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Conserved domains on  [gi|1021589368|ref|NP_001310884|]
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cytoplasmic dynein 1 light intermediate chain 2 isoform 3 [Homo sapiens]

Protein Classification

cytoplasmic dynein 1 light intermediate chain( domain architecture ID 12066078)

cytoplasmic dynein 1 light intermediate chain is a non-catalytic accessory component of the cytoplasmic dynein 1 complex and may be involved in linking dynein to cargos and to adapter proteins that regulate dynein function

CATH:  3.40.50.300
Gene Ontology:  GO:0005524|GO:0045504|GO:0005868|GO:0016020|GO:0007018
PubMed:  29515126|34014309|18466635|15037233

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DLIC pfam05783
Dynein light intermediate chain (DLIC); This family consists of several eukaryotic dynein ...
 30-449 0e+00

Dynein light intermediate chain (DLIC); This family consists of several eukaryotic dynein light intermediate chain proteins. The light intermediate chains (LICs) of cytoplasmic dynein consist of multiple isoforms, which undergo post-translational modification to produce a large number of species. DLIC1 is known to be involved in assembly, organization, and function of centrosomes and mitotic spindles when bound to pericentrin. DLIC2 is a subunit of cytoplasmic dynein 2 that may play a role in maintaining Golgi organization by binding cytoplasmic dynein 2 to its Golgi-associated cargo.


:

Pssm-ID: 368612  Cd Length: 468  Bit Score: 806.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589368  30 EEGQSLWSSILSEVSTRARSKLPSGKNILVF---------------------------------------DHTRCNVWIL 70
Cdd:pfam05783   1 DEGQNLWSSILSEVSTRSRSKLPSGKNVLVLgedgsgkttliaklqgvehpkkgrgleylylnvhdedrdDQTRCNVWIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589368  71 DGDLYHKGLLKFAVSAESLPETLVIFVADMSRPWTVMESLQKWASVLREHIDKMKIPPEKMRELERKFVKDFQDYMEPEE 150
Cdd:pfam05783  81 DGDLYHKGLLKFAVSAESLADTLVIFVVDMSRPWTWMESLQKWASVLREHIDKLKIPPEEMRELEQRLVKDFQEYVEPGE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589368 151 GCQGSPQRRGPLTSGSDEENVALPLGDNVLTHNLGIPVLVVCTKCDAVSVLEKEHDYRDEHLDFIQSHLRRFCLQYGAAL 230
Cdd:pfam05783 161 DLPGSPQRRTPRLSGSDEDSVLLPLGENVLTHNLGIPVVVVCTKCDAMSVLEKEHDYRDEHFDFIQSHIRRFCLQYGAAL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589368 231 IYTSVKEEKNLDLLYKYIVHKTYGFHFTTPALVVEKDAVFIPAGWDNEKKIAILHENFTTVKPEDAYEDFIVKPPVRKLV 310
Cdd:pfam05783 241 IYTSVKEEKNLDLLYKYLVHKIYGFPFRTPALVVEKDAVFIPAGWDNEKKIAILHENFQTVKPEDPYEDFIVKPPVRKLV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589368 311 HDKELAAEDEQVFLMKQQSLLAKQPATPTRASESPARGPSGSPRTQGRGGPASVPSSSPGTSVKKPDPNIKNNAASEGVL 390
Cdd:pfam05783 321 HDKEIQAEDEQVFLMKQQSLLAKQPATPTRGVESPARSPSGSPRTTNRSGPANVASVSPQTSVKKIDPNMKPGAASEGVL 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021589368 391 ASFFNSLLSKKTGSPGSPGA---------GGVQSTAKKSGQKTVLSNVQEELDRMTRKPDSMVTNSST 449
Cdd:pfam05783 401 ANFFNSLLSKKTGSPGGGSPgggtgsgrgSNVQDSAKKSGQKPVLTDVQAELDRMSRKPDSDVTPNSQ 468
 
Name Accession Description Interval E-value
DLIC pfam05783
Dynein light intermediate chain (DLIC); This family consists of several eukaryotic dynein ...
 30-449 0e+00

Dynein light intermediate chain (DLIC); This family consists of several eukaryotic dynein light intermediate chain proteins. The light intermediate chains (LICs) of cytoplasmic dynein consist of multiple isoforms, which undergo post-translational modification to produce a large number of species. DLIC1 is known to be involved in assembly, organization, and function of centrosomes and mitotic spindles when bound to pericentrin. DLIC2 is a subunit of cytoplasmic dynein 2 that may play a role in maintaining Golgi organization by binding cytoplasmic dynein 2 to its Golgi-associated cargo.


