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Conserved domains on  [gi|301897977|ref|NP_001180437|]
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RE1-silencing transcription factor [Homo sapiens]

Protein Classification

zf-H2C2_2 and zf-H2C2_5 domain-containing protein( domain architecture ID 12143203)

zf-H2C2_2 and zf-H2C2_5 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
599-767 1.01e-07

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 56.63  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  599 EPVEKGSAQMDPPQMGPAPTEAVQKGPVQVEPPPPMEHAQME-----GAQ-----IRPAPD--EPVQMEVVQEGPAQKEL 666
Cdd:PRK10263  318 EPVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAwqpvpGPQtgepvIAPAPEgyPQQSQYAQPAVQYNEPL 397
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  667 LPPVEPAQMVGAQIVLAHMELPPPMETAQTEVAQMGPAPMEPAQMEVAQVESAPMQ-VVQKEPVQMELSPPMEVVQKEP- 744
Cdd:PRK10263  398 QQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQsTFAPQSTYQTEQTYQQPAAQEPl 477
                         170       180
                  ....*....|....*....|....
gi 301897977  745 -VQIELSPPMEVVQKEPVKIELSP 767
Cdd:PRK10263  478 yQQPQPVEQQPVVEPEPVVEETKP 501
zf-H2C2_2 pfam13465
Zinc-finger double domain;
318-343 2.17e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.05  E-value: 2.17e-06
                           10        20
                   ....*....|....*....|....*.
gi 301897977   318 HLTRHMRTHSGEKPFKCDQCSYVASN 343
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_5 pfam13909
C2H2-type zinc-finger domain;
304-328 5.80e-06

C2H2-type zinc-finger domain;


:

Pssm-ID: 404746 [Multi-domain]  Cd Length: 25  Bit Score: 43.69  E-value: 5.80e-06
                           10        20
                   ....*....|....*....|....*
gi 301897977   304 YKCELCPYSSSQKTHLTRHMRTHSG 328
Cdd:pfam13909    1 YKCSQCDYSTAWKSNLKRHLRKHTG 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
290-315 3.61e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 3.61e-05
                           10        20
                   ....*....|....*....|....*.
gi 301897977   290 NYVQHVRTHTGERPYKCELCPYSSSQ 315
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_5 pfam13909
C2H2-type zinc-finger domain;
363-383 9.77e-04

C2H2-type zinc-finger domain;


:

Pssm-ID: 404746 [Multi-domain]  Cd Length: 25  Bit Score: 37.53  E-value: 9.77e-04
                           10        20
                   ....*....|....*....|.
gi 301897977   363 CPHCDYKTADRSNFKKHVELH 383
Cdd:pfam13909    3 CSQCDYSTAWKSNLKRHLRKH 23
 
Name Accession Description Interval E-value
PRK10263 PRK10263
DNA translocase FtsK; Provisional
599-767 1.01e-07

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 56.63  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  599 EPVEKGSAQMDPPQMGPAPTEAVQKGPVQVEPPPPMEHAQME-----GAQ-----IRPAPD--EPVQMEVVQEGPAQKEL 666
Cdd:PRK10263  318 EPVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAwqpvpGPQtgepvIAPAPEgyPQQSQYAQPAVQYNEPL 397
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  667 LPPVEPAQMVGAQIVLAHMELPPPMETAQTEVAQMGPAPMEPAQMEVAQVESAPMQ-VVQKEPVQMELSPPMEVVQKEP- 744
Cdd:PRK10263  398 QQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQsTFAPQSTYQTEQTYQQPAAQEPl 477
                         170       180
                  ....*....|....*....|....
gi 301897977  745 -VQIELSPPMEVVQKEPVKIELSP 767
Cdd:PRK10263  478 yQQPQPVEQQPVVEPEPVVEETKP 501
zf-H2C2_2 pfam13465
Zinc-finger double domain;
318-343 2.17e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.05  E-value: 2.17e-06
                           10        20
                   ....*....|....*....|....*.
gi 301897977   318 HLTRHMRTHSGEKPFKCDQCSYVASN 343
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_5 pfam13909
C2H2-type zinc-finger domain;
304-328 5.80e-06

