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Conserved domains on  [gi|22122795|ref|NP_666341|]
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cytoplasmic dynein 1 light intermediate chain 1 [Mus musculus]

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 ...
 43-517 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: 817.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122795    43 EDGQNLWSCILSEVSTRSRSKLPTGKNVLLLGEDGAGKTSLIRRIQGIEEYKKGRGLEYLYLNVHDEDRDDQTRCNVWIL 122
Cdd:pfam05783   1 DEGQNLWSSILSEVSTRSRSKLPSGKNVLVLGEDGSGKTTLIAKLQGVEHPKKGRGLEYLYLNVHDEDRDDQTRCNVWIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122795   123 DGDLYHKGLLKFSLDALSLRDTLVMLVVDMSKPWTALDSLQKWASVVREHVDKLKIPPEEMKEMEQKLIRDFQEYVEPGE 202
Cdd:pfam05783  81 DGDLYHKGLLKFAVSAESLADTLVIFVVDMSRPWTWMESLQKWASVLREHIDKLKIPPEEMRELEQRLVKDFQEYVEPGE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122795   203 DFPASPQRRTTGAQEDRGDSVVLPLGADTLTHNLGLPVLVVCTKCDAISVLEKEHDYRDEHFDFIQSHIRKFCLQYGAAL 282
Cdd:pfam05783 161 DLPGSPQRRTPRLSGSDEDSVLLPLGENVLTHNLGIPVVVVCTKCDAMSVLEKEHDYRDEHFDFIQSHIRRFCLQYGAAL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122795   283 IYTSVKENKNIDLVYKYIVQKLYGFPYKIPAVVVEKDAVFIPAGWDNDKKIGILHENFQTLKVEDNFEDIITKPPVRKFV 362
Cdd:pfam05783 241 IYTSVKEEKNLDLLYKYLVHKIYGFPFRTPALVVEKDAVFIPAGWDNEKKIAILHENFQTVKPEDPYEDFIVKPPVRKLV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122795   363 HEKEIMAEDDQVFLMKLQSLLAKQPPTAAgRPVDASPRVPGGSPRTPNRSVSSNVASVSPIPAgSKKIDPNMKAGATSEG 442
Cdd:pfam05783 321 HDKEIQAEDEQVFLMKQQSLLAKQPATPT-RGVESPARSPSGSPRTTNRSGPANVASVSPQTS-VKKIDPNMKPGAASEG 398

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22122795   443 VLANFFNSLLSKKTgspGGPGVGGSPGGGAAGASPSLPPSAKKSGQKPVLSDVHAELDRITRKPASVSptTPTSP 517
Cdd:pfam05783 399 VLANFFNSLLSKKT---GSPGGGSPGGGTGSGRGSNVQDSAKKSGQKPVLTDVQAELDRMSRKPDSDV--TPNSQ 468
 
Name Accession Description Interval E-value
DLIC pfam05783
Dynein light intermediate chain (DLIC); This family consists of several eukaryotic dynein ...
 43-517 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: 817.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122795    43 EDGQNLWSCILSEVSTRSRSKLPTGKNVLLLGEDGAGKTSLIRRIQGIEEYKKGRGLEYLYLNVHDEDRDDQTRCNVWIL 122
Cdd:pfam05783   1 DEGQNLWSSILSEVSTRSRSKLPSGKNVLVLGEDGSGKTTLIAKLQGVEHPKKGRGLEYLYLNVHDEDRDDQTRCNVWIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122795   123 DGDLYHKGLLKFSLDALSLRDTLVMLVVDMSKPWTALDSLQKWASVVREHVDKLKIPPEEMKEMEQKLIRDFQEYVEPGE 202
Cdd:pfam05783  81 DGDLYHKGLLKFAVSAESLADTLVIFVVDMSRPWTWMESLQKWASVLREHIDKLKIPPEEMRELEQRLVKDFQEYVEPGE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122795   203 DFPASPQRRTTGAQEDRGDSVVLPLGADTLTHNLGLPVLVVCTKCDAISVLEKEHDYRDEHFDFIQSHIRKFCLQYGAAL 282
Cdd:pfam05783 161 DLPGSPQRRTPRLSGSDEDSVLLPLGENVLTHNLGIPVVVVCTKCDAMSVLEKEHDYRDEHFDFIQSHIRRFCLQYGAAL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122795   283 IYTSVKENKNIDLVYKYIVQKLYGFPYKIPAVVVEKDAVFIPAGWDNDKKIGILHENFQTLKVEDNFEDIITKPPVRKFV 362
Cdd:pfam05783 241 IYTSVKEEKNLDLLYKYLVHKIYGFPFRTPALVVEKDAVFIPAGWDNEKKIAILHENFQTVKPEDPYEDFIVKPPVRKLV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122795   363 HEKEIMAEDDQVFLMKLQSLLAKQPPTAAgRPVDASPRVPGGSPRTPNRSVSSNVASVSPIPAgSKKIDPNMKAGATSEG 442
Cdd:pfam05783 321 HDKEIQAEDEQVFLMKQQSLLAKQPATPT-RGVESPARSPSGSPRTTNRSGPANVASVSPQTS-VKKIDPNMKPGAASEG 398

