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Conserved domains on  [gi|8922256|ref|NP_060480|]
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intraflagellar transport protein 57 homolog [Homo sapiens]

Protein Classification

IFT57 family protein( domain architecture ID 12106430)

intraflagellar transport protein 57 (IFT57) family protein similar to Homo sapiens intraflagellar transport protein 57 homolog and Caenorhabditis elegans intraflagellar transport protein che-13

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
IFT57 pfam10498
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ...
44-401 0e+00

Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles found at the periphery of cells of diverse organizms. Intra-flagellar transport (IFT) is required for the assembly and maintenance of eukaryotic cilia and flagella, and consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits. IFT57 is part of complex B but is not, however, required for the core subunits to stay associated. This protein is known as Huntington-interacting protein-1 in humans.


:

Pssm-ID: 463118 [Multi-domain]  Cd Length: 360  Bit Score: 543.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922256     44 MEDLVEKLKLLRYEEEFLRKSNLKAPSRHYFAL-PTNPGEQFYMFCTLAAWLINKAGRPFEQPQEYDDPNATISNILSEL 122
Cdd:pfam10498   1 MEDLLEKLKLLNYEKEFCKPLKMKPLSRYYFALlSTNPGEQFYYFTSLAAWLISLAGKSFEQPQEYDDPNATISNILDEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922256    123 RSFGRTADFPPSKLKSGYGEHVCYVLDCFAEEALKYIGFTWKRPIYPVEELEEES--VAEDDAELTLNKVDEEfVEEETD 200
Cdd:pfam10498  81 KKLGIKVDFPPSKLKQGYGEHVCYVLDDLADEALKRKNFKWKKPKYPPEEEFEEEdvVEEDDAELTLEKVEEE-MLIEGD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922256    201 NEENFIDLNVLKAQTYHLDMNETAKQEDILESTTDAAEWSLEVERVLPQLKVTIRTDNKDWRIHVDQMHQHRSGIESALK 280
Cdd:pfam10498 160 DFKEDDEDEDLYNESTKGEEAESSKPREIIESNVDAAEWKLELERVLPQLKVTIKADAKDWRAHLEQMKQHKKSIEESLP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922256    281 ETKGFLDKLHNEITRTLEKISSREKYINNQLENLVQEYRAAQAQLSEAKERYQQGNGGVTERTRLLSEVMEELEKVKQEM 360
Cdd:pfam10498 240 DTKSQLDKLHTDISKTLEKIESREKYINSQLEPLIQEYREAQDELSEVQEKYKQLSEGVTERTRELAEITEELEKVKQEM 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 8922256    361 EEKGSSMTDGAPLVKIKQSLTKLKQETVEMDIRIGIVEHTL 401
Cdd:pfam10498 320 EERGSSMTDGSPLVKIKQALTKLKEEIKQMDLRIGVLQHTL 360
 
Name Accession Description Interval E-value
IFT57 pfam10498
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ...
44-401 0e+00

Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles found at the periphery of cells of diverse organizms. Intra-flagellar transport (IFT) is required for the assembly and maintenance of eukaryotic cilia and flagella, and consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits. IFT57 is part of complex B but is not, however, required for the core subunits to stay associated. This protein is known as Huntington-interacting protein-1 in humans.


Pssm-ID: 463118 [Multi-domain]  Cd Length: 360  Bit Score: 543.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922256     44 MEDLVEKLKLLRYEEEFLRKSNLKAPSRHYFAL-PTNPGEQFYMFCTLAAWLINKAGRPFEQPQEYDDPNATISNILSEL 122
Cdd:pfam10498   1 MEDLLEKLKLLNYEKEFCKPLKMKPLSRYYFALlSTNPGEQFYYFTSLAAWLISLAGKSFEQPQEYDDPNATISNILDEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922256    123 RSFGRTADFPPSKLKSGYGEHVCYVLDCFAEEALKYIGFTWKRPIYPVEELEEES--VAEDDAELTLNKVDEEfVEEETD 200
Cdd:pfam10498  81 KKLGIKVDFPPSKLKQGYGEHVCYVLDDLADEALKRKNFKWKKPKYPPEEEFEEEdvVEEDDAELTLEKVEEE-MLIEGD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922256    201 NEENFIDLNVLKAQTYHLDMNETAKQEDILESTTDAAEWSLEVERVLPQLKVTIRTDNKDWRIHVDQMHQHRSGIESALK 280
Cdd:pfam10498 160 DFKEDDEDEDLYNESTKGEEAESSKPREIIESNVDAAEWKLELERVLPQLKVTIKADAKDWRAHLEQMKQHKKSIEESLP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922256    281 ETKGFLDKLHNEITRTLEKISSREKYINNQLENLVQEYRAAQAQLSEAKERYQQGNGGVTERTRLLSEVMEELEKVKQEM 360
Cdd:pfam10498 240 DTKSQLDKLHTDISKTLEKIESREKYINSQLEPLIQEYREAQDELSEVQEKYKQLSEGVTERTRELAEITEELEKVKQEM 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 8922256    361 EEKGSSMTDGAPLVKIKQSLTKLKQETVEMDIRIGIVEHTL 401
Cdd:pfam10498 320 EERGSSMTDGSPLVKIKQALTKLKEEIKQMDLRIGVLQHTL 360
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
276-368 7.99e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 7.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922256  276 ESALKETKGFLDKLHNEITRTLEKISSrekyINNQLENLVQEYRAAQAQLSEAKERYQQGNGGVTERTRLLSEVMEELEK 355
Cdd:COG3883  15 DPQIQAKQKELSELQAELEAAQAELDA----LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
                        90
                ....*....|...
gi 8922256  356 VKQEMEEKGSSMT 368
Cdd:COG3883  91 RARALYRSGGSVS 103
 
Name Accession Description Interval E-value
IFT57 pfam10498
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ...
44-401 0e+00

Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles found at the periphery of cells of diverse organizms. Intra-flagellar transport (IFT) is required for the assembly and maintenance of eukaryotic cilia and flagella, and consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits. IFT57 is part of complex B but is not, however, required for the core subunits to stay associated. This protein is known as Huntington-interacting protein-1 in humans.


