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Conserved domains on  [gi|1958682199|ref|XP_038949909|]
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cilium assembly protein DZIP1 isoform X4 [Rattus norvegicus]

Protein Classification

kinesin family protein; PEPP family PH domain-containing protein( domain architecture ID 13845323)

kinesin family protein is a microtubule-dependent molecular motor that plays an important role in intracellular transport and in cell division and has an ATPase-containing motor domain; similar to N-type kinesins that are (+) end-directed motors and have an N-terminal motor domain| PEPP (phosphoinositol 3-phosphate-binding protein) family PH (pleckstrin homology) domain-containing protein similar to PH domain region of vertebrate pleckstrin homology domain-containing family A member 4/5/6/7

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Dzip-like_N pfam13815
Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in ...
 43-163 8.32e-48

Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in Azoospermia - and a closely related sequence are required early in germ-cell development in order to maintain germ-cell populations. This family is the N-terminal region that is the only part of the protein in some fungi and lower metazoa.


:

Pssm-ID: 433498 [Multi-domain]  Cd Length: 118  Bit Score: 165.19  E-value: 8.32e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682199  43 FQFRPRLESVDWRRLSAIDVDKVAGAVDVLTLQENIMNITFCKLEDEKCPHcqsGVDPVLLKLIRLAQLTIEYLMHSQEF 122
Cdd:pfam13815   1 FQFRPRSERLDWRKLASVDVDRVARDTDVDTLQRNIENITFCNLTREEAPH---FVDPHFLKLFRLAQLTIEYLLHSQEC 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958682199 123 LTSQLNLVEERLRLSLMDYEQSKQLLTKQAGEIKLLKEECK 163
Cdd:pfam13815  78 LATILVKLEERLQEAQQRAEELEKELGRLEEELKKLKKESR 118
GumC super family cl34566
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
212-427 1.78e-03

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


The actual alignment was detected with superfamily member COG3206:

Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682199 212 LEYNTKAQTDRLQKEIDMLKEQLQLTRTQLESAQHshavrfskdyEMQKIKEEdfLKLFDrwkeeekeklleemekvkem 291
Cdd:COG3206   162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEA----------ALEEFRQK--NGLVD-------------------- 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682199 292 FMREFKKLTSKNSALEYQLLEIQRSNIQIKSNIGTLRDAHELREDHLPYPQD---FQNMLQLLDSQASKWSDRFQVLNEE 368
Cdd:COG3206   210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspvIQQLRAQLAELEAELAELSARYTPN 289

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958682199 369 HSK------EKGQLLSHIEKLRSSMMKDLSADNVFYKRRVEELGQKLQEQNEVIITQKQQIREFA 427
Cdd:COG3206   290 HPDvialraQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELR 354
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 183-206 5.57e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 5.57e-03
                          10        20
                  ....*....|....*....|....
gi 1958682199 183 YQCHLCDKAFMNQAFLQSHIqRRH 206
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHL-RTH 23
 
Name Accession Description Interval E-value
Dzip-like_N pfam13815
Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in ...
 43-163 8.32e-48

Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in Azoospermia - and a closely related sequence are required early in germ-cell development in order to maintain germ-cell populations. This family is the N-terminal region that is the only part of the protein in some fungi and lower metazoa.


Pssm-ID: 433498 [Multi-domain]  Cd Length: 118  Bit Score: 165.19  E-value: 8.32e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682199  43 FQFRPRLESVDWRRLSAIDVDKVAGAVDVLTLQENIMNITFCKLEDEKCPHcqsGVDPVLLKLIRLAQLTIEYLMHSQEF 122
Cdd:pfam13815   1 FQFRPRSERLDWRKLASVDVDRVARDTDVDTLQRNIENITFCNLTREEAPH---FVDPHFLKLFRLAQLTIEYLLHSQEC 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958682199 123 LTSQLNLVEERLRLSLMDYEQSKQLLTKQAGEIKLLKEECK 163
Cdd:pfam13815  78 LATILVKLEERLQEAQQRAEELEKELGRLEEELKKLKKESR 118
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
212-427 1.78e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682199 212 LEYNTKAQTDRLQKEIDMLKEQLQLTRTQLESAQHshavrfskdyEMQKIKEEdfLKLFDrwkeeekeklleemekvkem 291
Cdd:COG3206   162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEA----------ALEEFRQK--NGLVD-------------------- 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682199 292 FMREFKKLTSKNSALEYQLLEIQRSNIQIKSNIGTLRDAHELREDHLPYPQD---FQNMLQLLDSQASKWSDRFQVLNEE 368
Cdd:COG3206   210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspvIQQLRAQLAELEAELAELSARYTPN 289

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958682199 369 HSK------EKGQLLSHIEKLRSSMMKDLSADNVFYKRRVEELGQKLQEQNEVIITQKQQIREFA 427
Cdd:COG3206   290 HPDvialraQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELR 354
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 183-206 5.57e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 5.57e-03
                          10        20
                  ....*....|....*....|....
gi 1958682199 183 YQCHLCDKAFMNQAFLQSHIqRRH 206
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHL-RTH 23
 
Name Accession Description Interval E-value
Dzip-like_N pfam13815
Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in ...
 43-163 8.32e-48

Iguana/Dzip1-like DAZ-interacting protein N-terminal; The DAZ gene-product - Deleted in Azoospermia - and a closely related sequence are required early in germ-cell development in order to maintain germ-cell populations. This family is the N-terminal region that is the only part of the protein in some fungi and lower metazoa.


Pssm-ID: 433498 [Multi-domain]  Cd Length: 118  Bit Score: 165.19  E-value: 8.32e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682199  43 FQFRPRLESVDWRRLSAIDVDKVAGAVDVLTLQENIMNITFCKLEDEKCPHcqsGVDPVLLKLIRLAQLTIEYLMHSQEF 122
Cdd:pfam13815   1 FQFRPRSERLDWRKLASVDVDRVARDTDVDTLQRNIENITFCNLTREEAPH---FVDPHFLKLFRLAQLTIEYLLHSQEC 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958682199 123 LTSQLNLVEERLRLSLMDYEQSKQLLTKQAGEIKLLKEECK 163
Cdd:pfam13815  78 LATILVKLEERLQEAQQRAEELEKELGRLEEELKKLKKESR 118
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
212-427 1.78e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682199 212 LEYNTKAQTDRLQKEIDMLKEQLQLTRTQLESAQHshavrfskdyEMQKIKEEdfLKLFDrwkeeekeklleemekvkem 291
Cdd:COG3206   162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEA----------ALEEFRQK--NGLVD-------------------- 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682199 292 FMREFKKLTSKNSALEYQLLEIQRSNIQIKSNIGTLRDAHELREDHLPYPQD---FQNMLQLLDSQASKWSDRFQVLNEE 368
Cdd:COG3206   210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspvIQQLRAQLAELEAELAELSARYTPN 289

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958682199 369 HSK------EKGQLLSHIEKLRSSMMKDLSADNVFYKRRVEELGQKLQEQNEVIITQKQQIREFA 427
Cdd:COG3206   290 HPDvialraQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELR 354
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 183-206 5.57e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 5.57e-03
                          10        20
                  ....*....|....*....|....
gi 1958682199 183 YQCHLCDKAFMNQAFLQSHIqRRH 206
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHL-RTH 23
 
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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