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Conserved domains on  [gi|124517724|ref|NP_001001492|]
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lebercilin-like protein isoform 1 [Mus musculus]

Protein Classification

Lebercilin domain-containing protein( domain architecture ID 12174059)

Lebercilin domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 144-336 8.42e-75

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: 239.80  E-value: 8.42e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724  144 MTHRILSARLHKIKELKNELADVHRKLEASAIENQFLKQLQLRHLKAIGKYVNSQNNLPQITAKHQNEVKNLRQLLRKSQ 223
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724  224 EKERAVSRKLRETDGELLRTKDVLQALQRLSEDKNLAEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNRSYSRQLAK 303
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 124517724  304 ENRKTLAAQTATKTLQAEVRQLQQKLKEKDREL 336
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 ...
 144-336 8.42e-75

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: 239.80  E-value: 8.42e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724  144 MTHRILSARLHKIKELKNELADVHRKLEASAIENQFLKQLQLRHLKAIGKYVNSQNNLPQITAKHQNEVKNLRQLLRKSQ 223
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724  224 EKERAVSRKLRETDGELLRTKDVLQALQRLSEDKNLAEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNRSYSRQLAK 303
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 124517724  304 ENRKTLAAQTATKTLQAEVRQLQQKLKEKDREL 336
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 133-337 7.32e-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: 7.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 133 QIQTIAKRRDtmthriLSARLHKIKELKNELADVHRKLEASAIENQfLKQLQLRHLKAigkyvnsqnnlpQITAKHQnEV 212
Cdd:COG1196  217 ELKEELKELE------AELLLLKLRELEAELEELEAELEELEAELE-ELEAELAELEA------------ELEELRL-EL 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 213 KNLRQLLRKSQEKERAVSRKLRETDGEL----LRTKDVLQALQRLSEDKNL---------AEREELTDRLTDLTAKMEAN 279
Cdd:COG1196  277 EELELELEEAQAEEYELLAELARLEQDIarleERRRELEERLEELEEELAEleeeleeleEELEELEEELEEAEEELEEA 356

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 124517724 280 DKKIQNLEKQLRLNNRSYSRQLAKENRKTLAAQTATKTLQAEVRQLQQKLKEKDRELE 337
Cdd:COG1196  357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 156-337 4.29e-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: 4.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724   156 IKELKNELADVHRKLEAsAIENQFLKQlQLRHLKaIGKYVNSQNNLpqitakhQNEVKNLRQLLRKSQEKERAVSRKLRE 235
Cdd:TIGR02168  195 LNELERQLKSLERQAEK-AERYKELKA-ELRELE-LALLVLRLEEL-------REELEELQEELKEAEEELEELTAELQE 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724   236 TDGELLRTKDvlqALQRLSEDKNLAERE--ELTDRLTDLTAKMEANDKKIQNLEKQLRlnnrSYSRQLAKENRKTLAAQT 313
Cdd:TIGR02168  265 LEEKLEELRL---EVSELEEEIEELQKElyALANEISRLEQQKQILRERLANLERQLE----ELEAQLEELESKLDELAE 337

                          170       180
                   ....*....|....*....|....
gi 124517724   314 ATKTLQAEVRQLQQKLKEKDRELE 337
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELE 361
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 214-356 2.80e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.43  E-value: 2.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 214 NLRQLLRKSQEKERAVSRKLRETDGELLRTKDVLQALQRLSEdKNLAEREELTDRLTD-----LTAKMEANDKKIQNLEK 288
Cdd:PRK00409 517 KLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKE-KLQEEEDKLLEEAEKeaqqaIKEAKKEADEIIKELRQ 595

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 289 QLRLNNRSYSRQLAKENRKTL--AAQTATKTLQAEVRQlQQKLKEKDReLEIKNIYTNRILKNLNDKEDY 356
Cdd:PRK00409 596 LQKGGYASVKAHELIEARKRLnkANEKKEKKKKKQKEK-QEELKVGDE-VKYLSLGQKGEVLSIPDDKEA 663
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 201-328 4.40e-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: 40.00  E-value: 4.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724   201 LPQITAKHQNEVKNLRQLLRKSQEKERAVSRKLRETDGELLRTKDVLQALQRLSEDKNLaEREELTDRLTDLTAKMEAND 280
Cdd:smart00787 174 KPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEE-ELQELESKIEDLTNKKSELN 252

