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Conserved domains on  [gi|1015177037|ref|NP_001308993|]
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zinc finger and SCAN domain-containing protein 5A isoform b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 40-124 1.14e-33

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


:

Pssm-ID: 153421  Cd Length: 85  Bit Score: 121.98  E-value: 1.14e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037  40 PEISHVNFRMFSCPKESDPIQALRKLTELCHLWLRPDLHTKEQILDMLVMEQFMISMPQELQVLVMMNGVQSCKDLEDLL 119
Cdd:cd07936     1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                  ....*
gi 1015177037 120 RNNRR 124
Cdd:cd07936    81 EDLLA 85
zf-H2C2_2 pfam13465
Zinc-finger double domain;
454-479 1.20e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 1.20e-05
                          10        20
                  ....*....|....*....|....*.
gi 1015177037 454 SLKEHQRIHSGEKPYKCSKCPRAFSR 479
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
398-423 2.22e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 2.22e-05
                          10        20
                  ....*....|....*....|....*.
gi 1015177037 398 SLQFHQRTHTGERPYTCDVCQKQFTQ 423
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
Treacle super family cl25490
Treacher Collins syndrome protein Treacle;
156-355 8.10e-05

Treacher Collins syndrome protein Treacle;


The actual alignment was detected with superfamily member pfam03546:

Pssm-ID: 460967 [Multi-domain]  Cd Length: 531  Bit Score: 45.06  E-value: 8.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037 156 DDLKDVSSQRASSVNQMRPGEGQAHRELQILPRVPALSRRQGEDFLL-HKSIDVTGDPKSLRPKQTLE--KDLKENREEN 232
Cdd:pfam03546 166 EEDSESSSEESDSEGEAPPAATQAKPSGKILQVRPASGPAKGAAPAPpQKAGPVATQVKAERSKEDSEssEESSDSEEEA 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037 233 PGLTSP---EPQLPKSPTDLVRAKEGKDPPKIASVENVDADTPSACVVEREASTHSgnrgdalnLSSP------KRSKPD 303
Cdd:pfam03546 246 PAAATPaqaKPALKTPQTKASPRKGTPITPTSAKVPPVRVGTPAPWKAGTVTSPAC--------ASSPavargaQRPEED 317

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1015177037 304 ASSISQEEPQGEATPVGNReSPGQAGMNSIHSPGPASPVSHPDGQEAKALPP 355
Cdd:pfam03546 318 SSSSEESESEEETAPAAAV-GQAKSVGKGLQGKAASAPTKGPSGQGTAPVPP 368
zf-H2C2_2 pfam13465
Zinc-finger double domain;
430-451 1.98e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.98e-04
                          10        20
                  ....*....|....*....|..
gi 1015177037 430 HKRSHTGEKPFECKDCKKVFTY 451
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
371-393 3.58e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.58e-03
                          10        20
                  ....*....|....*....|...
gi 1015177037 371 LVIHKRSHTGERLFQCNLCGKRF 393
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
 
Name Accession Description Interval E-value
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 40-124 1.14e-33

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 121.98  E-value: 1.14e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037  40 PEISHVNFRMFSCPKESDPIQALRKLTELCHLWLRPDLHTKEQILDMLVMEQFMISMPQELQVLVMMNGVQSCKDLEDLL 119
Cdd:cd07936     1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                  ....*
gi 1015177037 120 RNNRR 124
Cdd:cd07936    81 EDLLA 85
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 40-124 1.25e-29

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 111.04  E-value: 1.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037  40 PEISHVNFRMFSCPKESDPIQALRKLTELCHLWLRPDLHTKEQILDMLVMEQFMISMPQELQVLVMMNGVQSCKD----L 115
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEavalA 80


                  ....*....
gi 1015177037 116 EDLLRNNRR 124
Cdd:pfam02023  81 EDLLLERGE 89
SCAN smart00431
leucine rich region;
40-137 7.61e-26

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 101.61  E-value: 7.61e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037   40 PEISHVNFRMFSCPKESDPIQALRKLTELCHLWLRPDLHTKEQILDMLVMEQFMISMPQELQVLVM----MNGVQSCKDL 115
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVRehhpESGEEAVTLL 80

