NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568997598|ref|XP_006523125|]
View 

lebercilin-like protein isoform X2 [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 ...
 139-331 1.15e-74

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: 239.42  E-value: 1.15e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598  139 MTHRILSARLHKIKELKNELADVHRKLEASAIENQFLKQLQLRHLKAIGKYVNSQNNLPQITAKHQNEVKNLRQLLRKSQ 218
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598  219 EKERAVSRKLRETDGELLRTKDVLQALQRLSEDKNLAEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNRSYSRQLAK 298
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 568997598  299 ENRKTLAAQTATKTLQAEVRQLQQKLKEKDREL 331
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 ...
 139-331 1.15e-74

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: 239.42  E-value: 1.15e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598  139 MTHRILSARLHKIKELKNELADVHRKLEASAIENQFLKQLQLRHLKAIGKYVNSQNNLPQITAKHQNEVKNLRQLLRKSQ 218
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598  219 EKERAVSRKLRETDGELLRTKDVLQALQRLSEDKNLAEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNRSYSRQLAK 298
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 568997598  299 ENRKTLAAQTATKTLQAEVRQLQQKLKEKDREL 331
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 128-332 8.03e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 8.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 128 QIQTIAKRRDtmthriLSARLHKIKELKNELADVHRKLEASAIENQfLKQLQLRHLKAigkyvnsqnnlpQITAKHQnEV 207
Cdd:COG1196  217 ELKEELKELE------AELLLLKLRELEAELEELEAELEELEAELE-ELEAELAELEA------------ELEELRL-EL 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 208 KNLRQLLRKSQEKERAVSRKLRETDGEL----LRTKDVLQALQRLSEDKNL---------AEREELTDRLTDLTAKMEAN 274
Cdd:COG1196  277 EELELELEEAQAEEYELLAELARLEQDIarleERRRELEERLEELEEELAEleeeleeleEELEELEEELEEAEEELEEA 356

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568997598 275 DKKIQNLEKQLRLNNRSYSRQLAKENRKTLAAQTATKTLQAEVRQLQQKLKEKDRELE 332
Cdd:COG1196  357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 151-332 4.83e-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: 46.97  E-value: 4.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598   151 IKELKNELADVHRKLEAsAIENQFLKQlQLRHLKaIGKYVNSQNNLpqitakhQNEVKNLRQLLRKSQEKERAVSRKLRE 230
Cdd:TIGR02168  195 LNELERQLKSLERQAEK-AERYKELKA-ELRELE-LALLVLRLEEL-------REELEELQEELKEAEEELEELTAELQE 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598   231 TDGELLRTKDvlqALQRLSEDKNLAERE--ELTDRLTDLTAKMEANDKKIQNLEKQLRlnnrSYSRQLAKENRKTLAAQT 308
Cdd:TIGR02168  265 LEEKLEELRL---EVSELEEEIEELQKElyALANEISRLEQQKQILRERLANLERQLE----ELEAQLEELESKLDELAE 337

                          170       180
                   ....*....|....*....|....
gi 568997598   309 ATKTLQAEVRQLQQKLKEKDRELE 332
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELE 361
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 209-351 2.92e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.43  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 209 NLRQLLRKSQEKERAVSRKLRETDGELLRTKDVLQALQRLSEdKNLAEREELTDRLTD-----LTAKMEANDKKIQNLEK 283
Cdd:PRK00409 517 KLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKE-KLQEEEDKLLEEAEKeaqqaIKEAKKEADEIIKELRQ 595

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 284 QLRLNNRSYSRQLAKENRKTL--AAQTATKTLQAEVRQlQQKLKEKDReLEIKNIYTNRILKNLNDKEDY 351
Cdd:PRK00409 596 LQKGGYASVKAHELIEARKRLnkANEKKEKKKKKQKEK-QEELKVGDE-VKYLSLGQKGEVLSIPDDKEA 663
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 196-323 4.68e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 39.62  E-value: 4.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598   196 LPQITAKHQNEVKNLRQLLRKSQEKERAVSRKLRETDGELLRTKDVLQALQRLSEDKNLaEREELTDRLTDLTAKMEAND 275
Cdd:smart00787 174 KPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEE-ELQELESKIEDLTNKKSELN 252