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 124517724   281 KKIQNLEKQlRLNNRSYSRqlaKENRKtlaaqtatktLQAEVRQLQQK 328
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 ...
 144-336 8.42e-75

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: 239.80  E-value: 8.42e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724  144 MTHRILSARLHKIKELKNELADVHRKLEASAIENQFLKQLQLRHLKAIGKYVNSQNNLPQITAKHQNEVKNLRQLLRKSQ 223
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724  224 EKERAVSRKLRETDGELLRTKDVLQALQRLSEDKNLAEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNRSYSRQLAK 303
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 124517724  304 ENRKTLAAQTATKTLQAEVRQLQQKLKEKDREL 336
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 133-337 7.32e-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: 7.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 133 QIQTIAKRRDtmthriLSARLHKIKELKNELADVHRKLEASAIENQfLKQLQLRHLKAigkyvnsqnnlpQITAKHQnEV 212
Cdd:COG1196  217 ELKEELKELE------AELLLLKLRELEAELEELEAELEELEAELE-ELEAELAELEA------------ELEELRL-EL 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 213 KNLRQLLRKSQEKERAVSRKLRETDGEL----LRTKDVLQALQRLSEDKNL---------AEREELTDRLTDLTAKMEAN 279
Cdd:COG1196  277 EELELELEEAQAEEYELLAELARLEQDIarleERRRELEERLEELEEELAEleeeleeleEELEELEEELEEAEEELEEA 356

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 124517724 280 DKKIQNLEKQLRLNNRSYSRQLAKENRKTLAAQTATKTLQAEVRQLQQKLKEKDRELE 337
Cdd:COG1196  357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
156-331 1.63e-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: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 156 IKELKNELADVHRKLEASaiENQfLKQLQLRHlkaigKYVNSQNNLPQITAK---HQNEVKNLRQLLRKSQEKERAVSRK 232
Cdd:COG3206  177 LEFLEEQLPELRKELEEA--EAA-LEEFRQKN-----GLVDLSEEAKLLLQQlseLESQLAEARAELAEAEARLAALRAQ 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 233 LRETDG---ELLRTKDVLQALQRLSEDKnlAEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNRSYSRQLAKENRktl 309
Cdd:COG3206  249 LGSGPDalpELLQSPVIQQLRAQLAELE--AELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELE--- 323

                        170       180
                 ....*....|....*....|..
gi 124517724 310 AAQTATKTLQAEVRQLQQKLKE 331
Cdd:COG3206  324 ALQAREASLQAQLAQLEARLAE 345
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
156-337 2.95e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 2.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 156 IKELKNELADVHRKLEASAIEN-QFLKQL--QLRHLKAI-GKYVNSQNNLPQITAKH---QNEVKNLRQLLRKSQEKERA 228
Cdd:COG4717   48 LERLEKEADELFKPQGRKPELNlKELKELeeELKEAEEKeEEYAELQEELEELEEELeelEAELEELREELEKLEKLLQL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 229 VS--RKLRETDGELLRTKDVLQALQRlsedkNLAEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNRSYSRQLAKENR 306
Cdd:COG4717  128 LPlyQELEALEAELAELPERLEELEE-----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202

