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Conserved domains on  [gi|1856631260|ref|NP_001371215|]
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lebercilin-like protein isoform a [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 ...
139-331 2.41e-73

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: 234.80  E-value: 2.41e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260 139 MAHRILSARLHKIKGLKNELADMHHKLEAILTENQFLKQLQLRHLKAIGKYENSQNNLPQIMAKHQNEVKNLRQLLRKSQ 218
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260 219 EKERTLSRKLRETDSQLLKTKDILQALQKLSEDKNLAEREELTHKLSIITTKMDANDKKIQSLEKQLRLNCRAFSRQLAI 298
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1856631260 299 ETRKTLAAQTATKTLQVEVKHLQQKLKEKDREL 331
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
 
Name Accession Description Interval E-value
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
139-331 2.41e-73

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: 234.80  E-value: 2.41e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260 139 MAHRILSARLHKIKGLKNELADMHHKLEAILTENQFLKQLQLRHLKAIGKYENSQNNLPQIMAKHQNEVKNLRQLLRKSQ 218
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260 219 EKERTLSRKLRETDSQLLKTKDILQALQKLSEDKNLAEREELTHKLSIITTKMDANDKKIQSLEKQLRLNCRAFSRQLAI 298
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1856631260 299 ETRKTLAAQTATKTLQVEVKHLQQKLKEKDREL 331
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
209-329 1.70e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 48.28  E-value: 1.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260 209 NLRQLLRKSQEKERTLSRKLRETDSQLLKTKDILQALQKLSEdKNLAEREELTHKL-----SIITTKMDANDKKIQSLEK 283
Cdd:PRK00409  517 KLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKE-KLQEEEDKLLEEAekeaqQAIKEAKKEADEIIKELRQ 595
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1856631260 284 QLRLNCRAFSRQLAIETRKTLA-AQTATKTLQVEVKHLQQKLKEKDR 329
Cdd:PRK00409  596 LQKGGYASVKAHELIEARKRLNkANEKKEKKKKKQKEKQEELKVGDE 642
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
204-332 4.25e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 4.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260 204 QNEVKNLRQLLRKSQEKERTLSRKLRETDSQLLKTKDILQALQKLSEDKNLAEREELTHKLSIITTKMDANDKKIQSLEK 283
Cdd:COG1196   238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1856631260 284 QLRLNcrafsRQLAIETRKTLAAQTATKTLQVEVKHLQQKLKEKDRELE 332
Cdd:COG1196   318 LEELE-----EELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
126-337 9.87e-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: 42.36  E-value: 9.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260  126 NSQIHMIAQRRDAMAHRILSARLHKIKGLKNELADMHHKLE----AILTENQFLKQLQLRHLKAIGKYENSQNNLPQIMA 201
Cdd:TIGR02169  264 EKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAslerSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER 343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260  202 KHQNEVKNLRQL---LRKSQEKERTLSRKLRETDSQLLKTKDILQALQKlsedknlaEREELTHKL-SIITTKMDANDKK 277
Cdd:TIGR02169  344 EIEEERKRRDKLteeYAELKEELEDLRAELEEVDKEFAETRDELKDYRE--------KLEKLKREInELKRELDRLQEEL 415
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1856631260  278 IQSLEKQLRLNcrafsRQLAIETRKTLAAQTATKTLQVEVKHLQQKLKE--KDRELEIKNIY 337
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 ...
157-250 5.43e-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: 38.89  E-value: 5.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260 157 ELADMHHKLEAILTEN--QFLKQLqLRHLKaiGKYENSQNNLPQIMAKHQNEVKNLRQLLRKSQEKERTLSRKLR----- 229
Cdd:cd07605    72 QIVDTHKSIEASLEQVakAFHGEL-ILPLE--KKLELDQKVINKFEKDYKKEYKQKREDLDKARSELKKLQKKSQksgtg 148
                          90       100
                  ....*....|....*....|.
gi 1856631260 230 ETDSQLLKTKDILQALQKLSE 250
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 ...
139-331 2.41e-73

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: 234.80  E-value: 2.41e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260 139 MAHRILSARLHKIKGLKNELADMHHKLEAILTENQFLKQLQLRHLKAIGKYENSQNNLPQIMAKHQNEVKNLRQLLRKSQ 218
Cdd:pfam15619   1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260 219 EKERTLSRKLRETDSQLLKTKDILQALQKLSEDKNLAEREELTHKLSIITTKMDANDKKIQSLEKQLRLNCRAFSRQLAI 298
Cdd:pfam15619  81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1856631260 299 ETRKTLAAQTATKTLQVEVKHLQQKLKEKDREL 331
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
209-329 1.70e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 48.28  E-value: 1.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260 209 NLRQLLRKSQEKERTLSRKLRETDSQLLKTKDILQALQKLSEdKNLAEREELTHKL-----SIITTKMDANDKKIQSLEK 283
Cdd:PRK00409  517 KLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKE-KLQEEEDKLLEEAekeaqQAIKEAKKEADEIIKELRQ 595
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1856631260 284 QLRLNCRAFSRQLAIETRKTLA-AQTATKTLQVEVKHLQQKLKEKDR 329
Cdd:PRK00409  596 LQKGGYASVKAHELIEARKRLNkANEKKEKKKKKQKEKQEELKVGDE 642
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
149-440 9.06e-05

