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Conserved domains on  [gi|1856628515|ref|NP_001371221|]
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lebercilin-like protein isoform b [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 ...
9-201 7.29e-71

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: 225.17  E-value: 7.29e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515   9 MAHRILSARLHKIKGLKNELADMHHKLEAILTENQFLKQLQLRHLKAIGKYENSQNNLPQIMAKHQNEVKNLRQLLRKSQ 88
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515  89 EKERTLSRKLRETDSQLLKTKDILQALQKLSEDKNLAEREELTHKLSIITTKMDANDKKIQSLEKQLRLNCRAFSRQLAI 168
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1856628515 169 ETRKTLAAQTATKTLQVEVKHLQQKLKEKDREL 201
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 ...
9-201 7.29e-71

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: 225.17  E-value: 7.29e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515   9 MAHRILSARLHKIKGLKNELADMHHKLEAILTENQFLKQLQLRHLKAIGKYENSQNNLPQIMAKHQNEVKNLRQLLRKSQ 88
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515  89 EKERTLSRKLRETDSQLLKTKDILQALQKLSEDKNLAEREELTHKLSIITTKMDANDKKIQSLEKQLRLNCRAFSRQLAI 168
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1856628515 169 ETRKTLAAQTATKTLQVEVKHLQQKLKEKDREL 201
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
79-199 2.84e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 47.13  E-value: 2.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515  79 NLRQLLRKSQEKERTLSRKLRETDSQLLKTKDILQALQKLSEdKNLAEREELTHKL-----SIITTKMDANDKKIQSLEK 153
Cdd:PRK00409  517 KLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKE-KLQEEEDKLLEEAekeaqQAIKEAKKEADEIIKELRQ 595
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1856628515 154 QLRLNCRAFSRQLAIETRKTLA-AQTATKTLQVEVKHLQQKLKEKDR 199
Cdd:PRK00409  596 LQKGGYASVKAHELIEARKRLNkANEKKEKKKKKQKEKQEELKVGDE 642
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
74-202 8.03e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 8.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515  74 QNEVKNLRQLLRKSQEKERTLSRKLRETDSQLLKTKDILQALQKLSEDKNLAEREELTHKLSIITTKMDANDKKIQSLEK 153
Cdd:COG1196   238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1856628515 154 QLRLNcrafsRQLAIETRKTLAAQTATKTLQVEVKHLQQKLKEKDRELE 202
Cdd:COG1196   318 LEELE-----EELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
I-BAR_IMD cd07605
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ...
27-120 8.53e-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: 38.12  E-value: 8.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515  27 ELADMHHKLEAILTEN--QFLKQLqLRHLKaiGKYENSQNNLPQIMAKHQNEVKNLRQLLRKSQEKERTLSRKLR----- 99
Cdd:cd07605    72 QIVDTHKSIEASLEQVakAFHGEL-ILPLE--KKLELDQKVINKFEKDYKKEYKQKREDLDKARSELKKLQKKSQksgtg 148
                          90       100
                  ....*....|....*....|.
gi 1856628515 100 ETDSQLLKTKDILQALQKLSE 120
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 ...
9-201 7.29e-71

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: 225.17  E-value: 7.29e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515   9 MAHRILSARLHKIKGLKNELADMHHKLEAILTENQFLKQLQLRHLKAIGKYENSQNNLPQIMAKHQNEVKNLRQLLRKSQ 88
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515  89 EKERTLSRKLRETDSQLLKTKDILQALQKLSEDKNLAEREELTHKLSIITTKMDANDKKIQSLEKQLRLNCRAFSRQLAI 168
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1856628515 169 ETRKTLAAQTATKTLQVEVKHLQQKLKEKDREL 201
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
79-199 2.84e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 47.13  E-value: 2.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515  79 NLRQLLRKSQEKERTLSRKLRETDSQLLKTKDILQALQKLSEdKNLAEREELTHKL-----SIITTKMDANDKKIQSLEK 153
Cdd:PRK00409  517 KLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKE-KLQEEEDKLLEEAekeaqQAIKEAKKEADEIIKELRQ 595
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1856628515 154 QLRLNCRAFSRQLAIETRKTLA-AQTATKTLQVEVKHLQQKLKEKDR 199
Cdd:PRK00409  596 LQKGGYASVKAHELIEARKRLNkANEKKEKKKKKQKEKQEELKVGDE 642
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
19-310 4.96e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 42.89  E-value: 4.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515  19 HKIKGLKNELADMHHKLEAILTENQFLKQLQLRHLKAIGKYENSQNNLPQIMAKHQNEVKNLRQLLrksQEKERTLSRKL 98
Cdd:pfam10174 289 NKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRL---EEKESFLNKKT 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515  99 REtdsqllktkdilqaLQKLSEDKN--LAEREELTHKLSIITTKMDANDKKIQSLEKQLRLNcrafSRQLAIETRKTLAA 176
Cdd:pfam10174 366 KQ--------------LQDLTEEKStlAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDK----DKQLAGLKERVKSL 427
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515 177 QTATKTLQVEVKHLQQKLKEKDRELEikniyshrILKNLHDTEDYPKVSSTKSVQADRKIL--PFTSMRHQGTQK----S 250
Cdd:pfam10174 428 QTDSSNTDTALTTLEEALSEKERIIE--------RLKEQREREDRERLEELESLKKENKDLkeKVSALQPELTEKesslI 499
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1856628515 251 DVPPLTTKGKKATGNIDHKEKSTEIN-----HEIPHCVNKLPK---QEDSKRKYEDLSGEEKHLEVQI 310
Cdd:pfam10174 500 DLKEHASSLASSGLKKDSKLKSLEIAveqkkEECSKLENQLKKahnAEEAVRTNPEINDRIRLLEQEV 567
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
74-202 8.03e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 8.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515  74 QNEVKNLRQLLRKSQEKERTLSRKLRETDSQLLKTKDILQALQKLSEDKNLAEREELTHKLSIITTKMDANDKKIQSLEK 153
Cdd:COG1196   238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1856628515 154 QLRLNcrafsRQLAIETRKTLAAQTATKTLQVEVKHLQQKLKEKDRELE 202
Cdd:COG1196   318 LEELE-----EELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
14-202 3.52e-03