                        170       180       190
                 ....*....|....*....|....*....|.
gi 124517724 307 KtlaAQTATKTLQAEVRQLQQKLKEKDRELE 337
Cdd:COG4717  203 E---LQQRLAELEEELEEAQEELEELEEELE 230
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 156-337 4.29e-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: 4.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724   156 IKELKNELADVHRKLEAsAIENQFLKQlQLRHLKaIGKYVNSQNNLpqitakhQNEVKNLRQLLRKSQEKERAVSRKLRE 235
Cdd:TIGR02168  195 LNELERQLKSLERQAEK-AERYKELKA-ELRELE-LALLVLRLEEL-------REELEELQEELKEAEEELEELTAELQE 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724   236 TDGELLRTKDvlqALQRLSEDKNLAERE--ELTDRLTDLTAKMEANDKKIQNLEKQLRlnnrSYSRQLAKENRKTLAAQT 313
Cdd:TIGR02168  265 LEEKLEELRL---EVSELEEEIEELQKElyALANEISRLEQQKQILRERLANLERQLE----ELEAQLEELESKLDELAE 337

                          170       180
                   ....*....|....*....|....
gi 124517724   314 ATKTLQAEVRQLQQKLKEKDRELE 337
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELE 361
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 209-353 7.33e-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: 7.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724   209 QNEVKNLRQLLRKSQEKERAVSRKLRETDGELLRTKDVLQALQRLSEDKN--LAEREELTDRLTD----LTAKMEANDKK 282
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqISALRKDLARLEAeveqLEERIAQLSKE 755

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124517724   283 IQNLEKQLrlnnRSYSRQLAKENRKTLAAQTATKTLQAEVRQLQQKLKEKDRELEIKniytNRILKNLNDK 353
Cdd:TIGR02168  756 LTELEAEI----EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEE 818
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
145-337 2.16e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724  145 THRILSARLHKIKELKnELADVHRKLEASAIENQFLKQLQ--LRHLKAIGKYVNSQNNLPQIT---AKHQNEVKNLRQLL 219
Cdd:COG4913   240 AHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRaaLRLWFAQRRLELLEAELEELRaelARLEAELERLEARL 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724  220 RKSQEKERAVSRKLRETDGellrtkDVLQALQRLSEDKNlAEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNRSYSR 299
Cdd:COG4913   319 DALREELDELEAQIRGNGG------DRLEQLEREIERLE-RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 124517724  300 QLAKENRKTLAAQTATKTLQAEVRQLQQKLKEKDRELE 337
Cdd:COG4913   392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 149-337 2.20e-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: 44.37  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 149 LSARLHKIKELKNELADVHRKLEAsaiENQFLKQLQLRHLKAIGKYVNSQNNLPQITAK---HQNEVKNLRQLLRKSQEK 225
Cdd:COG4942   15 AAAQADAAAEAEAELEQLQQEIAE---LEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 226 ERAVSRKLRETDGE-------------------LLRTKDVLQALQRLS-------EDKNLAE-----REELTDRLTDLTA 274
Cdd:COG4942   92 IAELRAELEAQKEElaellralyrlgrqpplalLLSPEDFLDAVRRLQylkylapARREQAEelradLAELAALRAELEA 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124517724 275 KMEANDKKIQNLEKQLRLNNRSYSRQ---LAKENRKTLAAQTATKTLQAEVRQLQQKLKEKDRELE 337
Cdd:COG4942  172 ERAELEALLAELEEERAALEALKAERqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 86-331 2.50e-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: 2.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724    86 RRLQSEKPLAKAKEKRKYNAGKLPQPRGQKDIPAEKKQFWNASLISSQIQTIAKRRdtmTHRILSARLHKIKE----LKN 161
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE---ALDELRAELTLLNEeaanLRE 824

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724   162 ELADVHRKLEASAIENQFLKQLQLRHLKAIGKYVNSQNNLPQITAKHQNEVKNLRQLLRKSQEKERAVSRKLRETDGELL 241
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724   242 RTKDVLQALQRlsedknlaEREELTDRLTDLTAKMEANDKKIQNLEKQLrlnNRSYSRQLAKENRKTLAAQTATKTLQAE 321
Cdd:TIGR02168  905 ELESKRSELRR--------ELEELREKLAQLELRLEGLEVRIDNLQERL---SEEYSLTLEEAEALENKIEDDEEEARRR 973