                           90       100
                   ....*....|....*....|..
gi 1015177037  116 EDLLRNNRRPKKWSVVTFHGKE 137
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQE 102
zf-H2C2_2 pfam13465
Zinc-finger double domain;
454-479 1.20e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 1.20e-05
                          10        20
                  ....*....|....*....|....*.
gi 1015177037 454 SLKEHQRIHSGEKPYKCSKCPRAFSR 479
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
398-423 2.22e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 2.22e-05
                          10        20
                  ....*....|....*....|....*.
gi 1015177037 398 SLQFHQRTHTGERPYTCDVCQKQFTQ 423
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
Treacle pfam03546
Treacher Collins syndrome protein Treacle;
156-355 8.10e-05

Treacher Collins syndrome protein Treacle;


Pssm-ID: 460967 [Multi-domain]  Cd Length: 531  Bit Score: 45.06  E-value: 8.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037 156 DDLKDVSSQRASSVNQMRPGEGQAHRELQILPRVPALSRRQGEDFLL-HKSIDVTGDPKSLRPKQTLE--KDLKENREEN 232
Cdd:pfam03546 166 EEDSESSSEESDSEGEAPPAATQAKPSGKILQVRPASGPAKGAAPAPpQKAGPVATQVKAERSKEDSEssEESSDSEEEA 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037 233 PGLTSP---EPQLPKSPTDLVRAKEGKDPPKIASVENVDADTPSACVVEREASTHSgnrgdalnLSSP------KRSKPD 303
Cdd:pfam03546 246 PAAATPaqaKPALKTPQTKASPRKGTPITPTSAKVPPVRVGTPAPWKAGTVTSPAC--------ASSPavargaQRPEED 317

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1015177037 304 ASSISQEEPQGEATPVGNReSPGQAGMNSIHSPGPASPVSHPDGQEAKALPP 355
Cdd:pfam03546 318 SSSSEESESEEETAPAAAV-GQAKSVGKGLQGKAASAPTKGPSGQGTAPVPP 368
zf-H2C2_2 pfam13465
Zinc-finger double domain;
430-451 1.98e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.98e-04
                          10        20
                  ....*....|....*....|..
gi 1015177037 430 HKRSHTGEKPFECKDCKKVFTY 451
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
339-492 3.71e-04

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 3.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037 339 ASPVSHPDGQEAKALPPFACDVCEKRFTCNSKLVIHKRS--HTGERL--FQC--NLCGKRFMQLISLQFHQRTHTGERPY 412
Cdd:COG5048   273 SSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGESLkpFSCpySLCGKLFSRNDALKRHILLHTSISPA 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037 413 TC--DVCQKQFTQKSYLK-----CHKRSHTGEKPFEC--KDCKKVFTYRGSLKEH--QRIHSGEKPYKCSKCPRAFSRLK 481
Cdd:COG5048   353 KEklLNSSSKFSPLLNNEppqslQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHiiTHLSFRPYNCKNPPCSKSFNRHY 432

                         170
                  ....*....|.
gi 1015177037 482 LLRRHQKTHPE 492
Cdd:COG5048   433 NLIPHKKIHTN 443
zf-H2C2_2 pfam13465
Zinc-finger double domain;
371-393 3.58e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.58e-03
                          10        20
                  ....*....|....*....|...
gi 1015177037 371 LVIHKRSHTGERLFQCNLCGKRF 393
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
2a38euk TIGR00934
potassium uptake protein, Trk family; The proteins of the Trk family are derived from ...
 117-328 4.11e-03

potassium uptake protein, Trk family; The proteins of the Trk family are derived from Gram-negative and Gram-positive bacteria, yeast and wheat. The proteins of E. coli K12 TrkH and TrkG as well as several yeast proteins have been functionally characterized.The E. coli TrkH and TrkG proteins are complexed to two peripheral membrane proteins, TrkA, an NAD-binding protein, and TrkE, an ATP-binding protein. This complex forms the potassium uptake system. This family is specific for the eukaryotic Trk system. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130009 [Multi-domain]  Cd Length: 800  Bit Score: 39.97  E-value: 4.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037 117 DLLRNNRRPKKWSVVTFHGKEYIVQDSDIEMAEAPSSVRDDL-KDVSSQRASSVNQMRPGEGQAHRELQILPRVPALSRR 195
Cdd:TIGR00934 203 DVKSDTRADESISDLEFEKFAKRRGSRDVDPEDLYRSIMMLQgIHERIREKSSANSRSDERSSESIQEQVERRPSTSDIE 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037 196 QGEdfllhKSIDVTGDPKSLRPKQTLEKDLKENREENPGLTSPE--PQLPKSPTDLVRAKEGKDPPKIASVENVDADTPS 273
Cdd:TIGR00934 283 RNS-----QSLTRRYDDKSFDKAVRLRRSKTIDRAEACDLEELDraKDFEKMTYDNWKAHHRKKKNFRPRGWNLKFRKAS 357

