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Conserved domains on  [gi|26986541|ref|NP_758460|]
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cytoplasmic dynein 2 light intermediate chain 1 [Mus musculus]

Protein Classification

dynein light intermediate chain family protein( domain architecture ID 706898)

dynein light intermediate chain (DLIC) family protein is a non-catalytic accessory component of the cytoplasmic dynein 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
PubMed:  29515126|34014309|18466635|15037233

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DLIC super family cl25911
Dynein light intermediate chain (DLIC); This family consists of several eukaryotic dynein ...
 2-268 5.24e-08

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.


The actual alignment was detected with superfamily member pfam05783:

Pssm-ID: 368612  Cd Length: 468  Bit Score: 54.08  E-value: 5.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986541     2 PSETLWEIAKAEVEKR-RSHGSEGdgaeigeKSVFFIGSKNGGKTTIILRcLDRDESAKPTLALEYTYgrkTKGHNTPKD 80
Cdd:pfam05783   2 EGQNLWSSILSEVSTRsRSKLPSG-------KNVLVLGEDGSGKTTLIAK-LQGVEHPKKGRGLEYLY---LNVHDEDRD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986541    81 ---IAHFWELGGGTSLLDLISIPITVDTLRTFSIVLVLDLSKPndlWSTMENLLQATK---SHVDKVimklgKTSSKASA 154
Cdd:pfam05783  71 dqtRCNVWILDGDLYHKGLLKFAVSAESLADTLVIFVVDMSRP---WTWMESLQKWASvlrEHIDKL-----KIPPEEMR 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986541   155 EMRQRMWSVVQ--------------KDHPDRELID------PFP---------IPLVIIGSKYDIF------QDFDPEKR 199
Cdd:pfam05783 143 ELEQRLVKDFQeyvepgedlpgspqRRTPRLSGSDedsvllPLGenvlthnlgIPVVVVCTKCDAMsvlekeHDYRDEHF 222

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26986541   200 KVICKTLRFVAHYYGASLMFTSKSEA----LLLKirgVINQLAFGIDKSKSICVDQNKPLFITAGLDSLCQIG 268
Cdd:pfam05783 223 DFIQSHIRRFCLQYGAALIYTSVKEEknldLLYK---YLVHKIYGFPFRTPALVVEKDAVFIPAGWDNEKKIA 292
 
Name Accession Description Interval E-value
DLIC pfam05783
Dynein light intermediate chain (DLIC); This family consists of several eukaryotic dynein ...
 2-268 5.24e-08

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: 54.08  E-value: 5.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986541     2 PSETLWEIAKAEVEKR-RSHGSEGdgaeigeKSVFFIGSKNGGKTTIILRcLDRDESAKPTLALEYTYgrkTKGHNTPKD 80
Cdd:pfam05783   2 EGQNLWSSILSEVSTRsRSKLPSG-------KNVLVLGEDGSGKTTLIAK-LQGVEHPKKGRGLEYLY---LNVHDEDRD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986541    81 ---IAHFWELGGGTSLLDLISIPITVDTLRTFSIVLVLDLSKPndlWSTMENLLQATK---SHVDKVimklgKTSSKASA 154
Cdd:pfam05783  71 dqtRCNVWILDGDLYHKGLLKFAVSAESLADTLVIFVVDMSRP---WTWMESLQKWASvlrEHIDKL-----KIPPEEMR 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986541   155 EMRQRMWSVVQ--------------KDHPDRELID------PFP---------IPLVIIGSKYDIF------QDFDPEKR 199
Cdd:pfam05783 143 ELEQRLVKDFQeyvepgedlpgspqRRTPRLSGSDedsvllPLGenvlthnlgIPVVVVCTKCDAMsvlekeHDYRDEHF 222

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26986541   200 KVICKTLRFVAHYYGASLMFTSKSEA----LLLKirgVINQLAFGIDKSKSICVDQNKPLFITAGLDSLCQIG 268
Cdd:pfam05783 223 DFIQSHIRRFCLQYGAALIYTSVKEEknldLLYK---YLVHKIYGFPFRTPALVVEKDAVFIPAGWDNEKKIA 292
Spg1 cd04128
Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in ...
 37-241 2.52e-05

Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in the fission yeast S. pombe, where it regulates septum formation in the septation initiation network (SIN) through the cdc7 protein kinase. Spg1p is an essential gene that localizes to the spindle pole bodies. When GTP-bound, it binds cdc7 and causes it to translocate to spindle poles. Sid4p (septation initiation defective) is required for localization of Spg1p to the spindle pole body, and the ability of Spg1p to promote septum formation from any point in the cell cycle depends on Sid4p. Spg1p is negatively regulated by Byr4 and cdc16, which form a two-component GTPase activating protein (GAP) for Spg1p. The existence of a SIN-related pathway in plants has been proposed. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization.


