LANLERQLEELEAQLEELESKLDELAEELAELE-EKLEELKEELESLEAELE----ELEAELEELESRLEELEEQLETLR 385

                          170       180       190
                   ....*....|....*....|....*....|..
gi 261245089   265 KRAFEAYDENKVLQKELQRLHHKLKEKEKELD 296
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRE 417
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 111-301 2.04e-07

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 53.01  E-value: 2.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 111 RLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEK---------ALNKFEDAENEISQLIhrhnNEITALKERLRKS 181
Cdd:PRK05771  44 RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVksleelikdVEEELEKIEKEIKELE----EEISELENEIKEL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 182 QEKERATE--KRVKETEGELFRTKFSLQKLKKISE--ARHLPERDDLAKKLVSAELKLDDT------ERKIKELSKnlEL 251
Cdd:PRK05771 120 EQEIERLEpwGNFDLDLSLLLGFKYVSVFVGTVPEdkLEELKLESDVENVEYISTDKGYVYvvvvvlKELSDEVEE--EL 197

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 261245089 252 STNSFQRQLLAERKRAFEAY----DENKVLQKELQRLHHKLKEKEKEL--DIKNIY 301
Cdd:PRK05771 198 KKLGFERLELEEEGTPSELIreikEELEEIEKERESLLEELKELAKKYleELLALY 253
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 114-295 5.18e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 5.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 114 KINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALN----KFEDAENEISQLIhrhnNEITALKERLRKSQEKERATE 189
Cdd:COG1196  247 ELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaEEYELLAELARLE----QDIARLEERRRELEERLEELE 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 190 KRVKETEGELFRTKFSLQKLKKiSEARHLPERDDLAKKLVSAELKLDDTERKIKELSKNLElstnSFQRQLLAERKRAFE 269
Cdd:COG1196  323 EELAELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE----ELAEELLEALRAAAE 397

                        170       180
                 ....*....|....*....|....*.
gi 261245089 270 AYDENKVLQKELQRLHHKLKEKEKEL 295
Cdd:COG1196  398 LAAQLEELEEAEEALLERLERLEEEL 423
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
108-295 1.86e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.30  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089  108 LSARLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIH---RHNNEITALKERLRKSQEK 184
Cdd:COG4913   656 YSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGeigRLEKELEQAEEELDELQDR 735

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089  185 ERATEKRVKETEGELFRTKFSLQKLKKIsearhlpeRDDLAKKLVSaelKLDDTERKIKELSKNLELSTNSFQRQ---LL 261
Cdd:COG4913   736 LEAAEDLARLELRALLEERFAAALGDAV--------ERELRENLEE---RIDALRARLNRAEEELERAMRAFNREwpaET 804

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 261245089  262 AERKRAFEAYDEnkvLQKELQRL-HHKLKEKEKEL 295
Cdd:COG4913   805 ADLDADLESLPE---YLALLDRLeEDGLPEYEERF 836
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 114-295 2.42e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.44  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 114 KINELQNEVSELQVKLAQLLKEnkaLKSLQYRQEKALNKFEDAENEISQLihrhNNEITALKERLRKSQEKERATEKRVK 193
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAE---LDALQAELEELNEEYNELQAELEAL----QAEIDKLQAEIAEAEAEIEERREELG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 194 ETEGELFRTKFSLQKLKKISEARHLPE---RDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQLLAERKRAFEA 270
Cdd:COG3883   90 ERARALYRSGGSVSYLDVLLGSESFSDfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169

                        170       180
                 ....*....|....*....|....*
gi 261245089 271 YDENKVLQKELQRLHHKLKEKEKEL 295
Cdd:COG3883  170 KAELEAQQAEQEALLAQLSAEEAAA 194
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 113-295 4.90e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 4.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 113 LKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKERATEKRV 192
Cdd:COG1196  274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 193 KETEGELfrtKFSLQKLKKISEARHlpERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQLLAERKRAFEAYD 272
Cdd:COG1196  354 EEAEAEL---AEAEEALLEAEAELA--EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428