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22122795   443 VLANFFNSLLSKKTgspGGPGVGGSPGGGAAGASPSLPPSAKKSGQKPVLSDVHAELDRITRKPASVSptTPTSP 517
Cdd:pfam05783 399 VLANFFNSLLSKKT---GSPGGGSPGGGTGSGRGSNVQDSAKKSGQKPVLTDVQAELDRMSRKPDSDV--TPNSQ 468
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
68-306 1.36e-05

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 45.74  E-value: 1.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122795  68 KNVLLLGEDGAGKTSLIRRIQG----IEEYK--KGRGLEYLYLNVHDEDRDdqtrcnVWILD--G-DLYHKgLLKFSLDA 138
Cdd:COG1100   4 KKIVVVGTGGVGKTSLVNRLVGdifsLEKYLstNGVTIDKKELKLDGLDVD------LVIWDtpGqDEFRE-TRQFYARQ 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122795 139 LSLRDtLVMLVVDMSKPWTaLDSLQKWASVVREhvdklkippeemkemeqklirdfqeyvepgedfpaspqrrttgaqed 218
Cdd:COG1100  77 LTGAS-LYLFVVDGTREET-LQSLYELLESLRR----------------------------------------------- 107

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122795 219 rgdsvvlplgadtltHNLGLPVLVVCTKCDAISVLEKEHDYRDEHFdfiqshirkFCLQYGAALIYTSVKENKNIDLVYK 298
Cdd:COG1100 108 ---------------LGKKSPIILVLNKIDLYDEEEIEDEERLKEA---------LSEDNIVEVVATSAKTGEGVEELFA 163


                ....*...
gi 22122795 299 YIVQKLYG 306
Cdd:COG1100 164 ALAEILRG 171
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
52-110 8.04e-04

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 41.61  E-value: 8.04e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 22122795   52 ILSEVSTrsrsKLPTGKNVLLLGEDGAGKTSLIRRIQGIEEYKKGrgleylYLNVHDED 110
Cdd:PRK10851  17 VLNDISL----DIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSG------HIRFHGTD 65
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 59-113 1.26e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 39.44  E-value: 1.26e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 22122795  59 RSRSKLPTGKNVLLLGEDGAGKTSLIRRiqgIEEYKKGRGLEYLYLNVHDEDRDD 113
Cdd:cd00009  11 REALELPPPKNLLLYGPPGTGKTTLARA---IANELFRPGAPFLYLNASDLLEGL 62
 
Name Accession Description Interval E-value
DLIC pfam05783
Dynein light intermediate chain (DLIC); This family consists of several eukaryotic dynein ...
 43-517 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: 817.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122795    43 EDGQNLWSCILSEVSTRSRSKLPTGKNVLLLGEDGAGKTSLIRRIQGIEEYKKGRGLEYLYLNVHDEDRDDQTRCNVWIL 122
Cdd:pfam05783   1 DEGQNLWSSILSEVSTRSRSKLPSGKNVLVLGEDGSGKTTLIAKLQGVEHPKKGRGLEYLYLNVHDEDRDDQTRCNVWIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122795   123 DGDLYHKGLLKFSLDALSLRDTLVMLVVDMSKPWTALDSLQKWASVVREHVDKLKIPPEEMKEMEQKLIRDFQEYVEPGE 202
Cdd:pfam05783  81 DGDLYHKGLLKFAVSAESLADTLVIFVVDMSRPWTWMESLQKWASVLREHIDKLKIPPEEMRELEQRLVKDFQEYVEPGE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122795   203 DFPASPQRRTTGAQEDRGDSVVLPLGADTLTHNLGLPVLVVCTKCDAISVLEKEHDYRDEHFDFIQSHIRKFCLQYGAAL 282
Cdd:pfam05783 161 DLPGSPQRRTPRLSGSDEDSVLLPLGENVLTHNLGIPVVVVCTKCDAMSVLEKEHDYRDEHFDFIQSHIRRFCLQYGAAL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122795   283 IYTSVKENKNIDLVYKYIVQKLYGFPYKIPAVVVEKDAVFIPAGWDNDKKIGILHENFQTLKVEDNFEDIITKPPVRKFV 362
Cdd:pfam05783 241 IYTSVKEEKNLDLLYKYLVHKIYGFPFRTPALVVEKDAVFIPAGWDNEKKIAILHENFQTVKPEDPYEDFIVKPPVRKLV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122795   363 HEKEIMAEDDQVFLMKLQSLLAKQPPTAAgRPVDASPRVPGGSPRTPNRSVSSNVASVSPIPAgSKKIDPNMKAGATSEG 442
Cdd:pfam05783 321 HDKEIQAEDEQVFLMKQQSLLAKQPATPT-RGVESPARSPSGSPRTTNRSGPANVASVSPQTS-VKKIDPNMKPGAASEG 398