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: 45.58  E-value: 9.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260 149 HKIKGLKNELADMHHKLEAILTENQFLKQLQLRHLKAIGKYENSQNNLPQIMAKHQNEVKNLRQLLrksQEKERTLSRKL 228
Cdd:pfam10174 289 NKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRL---EEKESFLNKKT 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260 229 REtdsqllktkdilqaLQKLSEDKN--LAEREELTHKLSIITTKMDANDKKIQSLEKQLRLNcrafSRQLAIETRKTLAA 306
Cdd:pfam10174 366 KQ--------------LQDLTEEKStlAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDK----DKQLAGLKERVKSL 427
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260 307 QTATKTLQVEVKHLQQKLKEKDRELEikniyshrILKNLHDTEDYPKVSSTKSVQADRKIL--PFTSMRHQGTQK----S 380
Cdd:pfam10174 428 QTDSSNTDTALTTLEEALSEKERIIE--------RLKEQREREDRERLEELESLKKENKDLkeKVSALQPELTEKesslI 499
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1856631260 381 DVPPLTTKGKKATGNIDHKEKSTEIN-----HEIPHCVNKLPK---QEDSKRKYEDLSGEEKHLEVQI 440
Cdd:pfam10174 500 DLKEHASSLASSGLKKDSKLKSLEIAveqkkEECSKLENQLKKahnAEEAVRTNPEINDRIRLLEQEV 567
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
204-332 4.25e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 4.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260 204 QNEVKNLRQLLRKSQEKERTLSRKLRETDSQLLKTKDILQALQKLSEDKNLAEREELTHKLSIITTKMDANDKKIQSLEK 283
Cdd:COG1196   238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1856631260 284 QLRLNcrafsRQLAIETRKTLAAQTATKTLQVEVKHLQQKLKEKDRELE 332
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 ...
144-332 7.97e-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: 42.85  E-value: 7.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260  144 LSARLHKIKGLKNELADMHHKLEAILTEnqflkqLQLRHlkaiGKYENSQNNLPQIMAKHQNEVKNLRQLLRKSQEKERT 223
Cdd:pfam01576  389 LQAELRTLQQAKQDSEHKRKKLEGQLQE------LQARL----SESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK 458
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260  224 LSRKLRETDSQLLKTKDILQ--ALQKLSEDKNL----AEREELTHKLSIITTKMDANDKKIQSLEKQLrlncRAFSRQLA 297
Cdd:pfam01576  459 LSKDVSSLESQLQDTQELLQeeTRQKLNLSTRLrqleDERNSLQEQLEEEEEAKRNVERQLSTLQAQL----SDMKKKLE 534
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1856631260  298 IETRKTLAAQTATKTLQVEVKHLQQKLKEKDRELE 332
Cdd:pfam01576  535 EDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD 569
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
142-332 8.70e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 8.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260 142 RILSARLHKIKGLKNELADMHHKLEAILTEN--------QFLKQLQLRHL-KAIGKYENSQNNLPQIMAKHQNEVKNLRQ 212
Cdd:COG4717     2 KIKELEIYGFGKFRDRTIEFSPGLNVIYGPNeagkstllAFIRAMLLERLeKEADELFKPQGRKPELNLKELKELEEELK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260 213 LLRKSQEKERTLSRKLRETDSQL----LKTKDILQALQKLSEDKNL----AEREELTHKLSIITTKMDANDKKIQSLE-- 282
Cdd:COG4717    82 EAEEKEEEYAELQEELEELEEELeeleAELEELREELEKLEKLLQLlplyQELEALEAELAELPERLEELEERLEELRel 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1856631260 283 -----------KQLRLNCRAFSRQLAIETRKTL--------AAQTATKTLQVEVKHLQQKLKEKDRELE 332
Cdd:COG4717   162 eeeleeleaelAELQEELEELLEQLSLATEEELqdlaeeleELQQRLAELEEELEEAQEELEELEEELE 230
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
126-337 9.87e-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: 42.36  E-value: 9.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260  126 NSQIHMIAQRRDAMAHRILSARLHKIKGLKNELADMHHKLE----AILTENQFLKQLQLRHLKAIGKYENSQNNLPQIMA 201
Cdd:TIGR02169  264 EKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAslerSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER 343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260  202 KHQNEVKNLRQL---LRKSQEKERTLSRKLRETDSQLLKTKDILQALQKlsedknlaEREELTHKL-SIITTKMDANDKK 277
Cdd:TIGR02169  344 EIEEERKRRDKLteeYAELKEELEDLRAELEEVDKEFAETRDELKDYRE--------KLEKLKREInELKRELDRLQEEL 415
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1856631260  278 IQSLEKQLRLNcrafsRQLAIETRKTLAAQTATKTLQVEVKHLQQKLKE--KDRELEIKNIY 337
Cdd:TIGR02169  416 QRLSEELADLN-----AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQlaADLSKYEQELY 472
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
164-337 2.20e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260 164 KLEAILTENQFLKQlQLRHLKAigKYENSQNNLPQIMAKHQ------------NEVKNLRQLLRKSQEKERTLSRKLRET 231
