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Conserved domains on  [gi|768020254|ref|XP_011527762|]
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lebercilin-like protein isoform X1 [Homo sapiens]

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 ...
188-380 4.67e-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: 240.19  E-value: 4.67e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254  188 MAHRILSARLHKIKGLKNELADMHHKLEAILTENQFLKQLQLRHLKAIGKYENSQNNLPQIMAKHQNEVKNLRQLLRKSQ 267
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254  268 EKERTLSRKLRETDSQLLKTKDILQALQKLSEDKNLAEREELTHKLSIITTKMDANDKKIQSLEKQLRLNCRAFSRQLAI 347
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 768020254  348 ETRKTLAAQTATKTLQVEVKHLQQKLKEKDREL 380
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 ...
188-380 4.67e-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: 240.19  E-value: 4.67e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254  188 MAHRILSARLHKIKGLKNELADMHHKLEAILTENQFLKQLQLRHLKAIGKYENSQNNLPQIMAKHQNEVKNLRQLLRKSQ 267
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254  268 EKERTLSRKLRETDSQLLKTKDILQALQKLSEDKNLAEREELTHKLSIITTKMDANDKKIQSLEKQLRLNCRAFSRQLAI 347
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 768020254  348 ETRKTLAAQTATKTLQVEVKHLQQKLKEKDREL 380
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
258-378 1.27e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 48.67  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254 258 NLRQLLRKSQEKERTLSRKLRETDSQLLKTKDILQALQKLSEdKNLAEREELTHKL-----SIITTKMDANDKKIQSLEK 332
Cdd:PRK00409 517 KLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKE-KLQEEEDKLLEEAekeaqQAIKEAKKEADEIIKELRQ 595
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 768020254 333 QLRLNCRAFSRQLAIETRKTLA-AQTATKTLQVEVKHLQQKLKEKDR 378
Cdd:PRK00409 596 LQKGGYASVKAHELIEARKRLNkANEKKEKKKKKQKEKQEELKVGDE 642
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
253-381 3.00e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 3.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254 253 QNEVKNLRQLLRKSQEKERTLSRKLRETDSQLLKTKDILQALQKLSEDKNLAEREELTHKLSIITTKMDANDKKIQSLEK 332
Cdd:COG1196  238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 768020254 333 QLRLNcrafsRQLAIETRKTLAAQTATKTLQVEVKHLQQKLKEKDRELE 381
Cdd:COG1196  318 LEELE-----EELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
175-386 5.16e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 5.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254   175 NSQIHMIAQRRDAMAHRILSARLHKIKGLKNELADMHHKLE----AILTENQFLKQLQLRHLKAIGKYENSQNNLPQIMA 250
Cdd:TIGR02169  264 EKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAslerSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER 343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254   251 KHQNEVKNLRQL---LRKSQEKERTLSRKLRETDSQLLKTKDILQALQKlsedknlaEREELTHKL-SIITTKMDANDKK 326
Cdd:TIGR02169  344 EIEEERKRRDKLteeYAELKEELEDLRAELEEVDKEFAETRDELKDYRE--------KLEKLKREInELKRELDRLQEEL 415
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768020254   327 IQSLEKQLRLNcrafsRQLAIETRKTLAAQTATKTLQVEVKHLQQKLKE--KDRELEIKNIY 386
Cdd:TIGR02169  416 QRLSEELADLN-----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQlaADLSKYEQELY 472
I-BAR_IMD cd07605
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ...
206-299 3.27e-03

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module that binds and bends membranes; Inverse (I)-BAR (or IMD) is a member of the Bin/Amphiphysin/Rvs (BAR) domain family. It is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. IMD domains are found in Insulin Receptor tyrosine kinase Substrate p53 (IRSp53), Missing in Metastasis (MIM), and Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-like (BAIAP2L) proteins. These are multi-domain proteins that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. Most members contain an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus, exccept for MIM which does not carry an SH3 domain. Some members contain additional domains and motifs. The IMD domain binds and bundles actin filaments, binds membranes and produces membrane protrusions, and interacts with the small GTPase Rac.


