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Conserved domains on  [gi|281361910|ref|NP_650534|]
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poils au dos [Drosophila melanogaster]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 10544446)

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 pfam07776
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 16-88 8.95e-20

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: 84.05  E-value: 8.95e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281361910   16 LCRICTDSSDHKTNIYSPEGRAKNLSQKILECLSLQIDEKDRLPKVVCAQCVQLVEQIHGLRATCRNSQTMLN 88
Cdd:pfam07776   1 VCRLCLDESDELIPIFDPSDSEKTLAEILEDCTGIELDPNDLLPKQICERCLSKLQEFYSFRERCLESQELLQ 73
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 766-788 2.19e-06

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: 44.60  E-value: 2.19e-06
                          10        20
                  ....*....|....*....|...
gi 281361910  766 YTCEVCKKPFSRKDNLNKHRRIH 788
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 497-709 3.24e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910  497 PTFKTPSPKQKPMPSPKSKTTVGPSSGGSNGTSTNEFKRLITQTKPQPQVKQQQTAGLSASGAPTATSANQAAMQRLSSN 576
Cdd:PHA03247 2743 AVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAA 2822

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910  577 TTITKVPKQPASLPAPAPTSN---PAKLPM---------LNKQNITISRISMQTAPKAQSKPSTTSPTPASQPIPVSVPA 644
Cdd:PHA03247 2823 SPAGPLPPPTSAQPTAPPPPPgppPPSLPLggsvapggdVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPP 2902

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281361910  645 LSQAQPPPLAAQHKKIVRKPPENQDT-SGQKVKAARPPQQILPSPQQEGQNATHSGSEAPTTSGLI 709
Cdd:PHA03247 2903 DQPERPPQPQAPPPPQPQPQPPPPPQpQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALV 2968
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 736-760 3.89e-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: 38.44  E-value: 3.89e-04
                          10        20
                  ....*....|....*....|....*
gi 281361910  736 FKCSEegCDKTFSRKEHLSRHLVSH 760
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 797-819 6.12e-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: 6.12e-03
                          10        20
                  ....*....|....*....|...
gi 281361910  797 YCCDVCNKNFATKLHYEKHREMH 819
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
zf-AD pfam07776
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 16-88 8.95e-20

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: 84.05  E-value: 8.95e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281361910   16 LCRICTDSSDHKTNIYSPEGRAKNLSQKILECLSLQIDEKDRLPKVVCAQCVQLVEQIHGLRATCRNSQTMLN 88
Cdd:pfam07776   1 VCRLCLDESDELIPIFDPSDSEKTLAEILEDCTGIELDPNDLLPKQICERCLSKLQEFYSFRERCLESQELLQ 73
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 16-87 1.94e-16

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: 74.47  E-value: 1.94e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281361910    16 LCRICTDSSDHKTNIYSPEGRAKnLSQKILECLSLQIDEKDRLPKVVCAQCVQLVEQIHGLRATCRNSQTML 87
Cdd:smart00868   1 VCRLCLSESENLVSIFDESSEAS-LAEKIEECTGIEIEPDDGLPKVICGDCLEKLESFHKFRERCRESDELL 71
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 766-788 2.19e-06

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: 44.60  E-value: 2.19e-06
                          10        20
                  ....*....|....*....|...
gi 281361910  766 YTCEVCKKPFSRKDNLNKHRRIH 788
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA03247 PHA03247
large tegument protein UL36; Provisional
 497-709 3.24e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910  497 PTFKTPSPKQKPMPSPKSKTTVGPSSGGSNGTSTNEFKRLITQTKPQPQVKQQQTAGLSASGAPTATSANQAAMQRLSSN 576
Cdd:PHA03247 2743 AVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAA 2822

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910  577 TTITKVPKQPASLPAPAPTSN---PAKLPM---------LNKQNITISRISMQTAPKAQSKPSTTSPTPASQPIPVSVPA 644
Cdd:PHA03247 2823 SPAGPLPPPTSAQPTAPPPPPgppPPSLPLggsvapggdVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPP 2902

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281361910  645 LSQAQPPPLAAQHKKIVRKPPENQDT-SGQKVKAARPPQQILPSPQQEGQNATHSGSEAPTTSGLI 709
Cdd:PHA03247 2903 DQPERPPQPQAPPPPQPQPQPPPPPQpQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALV 2968
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
566-825 1.15e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910 566 NQAAMQRLSSNTTITKVPKQPASLPAPAPT-SNPAKLPMLNKQNITISRISMQTAPKAQSKPSTTSPTPASQPIPVSVPA 644
Cdd:COG5048  144 SNLRNNPLPGNNSSSVNTPQSNSLHPPLPAnSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910 645 L-SQAQPPPLAAQHKKIVRKPPENQDTSGQKVKAARPPQQILPSPQQEGQNATHSGSEAPTTSGLI--CPTCKREFKKKE 721
Cdd:COG5048  224 SsSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGFSLPikSKQCNISFSRSS 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910 722 HLTQHVKLH----AGLRPFKCSEEGCDKTFSRKEHLSRHLVSHSGQKMYTC--EVCKKPFSRKDNLNKHRRIHTQTSTET 795
Cdd:COG5048  304 PLTRHLRSVnhsgESLKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQQYKDLKN 383