Cdd:COG3206   169 RREEARKALEFLEE-QLPELRK--ELEEAEAALEEFRQKNGlvdlseeaklllQQLSELESQLAEARAELAEAEARLAAL 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260 232 DSQLLKTKDILQALQKLSEDKNLAERE-ELTHKLSIITTK-------MDANDKKIQSLEKQLRLNCRAFSRQLAIEtRKT 303
Cdd:COG3206   246 RAQLGSGPDALPELLQSPVIQQLRAQLaELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILASLEAE-LEA 324
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1856631260 304 LAAQTAT-----KTLQVEVKHL---QQKLKEKDRELEI-KNIY 337
Cdd:COG3206   325 LQAREASlqaqlAQLEARLAELpelEAELRRLEREVEVaRELY 367
mukB PRK04863
chromosome partition protein MukB;
188-331 2.33e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.48  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260  188 KYENSQnnlpQIMAKHQNEVKNLRQLLRKSQEKERTLSRKLRETDSQLLKTKDILQALQKlSEDKNLAEREELTHKLSII 267
Cdd:PRK04863   972 SYEDAA----EMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKS-SYDAKRQMLQELKQELQDL 1046
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1856631260  268 TTKMDANdkkiqsLEKQLRLNCRAFSRQL-AIETRKTLAAQTATKTlQVEVKHLQQKLKEKDREL 331
Cdd:PRK04863  1047 GVPADSG------AEERARARRDELHARLsANRSRRNQLEKQLTFC-EAEMDNLTKKLRKLERDY 1104
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
150-342 2.41e-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: 41.11  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260  150 KIKGLKNELADMHHKLEAILTENQFLKQlQLRHLKAIGKYEN---SQNNLPQIMAKHQNEVKNLRQLLRKSQEKERTLSR 226
Cdd:TIGR00618  315 ELQSKMRSRAKLLMKRAAHVKQQSSIEE-QRRLLQTLHSQEIhirDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQ 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260  227 KLRetdsQLLKTKDILQALQKLSEDKNLAEREELTHKLSIittkmdandKKIQSLEKQLRLNCRAFS-RQLAIETRKTLA 305
Cdd:TIGR00618  394 KLQ----SLCKELDILQREQATIDTRTSAFRDLQGQLAHA---------KKQQELQQRYAELCAAAItCTAQCEKLEKIH 460
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1856631260  306 AQTATKTLQVEVKHLQQKLKEKDRELEIKNIYSHRIL 342
Cdd:TIGR00618  461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLL 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
133-334 4.92e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 4.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260 133 AQRRDAMAHRILSARLHKIKGLKNELADMHHKLE----AILTENQFLKQLQLRHLKAIGKYENSQNNLPQIMAKHQNEVK 208
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELAELEAELEelrlELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260 209 NLRQL---LRKSQEKERTLSRKLRETDSQLLKTKDILQALQKLSEDKNLAEREELTHKLSIITTKMDANDKKIQSLEKQL 285
Cdd:COG1196   317 RLEELeeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1856631260 286 RLNCRAFSRQLAIETRKTLAAQTATKTLQVEVKHLQQKLKEKDRELEIK 334
Cdd:COG1196   397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
I-BAR_IMD cd07605
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ...
157-250 5.43e-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: 38.89  E-value: 5.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260 157 ELADMHHKLEAILTEN--QFLKQLqLRHLKaiGKYENSQNNLPQIMAKHQNEVKNLRQLLRKSQEKERTLSRKLR----- 229
Cdd:cd07605    72 QIVDTHKSIEASLEQVakAFHGEL-ILPLE--KKLELDQKVINKFEKDYKKEYKQKREDLDKARSELKKLQKKSQksgtg 148
                          90       100
                  ....*....|....*....|.
gi 1856631260 230 ETDSQLLKTKDILQALQKLSE 250
Cdd:cd07605   149 KYQEKLDQALEELNDKQKELE 169
PRK11281 PRK11281
mechanosensitive channel MscK;
144-324 7.88e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.51  E-value: 7.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260  144 LSARLHKIKGLKNELADMHhKLEAILTENQ-FLKQLQlRHLKAIGKYENSQNNLPQIMAKHQNEVKNLRQLLrKSQEKER 222
Cdd:PRK11281    41 VQAQLDALNKQKLLEAEDK-LVQQDLEQTLaLLDKID-RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDN-DEETRET 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631260  223 TLSRKLRETDSQLLKTKDILQALQklsedKNLAEREELthklsIIT---------TKMDANDKKIQSLEKQLRlNCRAFS 293
Cdd:PRK11281   118 LSTLSLRQLESRLAQTLDQLQNAQ-----NDLAEYNSQ-----LVSlqtqperaqAALYANSQRLQQIRNLLK-GGKVGG 186
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1856631260  294 RQLAIETRKTLAAQTATKTLQVEvkhLQQKL 324
Cdd:PRK11281   187 KALRPSQRVLLQAEQALLNAQND---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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