Pssm-ID: 463118 [Multi-domain]  Cd Length: 360  Bit Score: 543.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922256     44 MEDLVEKLKLLRYEEEFLRKSNLKAPSRHYFAL-PTNPGEQFYMFCTLAAWLINKAGRPFEQPQEYDDPNATISNILSEL 122
Cdd:pfam10498   1 MEDLLEKLKLLNYEKEFCKPLKMKPLSRYYFALlSTNPGEQFYYFTSLAAWLISLAGKSFEQPQEYDDPNATISNILDEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922256    123 RSFGRTADFPPSKLKSGYGEHVCYVLDCFAEEALKYIGFTWKRPIYPVEELEEES--VAEDDAELTLNKVDEEfVEEETD 200
Cdd:pfam10498  81 KKLGIKVDFPPSKLKQGYGEHVCYVLDDLADEALKRKNFKWKKPKYPPEEEFEEEdvVEEDDAELTLEKVEEE-MLIEGD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922256    201 NEENFIDLNVLKAQTYHLDMNETAKQEDILESTTDAAEWSLEVERVLPQLKVTIRTDNKDWRIHVDQMHQHRSGIESALK 280
Cdd:pfam10498 160 DFKEDDEDEDLYNESTKGEEAESSKPREIIESNVDAAEWKLELERVLPQLKVTIKADAKDWRAHLEQMKQHKKSIEESLP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922256    281 ETKGFLDKLHNEITRTLEKISSREKYINNQLENLVQEYRAAQAQLSEAKERYQQGNGGVTERTRLLSEVMEELEKVKQEM 360
Cdd:pfam10498 240 DTKSQLDKLHTDISKTLEKIESREKYINSQLEPLIQEYREAQDELSEVQEKYKQLSEGVTERTRELAEITEELEKVKQEM 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 8922256    361 EEKGSSMTDGAPLVKIKQSLTKLKQETVEMDIRIGIVEHTL 401
Cdd:pfam10498 320 EERGSSMTDGSPLVKIKQALTKLKEEIKQMDLRIGVLQHTL 360
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
276-368 7.99e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 7.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922256  276 ESALKETKGFLDKLHNEITRTLEKISSrekyINNQLENLVQEYRAAQAQLSEAKERYQQGNGGVTERTRLLSEVMEELEK 355
Cdd:COG3883  15 DPQIQAKQKELSELQAELEAAQAELDA----LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
                        90
                ....*....|...
gi 8922256  356 VKQEMEEKGSSMT 368
Cdd:COG3883  91 RARALYRSGGSVS 103
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
275-386 8.79e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 8.79e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922256  275 IESALKETKGFLDKLHNEITRTLEK-----ISSREKYINNQLENLVQEYRAAQAQLSEAKERYQQGNGGVTERTRLLSEV 349
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 8922256  350 M---------EELEKVKQEMEEKGSSMTDGAP-LVKIKQSLTKLKQE 386
Cdd:COG3206 260 LqspviqqlrAQLAELEAELAELSARYTPNHPdVIALRAQIAALRAQ 306
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
218-386 4.20e-03

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: 39.42  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922256    218 LDMNETAKQEDI--LESTTDAAEWSLEVERVLPQLKVTIRTDNKDWRIHVDQMHQHRSGIE---SALKET---KGFLDKL 289
Cdd:pfam10174 522 LEIAVEQKKEECskLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVErllGILREVeneKNDKDKK 601
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922256    290 HNEI-TRTLEKISSREKYINNQLENLVQEYRAAQAQLSEAkeRYQQGNGGVTERTRLLSEVMEELEKVKQEMEEKGSSMT 368
Cdd:pfam10174 602 IAELeSLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEA--RRREDNLADNSQQLQLEELMGALEKTRQELDATKARLS 679
                         170
                  ....*....|....*....
gi 8922256    369 DGAPLVKIKQS-LTKLKQE 386
Cdd:pfam10174 680 STQQSLAEKDGhLTNLRAE 698
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
262-362 9.26e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 38.39  E-value: 9.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922256   262 RIHVDQMHQHRSgiesALKETKGFLDK---LHNEITRTLEKISSREKYINNQLE------NLVQEyrAAQAQlsEAKERY 332
Cdd:COG3096  281 RELSERALELRR----ELFGARRQLAEeqyRLVEMARELEELSARESDLEQDYQaasdhlNLVQT--ALRQQ--EKIERY 352
                         90       100       110
                 ....*....|....*....|....*....|
gi 8922256   333 QQGNGGVTERTRLLSEVMEELEKVKQEMEE 362
Cdd:COG3096  353 QEDLEELTERLEEQEEVVEEAAEQLAEAEA 382
 
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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