                        250       260       270
                 ....*....|....*....|....*....|....
gi 281361910 796 --LYCCDV--CNKNFATKLHYEKHREMHKKIRPE 825
Cdd:COG5048  384 dkKSETLSnsCIRNFKRDSNLSLHIITHLSFRPY 417
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 577-751 2.07e-04

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 44.86  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910 577 TTITKVPKQPASLPAPAPTSNPAKLPMLNKQNITISRISMQTAPKAQSKPSTTSPTP-ASQPIPVSVPALSQAQPPPlaa 655
Cdd:cd23959  129 THKTAQVAPPKAEPQTAPVTPFGQLPMFGQHPPPAKPLPAAAAAQQSSASPGEVASPfASGTVSASPFATATDTAPS--- 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910 656 qhkkivrkpPENQDTSGQKVKAARPPQQIlPSPQQEGQNATHSGSEAPTTSGliCPTCKREFKKKEHLTQHVKLHAGLRP 735
Cdd:cd23959  206 ---------SGAPDGFPAEASAPSPFAAP-ASAASFPAAPVANGEAATPTHA--CTICGKAFSTHEGLRMHSKAKHGVEL 273

                        170
                 ....*....|....*.
gi 281361910 736 FKcseegcDKTFSRKE 751
Cdd:cd23959  274 EK------AKTAKRKK 283
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 736-760 3.89e-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: 38.44  E-value: 3.89e-04
                          10        20
                  ....*....|....*....|....*
gi 281361910  736 FKCSEegCDKTFSRKEHLSRHLVSH 760
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 584-690 6.62e-04

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: 43.49  E-value: 6.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910  584 KQPASLPAPAPTSNPAKLPMLNKQNITISRIsmQTAPKAQSKPSTTSPTPASQPIPVSVPAlSQAQPPPLAAQHKKIVRK 663
Cdd:pfam09770 169 KAAAPAPAPQPAAQPASLPAPSRKMMSLEEV--EAAMRAQAKKPAQQPAPAPAQPPAAPPA-QQAQQQQQFPPQIQQQQQ 245

                          90       100
                  ....*....|....*....|....*..
gi 281361910  664 PPENQDTSGQKVKAARPPQqILPSPQQ 690
Cdd:pfam09770 246 PQQQPQQPQQHPGQGHPVT-ILQRPQS 271
ZnF_C2H2 smart00355
zinc finger;
766-788 8.14e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 37.45  E-value: 8.14e-04
                           10        20
                   ....*....|....*....|...
gi 281361910   766 YTCEVCKKPFSRKDNLNKHRRIH 788
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 797-819 6.12e-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: 6.12e-03
                          10        20
                  ....*....|....*....|...
gi 281361910  797 YCCDVCNKNFATKLHYEKHREMH 819
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
zf-AD pfam07776
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 16-88 8.95e-20

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: 84.05  E-value: 8.95e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281361910   16 LCRICTDSSDHKTNIYSPEGRAKNLSQKILECLSLQIDEKDRLPKVVCAQCVQLVEQIHGLRATCRNSQTMLN 88
Cdd:pfam07776   1 VCRLCLDESDELIPIFDPSDSEKTLAEILEDCTGIELDPNDLLPKQICERCLSKLQEFYSFRERCLESQELLQ 73
zf-AD smart00868
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ...
 16-87 1.94e-16

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: 74.47  E-value: 1.94e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281361910    16 LCRICTDSSDHKTNIYSPEGRAKnLSQKILECLSLQIDEKDRLPKVVCAQCVQLVEQIHGLRATCRNSQTML 87
Cdd:smart00868   1 VCRLCLSESENLVSIFDESSEAS-LAEKIEECTGIEIEPDDGLPKVICGDCLEKLESFHKFRERCRESDELL 71
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 766-788 2.19e-06

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: 44.60  E-value: 2.19e-06
                          10        20
                  ....*....|....*....|...
gi 281361910  766 YTCEVCKKPFSRKDNLNKHRRIH 788
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA03247 PHA03247
large tegument protein UL36; Provisional
 497-709 3.24e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910  497 PTFKTPSPKQKPMPSPKSKTTVGPSSGGSNGTSTNEFKRLITQTKPQPQVKQQQTAGLSASGAPTATSANQAAMQRLSSN 576
Cdd:PHA03247 2743 AVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAA 2822