Pssm-ID: 368612  Cd Length: 468  Bit Score: 806.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589368  30 EEGQSLWSSILSEVSTRARSKLPSGKNILVF---------------------------------------DHTRCNVWIL 70
Cdd:pfam05783   1 DEGQNLWSSILSEVSTRSRSKLPSGKNVLVLgedgsgkttliaklqgvehpkkgrgleylylnvhdedrdDQTRCNVWIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589368  71 DGDLYHKGLLKFAVSAESLPETLVIFVADMSRPWTVMESLQKWASVLREHIDKMKIPPEKMRELERKFVKDFQDYMEPEE 150
Cdd:pfam05783  81 DGDLYHKGLLKFAVSAESLADTLVIFVVDMSRPWTWMESLQKWASVLREHIDKLKIPPEEMRELEQRLVKDFQEYVEPGE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589368 151 GCQGSPQRRGPLTSGSDEENVALPLGDNVLTHNLGIPVLVVCTKCDAVSVLEKEHDYRDEHLDFIQSHLRRFCLQYGAAL 230
Cdd:pfam05783 161 DLPGSPQRRTPRLSGSDEDSVLLPLGENVLTHNLGIPVVVVCTKCDAMSVLEKEHDYRDEHFDFIQSHIRRFCLQYGAAL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589368 231 IYTSVKEEKNLDLLYKYIVHKTYGFHFTTPALVVEKDAVFIPAGWDNEKKIAILHENFTTVKPEDAYEDFIVKPPVRKLV 310
Cdd:pfam05783 241 IYTSVKEEKNLDLLYKYLVHKIYGFPFRTPALVVEKDAVFIPAGWDNEKKIAILHENFQTVKPEDPYEDFIVKPPVRKLV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589368 311 HDKELAAEDEQVFLMKQQSLLAKQPATPTRASESPARGPSGSPRTQGRGGPASVPSSSPGTSVKKPDPNIKNNAASEGVL 390
Cdd:pfam05783 321 HDKEIQAEDEQVFLMKQQSLLAKQPATPTRGVESPARSPSGSPRTTNRSGPANVASVSPQTSVKKIDPNMKPGAASEGVL 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021589368 391 ASFFNSLLSKKTGSPGSPGA---------GGVQSTAKKSGQKTVLSNVQEELDRMTRKPDSMVTNSST 449
Cdd:pfam05783 401 ANFFNSLLSKKTGSPGGGSPgggtgsgrgSNVQDSAKKSGQKPVLTDVQAELDRMSRKPDSDVTPNSQ 468
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 179-255 1.90e-03

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 39.69  E-value: 1.90e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021589368 179 VLTHNLGIPVLVVCTKCDAVSvlekehdyrDEHLDFIQSHLRrfclQYGAALIYTSVKEEKNLDLLYKYIVHKTYGF 255
Cdd:cd01854    27 VAAEASGIEPVIVLNKADLVD---------DEELEELLEIYE----KLGYPVLAVSAKTGEGLDELRELLKGKTSVL 90
 
Name Accession Description Interval E-value
DLIC pfam05783
Dynein light intermediate chain (DLIC); This family consists of several eukaryotic dynein ...
 30-449 0e+00

Dynein light intermediate chain (DLIC); This family consists of several eukaryotic dynein light intermediate chain proteins. The light intermediate chains (LICs) of cytoplasmic dynein consist of multiple isoforms, which undergo post-translational modification to produce a large number of species. DLIC1 is known to be involved in assembly, organization, and function of centrosomes and mitotic spindles when bound to pericentrin. DLIC2 is a subunit of cytoplasmic dynein 2 that may play a role in maintaining Golgi organization by binding cytoplasmic dynein 2 to its Golgi-associated cargo.