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1015177037 274 acvveREASTHSGNRGDALN-LSSPKRSKPDASSISQEEPQGEATPvGNRESPGQA 328
Cdd:TIGR00934 358 -----RFPKDSDRNYEDNGNhLSASSSFGSEEPSLSSEENLYPTYN-KKREDSRHT 407
 
Name Accession Description Interval E-value
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 40-124 1.14e-33

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 121.98  E-value: 1.14e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037  40 PEISHVNFRMFSCPKESDPIQALRKLTELCHLWLRPDLHTKEQILDMLVMEQFMISMPQELQVLVMMNGVQSCKDLEDLL 119
Cdd:cd07936     1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80


                  ....*
gi 1015177037 120 RNNRR 124
Cdd:cd07936    81 EDLLA 85
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 40-124 1.25e-29

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 111.04  E-value: 1.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037  40 PEISHVNFRMFSCPKESDPIQALRKLTELCHLWLRPDLHTKEQILDMLVMEQFMISMPQELQVLVMMNGVQSCKD----L 115
Cdd:pfam02023   1 PEASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEavalA 80


                  ....*....
gi 1015177037 116 EDLLRNNRR 124
Cdd:pfam02023  81 EDLLLERGE 89
SCAN smart00431
leucine rich region;
40-137 7.61e-26

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 101.61  E-value: 7.61e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037   40 PEISHVNFRMFSCPKESDPIQALRKLTELCHLWLRPDLHTKEQILDMLVMEQFMISMPQELQVLVM----MNGVQSCKDL 115
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVRehhpESGEEAVTLL 80

                           90       100
                   ....*....|....*....|..
gi 1015177037  116 EDLLRNNRRPKKWSVVTFHGKE 137
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQE 102
zf-H2C2_2 pfam13465
Zinc-finger double domain;
454-479 1.20e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 1.20e-05
                          10        20
                  ....*....|....*....|....*.
gi 1015177037 454 SLKEHQRIHSGEKPYKCSKCPRAFSR 479
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
398-423 2.22e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.20  E-value: 2.22e-05
                          10        20
                  ....*....|....*....|....*.
gi 1015177037 398 SLQFHQRTHTGERPYTCDVCQKQFTQ 423
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
Treacle pfam03546
Treacher Collins syndrome protein Treacle;
156-355 8.10e-05

Treacher Collins syndrome protein Treacle;


Pssm-ID: 460967 [Multi-domain]  Cd Length: 531  Bit Score: 45.06  E-value: 8.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037 156 DDLKDVSSQRASSVNQMRPGEGQAHRELQILPRVPALSRRQGEDFLL-HKSIDVTGDPKSLRPKQTLE--KDLKENREEN 232
Cdd:pfam03546 166 EEDSESSSEESDSEGEAPPAATQAKPSGKILQVRPASGPAKGAAPAPpQKAGPVATQVKAERSKEDSEssEESSDSEEEA 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037 233 PGLTSP---EPQLPKSPTDLVRAKEGKDPPKIASVENVDADTPSACVVEREASTHSgnrgdalnLSSP------KRSKPD 303
Cdd:pfam03546 246 PAAATPaqaKPALKTPQTKASPRKGTPITPTSAKVPPVRVGTPAPWKAGTVTSPAC--------ASSPavargaQRPEED 317

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1015177037 304 ASSISQEEPQGEATPVGNReSPGQAGMNSIHSPGPASPVSHPDGQEAKALPP 355
Cdd:pfam03546 318 SSSSEESESEEETAPAAAV-GQAKSVGKGLQGKAASAPTKGPSGQGTAPVPP 368
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 468-490 1.67e-04

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: 38.82  E-value: 1.67e-04
                          10        20
                  ....*....|....*....|...
gi 1015177037 468 YKCSKCPRAFSRLKLLRRHQKTH 490
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
430-451 1.98e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.98e-04
                          10        20
                  ....*....|....*....|..
gi 1015177037 430 HKRSHTGEKPFECKDCKKVFTY 451
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 440-462 2.98e-04

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: 38.05  E-value: 2.98e-04
                          10        20
                  ....*....|....*....|...
gi 1015177037 440 FECKDCKKVFTYRGSLKEHQRIH 462
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
339-492 3.71e-04