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910  577 TTITKVPKQPASLPAPAPTSN---PAKLPM---------LNKQNITISRISMQTAPKAQSKPSTTSPTPASQPIPVSVPA 644
Cdd:PHA03247 2823 SPAGPLPPPTSAQPTAPPPPPgppPPSLPLggsvapggdVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPP 2902

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281361910  645 LSQAQPPPLAAQHKKIVRKPPENQDT-SGQKVKAARPPQQILPSPQQEGQNATHSGSEAPTTSGLI 709
Cdd:PHA03247 2903 DQPERPPQPQAPPPPQPQPQPPPPPQpQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALV 2968
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
566-825 1.15e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.84  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910 566 NQAAMQRLSSNTTITKVPKQPASLPAPAPT-SNPAKLPMLNKQNITISRISMQTAPKAQSKPSTTSPTPASQPIPVSVPA 644
Cdd:COG5048  144 SNLRNNPLPGNNSSSVNTPQSNSLHPPLPAnSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910 645 L-SQAQPPPLAAQHKKIVRKPPENQDTSGQKVKAARPPQQILPSPQQEGQNATHSGSEAPTTSGLI--CPTCKREFKKKE 721
Cdd:COG5048  224 SsSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSSSEKGFSLPikSKQCNISFSRSS 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910 722 HLTQHVKLH----AGLRPFKCSEEGCDKTFSRKEHLSRHLVSHSGQKMYTC--EVCKKPFSRKDNLNKHRRIHTQTSTET 795
Cdd:COG5048  304 PLTRHLRSVnhsgESLKPFSCPYSLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPQSLQQYKDLKN 383

                        250       260       270
                 ....*....|....*....|....*....|....
gi 281361910 796 --LYCCDV--CNKNFATKLHYEKHREMHKKIRPE 825
Cdd:COG5048  384 dkKSETLSnsCIRNFKRDSNLSLHIITHLSFRPY 417
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 577-751 2.07e-04

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 44.86  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910 577 TTITKVPKQPASLPAPAPTSNPAKLPMLNKQNITISRISMQTAPKAQSKPSTTSPTP-ASQPIPVSVPALSQAQPPPlaa 655
Cdd:cd23959  129 THKTAQVAPPKAEPQTAPVTPFGQLPMFGQHPPPAKPLPAAAAAQQSSASPGEVASPfASGTVSASPFATATDTAPS--- 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910 656 qhkkivrkpPENQDTSGQKVKAARPPQQIlPSPQQEGQNATHSGSEAPTTSGliCPTCKREFKKKEHLTQHVKLHAGLRP 735
Cdd:cd23959  206 ---------SGAPDGFPAEASAPSPFAAP-ASAASFPAAPVANGEAATPTHA--CTICGKAFSTHEGLRMHSKAKHGVEL 273

                        170
                 ....*....|....*.
gi 281361910 736 FKcseegcDKTFSRKE 751
Cdd:cd23959  274 EK------AKTAKRKK 283
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 736-760 3.89e-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: 38.44  E-value: 3.89e-04
                          10        20
                  ....*....|....*....|....*
gi 281361910  736 FKCSEegCDKTFSRKEHLSRHLVSH 760
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 584-690 6.62e-04

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: 43.49  E-value: 6.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910  584 KQPASLPAPAPTSNPAKLPMLNKQNITISRIsmQTAPKAQSKPSTTSPTPASQPIPVSVPAlSQAQPPPLAAQHKKIVRK 663
Cdd:pfam09770 169 KAAAPAPAPQPAAQPASLPAPSRKMMSLEEV--EAAMRAQAKKPAQQPAPAPAQPPAAPPA-QQAQQQQQFPPQIQQQQQ 245

                          90       100
                  ....*....|....*....|....*..
gi 281361910  664 PPENQDTSGQKVKAARPPQqILPSPQQ 690
Cdd:pfam09770 246 PQQQPQQPQQHPGQGHPVT-ILQRPQS 271
ZnF_C2H2 smart00355
zinc finger;
766-788 8.14e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 37.45  E-value: 8.14e-04
                           10        20
                   ....*....|....*....|...
gi 281361910   766 YTCEVCKKPFSRKDNLNKHRRIH 788
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 556-705 2.75e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 41.24  E-value: 2.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910 556 ASGAPTATSANQAAMQRlssnttitkvPKQPASLPAPAPTSNPAKLPmlnkqnitisrismQTAPkaqskPSTTSPTPAS 635
Cdd:PRK14951 367 AAAAEAAAPAEKKTPAR----------PEAAAPAAAPVAQAAAAPAP--------------AAAP-----AAAASAPAAP 417