Pssm-ID: 368612  Cd Length: 468  Bit Score: 806.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589368  30 EEGQSLWSSILSEVSTRARSKLPSGKNILVF---------------------------------------DHTRCNVWIL 70
Cdd:pfam05783   1 DEGQNLWSSILSEVSTRSRSKLPSGKNVLVLgedgsgkttliaklqgvehpkkgrgleylylnvhdedrdDQTRCNVWIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589368  71 DGDLYHKGLLKFAVSAESLPETLVIFVADMSRPWTVMESLQKWASVLREHIDKMKIPPEKMRELERKFVKDFQDYMEPEE 150
Cdd:pfam05783  81 DGDLYHKGLLKFAVSAESLADTLVIFVVDMSRPWTWMESLQKWASVLREHIDKLKIPPEEMRELEQRLVKDFQEYVEPGE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589368 151 GCQGSPQRRGPLTSGSDEENVALPLGDNVLTHNLGIPVLVVCTKCDAVSVLEKEHDYRDEHLDFIQSHLRRFCLQYGAAL 230
Cdd:pfam05783 161 DLPGSPQRRTPRLSGSDEDSVLLPLGENVLTHNLGIPVVVVCTKCDAMSVLEKEHDYRDEHFDFIQSHIRRFCLQYGAAL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589368 231 IYTSVKEEKNLDLLYKYIVHKTYGFHFTTPALVVEKDAVFIPAGWDNEKKIAILHENFTTVKPEDAYEDFIVKPPVRKLV 310
Cdd:pfam05783 241 IYTSVKEEKNLDLLYKYLVHKIYGFPFRTPALVVEKDAVFIPAGWDNEKKIAILHENFQTVKPEDPYEDFIVKPPVRKLV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589368 311 HDKELAAEDEQVFLMKQQSLLAKQPATPTRASESPARGPSGSPRTQGRGGPASVPSSSPGTSVKKPDPNIKNNAASEGVL 390
Cdd:pfam05783 321 HDKEIQAEDEQVFLMKQQSLLAKQPATPTRGVESPARSPSGSPRTTNRSGPANVASVSPQTSVKKIDPNMKPGAASEGVL 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021589368 391 ASFFNSLLSKKTGSPGSPGA---------GGVQSTAKKSGQKTVLSNVQEELDRMTRKPDSMVTNSST 449
Cdd:pfam05783 401 ANFFNSLLSKKTGSPGGGSPgggtgsgrgSNVQDSAKKSGQKPVLTDVQAELDRMSRKPDSDVTPNSQ 468
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 179-255 1.90e-03

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 39.69  E-value: 1.90e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021589368 179 VLTHNLGIPVLVVCTKCDAVSvlekehdyrDEHLDFIQSHLRrfclQYGAALIYTSVKEEKNLDLLYKYIVHKTYGF 255
Cdd:cd01854    27 VAAEASGIEPVIVLNKADLVD---------DEELEELLEIYE----KLGYPVLAVSAKTGEGLDELRELLKGKTSVL 90
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 185-250 2.57e-03

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 38.59  E-value: 2.57e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021589368 185 GIPVLVVCTKCDAVSVLEKEHDYRdehldfiqshLRRFCLQYGAALIYTSVKEEKNLDLLYKYIVH 250
Cdd:cd00882   106 GIPIILVGNKIDLLEEREVEELLR----------LEELAKILGVPVFEVSAKTGEGVDELFEKLIE 161
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 182-252 5.19e-03

YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 37.88  E-value: 5.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021589368 182 HNLGIPVLVVCTKCDAVSvlekeHDYRDEHLDFIQSHLRRFCLQYGaaLIYTSVKEEKNLDLLYKYIVHKT 252
Cdd:cd01876   107 EELGIPFLIVLTKADKLK-----KSELAKVLKKIKEELNLFNILPP--VILFSSKKGTGIDELRALIAEWL 170
 
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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