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Conserved domains on  [gi|1695739144|gb|TPX19159|]
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hypothetical protein DIZ76_016945 [Coccidioides immitis]

Protein Classification

Kelch repeat-containing protein( domain architecture ID 15620386)

Kelch repeat-containing protein, member of a superfamily of proteins with diverse functions

CATH:  2.120.10.80
Gene Ontology:  GO:0005515
PubMed:  10603472|31442578|24959344
SCOP:  3000448

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 336-384 2.40e-09

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


:

Pssm-ID: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 53.34  E-value: 2.40e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1695739144 336 PPARSDFCSVVASakdgssHNIYIYGGYggSHRNETSSDDVYILSVPSF 384
Cdd:pfam13854   1 PVPRYGHCAVTVG------DYIYLYGGY--TGGEGQPSDDVYVLSLPTF 41
NanM super family cl34543
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
309-417 5.53e-05

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


The actual alignment was detected with superfamily member COG3055:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 45.53  E-value: 5.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1695739144 309 GESFMKTVPVYDIDSGNWYTqntTGEHP-PARSDFCSVVASAKdgsshnIYIYGGYGGSHRNETSSDDVYILSVPSFEWI 387
Cdd:COG3055    33 GGSASNSFEVYDPATNTWSE---LAPLPgPPRHHAAAVAQDGK------LYVFGGFTGANPSSTPLNDVYVYDPATNTWT 103

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1695739144 388 KA---PQGRSQHGrrghqcVKPYPDKMLVIGGI 417
Cdd:COG3055   104 KLapmPTPRGGAT------ALLLDGKIYVVGGW 130
 
Name Accession Description Interval E-value
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 336-384 2.40e-09

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 53.34  E-value: 2.40e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1695739144 336 PPARSDFCSVVASakdgssHNIYIYGGYggSHRNETSSDDVYILSVPSF 384
Cdd:pfam13854   1 PVPRYGHCAVTVG------DYIYLYGGY--TGGEGQPSDDVYVLSLPTF 41
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
309-417 5.53e-05

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 45.53  E-value: 5.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1695739144 309 GESFMKTVPVYDIDSGNWYTqntTGEHP-PARSDFCSVVASAKdgsshnIYIYGGYGGSHRNETSSDDVYILSVPSFEWI 387
Cdd:COG3055    33 GGSASNSFEVYDPATNTWSE---LAPLPgPPRHHAAAVAQDGK------LYVFGGFTGANPSSTPLNDVYVYDPATNTWT 103

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1695739144 388 KA---PQGRSQHGrrghqcVKPYPDKMLVIGGI 417
Cdd:COG3055   104 KLapmPTPRGGAT------ALLLDGKIYVVGGW 130
 
Name Accession Description Interval E-value
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 336-384 2.40e-09

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 53.34  E-value: 2.40e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1695739144 336 PPARSDFCSVVASakdgssHNIYIYGGYggSHRNETSSDDVYILSVPSF 384
Cdd:pfam13854   1 PVPRYGHCAVTVG------DYIYLYGGY--TGGEGQPSDDVYVLSLPTF 41
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
309-417 5.53e-05

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 45.53  E-value: 5.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1695739144 309 GESFMKTVPVYDIDSGNWYTqntTGEHP-PARSDFCSVVASAKdgsshnIYIYGGYGGSHRNETSSDDVYILSVPSFEWI 387
Cdd:COG3055    33 GGSASNSFEVYDPATNTWSE---LAPLPgPPRHHAAAVAQDGK------LYVFGGFTGANPSSTPLNDVYVYDPATNTWT 103

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1695739144 388 KA---PQGRSQHGrrghqcVKPYPDKMLVIGGI 417
Cdd:COG3055   104 KLapmPTPRGGAT------ALLLDGKIYVVGGW 130
 
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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