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 568997598   276 KKIQNLEKQlRLNNRSYSRqlaKENRKtlaaqtatktLQAEVRQLQQK 323
Cdd:smart00787 253 TEIAEAEKK-LEQCRGFTF---KEIEK----------LKEQLKLLQSL 286
 
Name Accession Description Interval E-value
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 139-331 1.15e-74

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: 239.42  E-value: 1.15e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598  139 MTHRILSARLHKIKELKNELADVHRKLEASAIENQFLKQLQLRHLKAIGKYVNSQNNLPQITAKHQNEVKNLRQLLRKSQ 218
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598  219 EKERAVSRKLRETDGELLRTKDVLQALQRLSEDKNLAEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNRSYSRQLAK 298
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 568997598  299 ENRKTLAAQTATKTLQAEVRQLQQKLKEKDREL 331
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 128-332 8.03e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 8.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 128 QIQTIAKRRDtmthriLSARLHKIKELKNELADVHRKLEASAIENQfLKQLQLRHLKAigkyvnsqnnlpQITAKHQnEV 207
Cdd:COG1196  217 ELKEELKELE------AELLLLKLRELEAELEELEAELEELEAELE-ELEAELAELEA------------ELEELRL-EL 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 208 KNLRQLLRKSQEKERAVSRKLRETDGEL----LRTKDVLQALQRLSEDKNL---------AEREELTDRLTDLTAKMEAN 274
Cdd:COG1196  277 EELELELEEAQAEEYELLAELARLEQDIarleERRRELEERLEELEEELAEleeeleeleEELEELEEELEEAEEELEEA 356

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568997598 275 DKKIQNLEKQLRLNNRSYSRQLAKENRKTLAAQTATKTLQAEVRQLQQKLKEKDRELE 332
Cdd:COG1196  357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
151-326 1.79e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.56  E-value: 1.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 151 IKELKNELADVHRKLEASaiENQfLKQLQLRHlkaigKYVNSQNNLPQITAK---HQNEVKNLRQLLRKSQEKERAVSRK 227
Cdd:COG3206  177 LEFLEEQLPELRKELEEA--EAA-LEEFRQKN-----GLVDLSEEAKLLLQQlseLESQLAEARAELAEAEARLAALRAQ 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 228 LRETDG---ELLRTKDVLQALQRLSEDKnlAEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNRSYSRQLAKENRktl 304
Cdd:COG3206  249 LGSGPDalpELLQSPVIQQLRAQLAELE--AELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELE--- 323

                        170       180
                 ....*....|....*....|..
gi 568997598 305 AAQTATKTLQAEVRQLQQKLKE 326
Cdd:COG3206  324 ALQAREASLQAQLAQLEARLAE 345
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
151-332 3.07e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 3.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 151 IKELKNELADVHRKLEASAIEN-QFLKQL--QLRHLKAI-GKYVNSQNNLPQITAKH---QNEVKNLRQLLRKSQEKERA 223
Cdd:COG4717   48 LERLEKEADELFKPQGRKPELNlKELKELeeELKEAEEKeEEYAELQEELEELEEELeelEAELEELREELEKLEKLLQL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 224 VS--RKLRETDGELLRTKDVLQALQRlsedkNLAEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNRSYSRQLAKENR 301
Cdd:COG4717  128 LPlyQELEALEAELAELPERLEELEE-----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568997598 302 KtlaAQTATKTLQAEVRQLQQKLKEKDRELE 332
Cdd:COG4717  203 E---LQQRLAELEEELEEAQEELEELEEELE 230
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 151-332 4.83e-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: 46.97  E-value: 4.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598   151 IKELKNELADVHRKLEAsAIENQFLKQlQLRHLKaIGKYVNSQNNLpqitakhQNEVKNLRQLLRKSQEKERAVSRKLRE 230
Cdd:TIGR02168  195 LNELERQLKSLERQAEK-AERYKELKA-ELRELE-LALLVLRLEEL-------REELEELQEELKEAEEELEELTAELQE 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598   231 TDGELLRTKDvlqALQRLSEDKNLAERE--ELTDRLTDLTAKMEANDKKIQNLEKQLRlnnrSYSRQLAKENRKTLAAQT 308
Cdd:TIGR02168  265 LEEKLEELRL---EVSELEEEIEELQKElyALANEISRLEQQKQILRERLANLERQLE----ELEAQLEELESKLDELAE 337