C2H2-type zinc-finger domain;


Pssm-ID: 404746 [Multi-domain]  Cd Length: 25  Bit Score: 43.69  E-value: 5.80e-06
                           10        20
                   ....*....|....*....|....*
gi 301897977   304 YKCELCPYSSSQKTHLTRHMRTHSG 328
Cdd:pfam13909    1 YKCSQCDYSTAWKSNLKRHLRKHTG 25
zf-H2C2_2 pfam13465
Zinc-finger double domain;
290-315 3.61e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 3.61e-05
                           10        20
                   ....*....|....*....|....*.
gi 301897977   290 NYVQHVRTHTGERPYKCELCPYSSSQ 315
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
302-381 2.47e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  302 RPYKCELCPYSSSQKTHLTRHMRTHSGEKPFKC--DQCSYVASNQHEVTRHARQVHNGPKPLNC---PHCDYKTADRSNF 376
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSkslPLSNSKASSSSLS 111

                  ....*
gi 301897977  377 KKHVE 381
Cdd:COG5048   112 SSSSN 116
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
598-828 3.71e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 44.37  E-value: 3.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  598 KEPVEKgSAQMDPPQMGPAPTEAVQKGPVQVEPPPPMEHAQME--GAQIRPAPDEPVQMEVVQEGPAQKELLP-PVEPAQ 674
Cdd:NF033839  285 KEPGNK-KPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEkpKPEVKPQPEKPKPEVKPQLETPKPEVKPqPEKPKP 363
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  675 MVGAQIVLAHMELPPPMETAQTEVAQM--GPAPMEPAQMEVAQVESAPMQVVQKEPVQMELSPPMEVVQKEPVQielsPP 752
Cdd:NF033839  364 EVKPQPEKPKPEVKPQPETPKPEVKPQpeKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEK----PK 439
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 301897977  753 MEVV-QKEPVKIELSPPIEVVQKEpVQMELSPPMGVVQKEPAQREPPPPREPPLHMEPiSKKPPLRKDkKEKSNMQS 828
Cdd:NF033839  440 PEVKpQPEKPKPEVKPQPETPKPE-VKPQPEKPKPEVKPQPEKPKPDNSKPQADDKKP-STPNNLSKD-KQPSNQAS 513
zf-H2C2_5 pfam13909
C2H2-type zinc-finger domain;
363-383 9.77e-04

C2H2-type zinc-finger domain;


Pssm-ID: 404746 [Multi-domain]  Cd Length: 25  Bit Score: 37.53  E-value: 9.77e-04
                           10        20
                   ....*....|....*....|.
gi 301897977   363 CPHCDYKTADRSNFKKHVELH 383
Cdd:pfam13909    3 CSQCDYSTAWKSNLKRHLRKH 23
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
595-817 1.60e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.83  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977   595 PPQKEPVEKGSAQMDP--PQMGPAPTEAVQKGPVQVEPPPPMEHAQMEGAQIR----PAPDEPVQMEVVQEGPAQKELLP 668
Cdd:pfam03154  186 PPPPGTTQAATAGPTPsaPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHpqrlPSPHPPLQPMTQPPPPSQVSPQP 265
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977   669 PVEPAQmvgaqivlaHMELPPPMETAQTEVAQMG-PAPMEP----AQMEVAQVESAPMQVVQKEPVQMELSPPMEVV--- 740
Cdd:pfam03154  266 LPQPSL---------HGQMPPMPHSLQTGPSHMQhPVPPQPfpltPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQlqs 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977   741 QKEPVQIELSP-PMEVVQKEPVKIELSPPIEVVQ--KEPVQMELSPPMGVVQKEPAQREPPPPREPPLHMEPISKKPPLR 817
Cdd:pfam03154  337 QQPPREQPLPPaPLSMPHIKPPPTTPIPQLPNPQshKHPPHLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQ 416
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
605-831 2.46e-03