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.76  E-value: 3.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037 339 ASPVSHPDGQEAKALPPFACDVCEKRFTCNSKLVIHKRS--HTGERL--FQC--NLCGKRFMQLISLQFHQRTHTGERPY 412
Cdd:COG5048   273 SSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGESLkpFSCpySLCGKLFSRNDALKRHILLHTSISPA 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037 413 TC--DVCQKQFTQKSYLK-----CHKRSHTGEKPFEC--KDCKKVFTYRGSLKEH--QRIHSGEKPYKCSKCPRAFSRLK 481
Cdd:COG5048   353 KEklLNSSSKFSPLLNNEppqslQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHiiTHLSFRPYNCKNPPCSKSFNRHY 432

                         170
                  ....*....|.
gi 1015177037 482 LLRRHQKTHPE 492
Cdd:COG5048   433 NLIPHKKIHTN 443
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
410-473 8.93e-04

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.61  E-value: 8.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1015177037 410 RPYTCDVCQKQFTQKSYLKCHKRSHTGEKPFECKD--CKKVFTYRGSLKEHQRIHSGEKPYKCSKC 473
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKS 97
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 324-488 1.29e-03

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 41.24  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037 324 SPGQAGMNSIH--SPGPASPVSHPDGQEAKALPPFACDVCEK--RFTCNSKLVIHKRSHTGERlfqcNLCGKRFMQLIsl 399
Cdd:COG5189   271 SPSQGSAELFEesSLGFDYEFIHKSVGNKEIRGGISTGEMIDvrKLPCTNSSSNGKLAHGGER----NIDTPSRMLKV-- 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037 400 qfhqrthTGERPYTCDV--CQKQFTQKSYLKCHKR-SHTGEKPFECKDCKKvftyrgslkeHQRIHSGEKPYKCSKCPRA 476
Cdd:COG5189   345 -------KDGKPYKCPVegCNKKYKNQNGLKYHMLhGHQNQKLHENPSPEK----------MNIFSAKDKPYRCEVCDKR 407

                         170
                  ....*....|..
gi 1015177037 477 FSRLKLLRRHQK 488
Cdd:COG5189   408 YKNLNGLKYHRK 419
zf-H2C2_2 pfam13465
Zinc-finger double domain;
371-393 3.58e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.58e-03
                          10        20
                  ....*....|....*....|...
gi 1015177037 371 LVIHKRSHTGERLFQCNLCGKRF 393
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
2a38euk TIGR00934
potassium uptake protein, Trk family; The proteins of the Trk family are derived from ...
 117-328 4.11e-03

potassium uptake protein, Trk family; The proteins of the Trk family are derived from Gram-negative and Gram-positive bacteria, yeast and wheat. The proteins of E. coli K12 TrkH and TrkG as well as several yeast proteins have been functionally characterized.The E. coli TrkH and TrkG proteins are complexed to two peripheral membrane proteins, TrkA, an NAD-binding protein, and TrkE, an ATP-binding protein. This complex forms the potassium uptake system. This family is specific for the eukaryotic Trk system. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130009 [Multi-domain]  Cd Length: 800  Bit Score: 39.97  E-value: 4.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037 117 DLLRNNRRPKKWSVVTFHGKEYIVQDSDIEMAEAPSSVRDDL-KDVSSQRASSVNQMRPGEGQAHRELQILPRVPALSRR 195
Cdd:TIGR00934 203 DVKSDTRADESISDLEFEKFAKRRGSRDVDPEDLYRSIMMLQgIHERIREKSSANSRSDERSSESIQEQVERRPSTSDIE 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015177037 196 QGEdfllhKSIDVTGDPKSLRPKQTLEKDLKENREENPGLTSPE--PQLPKSPTDLVRAKEGKDPPKIASVENVDADTPS 273
Cdd:TIGR00934 283 RNS-----QSLTRRYDDKSFDKAVRLRRSKTIDRAEACDLEELDraKDFEKMTYDNWKAHHRKKKNFRPRGWNLKFRKAS 357

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1015177037 274 acvveREASTHSGNRGDALN-LSSPKRSKPDASSISQEEPQGEATPvGNRESPGQA 328
Cdd:TIGR00934 358 -----RFPKDSDRNYEDNGNhLSASSSFGSEEPSLSSEENLYPTYN-KKREDSRHT 407
 
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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