Pssm-ID: 153289 [Multi-domain]  Cd Length: 223  Bit Score: 39.66  E-value: 3.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254 206 ELADMHHKLEAILTEN--QFLKQLqLRHLKaiGKYENSQNNLPQIMAKHQNEVKNLRQLLRKSQEKERTLSRKLR----- 278
Cdd:cd07605   72 QIVDTHKSIEASLEQVakAFHGEL-ILPLE--KKLELDQKVINKFEKDYKKEYKQKREDLDKARSELKKLQKKSQksgtg 148
                         90       100
                 ....*....|....*....|.
gi 768020254 279 ETDSQLLKTKDILQALQKLSE 299
Cdd:cd07605  149 KYQEKLDQALEELNDKQKELE 169
 
Name Accession Description Interval E-value
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
188-380 4.67e-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: 240.19  E-value: 4.67e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254  188 MAHRILSARLHKIKGLKNELADMHHKLEAILTENQFLKQLQLRHLKAIGKYENSQNNLPQIMAKHQNEVKNLRQLLRKSQ 267
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254  268 EKERTLSRKLRETDSQLLKTKDILQALQKLSEDKNLAEREELTHKLSIITTKMDANDKKIQSLEKQLRLNCRAFSRQLAI 347
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 768020254  348 ETRKTLAAQTATKTLQVEVKHLQQKLKEKDREL 380
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
258-378 1.27e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 48.67  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254 258 NLRQLLRKSQEKERTLSRKLRETDSQLLKTKDILQALQKLSEdKNLAEREELTHKL-----SIITTKMDANDKKIQSLEK 332
Cdd:PRK00409 517 KLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKE-KLQEEEDKLLEEAekeaqQAIKEAKKEADEIIKELRQ 595
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 768020254 333 QLRLNCRAFSRQLAIETRKTLA-AQTATKTLQVEVKHLQQKLKEKDR 378
Cdd:PRK00409 596 LQKGGYASVKAHELIEARKRLNkANEKKEKKKKKQKEKQEELKVGDE 642
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
193-381 2.94e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.40  E-value: 2.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254   193 LSARLHKIKGLKNELADMHHKLEAILTEnqflkqLQLRHlkaiGKYENSQNNLPQIMAKHQNEVKNLRQLLRKSQEKERT 272
Cdd:pfam01576  389 LQAELRTLQQAKQDSEHKRKKLEGQLQE------LQARL----SESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK 458
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254   273 LSRKLRETDSQLLKTKDILQ--ALQKLSEDKNL----AEREELTHKLSIITTKMDANDKKIQSLEKQLrlncRAFSRQLA 346
Cdd:pfam01576  459 LSKDVSSLESQLQDTQELLQeeTRQKLNLSTRLrqleDERNSLQEQLEEEEEAKRNVERQLSTLQAQL----SDMKKKLE 534
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 768020254   347 IETRKTLAAQTATKTLQVEVKHLQQKLKEKDRELE 381
Cdd:pfam01576  535 EDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD 569
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
253-381 3.00e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 3.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254 253 QNEVKNLRQLLRKSQEKERTLSRKLRETDSQLLKTKDILQALQKLSEDKNLAEREELTHKLSIITTKMDANDKKIQSLEK 332
Cdd:COG1196  238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 768020254 333 QLRLNcrafsRQLAIETRKTLAAQTATKTLQVEVKHLQQKLKEKDRELE 381
Cdd:COG1196  318 LEELE-----EELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
191-381 3.53e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 3.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254 191 RILSARLHKIKGLKNELADMHHKLEAILTEN--------QFLKQLQLRHL-KAIGKYENSQNNLPQIMAKHQNEVKNLRQ 261
Cdd:COG4717    2 KIKELEIYGFGKFRDRTIEFSPGLNVIYGPNeagkstllAFIRAMLLERLeKEADELFKPQGRKPELNLKELKELEEELK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254 262 LLRKSQEKERTLSRKLRETDSQL----LKTKDILQALQKLSEDKNL----AEREELTHKLSIITTKMDANDKKIQSLE-- 331
Cdd:COG4717   82 EAEEKEEEYAELQEELEELEEELeeleAELEELREELEKLEKLLQLlplyQELEALEAELAELPERLEELEERLEELRel 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768020254 332 -----------KQLRLNCRAFSRQLAIETRKTL--------AAQTATKTLQVEVKHLQQKLKEKDRELE 381
Cdd:COG4717  162 eeeleeleaelAELQEELEELLEQLSLATEEELqdlaeeleELQQRLAELEEELEEAQEELEELEEELE 230
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