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 41.84  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  605 SAQMDPPQMGPAPTEAVQKGPVQVEPPPP----MEHAQMEGAQIR------PAPDEPVQMEVVQEGPAQKELLP--PVEP 672
Cdd:cd22540   152 QAIITPVQVLQQPQQAHKPVPIKPAPLQTsntnSASLQVPGNVIKlqsggnVALTLPVNNLVGTQDGATQLQLAaaPSKP 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  673 AQMVGAQiVLAHMELPPPM---------ETAQTEVAQMG--------PAPMEPAQMEVAQVesapMQVVQKEPVQMELSP 735
Cdd:cd22540   232 SKKIRKK-SAQAAQPAVTVaeqvetvliETTADNIIQAGnnllivqsPGTGQPAVLQQVQV----LQPKQEQQVVQIPQQ 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  736 PMEVVQkepVQIELSPPMEVVQKEPVKIELSPPievvqkEPVQMELSPPMGVVQKEPAQREPPPPREPPLHMEPISKKPP 815
Cdd:cd22540   307 ALRVVQ---AASATLPTVPQKPLQNIQIQNSEP------TPTQVYIKTPSGEVQTVLLQEAPAATATPSSSTSTVQQQVT 377
                         250
                  ....*....|....*....
gi 301897977  816 LR---KDKKEKSNMQSERA 831
Cdd:cd22540   378 ANngtGTSKPNYNVRKERT 396
ZnF_C2H2 smart00355
zinc finger;
304-326 3.01e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.90  E-value: 3.01e-03
                            10        20
                    ....*....|....*....|...
gi 301897977    304 YKCELCPYSSSQKTHLTRHMRTH 326
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
 
Name Accession Description Interval E-value
PRK10263 PRK10263
DNA translocase FtsK; Provisional
599-767 1.01e-07

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 56.63  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  599 EPVEKGSAQMDPPQMGPAPTEAVQKGPVQVEPPPPMEHAQME-----GAQ-----IRPAPD--EPVQMEVVQEGPAQKEL 666
Cdd:PRK10263  318 EPVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAwqpvpGPQtgepvIAPAPEgyPQQSQYAQPAVQYNEPL 397
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  667 LPPVEPAQMVGAQIVLAHMELPPPMETAQTEVAQMGPAPMEPAQMEVAQVESAPMQ-VVQKEPVQMELSPPMEVVQKEP- 744
Cdd:PRK10263  398 QQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQsTFAPQSTYQTEQTYQQPAAQEPl 477
                         170       180
                  ....*....|....*....|....
gi 301897977  745 -VQIELSPPMEVVQKEPVKIELSP 767
Cdd:PRK10263  478 yQQPQPVEQQPVVEPEPVVEETKP 501
zf-H2C2_2 pfam13465
Zinc-finger double domain;
318-343 2.17e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.05  E-value: 2.17e-06
                           10        20
                   ....*....|....*....|....*.
gi 301897977   318 HLTRHMRTHSGEKPFKCDQCSYVASN 343
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_5 pfam13909
C2H2-type zinc-finger domain;
304-328 5.80e-06

C2H2-type zinc-finger domain;