Pssm-ID: 206701 [Multi-domain]  Cd Length: 182  Bit Score: 44.31  E-value: 2.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986541  37 IGSKNGGKTTIILRCL--DRDESAKPTLALEYTyGRKTKGHNTPKdIAHFWELGGGTSLLDLIsiPITVDTLRtfSIVLV 114
Cdd:cd04128   6 LGDAQIGKTSLMVKYVegEFDEEYIQTLGVNFM-EKTISIRGTEI-TFSIWDLGGQREFINML--PLVCKDAV--AILFM 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986541 115 LDLSKPNDLWSTMENLLQATKshvdkvimkLGKTSskasaemrqrmwsvvqkdhpdrelidpfpIPlVIIGSKYDIFQDF 194
Cdd:cd04128  80 FDLTRKSTLNSIKEWYRQARG---------FNKTA-----------------------------IP-ILVGTKYDLFADL 120

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 26986541 195 DPEKRKVICKTLRFVAHYYGASLMFTSKSEAL-LLKIRGVINQLAFGI 241
Cdd:cd04128 121 PPEEQEEITKQARKYAKAMKAPLIFCSTSHSInVQKIFKFVLAKVFDL 168
 
Name Accession Description Interval E-value
DLIC pfam05783
Dynein light intermediate chain (DLIC); This family consists of several eukaryotic dynein ...
 2-268 5.24e-08

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: 54.08  E-value: 5.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986541     2 PSETLWEIAKAEVEKR-RSHGSEGdgaeigeKSVFFIGSKNGGKTTIILRcLDRDESAKPTLALEYTYgrkTKGHNTPKD 80
Cdd:pfam05783   2 EGQNLWSSILSEVSTRsRSKLPSG-------KNVLVLGEDGSGKTTLIAK-LQGVEHPKKGRGLEYLY---LNVHDEDRD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986541    81 ---IAHFWELGGGTSLLDLISIPITVDTLRTFSIVLVLDLSKPndlWSTMENLLQATK---SHVDKVimklgKTSSKASA 154
Cdd:pfam05783  71 dqtRCNVWILDGDLYHKGLLKFAVSAESLADTLVIFVVDMSRP---WTWMESLQKWASvlrEHIDKL-----KIPPEEMR 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986541   155 EMRQRMWSVVQ--------------KDHPDRELID------PFP---------IPLVIIGSKYDIF------QDFDPEKR 199
Cdd:pfam05783 143 ELEQRLVKDFQeyvepgedlpgspqRRTPRLSGSDedsvllPLGenvlthnlgIPVVVVCTKCDAMsvlekeHDYRDEHF 222

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26986541   200 KVICKTLRFVAHYYGASLMFTSKSEA----LLLKirgVINQLAFGIDKSKSICVDQNKPLFITAGLDSLCQIG 268
Cdd:pfam05783 223 DFIQSHIRRFCLQYGAALIYTSVKEEknldLLYK---YLVHKIYGFPFRTPALVVEKDAVFIPAGWDNEKKIA 292
Spg1 cd04128
Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in ...
 37-241 2.52e-05

Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in the fission yeast S. pombe, where it regulates septum formation in the septation initiation network (SIN) through the cdc7 protein kinase. Spg1p is an essential gene that localizes to the spindle pole bodies. When GTP-bound, it binds cdc7 and causes it to translocate to spindle poles. Sid4p (septation initiation defective) is required for localization of Spg1p to the spindle pole body, and the ability of Spg1p to promote septum formation from any point in the cell cycle depends on Sid4p. Spg1p is negatively regulated by Byr4 and cdc16, which form a two-component GTPase activating protein (GAP) for Spg1p. The existence of a SIN-related pathway in plants has been proposed. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization.


Pssm-ID: 206701 [Multi-domain]  Cd Length: 182  Bit Score: 44.31  E-value: 2.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986541  37 IGSKNGGKTTIILRCL--DRDESAKPTLALEYTyGRKTKGHNTPKdIAHFWELGGGTSLLDLIsiPITVDTLRtfSIVLV 114
Cdd:cd04128   6 LGDAQIGKTSLMVKYVegEFDEEYIQTLGVNFM-EKTISIRGTEI-TFSIWDLGGQREFINML--PLVCKDAV--AILFM 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26986541 115 LDLSKPNDLWSTMENLLQATKshvdkvimkLGKTSskasaemrqrmwsvvqkdhpdrelidpfpIPlVIIGSKYDIFQDF 194
Cdd:cd04128  80 FDLTRKSTLNSIKEWYRQARG---------FNKTA-----------------------------IP-ILVGTKYDLFADL 120

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 26986541 195 DPEKRKVICKTLRFVAHYYGASLMFTSKSEAL-LLKIRGVINQLAFGI 241
Cdd:cd04128 121 PPEEQEEITKQARKYAKAMKAPLIFCSTSHSInVQKIFKFVLAKVFDL 168
 
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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