                        170       180
                 ....*....|....*....|...
gi 261245089 273 ENKVLQKELQRLHHKLKEKEKEL 295
Cdd:COG1196  429 ALAELEEEEEEEEEALEEAAEEE 451
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
111-290 2.18e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089  111 RLLKINELQNEVSELQVKLAQLlkenKALKSL--QYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKERAT 188
Cdd:COG4913   253 LLEPIRELAERYAAARERLAEL----EYLRAAlrLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089  189 EKRVKETEGElfrtkfSLQKLKK-ISEA-----RHLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQLLA 262
Cdd:COG4913   329 EAQIRGNGGD------RLEQLEReIERLereleERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA 402

                         170       180
                  ....*....|....*....|....*...
gi 261245089  263 ERKRAFEAYDENKVLQKELQRLHHKLKE 290
Cdd:COG4913   403 LEEALAEAEAALRDLRRELRELEAEIAS 430
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 114-318 4.10e-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: 45.82  E-value: 4.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089   114 KINELQNEVSELQVKLAQLlkeNKALKSLQYRQEKALNKFEDAEneisQLIHRHNNEITALKERLRKSQEKERATEKRVK 193
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAEL---EKALAELRKELEELEEELEQLR----KELEELSRQISALRKDLARLEAEVEQLEERIA 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089   194 ETEGELfrtkfslqklkkiseARHLPERDDLAKKLVSAELKLDDTERKIKElsknLELSTNSFQRQLLAERKRAFEAYDE 273
Cdd:TIGR02168  751 QLSKEL---------------TELEAEIEELEERLEEAEEELAEAEAEIEE----LEAQIEQLKEELKALREALDELRAE 811

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 261245089   274 NKVLQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIER 318
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 105-199 7.18e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 7.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 105 KRVLSARLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEK 184
Cdd:COG4942  142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221

                         90
                 ....*....|....*
gi 261245089 185 ERATEKRVKETEGEL 199
Cdd:COG4942  222 AEELEALIARLEAEA 236
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 115-305 1.02e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 44.72  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089   115 INELQNEVSELQVKLAQLLKENKALKS-LQYRQEKALNKFEDaenEISQLIHRHNNEITALKERLRKSQEKERATEKRVk 193
Cdd:pfam15921  226 LRELDTEISYLKGRIFPVEDQLEALKSeSQNKIELLLQQHQD---RIEQLISEHEVEITGLTEKASSARSQANSIQSQL- 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089   194 ETEGELFRTKFSLQklkkiseARHLPERDDLAKKLVSAELKLDDT-ERKIKELSKNLELSTNsfqrQLLAERKRAFEAYD 272
Cdd:pfam15921  302 EIIQEQARNQNSMY-------MRQLSDLESTVSQLRSELREAKRMyEDKIEELEKQLVLANS----ELTEARTERDQFSQ 370

                          170       180       190
                   ....*....|....*....|....*....|...
gi 261245089   273 ENKVLQKELQRLHHKLKEKEKELDIKNIYANRL 305
Cdd:pfam15921  371 ESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 115-315 1.18e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 115 INELQNEVSELQVKLAQLLKEnkaLKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKERATEKRVKE 194
Cdd:COG1196  325 LAELEEELEELEEELEELEEE---LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 195 TEGELFRTKFSLQKLkkiseARHLPERDDLAKKLVSAELKLDDTERKIKELSKNLElstNSFQRQLLAERKRAFEAYDEN 274
Cdd:COG1196  402 LEELEEAEEALLERL-----ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA---ELEEEEEALLELLAELLEEAA 473

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 261245089 275 KVLQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKE 315
Cdd:COG1196  474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
105-317 1.69e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 105 KRVLSARLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAEneisQLIHRHNNEITALKERLRKSQEK 184
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE----QLKELEEKLKKYNLEELEKKAEE 526