175-386 5.16e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 5.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254   175 NSQIHMIAQRRDAMAHRILSARLHKIKGLKNELADMHHKLE----AILTENQFLKQLQLRHLKAIGKYENSQNNLPQIMA 250
Cdd:TIGR02169  264 EKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAslerSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER 343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254   251 KHQNEVKNLRQL---LRKSQEKERTLSRKLRETDSQLLKTKDILQALQKlsedknlaEREELTHKL-SIITTKMDANDKK 326
Cdd:TIGR02169  344 EIEEERKRRDKLteeYAELKEELEDLRAELEEVDKEFAETRDELKDYRE--------KLEKLKREInELKRELDRLQEEL 415
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768020254   327 IQSLEKQLRLNcrafsRQLAIETRKTLAAQTATKTLQVEVKHLQQKLKE--KDRELEIKNIY 386
Cdd:TIGR02169  416 QRLSEELADLN-----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQlaADLSKYEQELY 472
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
199-391 1.08e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.65  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254   199 KIKGLKNELADMHHKLEAILTENQFLKQlQLRHLKAIGKYEN---SQNNLPQIMAKHQNEVKNLRQLLRKSQEKERTLSR 275
Cdd:TIGR00618  315 ELQSKMRSRAKLLMKRAAHVKQQSSIEE-QRRLLQTLHSQEIhirDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQ 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254   276 KLRetdsQLLKTKDILQALQKLSEDKNLAEREELTHKLSIittkmdandKKIQSLEKQLRLNCRAFS-RQLAIETRKTLA 354
Cdd:TIGR00618  394 KLQ----SLCKELDILQREQATIDTRTSAFRDLQGQLAHA---------KKQQELQQRYAELCAAAItCTAQCEKLEKIH 460
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 768020254   355 AQTATKTLQVEVKHLQQKLKEKDRELEIKNIYSHRIL 391
Cdd:TIGR00618  461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLL 497
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
213-386 1.10e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.31  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254 213 KLEAILTENQFLKQlQLRHLKAigKYENSQNNLPQIMAKHQ------------NEVKNLRQLLRKSQEKERTLSRKLRET 280
Cdd:COG3206  169 RREEARKALEFLEE-QLPELRK--ELEEAEAALEEFRQKNGlvdlseeaklllQQLSELESQLAEARAELAEAEARLAAL 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254 281 DSQLLKTKDILQALQKLSEDKNLAERE-ELTHKLSIITTK-------MDANDKKIQSLEKQLRLNCRAFSRQLAIEtRKT 352
Cdd:COG3206  246 RAQLGSGPDALPELLQSPVIQQLRAQLaELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILASLEAE-LEA 324
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 768020254 353 LAAQTAT-----KTLQVEVKHL---QQKLKEKDRELEI-KNIY 386
Cdd:COG3206  325 LQAREASlqaqlAQLEARLAELpelEAELRRLEREVEVaRELY 367
mukB PRK04863
chromosome partition protein MukB;
237-380 1.64e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.87  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254  237 KYENSQnnlpQIMAKHQNEVKNLRQLLRKSQEKERTLSRKLRETDSQLLKTKDILQALQKlSEDKNLAEREELTHKLSII 316
Cdd:PRK04863  972 SYEDAA----EMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKS-SYDAKRQMLQELKQELQDL 1046
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768020254  317 TTKMDANdkkiqsLEKQLRLNCRAFSRQL-AIETRKTLAAQTATKTlQVEVKHLQQKLKEKDREL 380
Cdd:PRK04863 1047 GVPADSG------AEERARARRDELHARLsANRSRRNQLEKQLTFC-EAEMDNLTKKLRKLERDY 1104
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
182-383 2.99e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254 182 AQRRDAMAHRILSARLHKIKGLKNELADMHHKLE----AILTENQFLKQLQLRHLKAIGKYENSQNNLPQIMAKHQNEVK 257
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAELEAELEelrlELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254 258 NLRQL---LRKSQEKERTLSRKLRETDSQLLKTKDILQALQKLSEDKNLAEREELTHKLSIITTKMDANDKKIQSLEKQL 334
Cdd:COG1196  317 RLEELeeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 768020254 335 RLNCRAFSRQLAIETRKTLAAQTATKTLQVEVKHLQQKLKEKDRELEIK 383
Cdd:COG1196  397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
I-BAR_IMD cd07605
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ...
206-299 3.27e-03