                          170       180
                   ....*....|....*....|....
gi 568997598   309 ATKTLQAEVRQLQQKLKEKDRELE 332
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELE 361
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 204-348 8.25e-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: 46.20  E-value: 8.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598   204 QNEVKNLRQLLRKSQEKERAVSRKLRETDGELLRTKDVLQALQRLSEDKN--LAEREELTDRLTD----LTAKMEANDKK 277
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqISALRKDLARLEAeveqLEERIAQLSKE 755

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568997598   278 IQNLEKQLrlnnRSYSRQLAKENRKTLAAQTATKTLQAEVRQLQQKLKEKDRELEIKniytNRILKNLNDK 348
Cdd:TIGR02168  756 LTELEAEI----EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEE 818
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
140-332 2.33e-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: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598  140 THRILSARLHKIKELKnELADVHRKLEASAIENQFLKQLQ--LRHLKAIGKYVNSQNNLPQIT---AKHQNEVKNLRQLL 214
Cdd:COG4913   240 AHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRaaLRLWFAQRRLELLEAELEELRaelARLEAELERLEARL 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598  215 RKSQEKERAVSRKLRETDGellrtkDVLQALQRLSEDKNlAEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNRSYSR 294
Cdd:COG4913   319 DALREELDELEAQIRGNGG------DRLEQLEREIERLE-RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568997598  295 QLAKENRKTLAAQTATKTLQAEVRQLQQKLKEKDRELE 332
Cdd:COG4913   392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 144-332 2.58e-04

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: 43.98  E-value: 2.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 144 LSARLHKIKELKNELADVHRKLEAsaiENQFLKQLQLRHLKAIGKYVNSQNNLPQITAK---HQNEVKNLRQLLRKSQEK 220
Cdd:COG4942   15 AAAQADAAAEAEAELEQLQQEIAE---LEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 221 ERAVSRKLRETDGE-------------------LLRTKDVLQALQRLS-------EDKNLAE-----REELTDRLTDLTA 269
Cdd:COG4942   92 IAELRAELEAQKEElaellralyrlgrqpplalLLSPEDFLDAVRRLQylkylapARREQAEelradLAELAALRAELEA 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568997598 270 KMEANDKKIQNLEKQLRLNNRSYSRQ---LAKENRKTLAAQTATKTLQAEVRQLQQKLKEKDRELE 332
Cdd:COG4942  172 ERAELEALLAELEEERAALEALKAERqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 81-326 2.72e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 2.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598    81 RRLQSEKPLAKAKEKRKYNAGKLPQPRGQKDIPAEKKQFWNASLISSQIQTIAKRRdtmTHRILSARLHKIKE----LKN 156
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE---ALDELRAELTLLNEeaanLRE 824

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598   157 ELADVHRKLEASAIENQFLKQLQLRHLKAIGKYVNSQNNLPQITAKHQNEVKNLRQLLRKSQEKERAVSRKLRETDGELL 236
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598   237 RTKDVLQALQRlsedknlaEREELTDRLTDLTAKMEANDKKIQNLEKQLrlnNRSYSRQLAKENRKTLAAQTATKTLQAE 316
Cdd:TIGR02168  905 ELESKRSELRR--------ELEELREKLAQLELRLEGLEVRIDNLQERL---SEEYSLTLEEAEALENKIEDDEEEARRR 973

