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Conserved domains on  [gi|47551013|ref|NP_999680|]
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33 kDa inner dynein arm light chain, axonemal [Strongylocentrotus purpuratus]

Protein Classification

dynein arm light chain( domain architecture ID 11185876)

axonemal dynein arm light chain plays a dynamic role in flagellar and cilia motility

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ax_dynein_light pfam10211
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ...
67-253 3.57e-123

Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organizms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.


:

Pssm-ID: 463000 [Multi-domain]  Cd Length: 187  Bit Score: 348.02  E-value: 3.57e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47551013    67 DEILNSILPPREWTESGQLWVQQVSSTPATRLDVVNLQEQLDMRLQQRQARETGICPVRRELYSQCFDELIRQVTIECAE 146
Cdd:pfam10211   1 EDILNSILPPREWEEDGQLWIQQVSSTPATRLDVINLQEKLDTRLQQRQARETGICPIREELYSQCFDELIRQVTINCPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47551013   147 RGLLLLRVRDEIRMTIAAYQTLYESSVAFGMRKALQAEQGKSDMEKKITDLGQEKRELERQVNELKAKCEAIEKREAERR 226
Cdd:pfam10211  81 RGLLLLRVRDELRMTIAAYQTLYESSVAFGMRKALQAEQGKAELEKKIADLEEEKEELEKQVAELKAKCEAIEKREEERR 160
                         170       180
                  ....*....|....*....|....*..
gi 47551013   227 QVEEKKHAEEIQFLKRTNQQLKTQLEG 253
Cdd:pfam10211 161 QAEEKKHAEEIAFLKKTNQQLKAQLER 187
 
Name Accession Description Interval E-value
Ax_dynein_light pfam10211
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ...
67-253 3.57e-123

Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organizms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.


Pssm-ID: 463000 [Multi-domain]  Cd Length: 187  Bit Score: 348.02  E-value: 3.57e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47551013    67 DEILNSILPPREWTESGQLWVQQVSSTPATRLDVVNLQEQLDMRLQQRQARETGICPVRRELYSQCFDELIRQVTIECAE 146
Cdd:pfam10211   1 EDILNSILPPREWEEDGQLWIQQVSSTPATRLDVINLQEKLDTRLQQRQARETGICPIREELYSQCFDELIRQVTINCPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47551013   147 RGLLLLRVRDEIRMTIAAYQTLYESSVAFGMRKALQAEQGKSDMEKKITDLGQEKRELERQVNELKAKCEAIEKREAERR 226
Cdd:pfam10211  81 RGLLLLRVRDELRMTIAAYQTLYESSVAFGMRKALQAEQGKAELEKKIADLEEEKEELEKQVAELKAKCEAIEKREEERR 160
                         170       180
                  ....*....|....*....|....*..
gi 47551013   227 QVEEKKHAEEIQFLKRTNQQLKTQLEG 253
Cdd:pfam10211 161 QAEEKKHAEEIAFLKKTNQQLKAQLER 187
PTZ00121 PTZ00121
MAEBL; Provisional
146-252 5.47e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.20  E-value: 5.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47551013   146 ERGLLLLRVRDEIRMTIAAYQTLY----ESSVAFGMRKALQ---AEQGKSDMEKKITDLGQEKRELERQVNELKAKCEAI 218
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAikaeEARKADELKKAEEkkkADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1327
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 47551013   219 EKR-EAERRQVEEKKHAEEIQflKRTNQQLKTQLE 252
Cdd:PTZ00121 1328 KKKaDAAKKKAEEAKKAAEAA--KAEAEAAADEAE 1360
 
Name Accession Description Interval E-value
Ax_dynein_light pfam10211
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ...
67-253 3.57e-123

Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organizms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.


Pssm-ID: 463000 [Multi-domain]  Cd Length: 187  Bit Score: 348.02  E-value: 3.57e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47551013    67 DEILNSILPPREWTESGQLWVQQVSSTPATRLDVVNLQEQLDMRLQQRQARETGICPVRRELYSQCFDELIRQVTIECAE 146
Cdd:pfam10211   1 EDILNSILPPREWEEDGQLWIQQVSSTPATRLDVINLQEKLDTRLQQRQARETGICPIREELYSQCFDELIRQVTINCPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47551013   147 RGLLLLRVRDEIRMTIAAYQTLYESSVAFGMRKALQAEQGKSDMEKKITDLGQEKRELERQVNELKAKCEAIEKREAERR 226
Cdd:pfam10211  81 RGLLLLRVRDELRMTIAAYQTLYESSVAFGMRKALQAEQGKAELEKKIADLEEEKEELEKQVAELKAKCEAIEKREEERR 160
                         170       180
                  ....*....|....*....|....*..
gi 47551013   227 QVEEKKHAEEIQFLKRTNQQLKTQLEG 253
Cdd:pfam10211 161 QAEEKKHAEEIAFLKKTNQQLKAQLER 187
PTZ00121 PTZ00121
MAEBL; Provisional
146-252 5.47e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.20  E-value: 5.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47551013   146 ERGLLLLRVRDEIRMTIAAYQTLY----ESSVAFGMRKALQ---AEQGKSDMEKKITDLGQEKRELERQVNELKAKCEAI 218
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAikaeEARKADELKKAEEkkkADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1327
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 47551013   219 EKR-EAERRQVEEKKHAEEIQflKRTNQQLKTQLE 252
Cdd:PTZ00121 1328 KKKaDAAKKKAEEAKKAAEAA--KAEAEAAADEAE 1360
PTZ00121 PTZ00121
MAEBL; Provisional
178-252 6.03e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 6.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47551013   178 RKALQAEQGKSDMEKKITDL---GQEKR---ELERQVNELKAKCEAIEKREAERRQVEE-KKHAEEiqflKRTNQQLKTQ 250
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAkkkAEEKKkadEAKKKAEEDKKKADELKKAAAAKKKADEaKKKAEE----KKKADEAKKK 1439

                  ..
gi 47551013   251 LE 252
Cdd:PTZ00121 1440 AE 1441
PTZ00121 PTZ00121
MAEBL; Provisional
184-238 7.32e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 7.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 47551013   184 EQGKSDMEKKITDLGQEKRELERQVNELKAKCEAIEKREAERRQVEEKKHAEEIQ 238
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAK 1463
PTZ00121 PTZ00121
MAEBL; Provisional
178-238 8.00e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.43  E-value: 8.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47551013   178 RKALQAEQgKSDMEKKITDLGQEKRELERQVNELKAKCEAIEKREAERRQVEEKKHAEEIQ 238
Cdd:PTZ00121 1391 KKADEAKK-KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK 1450
 
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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