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 185 ERATEKRVKETEGELFRTKFSLQKLKkisearhlperdDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQL---L 261
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLE------------ELKKKLAELEKKLDELEEELAELLKELEELGFESVEELeerL 594

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 261245089 262 AERKRAFEAYDENKVLQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIE 317
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
120-296 3.12e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 3.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 120 NEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNnEITALKERLRKSQEKERATEKRVKETEGel 199
Cdd:COG4717   71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE-KLEKLLQLLPLYQELEALEAELAELPER-- 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 200 frtkfsLQKLKkiseaRHLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQLLAERKRAFEAYDEnkvLQK 279
Cdd:COG4717  148 ------LEELE-----ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE---LEE 213

                        170
                 ....*....|....*..
gi 261245089 280 ELQRLHHKLKEKEKELD 296
Cdd:COG4717  214 ELEEAQEELEELEEELE 230
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 86-249 3.98e-04

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 42.72  E-value: 3.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089   86 FRSQSLNREPLRKDPdiVTKRVLSARLLKINELQnevsELQvklaqLLKENKalKSLQYRQEKALNKFEDAENEISQLIH 165
Cdd:pfam10168 544 FREEYLKKHDLAREE--IQKRVKLLKLQKEQQLQ----ELQ-----SLEEER--KSLSERAEKLAEKYEEIKDKQEKLMR 610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089  166 RHNNEITALKERLRKSQEKERATEKRVKETEGELFRTKFSLQKLK-KISEARHLPERDDLAKKLVSAELKlDDTERKIKE 244
Cdd:pfam10168 611 RCKKVLQRLNSQLPVLSDAEREMKKELETINEQLKHLANAIKQAKkKMNYQRYQIAKSQSIRKKSSLSLS-EKQRKTIKE 689


                  ....*
gi 261245089  245 LSKNL 249
Cdd:pfam10168 690 ILKQL 694
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 110-296 6.98e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 6.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 110 ARLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEkerate 189
Cdd:COG1579    7 RALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE------ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 190 krvketegelfrtkfslqKLKKISEARhlpERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQ--RQLLAERKRA 267
Cdd:COG1579   81 ------------------QLGNVRNNK---EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAelEAELAELEAE 139

                        170       180       190
                 ....*....|....*....|....*....|....
gi 261245089 268 FEAY-----DENKVLQKELQRLHHKLKEKEKELD 296
Cdd:COG1579  140 LEEKkaeldEELAELEAELEELEAEREELAAKIP 173
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
115-318 7.91e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 7.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 115 INELQNEVSELQVKLAqllkenkalkslQYRQEkalNKFEDAENEISQLIhrhnNEITALKERLRKSQEKERATEKRVKE 194
Cdd:COG3206  184 LPELRKELEEAEAALE------------EFRQK---NGLVDLSEEAKLLL----QQLSELESQLAEARAELAEAEARLAA 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 195 TEGELFRTKFSLQKLKKISEARHLPER-DDLAKKLVSAELKLDDTERKIKELSKNLElstnSFQRQLLAERKRAFEAYD- 272
Cdd:COG3206  245 LRAQLGSGPDALPELLQSPVIQQLRAQlAELEAELAELSARYTPNHPDVIALRAQIA----ALRAQLQQEAQRILASLEa 320