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910 636 QPIPVSVPALSQAQPPPLAAQHKKIVRKPPENQDTSGQKVKAARPPQQILPSPQQEGQNATHSGSEAPTT 705
Cdd:PRK14951 418 PAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAAR 487
PHA03247 PHA03247
large tegument protein UL36; Provisional
 418-692 2.77e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910  418 QLTPQTLGNPGSAFQGTTvtQNQFLAPQQPLTQLPNTAQVTSQQIIRSPHTSTTNSQLVIRNVTNIPPTPTTPTSSKKAP 497
Cdd:PHA03247 2595 SARPRAPVDDRGDPRGPA--PPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGR 2672

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910  498 TFKTPSPKQKPMPsPKSKTTVGP-SSGGSNGTSTNEFKRLITQTKPQPQVKQQQTAGLSASGAPTATSANQAAMQRLSSN 576
Cdd:PHA03247 2673 AAQASSPPQRPRR-RAARPTVGSlTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATP 2751

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910  577 TTITKVPKQPAslPAPAPTSNPAKLPMLNKQNITISRISMQTAPKAQSKPSTTSPTPASQPIPVSVPALSQAQPPplaaq 656
Cdd:PHA03247 2752 GGPARPARPPT--TAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP----- 2824

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 281361910  657 hkkivrKPPENQDTSGQKVKAARPPQQILPSPQQEG 692
Cdd:PHA03247 2825 ------AGPLPPPTSAQPTAPPPPPGPPPPSLPLGG 2854
zf-H2C2_2 pfam13465
Zinc-finger double domain;
752-777 3.13e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 3.13e-03
                          10        20
                  ....*....|....*....|....*.
gi 281361910  752 HLSRHLVSHSGQKMYTCEVCKKPFSR 777
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 766-788 3.17e-03

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.


Pssm-ID: 464025  Cd Length: 24  Bit Score: 35.70  E-value: 3.17e-03
                          10        20
                  ....*....|....*....|...
gi 281361910  766 YTCEVCKKPFSRKDNLNKHRRIH 788
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTH 23
PHA03247 PHA03247
large tegument protein UL36; Provisional
 556-715 3.45e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910  556 ASGAPTATSANQAAMQRLSSNTTitkVPKQPASLPAPAPTS------NPAKLPMLNKQNITISRISMQTAPKAQSKPSTT 629
Cdd:PHA03247 2600 APVDDRGDPRGPAPPSPLPPDTH---APDPPPPSPSPAANEpdphppPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQA 2676

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910  630 SPTP------ASQPIPVSVPALSQAQPPPLAAQHKKIVRKPPENQDTSGQKVKAARPPQQILPSPQQEGQNATHSGSEA- 702
Cdd:PHA03247 2677 SSPPqrprrrAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPAr 2756

                         170
                  ....*....|....*..
gi 281361910  703 ----PTTSGLICPTCKR 715
Cdd:PHA03247 2757 parpPTTAGPPAPAPPA 2773
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
555-691 4.06e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.01  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910 555 SASGAPTATSANQAAMQRLSSNTTITKVPKQPASLPAPAPTSNPAKLPmlnkQNITISRISMQTAPKAQSKPSTTSPTPA 634
Cdd:PRK12323 376 TAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAP----ARRSPAPEALAAARQASARGPGGAPAPA 451

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281361910 635 SQPIPVSV----PALSQAQPPPLAAQHKKIVRKPPenqdtsgqkvkAARPPQQILPSPQQE 691
Cdd:PRK12323 452 PAPAAAPAaaarPAAAGPRPVAAAAAAAPARAAPA-----------AAPAPADDDPPPWEE 501
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 552-655 5.07e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 5.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910 552 AGLSASGAPTATSANQAAMQRLSSNTTITKVPKQPASLPAPAPTSNPAKLPMLNKQNITISRismQTAPKAQSKP---ST 628
Cdd:PRK07764 397 AAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPP---AAAPSAQPAPapaAA 473

                         90       100
                 ....*....|....*....|....*..
gi 281361910 629 TSPTPASQPIPVSVPALSQAQPPPLAA 655
Cdd:PRK07764 474 PEPTAAPAPAPPAAPAPAAAPAAPAAP 500
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 797-819 6.12e-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: 6.12e-03
                          10        20
                  ....*....|....*....|...
gi 281361910  797 YCCDVCNKNFATKLHYEKHREMH 819
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 563-664 7.18e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 40.18  E-value: 7.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361910 563 TSANQAAMQRLSSNTTITKVP-KQPASLPAPAPTSNPAKLPMLNKQNITISRISMQTAPKAQSK-PSTTSPTPASQPIPV 640
Cdd:PRK14950 344 TSYGQLPLELAVIEALLVPVPaPQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVRETAtPPPVPPRPVAPPVPH 423

                         90       100
                 ....*....|....*....|....
gi 281361910 641 svpalSQAQPPPLAAQHKKIVRKP 664
Cdd:PRK14950 424 -----TPESAPKLTRAAIPVDEKP 442
 
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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