                          250
                   ....*....|
gi 124517724   322 VRQLQQKLKE 331
Cdd:TIGR02168  974 LKRLENKIKE 983
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 225-340 2.76e-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: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 225 KERAVsRKLRETDGELLRTKDVLQALQR----LSEDKNLAER-EELTDRLTDLTAKMEANdkKIQNLEKQLRLnnrsYSR 299
Cdd:COG1196  174 KEEAE-RKLEATEENLERLEDILGELERqlepLERQAEKAERyRELKEELKELEAELLLL--KLRELEAELEE----LEA 246

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 124517724 300 QLAKENRKTLAAQTATKTLQAEVRQLQQKLKEKDRELEIKN 340
Cdd:COG1196  247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 128-378 2.76e-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: 44.67  E-value: 2.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724   128 SLISSQIQTIAKRRDTMTHRILSARlHKIKELKNELADVHRKLEASAIEnqfLKQLQLrhlkAIGKYVNSQNNLPQITAK 207
Cdd:TIGR02169  719 GEIEKEIEQLEQEEEKLKERLEELE-EDLSSLEQEIENVKSELKELEAR---IEELEE----DLHKLEEALNDLEARLSH 790

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724   208 HQneVKNLRQLLRKSQEKERAVSRKLRETDGELLRTKDVLQALQRLSEDK-------------NLAEREELTDRLTDLTA 274
Cdd:TIGR02169  791 SR--IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELqeqridlkeqiksIEKEIENLNGKKEELEE 868

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724   275 KMEANDKKIQNLEKQLRlNNRSYSRQLAKENRktlAAQTATKTLQAEVRQLQQKLKEKDRELEIKNIYTNRILKNLN-DK 353
Cdd:TIGR02169  869 ELEELEAALRDLESRLG-DLKKERDELEAQLR---ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGeDE 944

                          250       260       270
                   ....*....|....*....|....*....|..
gi 124517724   354 EDYPKVSSTKSVQADRK-------SLPSVNMR 378
Cdd:TIGR02169  945 EIPEEELSLEDVQAELQrveeeirALEPVNML 976
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 214-356 2.80e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.43  E-value: 2.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 214 NLRQLLRKSQEKERAVSRKLRETDGELLRTKDVLQALQRLSEdKNLAEREELTDRLTD-----LTAKMEANDKKIQNLEK 288
Cdd:PRK00409 517 KLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKE-KLQEEEDKLLEEAEKeaqqaIKEAKKEADEIIKELRQ 595

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 289 QLRLNNRSYSRQLAKENRKTL--AAQTATKTLQAEVRQlQQKLKEKDReLEIKNIYTNRILKNLNDKEDY 356
Cdd:PRK00409 596 LQKGGYASVKAHELIEARKRLnkANEKKEKKKKKQKEK-QEELKVGDE-VKYLSLGQKGEVLSIPDDKEA 663
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 120-381 5.21e-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: 5.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724   120 EKKQFW-NASLISSQ--IQTIAKRRDTMTHrILSARLHKIKELKNELADVHRKLEA-----------SAIENQFLKQLQL 185
Cdd:pfam15921  102 EKQKFYlRQSVIDLQtkLQEMQMERDAMAD-IRRRESQSQEDLRNQLQNTVHELEAakclkedmledSNTQIEQLRKMML 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724   186 RHLKAIGKYVNSQNNLPQITAKHQNEVKNLRQLLRKSQEKerAVSRKLRETD-------GELLRTKDVLQALQRLSEDKN 258
Cdd:pfam15921  181 SHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGS--AISKILRELDteisylkGRIFPVEDQLEALKSESQNKI 258

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724   259 LAEREELTDRLTDL----------------TAKMEAND--KKIQNLEKQLRLNNRSYSRQLAKenrktlaAQTATKTLQA 320
Cdd:pfam15921  259 ELLLQQHQDRIEQLiseheveitgltekasSARSQANSiqSQLEIIQEQARNQNSMYMRQLSD-------LESTVSQLRS 331