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22122795   443 VLANFFNSLLSKKTgspGGPGVGGSPGGGAAGASPSLPPSAKKSGQKPVLSDVHAELDRITRKPASVSptTPTSP 517
Cdd:pfam05783 399 VLANFFNSLLSKKT---GSPGGGSPGGGTGSGRGSNVQDSAKKSGQKPVLTDVQAELDRMSRKPDSDV--TPNSQ 468
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
68-306 1.36e-05

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 45.74  E-value: 1.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122795  68 KNVLLLGEDGAGKTSLIRRIQG----IEEYK--KGRGLEYLYLNVHDEDRDdqtrcnVWILD--G-DLYHKgLLKFSLDA 138
Cdd:COG1100   4 KKIVVVGTGGVGKTSLVNRLVGdifsLEKYLstNGVTIDKKELKLDGLDVD------LVIWDtpGqDEFRE-TRQFYARQ 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122795 139 LSLRDtLVMLVVDMSKPWTaLDSLQKWASVVREhvdklkippeemkemeqklirdfqeyvepgedfpaspqrrttgaqed 218
Cdd:COG1100  77 LTGAS-LYLFVVDGTREET-LQSLYELLESLRR----------------------------------------------- 107

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122795 219 rgdsvvlplgadtltHNLGLPVLVVCTKCDAISVLEKEHDYRDEHFdfiqshirkFCLQYGAALIYTSVKENKNIDLVYK 298
Cdd:COG1100 108 ---------------LGKKSPIILVLNKIDLYDEEEIEDEERLKEA---------LSEDNIVEVVATSAKTGEGVEELFA 163


                ....*...
gi 22122795 299 YIVQKLYG 306
Cdd:COG1100 164 ALAEILRG 171
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
52-110 8.04e-04

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 41.61  E-value: 8.04e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 22122795   52 ILSEVSTrsrsKLPTGKNVLLLGEDGAGKTSLIRRIQGIEEYKKGrgleylYLNVHDED 110
Cdd:PRK10851  17 VLNDISL----DIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSG------HIRFHGTD 65
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 59-113 1.26e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 39.44  E-value: 1.26e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 22122795  59 RSRSKLPTGKNVLLLGEDGAGKTSLIRRiqgIEEYKKGRGLEYLYLNVHDEDRDD 113
Cdd:cd00009  11 REALELPPPKNLLLYGPPGTGKTTLARA---IANELFRPGAPFLYLNASDLLEGL 62
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 67-97 1.42e-03

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 39.44  E-value: 1.42e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 22122795  67 GKNVLLLGEDGAGKTSLIRRIQGIEEYKKGR 97
Cdd:cd03223  27 GDRLLITGPSGTGKSSLFRALAGLWPWGSGR 57
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 63-113 3.20e-03

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 38.40  E-value: 3.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 22122795    63 KLPTGKNVLLLGEDGAGKTSLIRRIQGIEEYKKGRgleyLYLNVHDEDRDD 113
Cdd:pfam00005   7 TLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGT----ILLDGQDLTDDE 53
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 64-97 6.14e-03

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 38.47  E-value: 6.14e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 22122795  64 LPTGKNVLLLGEDGAGKTSLIRRIQGIEEYKKGR 97
Cdd:cd03296  25 IPSGELVALLGPSGSGKTTLLRLIAGLERPDSGT 58
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 52-97 6.34e-03

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 37.61  E-value: 6.34e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 22122795  52 ILSEVSTrsrsKLPTGKNVLLLGEDGAGKTSLIRRIQGIEEYKKGR 97
Cdd:cd00267  14 ALDNVSL----TLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGE 55
Spg1 cd04128
Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in ...
 238-315 7.77e-03

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: 37.76  E-value: 7.77e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22122795 238 LPVLVvCTKCDAISVLEKEhdYRDEhfdfIQSHIRKFCLQYGAALIYTSVKENKNIDLVYKYIVQKLYGFPYKIPAVV 315
Cdd:cd04128 106 IPILV-GTKYDLFADLPPE--EQEE----ITKQARKYAKAMKAPLIFCSTSHSINVQKIFKFVLAKVFDLPLTIPEIL 176
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 237-302 7.84e-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: 37.44  E-value: 7.84e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22122795 237 GLPVLVVCTKCDAISVLEKEHDYRdehfdfiqshIRKFCLQYGAALIYTSVKENKNIDLVYKYIVQ 302
Cdd:cd00882 106 GIPIILVGNKIDLLEEREVEELLR----------LEELAKILGVPVFEVSAKTGEGVDELFEKLIE 161
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 234-304 8.82e-03

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 37.23  E-value: 8.82e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22122795 234 HNLGLPVLVVCTKCDAISVLEKEHDYRDehfdfiqshiRKFCLQYGAALIYTSVKENKNIDLVYKYIVQKL 304
Cdd:cd00880 101 RERGKPVLLVLNKIDLVPESEEEELLRE----------RKLELLPDLPVIAVSALPGEGIDELRKKIAELL 161
 
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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