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 261245089 273 ENKVLQKELQRLHHKLKEKEKELdikniyanrlpKSSPKKEKEIER 318
Cdd:COG3206  321 ELEALQAREASLQAQLAQLEARL-----------AELPELEAELRR 355
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 151-295 1.81e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 39.50  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089  151 NKFEDAENEISQLIHRHNNEITALKERLRKSQEKERATEKRVKETEGELFRTKFSLQKLKKISEA--RHLPERDDLAKKL 228
Cdd:pfam13851   8 KAFNEIKNYYNDITRNNLELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEElrKQLENYEKDKQSL 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261245089  229 VSAELKLDDTERKIKELSKNLELSTNSFQrQLLAERKRAFEAYDE------------NKVLQKELQRLHHKLKEKEKEL 295
Cdd:pfam13851  88 KNLKARLKVLEKELKDLKWEHEVLEQRFE-KVERERDELYDKFEAaiqdvqqktglkNLLLEKKLQALGETLEKKEAQL 165
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 114-295 2.08e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089   114 KINELQNEVSELQVKLAQLLKENKALKSLQYRQEKalnKFEDAENEISQLihrhNNEITALKERLRKSQEKERATEKRVK 193
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASR---KIGEIEKEIEQL----EQEEEKLKERLEELEEDLSSLEQEIE 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089   194 ETEGELFRTKFSLQ----KLKKISEARHLPER--------------DDLAKKLVSAELKLDDTERKIKELSKNLELSTNS 255
Cdd:TIGR02169  755 NVKSELKELEARIEeleeDLHKLEEALNDLEArlshsripeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 261245089   256 FQ-----RQLLAERKRAFEAYDENkvLQKELQRLHHKLKEKEKEL 295
Cdd:TIGR02169  835 IQelqeqRIDLKEQIKSIEKEIEN--LNGKKEELEEELEELEAAL 877
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
117-319 2.10e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 117 ELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQlihrHNNEITALKERLRKSQEKERATEKRVKETE 196
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELESLEGSKRKLEEKIRELE 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 197 GELFRTKFSLQKL-KKISEARHLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQL--------------- 260
Cdd:PRK03918 266 ERIEELKKEIEELeEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIkeleekeerleelkk 345

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261245089 261 --------LAERKRAFEAYDENKVLQKELQRLHHKLKEKEKEldikniYANRLPKSSPKKEKEIERK 319
Cdd:PRK03918 346 klkelekrLEELEERHELYEEAKAKKEELERLKKRLTGLTPE------KLEKELEELEKAKEEIEEE 406
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 114-295 3.17e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 3.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089   114 KINELQNEVSELQVKLAQLLKEnkaLKSLQYRQEKALNKFEDAENEISQLIHRHNNeitaLKERLRKSQEKERATEKRVK 193
Cdd:TIGR02169  834 EIQELQEQRIDLKEQIKSIEKE---IENLNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELERKIE 906

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089   194 ETEGELFRTKFSLQKLKKISEA--RHLPERDDLAKKLVS---AELKLDDTERKIKELSKNLelstnsfqRQLLAERKRAF 268
Cdd:TIGR02169  907 ELEAQIEKKRKRLSELKAKLEAleEELSEIEDPKGEDEEipeEELSLEDVQAELQRVEEEI--------RALEPVNMLAI 978

                          170       180
                   ....*....|....*....|....*..
gi 261245089   269 EAYDENKVLQKELQRLHHKLKEKEKEL 295
Cdd:TIGR02169  979 QEYEEVLKRLDELKEKRAKLEEERKAI 1005
PTZ00121 PTZ00121
MAEBL; Provisional
 110-319 3.36e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089  110 ARLLKINELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAEnEISQLIHRHNNEITALKERLRKSQEKERATE 189
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089  190 KRVKETEGELFRTKFSLQKLKKISEARHLPERD----DLAKKLVSAELKLDDTE------RKIKELSKNLELSTNSFQRQ 259
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDkkkaDELKKAAAAKKKADEAKkkaeekKKADEAKKKAEEAKKADEAK 1450

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089  260 LLAERKRAFEAYDENKVLQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIERK 319
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK 1510
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 114-328 3.55e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 39.64  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089  114 KINELQNEVSELQVKLAQLLK---ENKALKSLQyRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKERATEK 190
Cdd:PTZ00108 1103 KVEKLNAELEKKEKELEKLKNttpKDMWLEDLD-KFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKK 1181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089  191 RVKETEGELFRTKFSLQKLKKISEARHLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSfqrqllaerkrafEA 270
Cdd:PTZ00108 1182 KKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSK-------------KN 1248