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124517724   321 EVRQLQQKLKEKDRELEIKNIYTNRILKNLNDKEDYPKVSSTKSVQADRKSLPSVNMRHQE 381
Cdd:pfam15921  332 ELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKE 392
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
212-337 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 124517724  212 VKNLRQLLRKSQEKERAVSRKLRETDGELLRTKDVLQALQRLSE----DKNLA----EREELTDRLTDLtakmEANDKKI 283
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdEIDVAsaerEIAELEAELERL----DASSDDL 687

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 124517724  284 QNLEKQLRLNNRSYsRQLAKENRktlAAQTATKTLQAEVRQLQQKLKEKDRELE 337
Cdd:COG4913   688 AALEEQLEELEAEL-EELEEELD---ELKGEIGRLEKELEQAEEELDELQDRLE 737
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 155-340 8.56e-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: 8.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724   155 KIKELKNELADVHRKLEASAIEnqfLKQLQLRHLKAIGKYVNSQNNLPQITAK---HQNEVKNLRQLLRKSQEKERAVSR 231
Cdd:TIGR02168  240 ELEELQEELKEAEEELEELTAE---LQELEEKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILRERLANLER 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724   232 KLRETDGELLRTKdvlQALQRLSEDKNL--AEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNRSYSRQLAKENRKTL 309
Cdd:TIGR02168  317 QLEELEAQLEELE---SKLDELAEELAEleEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393

                          170       180       190
                   ....*....|....*....|....*....|.
gi 124517724   310 AAQTATKTLQAEVRQLQQKLKEKDRELEIKN 340
Cdd:TIGR02168  394 QIASLNNEIERLEARLERLEDRRERLQQEIE 424
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 120-353 1.44e-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: 41.93  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724  120 EKKQFWNASLiSSQIQTIAKRRDTMTHRIlSARLHKIKELKNELADVHRKLEASAIENQFLKQLQLRHLKAIGKYVNSQN 199
Cdd:TIGR04523 303 QKEQDWNKEL-KSELKNQEKKLEEIQNQI-SQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ 380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724  200 NLPQITAKHQNEVKNLRQLLRKSQEKERAVSRKLR--ETDGELLrtkdvLQALQRLSED--KNLAEREELTDRLTDLTAK 275
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKklQQEKELL-----EKEIERLKETiiKNNSEIKDLTNQDSVKELI 455

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724  276 MEANDKKIQNLEKQLRLNNRSYS--RQLAKENRKTLAAQTAT-KTLQAEVRQLQQK----------LKEKDRELEIKNIY 342
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINkiKQNLEQKQKELKSKEKElKKLNEEKKELEEKvkdltkkissLKEKIEKLESEKKE 535

                         250
                  ....*....|.
gi 124517724  343 TNRILKNLNDK 353
Cdd:TIGR04523 536 KESKISDLEDE 546
PRK01156 PRK01156
chromosome segregation protein; Provisional
 149-340 2.05e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.43  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 149 LSARLHKIKELKNELADVHRKLEASAIENQFLKQLQLRHLKAIGKYVNSQNNLPQITAKHQNEVKNLRQLLR--KSQ-EK 225
Cdd:PRK01156 244 LSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSniDAEiNK 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 226 ERAVSRKLRETDGEllrTKDVLQALQRLSE-DKNLAEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNRSYSRQLAKE 304
Cdd:PRK01156 324 YHAIIKKLSVLQKD---YNDYIKKKSRYDDlNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQ 400

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 124517724 305 --------------NRKTLAAQTATKTLQAEVRQLQQKLKEKDRELEIKN 340
Cdd:PRK01156 401 eidpdaikkelneiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLN 450
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 154-335 2.28e-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: 41.58  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724   154 HKIKELKNELADVHRKLEASAIENQFLKQLQLRHLKAIGKYVNSQNNLPQITAKHQNEVKNLRQLLRKSQEKERAVSRKL 233
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724   234 RETDGELLRTKDVLQALQ------RLSEDKNLAEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNrsySRQLAKENRK 307
Cdd:TIGR02168  333 DELAEELAELEEKLEELKeeleslEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN---NEIERLEARL 409