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module that binds and bends membranes; Inverse (I)-BAR (or IMD) is a member of the Bin/Amphiphysin/Rvs (BAR) domain family. It is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. IMD domains are found in Insulin Receptor tyrosine kinase Substrate p53 (IRSp53), Missing in Metastasis (MIM), and Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-like (BAIAP2L) proteins. These are multi-domain proteins that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. Most members contain an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus, exccept for MIM which does not carry an SH3 domain. Some members contain additional domains and motifs. The IMD domain binds and bundles actin filaments, binds membranes and produces membrane protrusions, and interacts with the small GTPase Rac.


Pssm-ID: 153289 [Multi-domain]  Cd Length: 223  Bit Score: 39.66  E-value: 3.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254 206 ELADMHHKLEAILTEN--QFLKQLqLRHLKaiGKYENSQNNLPQIMAKHQNEVKNLRQLLRKSQEKERTLSRKLR----- 278
Cdd:cd07605   72 QIVDTHKSIEASLEQVakAFHGEL-ILPLE--KKLELDQKVINKFEKDYKKEYKQKREDLDKARSELKKLQKKSQksgtg 148
                         90       100
                 ....*....|....*....|.
gi 768020254 279 ETDSQLLKTKDILQALQKLSE 299
Cdd:cd07605  149 KYQEKLDQALEELNDKQKELE 169
PRK11281 PRK11281
mechanosensitive channel MscK;
193-373 5.83e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.28  E-value: 5.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254  193 LSARLHKIKGLKNELADMhhKL-EAILTENQ-FLKQLQlRHLKAIGKYENSQNNLPQIMAKHQNEVKNLRQLLrKSQEKE 270
Cdd:PRK11281   41 VQAQLDALNKQKLLEAED--KLvQQDLEQTLaLLDKID-RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDN-DEETRE 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020254  271 RTLSRKLRETDSQLLKTKDILQALQklsedKNLAEREELthklsIIT---------TKMDANDKKIQSLEKQLRlNCRAF 341
Cdd:PRK11281  117 TLSTLSLRQLESRLAQTLDQLQNAQ-----NDLAEYNSQ-----LVSlqtqperaqAALYANSQRLQQIRNLLK-GGKVG 185
                         170       180       190
                  ....*....|....*....|....*....|..
gi 768020254  342 SRQLAIETRKTLAAQTATKTLQVEvkhLQQKL 373
Cdd:PRK11281  186 GKALRPSQRVLLQAEQALLNAQND---LQRKS 214
 
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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