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Conserved domains on  [gi|1616589153|ref|NP_001356665|]
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paternally-expressed gene 3 protein isoform 6 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PHA03169 super family cl27451
hypothetical protein; Provisional
1264-1348 1.40e-04

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PHA03169:

Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 46.12  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589153 1264 NGEAEGPDGEAAE--PIGEAGQP----NGEAEQPNGDADE-PDGAGIEDPEERAEEPEGKAEEPEGDAdePDGVGIEDPE 1336
Cdd:PHA03169   122 NTSGSSPESPASHspPPSPPSHPgphePAPPESHNPSPNQqPSSFLQPSHEDSPEEPEPPTSEPEPDS--PGPPQSETPT 199
                           90
                   ....*....|..
gi 1616589153 1337 EGEDQEIQVEEP 1348
Cdd:PHA03169   200 SSPPPQSPPDEP 211
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
814-836 1.30e-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: 37.28  E-value: 1.30e-03
                           10        20
                   ....*....|....*....|...
gi 1616589153  814 YECQECGECFAHSSDLTEHQKIH 836
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
1008-1030 1.52e-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: 37.28  E-value: 1.52e-03
                           10        20
                   ....*....|....*....|...
gi 1616589153 1008 YECPKCGESFIHSSFLFEHQRIH 1030
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
472-494 8.65e-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: 8.65e-03
                           10        20
                   ....*....|....*....|...
gi 1616589153  472 YECKVCGETFLHSSSLKEHQKIH 494
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
PHA03169 PHA03169
hypothetical protein; Provisional
1264-1348 1.40e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 46.12  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589153 1264 NGEAEGPDGEAAE--PIGEAGQP----NGEAEQPNGDADE-PDGAGIEDPEERAEEPEGKAEEPEGDAdePDGVGIEDPE 1336
Cdd:PHA03169   122 NTSGSSPESPASHspPPSPPSHPgphePAPPESHNPSPNQqPSSFLQPSHEDSPEEPEPPTSEPEPDS--PGPPQSETPT 199
                           90
                   ....*....|..
gi 1616589153 1337 EGEDQEIQVEEP 1348
Cdd:PHA03169   200 SSPPPQSPPDEP 211
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
1265-1347 3.45e-04

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 45.37  E-value: 3.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589153 1265 GEAEGPDGEAAEPIGEAGQPNGEAEQPNGDADEPDGAGIEDPEERAEEPEGKAE-----EPEGDADEPDGVGIEDPEEGE 1339
Cdd:TIGR00927  697 GEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEgkhevETEGDRKETEHEGETEAEGKE 776
                           90
                   ....*....|.
gi 1616589153 1340 DQ---EIQVEE 1347
Cdd:TIGR00927  777 DEdegEIQAGE 787
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
814-836 1.30e-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: 37.28  E-value: 1.30e-03
                           10        20
                   ....*....|....*....|...
gi 1616589153  814 YECQECGECFAHSSDLTEHQKIH 836
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
1008-1030 1.52e-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: 37.28  E-value: 1.52e-03
                           10        20
                   ....*....|....*....|...
gi 1616589153 1008 YECPKCGESFIHSSFLFEHQRIH 1030
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
472-494 8.65e-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: 8.65e-03
                           10        20
                   ....*....|....*....|...
gi 1616589153  472 YECKVCGETFLHSSSLKEHQKIH 494
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
PHA03169 PHA03169
hypothetical protein; Provisional
1264-1348 1.40e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 46.12  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589153 1264 NGEAEGPDGEAAE--PIGEAGQP----NGEAEQPNGDADE-PDGAGIEDPEERAEEPEGKAEEPEGDAdePDGVGIEDPE 1336
Cdd:PHA03169   122 NTSGSSPESPASHspPPSPPSHPgphePAPPESHNPSPNQqPSSFLQPSHEDSPEEPEPPTSEPEPDS--PGPPQSETPT 199
                           90
                   ....*....|..
gi 1616589153 1337 EGEDQEIQVEEP 1348
Cdd:PHA03169   200 SSPPPQSPPDEP 211
PHA00666 PHA00666
putative protease
1266-1346 1.69e-04

putative protease


Pssm-ID: 222808 [Multi-domain]  Cd Length: 233  Bit Score: 44.65  E-value: 1.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589153 1266 EAEGPDGEAAEPIGEAGQPNGEAEQPNGDADEPDG---AGIEDPEER--AEEPEGKAEEPEGDAdePDGVGIEDPEEGED 1340
Cdd:PHA00666    28 EPAAGAGDNPAPQGDPTQEEGDKPQPAAGADKPEGdkkADGDKPEEKkpGEKPEGAPEKYEFQA--AEGVELDTGALGAF 105

                   ....*.
gi 1616589153 1341 QEIQVE 1346
Cdd:PHA00666   106 EPVARE 111
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
1265-1347 3.45e-04

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 45.37  E-value: 3.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589153 1265 GEAEGPDGEAAEPIGEAGQPNGEAEQPNGDADEPDGAGIEDPEERAEEPEGKAE-----EPEGDADEPDGVGIEDPEEGE 1339
Cdd:TIGR00927  697 GEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEgkhevETEGDRKETEHEGETEAEGKE 776
                           90
                   ....*....|.
gi 1616589153 1340 DQ---EIQVEE 1347
Cdd:TIGR00927  777 DEdegEIQAGE 787
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
814-836 1.30e-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: 37.28  E-value: 1.30e-03
                           10        20
                   ....*....|....*....|...
gi 1616589153  814 YECQECGECFAHSSDLTEHQKIH 836
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
1008-1030 1.52e-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: 37.28  E-value: 1.52e-03
                           10        20
                   ....*....|....*....|...
gi 1616589153 1008 YECPKCGESFIHSSFLFEHQRIH 1030
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
472-494 8.65e-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: 8.65e-03
                           10        20
                   ....*....|....*....|...
gi 1616589153  472 YECKVCGETFLHSSSLKEHQKIH 494
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 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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