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: 40.16  E-value: 3.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515   14 LSARLHKIKGLKNELADMHHKLEAILTEnqflkqLQLRHlkaiGKYENSQNNLPQIMAKHQNEVKNLRQLLRKSQEKERT 93
Cdd:pfam01576  389 LQAELRTLQQAKQDSEHKRKKLEGQLQE------LQARL----SESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK 458
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515   94 LSRKLRETDSQLLKTKDILQ--ALQKLSEDKNL----AEREELTHKLSIITTKMDANDKKIQSLEKQLrlncRAFSRQLA 167
Cdd:pfam01576  459 LSKDVSSLESQLQDTQELLQeeTRQKLNLSTRLrqleDERNSLQEQLEEEEEAKRNVERQLSTLQAQL----SDMKKKLE 534
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1856628515  168 IETRKTLAAQTATKTLQVEVKHLQQKLKEKDRELE 202
Cdd:pfam01576  535 EDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD 569
mukB PRK04863
chromosome partition protein MukB;
58-201 3.56e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515   58 KYENSQnnlpQIMAKHQNEVKNLRQLLRKSQEKERTLSRKLRETDSQLLKTKDILQALQKlSEDKNLAEREELTHKLSII 137
Cdd:PRK04863   972 SYEDAA----EMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKS-SYDAKRQMLQELKQELQDL 1046
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1856628515  138 TTKMDANdkkiqsLEKQLRLNCRAFSRQL-AIETRKTLAAQTATKTlQVEVKHLQQKLKEKDREL 201
Cdd:PRK04863  1047 GVPADSG------AEERARARRDELHARLsANRSRRNQLEKQLTFC-EAEMDNLTKKLRKLERDY 1104
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
12-202 6.99e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 6.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515  12 RILSARLHKIKGLKNELADMHHKLEAILTEN--------QFLKQLQLRHL-KAIGKYENSQNNLPQIMAKHQNEVKNLRQ 82
Cdd:COG4717     2 KIKELEIYGFGKFRDRTIEFSPGLNVIYGPNeagkstllAFIRAMLLERLeKEADELFKPQGRKPELNLKELKELEEELK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515  83 LLRKSQEKERTLSRKLRETDSQL----LKTKDILQALQKLSEDKNL----AEREELTHKLSIITTKMDANDKKIQSLE-- 152
Cdd:COG4717    82 EAEEKEEEYAELQEELEELEEELeeleAELEELREELEKLEKLLQLlplyQELEALEAELAELPERLEELEERLEELRel 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1856628515 153 -----------KQLRLNCRAFSRQLAIETRKTL--------AAQTATKTLQVEVKHLQQKLKEKDRELE 202
Cdd:COG4717   162 eeeleeleaelAELQEELEELLEQLSLATEEELqdlaeeleELQQRLAELEEELEEAQEELEELEEELE 230
I-BAR_IMD cd07605
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ...
27-120 8.53e-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: 38.12  E-value: 8.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515  27 ELADMHHKLEAILTEN--QFLKQLqLRHLKaiGKYENSQNNLPQIMAKHQNEVKNLRQLLRKSQEKERTLSRKLR----- 99
Cdd:cd07605    72 QIVDTHKSIEASLEQVakAFHGEL-ILPLE--KKLELDQKVINKFEKDYKKEYKQKREDLDKARSELKKLQKKSQksgtg 148
                          90       100
                  ....*....|....*....|.
gi 1856628515 100 ETDSQLLKTKDILQALQKLSE 120
Cdd:cd07605   149 KYQEKLDQALEELNDKQKELE 169
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3-204 9.38e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 9.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515   3 AQRRDAMAHRILSARLHKIKGLKNELADMHHKLE----AILTENQFLKQLQLRHLKAIGKYENSQNNLPQIMAKHQNEVK 78
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELAELEAELEelrlELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856628515  79 NLRQL---LRKSQEKERTLSRKLRETDSQLLKTKDILQALQKLSEDKNLAEREELTHKLSIITTKMDANDKKIQSLEKQL 155
Cdd:COG1196   317 RLEELeeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1856628515 156 RLNCRAFSRQLAIETRKTLAAQTATKTLQVEVKHLQQKLKEKDRELEIK 204
Cdd:COG1196   397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
 
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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