                          250
                   ....*....|
gi 568997598   317 VRQLQQKLKE 326
Cdd:TIGR02168  974 LKRLENKIKE 983
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 220-335 2.88e-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: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 220 KERAVsRKLRETDGELLRTKDVLQALQR----LSEDKNLAER-EELTDRLTDLTAKMEANdkKIQNLEKQLRLnnrsYSR 294
Cdd:COG1196  174 KEEAE-RKLEATEENLERLEDILGELERqlepLERQAEKAERyRELKEELKELEAELLLL--KLRELEAELEE----LEA 246

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568997598 295 QLAKENRKTLAAQTATKTLQAEVRQLQQKLKEKDRELEIKN 335
Cdd:COG1196  247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 209-351 2.92e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.43  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 209 NLRQLLRKSQEKERAVSRKLRETDGELLRTKDVLQALQRLSEdKNLAEREELTDRLTD-----LTAKMEANDKKIQNLEK 283
Cdd:PRK00409 517 KLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKE-KLQEEEDKLLEEAEKeaqqaIKEAKKEADEIIKELRQ 595

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 284 QLRLNNRSYSRQLAKENRKTL--AAQTATKTLQAEVRQlQQKLKEKDReLEIKNIYTNRILKNLNDKEDY 351
Cdd:PRK00409 596 LQKGGYASVKAHELIEARKRLnkANEKKEKKKKKQKEK-QEELKVGDE-VKYLSLGQKGEVLSIPDDKEA 663
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 123-373 3.22e-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: 44.29  E-value: 3.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598   123 SLISSQIQTIAKRRDTMTHRILSARlHKIKELKNELADVHRKLEASAIEnqfLKQLQLrhlkAIGKYVNSQNNLPQITAK 202
Cdd:TIGR02169  719 GEIEKEIEQLEQEEEKLKERLEELE-EDLSSLEQEIENVKSELKELEAR---IEELEE----DLHKLEEALNDLEARLSH 790

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598   203 HQneVKNLRQLLRKSQEKERAVSRKLRETDGELLRTKDVLQALQRLSEDK-------------NLAEREELTDRLTDLTA 269
Cdd:TIGR02169  791 SR--IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELqeqridlkeqiksIEKEIENLNGKKEELEE 868

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598   270 KMEANDKKIQNLEKQLRlNNRSYSRQLAKENRktlAAQTATKTLQAEVRQLQQKLKEKDRELEIKNIYTNRILKNLN-DK 348
Cdd:TIGR02169  869 ELEELEAALRDLESRLG-DLKKERDELEAQLR---ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGeDE 944

                          250       260       270
                   ....*....|....*....|....*....|..
gi 568997598   349 EDYPKVSSTKSVQADRK-------SLPSVNMR 373
Cdd:TIGR02169  945 EIPEEELSLEDVQAELQrveeeirALEPVNML 976
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 115-376 5.52e-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: 43.57  E-value: 5.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598   115 EKKQFW-NASLISSQ--IQTIAKRRDTMTHrILSARLHKIKELKNELADVHRKLEA-----------SAIENQFLKQLQL 180
Cdd:pfam15921  102 EKQKFYlRQSVIDLQtkLQEMQMERDAMAD-IRRRESQSQEDLRNQLQNTVHELEAakclkedmledSNTQIEQLRKMML 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598   181 RHLKAIGKYVNSQNNLPQITAKHQNEVKNLRQLLRKSQEKerAVSRKLRETD-------GELLRTKDVLQALQRLSEDKN 253
Cdd:pfam15921  181 SHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGS--AISKILRELDteisylkGRIFPVEDQLEALKSESQNKI 258