Pssm-ID: 404746 [Multi-domain]  Cd Length: 25  Bit Score: 43.69  E-value: 5.80e-06
                           10        20
                   ....*....|....*....|....*
gi 301897977   304 YKCELCPYSSSQKTHLTRHMRTHSG 328
Cdd:pfam13909    1 YKCSQCDYSTAWKSNLKRHLRKHTG 25
PHA03378 PHA03378
EBNA-3B; Provisional
599-749 8.27e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 50.07  E-value: 8.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  599 EPVEKGSAQMDPPQMGPA----PTEAVQKGPVQVEPPPPMEHAQMEGAQIRPAPDEPVQMEVVQEGPAQkelLPPVEPAQ 674
Cdd:PHA03378  675 QPSPTGANTMLPIQWAPGtmqpPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGR---ARPPAAAP 751
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 301897977  675 MVGAQIVLAHMELPPPmETAQTEVAQMGPAPMEPAQMEVAQVESAPMQVVQKEPVQMELSPPMEVVQKEPVQIEL 749
Cdd:PHA03378  752 GRARPPAAAPGRARPP-AAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQIL 825
zf-H2C2_2 pfam13465
Zinc-finger double domain;
290-315 3.61e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.59  E-value: 3.61e-05
                           10        20
                   ....*....|....*....|....*.
gi 301897977   290 NYVQHVRTHTGERPYKCELCPYSSSQ 315
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
rne PRK10811
ribonuclease E; Reviewed
619-773 3.77e-05

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 48.11  E-value: 3.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  619 EAVQKGPVQVEPPPPMEHAQMEGAQIRPAPDEPVQMEVVQEGPAQKElLPPVEPAQmvGAQIVLAHMELPPPMETAQTEV 698
Cdd:PRK10811  862 EEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEE-VVVVETTH--PEVIAAPVTEQPQVITESDVAV 938
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 301897977  699 AQMGPAPMEPAQMEVAQVESapmqVVQKEPVQMELSPPMEVVQKEPVQIELSPPMEVVQKEPVKIELSPPIEVVQ 773
Cdd:PRK10811  939 AQEVAEHAEPVVEPQDETAD----IEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEA 1009
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
304-326 8.04e-05

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: 40.36  E-value: 8.04e-05
                           10        20
                   ....*....|....*....|...
gi 301897977   304 YKCELCPYSSSQKTHLTRHMRTH 326
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
302-381 2.47e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  302 RPYKCELCPYSSSQKTHLTRHMRTHSGEKPFKC--DQCSYVASNQHEVTRHARQVHNGPKPLNC---PHCDYKTADRSNF 376
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSkslPLSNSKASSSSLS 111

                  ....*
gi 301897977  377 KKHVE 381
Cdd:COG5048   112 SSSSN 116
PRK10263 PRK10263
DNA translocase FtsK; Provisional
595-776 3.36e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.08  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  595 PPQKEPVEKGSAQMDPPQMGPAPTEAVQKGPVQVEPPPPMEHAQMEGAQIRPAPdepvQMEVVQEGPAQKELLPPVEPAQ 674
Cdd:PRK10263  366 PQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQP----YYAPAPEQPAQQPYYAPAPEQP 441
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  675 MVGAQIVLAHMELP-PPMETAQTEVAQMGPAPMEPAQMEVAQVEsaPMQVVQKEPVQMELS---PPM----EVVQKEPVQ 746
Cdd:PRK10263  442 VAGNAWQAEEQQSTfAPQSTYQTEQTYQQPAAQEPLYQQPQPVE--QQPVVEPEPVVEETKparPPLyyfeEVEEKRARE 519
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 301897977  747 IE-----LSPPMEVVqKEPVKIELSPPIEVVQKEP 776
Cdd:PRK10263  520 REqlaawYQPIPEPV-KEPEPIKSSLKAPSVAAVP 553
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
598-828 3.71e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 44.37  E-value: 3.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  598 KEPVEKgSAQMDPPQMGPAPTEAVQKGPVQVEPPPPMEHAQME--GAQIRPAPDEPVQMEVVQEGPAQKELLP-PVEPAQ 674
Cdd:NF033839  285 KEPGNK-KPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEkpKPEVKPQPEKPKPEVKPQLETPKPEVKPqPEKPKP 363
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  675 MVGAQIVLAHMELPPPMETAQTEVAQM--GPAPMEPAQMEVAQVESAPMQVVQKEPVQMELSPPMEVVQKEPVQielsPP 752
Cdd:NF033839  364 EVKPQPEKPKPEVKPQPETPKPEVKPQpeKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEK----PK 439
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 301897977  753 MEVV-QKEPVKIELSPPIEVVQKEpVQMELSPPMGVVQKEPAQREPPPPREPPLHMEPiSKKPPLRKDkKEKSNMQS 828
Cdd:NF033839  440 PEVKpQPEKPKPEVKPQPETPKPE-VKPQPEKPKPEVKPQPEKPKPDNSKPQADDKKP-STPNNLSKD-KQPSNQAS 513
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
625-778 6.49e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 43.70  E-value: 6.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  625 PVQVEPPPPMEHAQMEGAQIRPAPDEPVQmevVQEGPAQKELLPPVEPAQMVgaqivlahmeLPPPMETAQTEVAQMGPA 704
Cdd:PRK07994  361 PAAPLPEPEVPPQSAAPAASAQATAAPTA---AVAPPQAPAVPPPPASAPQQ----------APAVPLPETTSQLLAARQ 427
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 301897977  705 PMEPAQMEVAQVESAPMQVVQKEPVQmelSPPMEVVQKEPVQIELSPpmEVVQKEPVKIELSPPIEVVQKEPVQ 778
Cdd:PRK07994  428 QLQRAQGATKAKKSEPAAASRARPVN---SALERLASVRPAPSALEK--APAKKEAYRWKATNPVEVKKEPVAT 496
rne PRK10811
ribonuclease E; Reviewed
617-784 9.18e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 43.49  E-value: 9.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  617 PTEAVQKGPVQVEPPPPMEHAQMEGAQIR-PAPDEPVQMEVVQEGPAQkellPPVEPAQMVGAQIVLAhmelpPPMETAQ 695
Cdd:PRK10811  846 PVVRPQDVQVEEQREAEEVQVQPVVAEVPvAAAVEPVVSAPVVEAVAE----VVEEPVVVAEPQPEEV-----VVVETTH 916
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  696 TEVAQmGPAPMEPAQMEVAQVESAPMQVVQKEPVQMELSPPMEVVQKEPVQIELSPPMEVVQKEPVKIELSPPIEVVQKE 775
Cdd:PRK10811  917 PEVIA-APVTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVT 995

                  ....*....
gi 301897977  776 PVQMELSPP 784
Cdd:PRK10811  996 AVEPEVAPA 1004
zf-H2C2_5 pfam13909
C2H2-type zinc-finger domain;
363-383 9.77e-04

C2H2-type zinc-finger domain;


