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Conserved domains on  [gi|1024090204|gb|KZV81841|]
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hypothetical protein EXIGLDRAFT_755331 [Exidia glandulosa HHB12029]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZZ_RSC8 cd02336
Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of ...
 71-114 1.91e-17

Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of the RSC complex, which is closely related to the SWI/SNF complex and is involved in remodeling chromatin structure. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding.


:

Pssm-ID: 239076  Cd Length: 45  Bit Score: 74.28  E-value: 1.91e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1024090204  71 YACDTCGADCSRVRYHSLKA-KMEICASCYADGRFPRSMFSEDFV 114
Cdd:cd02336     1 YHCFTCGNDCTRVRYHNLKAkKYDLCPSCYQEGRFPSNFQSSDFI 45
RSC8 super family cl34960
RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / ...
 71-208 8.32e-17

RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / Transcription];


The actual alignment was detected with superfamily member COG5259:

Pssm-ID: 227584 [Multi-domain]  Cd Length: 531  Bit Score: 80.32  E-value: 8.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024090204  71 YACDTCGADCSRVRYHSLKA-KMEICASCYADGRFPRSMFSEDFVKLSHADPSFlsadgDHGWTDAET--LLWGCSTtIG 147
Cdd:COG5259   225 SSCSCCGNKSFNTRYHNLRAeKYNSCSECYDQGRFPSEFTSSDFKPVTISLLIR-----DKNWSRQELllLLEGIEM-YG 298

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024090204 148 IAW----LNMG------CA----GLRGTD--VRLGGAGALMYGGRLPFEKADNPVMSVVAFLAGAVGPAIASDAAST 208
Cdd:COG5259   299 DDWdkvaRHVGtktkeqCIlhflQLPIEDnyLSKGDGKGDNSKGRLPFDGSENPVLSTISFLAGIVNPRVQSEKQRA 375
SWIRM-assoc_1 super family cl24910
SWIRM-associated region 1; Much of the higher eukaryote SWI/SNF complex subunit SMARCC2 ...
 251-290 1.07e-03

SWIRM-associated region 1; Much of the higher eukaryote SWI/SNF complex subunit SMARCC2 proteins is of low-complexity and or disordered. However, there are several short regions that are quite highly conserved. This is one of these regions. The function of the individual regions is not known.


The actual alignment was detected with superfamily member pfam16495:

Pssm-ID: 465142 [Multi-domain]  Cd Length: 84  Bit Score: 37.11  E-value: 1.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1024090204 251 VKTLVGLTSKTLELKMEAFEELEAVLEDEasvkiREAPER 290
Cdd:pfam16495  26 VALLVETQLKKLELKLKQFEELEKLLERE-----RRQLER 60
 
Name Accession Description Interval E-value
ZZ_RSC8 cd02336
Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of ...
 71-114 1.91e-17

Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of the RSC complex, which is closely related to the SWI/SNF complex and is involved in remodeling chromatin structure. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239076  Cd Length: 45  Bit Score: 74.28  E-value: 1.91e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1024090204  71 YACDTCGADCSRVRYHSLKA-KMEICASCYADGRFPRSMFSEDFV 114
Cdd:cd02336     1 YHCFTCGNDCTRVRYHNLKAkKYDLCPSCYQEGRFPSNFQSSDFI 45
RSC8 COG5259
RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / ...
 71-208 8.32e-17

RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227584 [Multi-domain]  Cd Length: 531  Bit Score: 80.32  E-value: 8.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024090204  71 YACDTCGADCSRVRYHSLKA-KMEICASCYADGRFPRSMFSEDFVKLSHADPSFlsadgDHGWTDAET--LLWGCSTtIG 147
Cdd:COG5259   225 SSCSCCGNKSFNTRYHNLRAeKYNSCSECYDQGRFPSEFTSSDFKPVTISLLIR-----DKNWSRQELllLLEGIEM-YG 298

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024090204 148 IAW----LNMG------CA----GLRGTD--VRLGGAGALMYGGRLPFEKADNPVMSVVAFLAGAVGPAIASDAAST 208
Cdd:COG5259   299 DDWdkvaRHVGtktkeqCIlhflQLPIEDnyLSKGDGKGDNSKGRLPFDGSENPVLSTISFLAGIVNPRVQSEKQRA 375
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 71-104 2.40e-08

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 49.36  E-value: 2.40e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1024090204   71 YACDTCGADCSRVRYHSLK-AKMEICASCYADGRF 104
Cdd:smart00291   5 YSCDTCGKPIVGVRYHCLVcPDYDLCQSCFAKGSA 39
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 71-99 4.45e-04

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 37.46  E-value: 4.45e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1024090204  71 YACDTCGADCS-RVRYHSLKAK-MEICASCY 99
Cdd:pfam00569   5 YTCNGCSNDPSiGVRYHCLRCSdYDLCQSCF 35
SWIRM-assoc_1 pfam16495
SWIRM-associated region 1; Much of the higher eukaryote SWI/SNF complex subunit SMARCC2 ...
 251-290 1.07e-03

SWIRM-associated region 1; Much of the higher eukaryote SWI/SNF complex subunit SMARCC2 proteins is of low-complexity and or disordered. However, there are several short regions that are quite highly conserved. This is one of these regions. The function of the individual regions is not known.


Pssm-ID: 465142 [Multi-domain]  Cd Length: 84  Bit Score: 37.11  E-value: 1.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1024090204 251 VKTLVGLTSKTLELKMEAFEELEAVLEDEasvkiREAPER 290
Cdd:pfam16495  26 VALLVETQLKKLELKLKQFEELEKLLERE-----RRQLER 60
 
Name Accession Description Interval E-value
ZZ_RSC8 cd02336
Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of ...
 71-114 1.91e-17

Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of the RSC complex, which is closely related to the SWI/SNF complex and is involved in remodeling chromatin structure. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239076  Cd Length: 45  Bit Score: 74.28  E-value: 1.91e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1024090204  71 YACDTCGADCSRVRYHSLKA-KMEICASCYADGRFPRSMFSEDFV 114
Cdd:cd02336     1 YHCFTCGNDCTRVRYHNLKAkKYDLCPSCYQEGRFPSNFQSSDFI 45
RSC8 COG5259
RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / ...
 71-208 8.32e-17

RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227584 [Multi-domain]  Cd Length: 531  Bit Score: 80.32  E-value: 8.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024090204  71 YACDTCGADCSRVRYHSLKA-KMEICASCYADGRFPRSMFSEDFVKLSHADPSFlsadgDHGWTDAET--LLWGCSTtIG 147
Cdd:COG5259   225 SSCSCCGNKSFNTRYHNLRAeKYNSCSECYDQGRFPSEFTSSDFKPVTISLLIR-----DKNWSRQELllLLEGIEM-YG 298

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024090204 148 IAW----LNMG------CA----GLRGTD--VRLGGAGALMYGGRLPFEKADNPVMSVVAFLAGAVGPAIASDAAST 208
Cdd:COG5259   299 DDWdkvaRHVGtktkeqCIlhflQLPIEDnyLSKGDGKGDNSKGRLPFDGSENPVLSTISFLAGIVNPRVQSEKQRA 375
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 71-104 2.40e-08

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 49.36  E-value: 2.40e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1024090204   71 YACDTCGADCSRVRYHSLK-AKMEICASCYADGRF 104
Cdd:smart00291   5 YSCDTCGKPIVGVRYHCLVcPDYDLCQSCFAKGSA 39
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 71-99 4.45e-04

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 37.46  E-value: 4.45e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1024090204  71 YACDTCGADCS-RVRYHSLKAK-MEICASCY 99
Cdd:pfam00569   5 YTCNGCSNDPSiGVRYHCLRCSdYDLCQSCF 35
SWIRM-assoc_1 pfam16495
SWIRM-associated region 1; Much of the higher eukaryote SWI/SNF complex subunit SMARCC2 ...
 251-290 1.07e-03

SWIRM-associated region 1; Much of the higher eukaryote SWI/SNF complex subunit SMARCC2 proteins is of low-complexity and or disordered. However, there are several short regions that are quite highly conserved. This is one of these regions. The function of the individual regions is not known.


Pssm-ID: 465142 [Multi-domain]  Cd Length: 84  Bit Score: 37.11  E-value: 1.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1024090204 251 VKTLVGLTSKTLELKMEAFEELEAVLEDEasvkiREAPER 290
Cdd:pfam16495  26 VALLVETQLKKLELKLKQFEELEKLLERE-----RRQLER 60
 
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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