                          170       180
                   ....*....|....*....|....*...
gi 124517724   308 TLAAQTATKtLQAEVRQLQQKLKEKDRE 335
Cdd:TIGR02168  410 ERLEDRRER-LQQEIEELLKKLEEAELK 436
46 PHA02562
endonuclease subunit; Provisional
 155-350 2.79e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 155 KIKELKNELADVhrKLEASAIENQflkqlqlrhLKAIGKYVNSQNNLP-QITAKHQNEVKNLRQLLR--KSQEKERavSR 231
Cdd:PHA02562 175 KIRELNQQIQTL--DMKIDHIQQQ---------IKTYNKNIEEQRKKNgENIARKQNKYDELVEEAKtiKAEIEEL--TD 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 232 KLRETDGELLRTKDVLQAL-------------------------------QRLSEDKNLAEreELTDRLTDLTAKMEAND 280
Cdd:PHA02562 242 ELLNLVMDIEDPSAALNKLntaaakikskieqfqkvikmyekggvcptctQQISEGPDRIT--KIKDKLKELQHSLEKLD 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 281 KKIQNLEKQ----------LRLNNRSYS---RQLAKENRKTLAAQTATKTLQA-------EVRQLQQKLKEKDRELE--I 338
Cdd:PHA02562 320 TAIDELEEImdefneqskkLLELKNKIStnkQSLITLVDKAKKVKAAIEELQAefvdnaeELAKLQDELDKIVKTKSelV 399

                        250
                 ....*....|..
gi 124517724 339 KNIYTNRILKNL 350
Cdd:PHA02562 400 KEKYHRGIVTDL 411
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 118-331 3.67e-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: 3.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 118 PAEKKQFWNASLISSQIQTIAKRRDTMTHRIlsarlhkiKELKNELADVHRKLEASAIEnqfLKQLQLRHlkaigkyvns 197
Cdd:COG1579    3 PEDLRALLDLQELDSELDRLEHRLKELPAEL--------AELEDELAALEARLEAAKTE---LEDLEKEI---------- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 198 qnnlpqitAKHQNEVKNLRQLLRKSQEKERAVsRKLREtdgellrtkdvLQALQRlSEDKNLAEREELTDRLTDLTAKME 277
Cdd:COG1579   62 --------KRLELEIEEVEARIKKYEEQLGNV-RNNKE-----------YEALQK-EIESLKRRISDLEDEILELMERIE 120

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 124517724 278 ANDKKIQNLEKQLrlnnrsySRQLAKENRKTLAAQTATKTLQAEVRQLQQKLKE 331
Cdd:COG1579  121 ELEEELAELEAEL-------AELEAELEEKKAELDEELAELEAELEELEAEREE 167
TMCO5 pfam14992
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing ...
 218-338 4.39e-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: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724  218 LLRKSQEKERAVSRklreTDGELLRTKDVLQALQRLSEDKNLAEREELTDRLTDLTAKMEAND----KKIQNLEKQLrln 293
Cdd:pfam14992  22 LLLKIQEKEEEIQS----LEREITLTRSLAEDEEREELNFTIMEKEDALQELELETAKLEKKNeilvKSVMELQRKL--- 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 124517724  294 nrsySRqlaKENRKTLAAQTATKTLQAEVRQLQQKLKEK--DRELEI 338
Cdd:pfam14992  95 ----SR---KSDKNTGLEQETLKQMLEELKVKLQQSEEScaDQEKEL 134
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 201-328 4.40e-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: 40.00  E-value: 4.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724   201 LPQITAKHQNEVKNLRQLLRKSQEKERAVSRKLRETDGELLRTKDVLQALQRLSEDKNLaEREELTDRLTDLTAKMEAND 280
Cdd:smart00787 174 KPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEE-ELQELESKIEDLTNKKSELN 252