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598   254 LAEREELTDRLTDL----------------TAKMEAND--KKIQNLEKQLRLNNRSYSRQLAKenrktlaAQTATKTLQA 315
Cdd:pfam15921  259 ELLLQQHQDRIEQLiseheveitgltekasSARSQANSiqSQLEIIQEQARNQNSMYMRQLSD-------LESTVSQLRS 331

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568997598   316 EVRQLQQKLKEKDRELEIKNIYTNRILKNLNDKEDYPKVSSTKSVQADRKSLPSVNMRHQE 376
Cdd:pfam15921  332 ELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKE 392
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
207-332 8.35e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 8.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598  207 VKNLRQLLRKSQEKERAVSRKLRETDGELLRTKDVLQALQRLSE----DKNLA----EREELTDRLTDLtakmEANDKKI 278
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdEIDVAsaerEIAELEAELERL----DASSDDL 687

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568997598  279 QNLEKQLRLNNRSYsRQLAKENRktlAAQTATKTLQAEVRQLQQKLKEKDRELE 332
Cdd:COG4913   688 AALEEQLEELEAEL-EELEEELD---ELKGEIGRLEKELEQAEEELDELQDRLE 737
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 150-335 9.24e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 9.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598   150 KIKELKNELADVHRKLEASAIEnqfLKQLQLRHLKAIGKYVNSQNNLPQITAK---HQNEVKNLRQLLRKSQEKERAVSR 226
Cdd:TIGR02168  240 ELEELQEELKEAEEELEELTAE---LQELEEKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILRERLANLER 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598   227 KLRETDGELLRTKdvlQALQRLSEDKNL--AEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNRSYSRQLAKENRKTL 304
Cdd:TIGR02168  317 QLEELEAQLEELE---SKLDELAEELAEleEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393

                          170       180       190
                   ....*....|....*....|....*....|.
gi 568997598   305 AAQTATKTLQAEVRQLQQKLKEKDRELEIKN 335
Cdd:TIGR02168  394 QIASLNNEIERLEARLERLEDRRERLQQEIE 424
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 115-348 1.94e-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: 41.54  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598  115 EKKQFWNASLiSSQIQTIAKRRDTMTHRIlSARLHKIKELKNELADVHRKLEASAIENQFLKQLQLRHLKAIGKYVNSQN 194
Cdd:TIGR04523 303 QKEQDWNKEL-KSELKNQEKKLEEIQNQI-SQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ 380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598  195 NLPQITAKHQNEVKNLRQLLRKSQEKERAVSRKLR--ETDGELLrtkdvLQALQRLSED--KNLAEREELTDRLTDLTAK 270
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKklQQEKELL-----EKEIERLKETiiKNNSEIKDLTNQDSVKELI 455

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598  271 MEANDKKIQNLEKQLRLNNRSYS--RQLAKENRKTLAAQTAT-KTLQAEVRQLQQK----------LKEKDRELEIKNIY 337
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINkiKQNLEQKQKELKSKEKElKKLNEEKKELEEKvkdltkkissLKEKIEKLESEKKE 535

                         250
                  ....*....|.
gi 568997598  338 TNRILKNLNDK 348
Cdd:TIGR04523 536 KESKISDLEDE 546
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 149-330 2.46e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598   149 HKIKELKNELADVHRKLEASAIENQFLKQLQLRHLKAIGKYVNSQNNLPQITAKHQNEVKNLRQLLRKSQEKERAVSRKL 228
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598   229 RETDGELLRTKDVLQALQ------RLSEDKNLAEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNrsySRQLAKENRK 302
Cdd:TIGR02168  333 DELAEELAELEEKLEELKeeleslEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN---NEIERLEARL 409

                          170       180
                   ....*....|....*....|....*...
gi 568997598   303 TLAAQTATKtLQAEVRQLQQKLKEKDRE 330
Cdd:TIGR02168  410 ERLEDRRER-LQQEIEELLKKLEEAELK 436
PRK01156 PRK01156
chromosome segregation protein; Provisional
 144-335 2.49e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.43  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 144 LSARLHKIKELKNELADVHRKLEASAIENQFLKQLQLRHLKAIGKYVNSQNNLPQITAKHQNEVKNLRQLLR--KSQ-EK 220
Cdd:PRK01156 244 LSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSniDAEiNK 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 221 ERAVSRKLRETDGEllrTKDVLQALQRLSE-DKNLAEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNRSYSRQLAKE 299
Cdd:PRK01156 324 YHAIIKKLSVLQKD---YNDYIKKKSRYDDlNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQ 400

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568997598 300 --------------NRKTLAAQTATKTLQAEVRQLQQKLKEKDRELEIKN 335
Cdd:PRK01156 401 eidpdaikkelneiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLN 450
46 PHA02562
endonuclease subunit; Provisional
 150-345 2.91e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.77  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 150 KIKELKNELADVhrKLEASAIENQflkqlqlrhLKAIGKYVNSQNNLP-QITAKHQNEVKNLRQLLR--KSQEKERavSR 226
Cdd:PHA02562 175 KIRELNQQIQTL--DMKIDHIQQQ---------IKTYNKNIEEQRKKNgENIARKQNKYDELVEEAKtiKAEIEEL--TD 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 227 KLRETDGELLRTKDVLQAL-------------------------------QRLSEDKNLAEreELTDRLTDLTAKMEAND 275
Cdd:PHA02562 242 ELLNLVMDIEDPSAALNKLntaaakikskieqfqkvikmyekggvcptctQQISEGPDRIT--KIKDKLKELQHSLEKLD 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 276 KKIQNLEKQ----------LRLNNRSYS---RQLAKENRKTLAAQTATKTLQA-------EVRQLQQKLKEKDRELE--I 333
Cdd:PHA02562 320 TAIDELEEImdefneqskkLLELKNKIStnkQSLITLVDKAKKVKAAIEELQAefvdnaeELAKLQDELDKIVKTKSelV 399

                        250
                 ....*....|..
gi 568997598 334 KNIYTNRILKNL 345
Cdd:PHA02562 400 KEKYHRGIVTDL 411
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 113-326 4.24e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.52  E-value: 4.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 113 PAEKKQFWNASLISSQIQTIAKRRDTMTHRIlsarlhkiKELKNELADVHRKLEASAIEnqfLKQLQLRHlkaigkyvns 192
Cdd:COG1579    3 PEDLRALLDLQELDSELDRLEHRLKELPAEL--------AELEDELAALEARLEAAKTE---LEDLEKEI---------- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 193 qnnlpqitAKHQNEVKNLRQLLRKSQEKERAVsRKLREtdgellrtkdvLQALQRlSEDKNLAEREELTDRLTDLTAKME 272
Cdd:COG1579   62 --------KRLELEIEEVEARIKKYEEQLGNV-RNNKE-----------YEALQK-EIESLKRRISDLEDEILELMERIE 120

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568997598 273 ANDKKIQNLEKQLrlnnrsySRQLAKENRKTLAAQTATKTLQAEVRQLQQKLKE 326
Cdd:COG1579  121 ELEEELAELEAEL-------AELEAELEEKKAELDEELAELEAELEELEAEREE 167
TMCO5 pfam14992
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing ...
 213-333 4.51e-03

TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing proteins 5A and 5B.


Pssm-ID: 464427 [Multi-domain]  Cd Length: 278  Bit Score: 39.70  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598  213 LLRKSQEKERAVSRklreTDGELLRTKDVLQALQRLSEDKNLAEREELTDRLTDLTAKMEAND----KKIQNLEKQLrln 288
Cdd:pfam14992  22 LLLKIQEKEEEIQS----LEREITLTRSLAEDEEREELNFTIMEKEDALQELELETAKLEKKNeilvKSVMELQRKL--- 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568997598  289 nrsySRqlaKENRKTLAAQTATKTLQAEVRQLQQKLKEK--DRELEI 333
Cdd:pfam14992  95 ----SR---KSDKNTGLEQETLKQMLEELKVKLQQSEEScaDQEKEL 134
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 196-323 4.68e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 39.62  E-value: 4.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598   196 LPQITAKHQNEVKNLRQLLRKSQEKERAVSRKLRETDGELLRTKDVLQALQRLSEDKNLaEREELTDRLTDLTAKMEAND 275
Cdd:smart00787 174 KPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEE-ELQELESKIEDLTNKKSELN 252

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 568997598   276 KKIQNLEKQlRLNNRSYSRqlaKENRKtlaaqtatktLQAEVRQLQQK 323
Cdd:smart00787 253 TEIAEAEKK-LEQCRGFTF---KEIEK----------LKEQLKLLQSL 286
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 219-332 6.12e-03

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 39.24  E-value: 6.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598  219 EKERAVSRKLRETDGELLRTK----DVLQALQRLSEDKNLAEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNRSYSR 294
Cdd:pfam04849 142 ETESSCSTPLRRNESFSSLHGcvqlDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAE 221

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 568997598  295 ---QLAKENRKTLAAQTATKTLQAEVRQLQQKLKEKDRELE 332
Cdd:pfam04849 222 lseELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENE 262
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
142-327 8.19e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 8.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 142 RILSARLHKIKELKNELADVHRKLEASAIENQFLKQLQLRHLKAIGKYVNSQNNLPQITAKhQNEVKNLRQLLRksqEKE 221
Cdd:COG4717  340 LELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQEL-KEELEELEEQLE---ELL 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 222 RAVSRKLRETDGELLRTKdvlqaLQRLSEdknlaEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNRSYSRQLAKENR 301
Cdd:COG4717  416 GELEELLEALDEEELEEE-----LEELEE-----ELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAEL 485

                        170       180
                 ....*....|....*....|....*..
gi 568997598 302 KTLAAQ-TATKTLQAEVRQLQQKLKEK 327
Cdd:COG4717  486 RELAEEwAALKLALELLEEAREEYREE 512
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
143-332 8.33e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 8.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 143 ILSARLHKIKELKNELADVHRKLEASAIENqfLKQLQLRHLKAigKYVNSQNNLPQITAKHQNEVKNLRQLLRKSQEKER 222
Cdd:COG4717  286 LALLFLLLAREKASLGKEAEELQALPALEE--LEEEELEELLA--ALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 223 AvsrklretdgelLRTKDVLQALQRLSEDKNLAEREELTDRLTDLTAKMEANdKKIQNLEKQLRLNNRSYSRQLAKENRK 302
Cdd:COG4717  362 E------------LQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELK-EELEELEEQLEELLGELEELLEALDEE 428

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568997598 303 TLAA-----QTATKTLQAEVRQLQQKLKEKDRELE 332
Cdd:COG4717  429 ELEEeleelEEELEELEEELEELREELAELEAELE 463
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
97-305 9.31e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 9.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598  97 KYNAGKLPQPRGQKDIPaekkqfwNASLISSQIQTIAKRRDTmtHRILSARLHKIKELKNELADVHRKLEASAIENQFLK 176
Cdd:COG4717   52 EKEADELFKPQGRKPEL-------NLKELKELEEELKEAEEK--EEEYAELQEELEELEEELEELEAELEELREELEKLE 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997598 177 QLqLRHLKAIGKYVNSQNNLPQITAKHQNEVKNLRQLLRKSQEKERAvSRKLRETDGELLRTKDVLQALQRLSEDKNLAE 256
Cdd:COG4717  123 KL-LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEEL-EAELAELQEELEELLEQLSLATEEELQDLAEE 200

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568997598 257 REELTDRLTDLTAKMEANDKKIQNLEKQL-RLNNRSYSRQLAKENRKTLA 305
Cdd:COG4717  201 LEELQQRLAELEEELEEAQEELEELEEELeQLENELEAAALEERLKEARL 250
 
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