Pssm-ID: 404746 [Multi-domain]  Cd Length: 25  Bit Score: 37.53  E-value: 9.77e-04
                           10        20
                   ....*....|....*....|.
gi 301897977   363 CPHCDYKTADRSNFKKHVELH 383
Cdd:pfam13909    3 CSQCDYSTAWKSNLKRHLRKH 23
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
606-748 1.58e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 42.49  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  606 AQMDPPQmGPAPTeAVQKGPVQVEPPPPMEHAQMEGAQIRPAPDEPvqmevvqEGPAQKELLPPVEPAQMVGAqivlahm 685
Cdd:PRK14950  366 PQPAKPT-AAAPS-PVRPTPAPSTRPKAAAAANIPPKEPVRETATP-------PPVPPRPVAPPVPHTPESAP------- 429
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 301897977  686 elPPPMETAQTEVAQMGPAPMEPAQMEVA---------QVESAPMQVVQKEPVQmelSPPMEVVQK---EPVQIE 748
Cdd:PRK14950  430 --KLTRAAIPVDEKPKYTPPAPPKEEEKAliadgdvleQLEAIWKQILRDVPPR---SPAVQALLSsgvRPVSVE 499
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
595-817 1.60e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.83  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977   595 PPQKEPVEKGSAQMDP--PQMGPAPTEAVQKGPVQVEPPPPMEHAQMEGAQIR----PAPDEPVQMEVVQEGPAQKELLP 668
Cdd:pfam03154  186 PPPPGTTQAATAGPTPsaPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHpqrlPSPHPPLQPMTQPPPPSQVSPQP 265
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977   669 PVEPAQmvgaqivlaHMELPPPMETAQTEVAQMG-PAPMEP----AQMEVAQVESAPMQVVQKEPVQMELSPPMEVV--- 740
Cdd:pfam03154  266 LPQPSL---------HGQMPPMPHSLQTGPSHMQhPVPPQPfpltPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQlqs 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977   741 QKEPVQIELSP-PMEVVQKEPVKIELSPPIEVVQ--KEPVQMELSPPMGVVQKEPAQREPPPPREPPLHMEPISKKPPLR 817
Cdd:pfam03154  337 QQPPREQPLPPaPLSMPHIKPPPTTPIPQLPNPQshKHPPHLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQ 416
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
615-774 1.67e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 42.55  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  615 PAPTEAVQKGPVQVEPPPPMEHAQMEGAQIRPAPDEPVQMEVVQEGPAQKELLPPVEP-AQMVGA--QIVLAHMELPPPm 691
Cdd:PRK07994  361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETtSQLLAArqQLQRAQGATKAK- 439
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  692 etAQTEVAQMGPAPMEPAQMEVAQVESAPmQVVQKEPvqmelsPPMEVVQKEPVQIELSPPMEVVQKEPVK--IELSPPI 769
Cdd:PRK07994  440 --KSEPAAASRARPVNSALERLASVRPAP-SALEKAP------AKKEAYRWKATNPVEVKKEPVATPKALKkaLEHEKTP 510

                  ....*
gi 301897977  770 EVVQK 774
Cdd:PRK07994  511 ELAAK 515
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
604-794 1.74e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.56  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  604 GSAQMDPPQMGPAPTEAVQKGPVQVEPPPPMEHAQMEGAQIRPAPDEPVQMEVVQEGPAQKELLPPVEPAQMVGAQIVLA 683
Cdd:PRK12323  370 GGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPA 449
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  684 HMELPP--PMETAQTEVAQMGPAPMEPAQMEVAQVESAPMQVVQKEPVQMELSPPmEVVQKEPVQIELSPPMEVVQ--KE 759
Cdd:PRK12323  450 PAPAPAaaPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPP-EFASPAPAQPDAAPAGWVAEsiPD 528
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 301897977  760 PVKIELSPPIEVVQKEPVQMELSPPMGVVQKEPAQ 794
Cdd:PRK12323  529 PATADPDDAFETLAPAPAAAPAPRAAAATEPVVAP 563
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
661-794 2.00e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 42.16  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  661 PAQKELLPPVEPAQMVGAQIVLAHMELPPPMETAQTEVAQMGPAPMePAQMEVAQVESAPMQVVQKEPVQMELSPPMEVV 740
Cdd:PRK07994  361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASA-PQQAPAVPLPETTSQLLAARQQLQRAQGATKAK 439
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 301897977  741 QKEPVQIELSPPMEVVQKEPVKIELSP---PIEVVQKEPVQMELSPPMGVVQKEPAQ 794
Cdd:PRK07994  440 KSEPAAASRARPVNSALERLASVRPAPsalEKAPAKKEAYRWKATNPVEVKKEPVAT 496
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
605-831 2.46e-03