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 124517724   281 KKIQNLEKQlRLNNRSYSRqlaKENRKtlaaqtatktLQAEVRQLQQK 328
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 ...
 224-337 5.85e-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: 39.62  E-value: 5.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724  224 EKERAVSRKLRETDGELLRTK----DVLQALQRLSEDKNLAEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNRSYSR 299
Cdd:pfam04849 142 ETESSCSTPLRRNESFSSLHGcvqlDALQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAE 221

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 124517724  300 ---QLAKENRKTLAAQTATKTLQAEVRQLQQKLKEKDRELE 337
Cdd:pfam04849 222 lseELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENE 262
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
148-337 7.52e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 7.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 148 ILSARLHKIKELKNELADVHRKLEASAIENqfLKQLQLRHLKAigKYVNSQNNLPQITAKHQNEVKNLRQLLRKSQEKER 227
Cdd:COG4717  286 LALLFLLLAREKASLGKEAEELQALPALEE--LEEEELEELLA--ALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 228 AvsrklretdgelLRTKDVLQALQRLSEDKNLAEREELTDRLTDLTAKMEANdKKIQNLEKQLRLNNRSYSRQLAKENRK 307
Cdd:COG4717  362 E------------LQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELK-EELEELEEQLEELLGELEELLEALDEE 428

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 124517724 308 TLAA-----QTATKTLQAEVRQLQQKLKEKDRELE 337
Cdd:COG4717  429 ELEEeleelEEELEELEEELEELREELAELEAELE 463
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
147-332 7.58e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 7.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 147 RILSARLHKIKELKNELADVHRKLEASAIENQFLKQLQLRHLKAIGKYVNSQNNLPQITAKhQNEVKNLRQLLRksqEKE 226
Cdd:COG4717  340 LELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQEL-KEELEELEEQLE---ELL 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 227 RAVSRKLRETDGELLRTKdvlqaLQRLSEdknlaEREELTDRLTDLTAKMEANDKKIQNLEKQLRLNNRSYSRQLAKENR 306
Cdd:COG4717  416 GELEELLEALDEEELEEE-----LEELEE-----ELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAEL 485

                        170       180
                 ....*....|....*....|....*..
gi 124517724 307 KTLAAQ-TATKTLQAEVRQLQQKLKEK 332
Cdd:COG4717  486 RELAEEwAALKLALELLEEAREEYREE 512
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
102-310 8.92e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 8.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 102 KYNAGKLPQPRGQKDIPaekkqfwNASLISSQIQTIAKRRDTmtHRILSARLHKIKELKNELADVHRKLEASAIENQFLK 181
Cdd:COG4717   52 EKEADELFKPQGRKPEL-------NLKELKELEEELKEAEEK--EEEYAELQEELEELEEELEELEAELEELREELEKLE 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724 182 QLqLRHLKAIGKYVNSQNNLPQITAKHQNEVKNLRQLLRKSQEKERAvSRKLRETDGELLRTKDVLQALQRLSEDKNLAE 261
Cdd:COG4717  123 KL-LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEEL-EAELAELQEELEELLEQLSLATEEELQDLAEE 200

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 124517724 262 REELTDRLTDLTAKMEANDKKIQNLEKQL-RLNNRSYSRQLAKENRKTLA 310
Cdd:COG4717  201 LEELQQRLAELEEELEEAQEELEELEEELeQLENELEAAALEERLKEARL 250
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 204-351 9.51e-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: 37.96  E-value: 9.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124517724  204 ITAKHQNEVKNLRQLLRKSQEKERAVSRKLRETDGELLRTKDVLQALQRLSED--KNLAEREELTDRLTDLTAKMEANDK 281
Cdd:pfam13851  20 ITRNNLELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEElrKQLENYEKDKQSLKNLKARLKVLEK 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124517724  282 KIQNLEKQLRLNNRSYSrQLAKEnRKTLAAQTaTKTLQaEVRQ--------LQQKLKEKDRELEIKNIYTNRILKNLN 351
Cdd:pfam13851 100 ELKDLKWEHEVLEQRFE-KVERE-RDELYDKF-EAAIQ-DVQQktglknllLEKKLQALGETLEKKEAQLNEVLAAAN 173
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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