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 261245089  271 YDENKVLQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIERKHVSCQSDFT 328
Cdd:PTZ00108 1249 NSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPT 1306
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
115-247 3.67e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 3.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 115 INELQNEVSELQVKLAQLlKENKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKERLRKSQEKER---ATEKR 191
Cdd:PRK03918 268 IEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEErleELKKK 346

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 261245089 192 VKETEGELFRTKFSLQKLKKISEArhLPERDDLAKKLvsAELKLDDTERKIKELSK 247
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAK--KEELERLKKRL--TGLTPEKLEKELEELEK 398
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
117-296 4.22e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 4.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 117 ELQNEVSELQVKLAQLLKENKALKSLQYRQEKALNKFEDAENEISQLIHRhnneitaLKERLRKSQEKeraTEKRVKETE 196
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE-------LEELGFESVEE---LEERLKELE 598

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 197 gELFRTKFSLQKLKKISEARhLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQllaERKRAFEAYDEnkv 276
Cdd:PRK03918 599 -PFYNEYLELKDAEKELERE-EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE---EYEELREEYLE--- 670

                        170       180
                 ....*....|....*....|
gi 261245089 277 LQKELQRLHHKLKEKEKELD 296
Cdd:PRK03918 671 LSRELAGLRAELEELEKRRE 690
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
114-267 4.43e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 4.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 114 KINELQNEVSELQVKLAQLLKENKALKSLQyrqekalnKFEDAENEISQLIHRHNNEITALKERLRKSQEKERAtEKRVK 193
Cdd:COG4717  103 ELEELEAELEELREELEKLEKLLQLLPLYQ--------ELEALEAELAELPERLEELEERLEELRELEEELEEL-EAELA 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261245089 194 ETEGELFR--TKFSLQKLKKISEArhLPERDDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQLLAERKRA 267
Cdd:COG4717  174 ELQEELEEllEQLSLATEEELQDL--AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
122-296 7.26e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 7.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 122 VSELQVKLAQLLKENKALKSLQyrqekaLNKFEDAENEISQLIHRHnNEITALKERLRKSQEKERATEKRVKETEGELFR 201
Cdd:COG4717   48 LERLEKEADELFKPQGRKPELN------LKELKELEEELKEAEEKE-EEYAELQEELEELEEELEELEAELEELREELEK 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089 202 TKFSLQKLKKISEARHLPER----DDLAKKLVSAELKLDDTERKIKELSKNLELSTNSFQRQL----LAERKRAFEAYDE 273
Cdd:COG4717  121 LEKLLQLLPLYQELEALEAElaelPERLEELEERLEELRELEEELEELEAELAELQEELEELLeqlsLATEEELQDLAEE 200

                        170       180
                 ....*....|....*....|...
gi 261245089 274 NKVLQKELQRLHHKLKEKEKELD 296
Cdd:COG4717  201 LEELQQRLAELEEELEEAQEELE 223
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 114-318 8.61e-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: 38.46  E-value: 8.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089  114 KINELQNEVSELQVKLAQLlkeNKALKSLQYRQEKALNKFEDAENEISQLIHRHNNEITALKErlrKSQEKERaTEKRVK 193
Cdd:TIGR04523 212 KNKSLESQISELKKQNNQL---KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSE---KQKELEQ-NNKKIK 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261245089  194 ETEGELFRTKFSLQKLKKISEARHLP----ERDDLAKKLVSAELKLDDTERKIKEL----------SKNLELSTNSFQRQ 259
Cdd:TIGR04523 285 ELEKQLNQLKSEISDLNNQKEQDWNKelksELKNQEKKLEEIQNQISQNNKIISQLneqisqlkkeLTNSESENSEKQRE 364

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261245089  260 L------LAERKRAFEAY-DENKVLQKELQRLHHKLKEKEKELDIKNIYANRLPKSSPKKEKEIER 318
Cdd:TIGR04523 365 LeekqneIEKLKKENQSYkQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH