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Conserved domains on  [gi|386766415|ref|NP_001036755|]
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molting defective, isoform C [Drosophila melanogaster]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 10657771)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

CATH:  3.30.160.60
Gene Ontology:  GO:0008270|GO:0003677
PubMed:  22803940|11361095|11179890|12665246|10940247
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 186-255 5.63e-06

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


:

Pssm-ID: 214871  Cd Length: 73  Bit Score: 45.97  E-value: 5.63e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766415    186 GRSSDNAVDYTLSGAHSSMDIVLEEMTiwMLNINRDDGLPQEICRQCMAQFLMVAKFRRKCVRMQQRLQD 255
Cdd:smart00868    6 LSESENLVSIFDESSEASLAEKIEECT--GIEIEPDDGLPKVICGDCLEKLESFHKFRERCRESDELLRE 73
PAT1 super family cl37801
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 959-1109 1.81e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


The actual alignment was detected with superfamily member pfam09770:

Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 50.03  E-value: 1.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766415   959 QPSQSDPPAGEQVEKIeMETQPSTVQMDVQSNLPVQAA----DTQPQNESANHSP----FESPISSPQVQSQIELQMEPQ 1030
Cdd:pfam09770  178 QPAAQPASLPAPSRKM-MSLEEVEAAMRAQAKKPAQQPapapAQPPAAPPAQQAQqqqqFPPQIQQQQQPQQQPQQPQQH 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766415  1031 IETQMQPQIETRMQhdvlsVQSPQNHQPQVQSHDQSQMQHQIPPQIEP-QIeVQN------QEQNTLQLVPQAQHQVVPH 1103
Cdd:pfam09770  257 PGQGHPVTILQRPQ-----SPQPDPAQPSIQPQAQQFHQQPPPVPVQPtQI-LQNpnrlsaARVGYPQNPQPGVQPAPAH 330


                   ....*.
gi 386766415  1104 VQLQSQ 1109
Cdd:pfam09770  331 QAHRQQ 336
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 1812-1834 4.77e-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: 36.12  E-value: 4.77e-03
                           10        20
                   ....*....|....*....|...
gi 386766415  1812 HTCDECGKQFGTESALKTHIKFH 1834
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 186-255 5.63e-06

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 214871  Cd Length: 73  Bit Score: 45.97  E-value: 5.63e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766415    186 GRSSDNAVDYTLSGAHSSMDIVLEEMTiwMLNINRDDGLPQEICRQCMAQFLMVAKFRRKCVRMQQRLQD 255
Cdd:smart00868    6 LSESENLVSIFDESSEASLAEKIEECT--GIEIEPDDGLPKVICGDCLEKLESFHKFRERCRESDELLRE 73
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 959-1109 1.81e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 50.03  E-value: 1.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766415   959 QPSQSDPPAGEQVEKIeMETQPSTVQMDVQSNLPVQAA----DTQPQNESANHSP----FESPISSPQVQSQIELQMEPQ 1030
Cdd:pfam09770  178 QPAAQPASLPAPSRKM-MSLEEVEAAMRAQAKKPAQQPapapAQPPAAPPAQQAQqqqqFPPQIQQQQQPQQQPQQPQQH 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766415  1031 IETQMQPQIETRMQhdvlsVQSPQNHQPQVQSHDQSQMQHQIPPQIEP-QIeVQN------QEQNTLQLVPQAQHQVVPH 1103
Cdd:pfam09770  257 PGQGHPVTILQRPQ-----SPQPDPAQPSIQPQAQQFHQQPPPVPVQPtQI-LQNpnrlsaARVGYPQNPQPGVQPAPAH 330


                   ....*.
gi 386766415  1104 VQLQSQ 1109
Cdd:pfam09770  331 QAHRQQ 336
zf-AD pfam07776
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 200-254 1.11e-04

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 462262  Cd Length: 75  Bit Score: 42.45  E-value: 1.11e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 386766415   200 AHSSMDIV--LEEMTiwMLNINRDDGLPQEICRQCMAQFLMVAKFRRKCVRMQQRLQ 254
Cdd:pfam07776   19 SDSEKTLAeiLEDCT--GIELDPNDLLPKQICERCLSKLQEFYSFRERCLESQELLQ 73
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 1007-1111 1.90e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.54  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766415 1007 HSPFESPISSPQVQSQIELQMEPQIETQMQPQIETRMQHDVLSVQSPQNHQPQVQSHDQSQMQHQIPPQ-IEPQIEVQNQ 1085
Cdd:PRK10263  741 HEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQpVAPQPQYQQP 820

                          90       100
                  ....*....|....*....|....*.
gi 386766415 1086 EQNTLQLVPQAQHQVVPHVQLQSQLV 1111
Cdd:PRK10263  821 QQPVAPQPQYQQPQQPVAPQPQDTLL 846
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 1812-1834 4.77e-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: 36.12  E-value: 4.77e-03
                           10        20
                   ....*....|....*....|...
gi 386766415  1812 HTCDECGKQFGTESALKTHIKFH 1834
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 186-255 5.63e-06

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 214871  Cd Length: 73  Bit Score: 45.97  E-value: 5.63e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766415    186 GRSSDNAVDYTLSGAHSSMDIVLEEMTiwMLNINRDDGLPQEICRQCMAQFLMVAKFRRKCVRMQQRLQD 255
Cdd:smart00868    6 LSESENLVSIFDESSEASLAEKIEECT--GIEIEPDDGLPKVICGDCLEKLESFHKFRERCRESDELLRE 73
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 959-1109 1.81e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 50.03  E-value: 1.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766415   959 QPSQSDPPAGEQVEKIeMETQPSTVQMDVQSNLPVQAA----DTQPQNESANHSP----FESPISSPQVQSQIELQMEPQ 1030
Cdd:pfam09770  178 QPAAQPASLPAPSRKM-MSLEEVEAAMRAQAKKPAQQPapapAQPPAAPPAQQAQqqqqFPPQIQQQQQPQQQPQQPQQH 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766415  1031 IETQMQPQIETRMQhdvlsVQSPQNHQPQVQSHDQSQMQHQIPPQIEP-QIeVQN------QEQNTLQLVPQAQHQVVPH 1103
Cdd:pfam09770  257 PGQGHPVTILQRPQ-----SPQPDPAQPSIQPQAQQFHQQPPPVPVQPtQI-LQNpnrlsaARVGYPQNPQPGVQPAPAH 330


                   ....*.
gi 386766415  1104 VQLQSQ 1109
Cdd:pfam09770  331 QAHRQQ 336
zf-AD pfam07776
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 200-254 1.11e-04

Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.


Pssm-ID: 462262  Cd Length: 75  Bit Score: 42.45  E-value: 1.11e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 386766415   200 AHSSMDIV--LEEMTiwMLNINRDDGLPQEICRQCMAQFLMVAKFRRKCVRMQQRLQ 254
Cdd:pfam07776   19 SDSEKTLAeiLEDCT--GIELDPNDLLPKQICERCLSKLQEFYSFRERCLESQELLQ 73
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 1007-1111 1.90e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.54  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766415 1007 HSPFESPISSPQVQSQIELQMEPQIETQMQPQIETRMQHDVLSVQSPQNHQPQVQSHDQSQMQHQIPPQ-IEPQIEVQNQ 1085
Cdd:PRK10263  741 HEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQpVAPQPQYQQP 820

                          90       100
                  ....*....|....*....|....*.
gi 386766415 1086 EQNTLQLVPQAQHQVVPHVQLQSQLV 1111
Cdd:PRK10263  821 QQPVAPQPQYQQPQQPVAPQPQDTLL 846
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 1812-1834 4.77e-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: 36.12  E-value: 4.77e-03
                           10        20
                   ....*....|....*....|...
gi 386766415  1812 HTCDECGKQFGTESALKTHIKFH 1834
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2_6 pfam13912
C2H2-type zinc finger;
1812-1841 8.45e-03

C2H2-type zinc finger;


Pssm-ID: 433576  Cd Length: 27  Bit Score: 35.68  E-value: 8.45e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 386766415  1812 HTCDECGKQFGTESALkthikfhGAHMKTH 1841
Cdd:pfam13912    2 HECSECGKSFPSYQAL-------GGHKKSH 24
 
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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