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 41.84  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  605 SAQMDPPQMGPAPTEAVQKGPVQVEPPPP----MEHAQMEGAQIR------PAPDEPVQMEVVQEGPAQKELLP--PVEP 672
Cdd:cd22540   152 QAIITPVQVLQQPQQAHKPVPIKPAPLQTsntnSASLQVPGNVIKlqsggnVALTLPVNNLVGTQDGATQLQLAaaPSKP 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  673 AQMVGAQiVLAHMELPPPM---------ETAQTEVAQMG--------PAPMEPAQMEVAQVesapMQVVQKEPVQMELSP 735
Cdd:cd22540   232 SKKIRKK-SAQAAQPAVTVaeqvetvliETTADNIIQAGnnllivqsPGTGQPAVLQQVQV----LQPKQEQQVVQIPQQ 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  736 PMEVVQkepVQIELSPPMEVVQKEPVKIELSPPievvqkEPVQMELSPPMGVVQKEPAQREPPPPREPPLHMEPISKKPP 815
Cdd:cd22540   307 ALRVVQ---AASATLPTVPQKPLQNIQIQNSEP------TPTQVYIKTPSGEVQTVLLQEAPAATATPSSSTSTVQQQVT 377
                         250
                  ....*....|....*....
gi 301897977  816 LR---KDKKEKSNMQSERA 831
Cdd:cd22540   378 ANngtGTSKPNYNVRKERT 396
ZnF_C2H2 smart00355
zinc finger;
304-326 3.01e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.90  E-value: 3.01e-03
                            10        20
                    ....*....|....*....|...
gi 301897977    304 YKCELCPYSSSQKTHLTRHMRTH 326
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
271-414 3.12e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.22  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  271 FPRKVYTCGKCNYFSDRKNNYVQHVRT--HTGE--RPYKC--ELCPYSSSQKTHLTRHMRTHSGEKPFKC--DQCSY--- 339
Cdd:COG5048   285 GFSLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSkfs 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  340 --VASNQHEVTRHARQVHNGPKPLNCPHCDYK-TADRSNFKKHVELHVN--PRQFNCPVCdYAASKKCNLQYHFKSKHPT 414
Cdd:COG5048   365 plLNNEPPQSLQQYKDLKNDKKSETLSNSCIRnFKRDSNLSLHIITHLSfrPYNCKNPPC-SKSFNRHYNLIPHKKIHTN 443
PHA03379 PHA03379
EBNA-3A; Provisional
600-784 4.64e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 41.20  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  600 PVEKGSAQMDPPQMGPAPtEAVQK-------GPVQVEPPPPM---------EHAQMEG---AQIRPAPDEPVQMEVVQEG 660
Cdd:PHA03379  408 ASEPTYGTPRPPVEKPRP-EVPQSletatshGSAQVPEPPPVhdlepgplhDQHSMAPcpvAQLPPGPLQDLEPGDQLPG 486
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  661 PAQKELLPPVePAQMVGAQIVlahmelpPPMETAQTEVAQMGPAPMEPAQMEVAQV---ESAPMQVVQKEPVQMELSPPM 737
Cdd:PHA03379  487 VVQDGRPACA-PVPAPAGPIV-------RPWEASLSQVPGVAFAPVMPQPMPVEPVpvpTVALERPVCPAPPLIAMQGPG 558
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  738 EVVQKEPVQIELSP------PMEVVQKEPVKIELS-------PPIEVVQKEPVQMELSPP 784
Cdd:PHA03379  559 ETSGIVRVRERWRPapwtpnPPRSPSQMSVRDRLArlraeaqPYQASVEVQPPQLTQVSP 618
rne PRK10811
ribonuclease E; Reviewed
605-753 5.17e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 41.18  E-value: 5.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301897977  605 SAQMDPPQMGPAPTEAVQKGPVQVEPPPPMEHAQMEGAQIRPAPDEPVQMEVVQEGPaqkellPPVEPAQMVGAQIVLAH 684
Cdd:PRK10811  872 EVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQP------QVITESDVAVAQEVAEH 945
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 301897977  685 ME---LPPPMETAQTEVAQMgpAPMEPAQMEVAQVESAPMQVVQKEPVQMELSPPMEVVQKEPVQIEL-----SPPM 753
Cdd:PRK10811  946 AEpvvEPQDETADIEEAAET--AEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATVehnhaTAPM 1020
 
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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