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Conserved domains on  [gi|1039778959|ref|XP_017177789|]
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zinc finger protein 865 isoform X3 [Mus musculus]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 11473154)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
623-645 9.30e-07

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.83  E-value: 9.30e-07
                          10        20
                  ....*....|....*....|...
gi 1039778959 623 LKRHERIHTGEKPHQCPVCGKRF 645
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
KREPA super family cl49620
Kinetoplastid RNA Editing Protein A (KREPA); The KREPA 1-6 (TbMP81, 63, 42, 24, 19, and 18, ...
 335-468 9.37e-07

Kinetoplastid RNA Editing Protein A (KREPA); The KREPA 1-6 (TbMP81, 63, 42, 24, 19, and 18, respectively) proteins are components of the RNA editing complex of parasitic protozoans such as Trypanosoma and Leishmania species. These parasites have a uniquely organized mitochondrial genome, the kinetoplast. Most kinetoplast-transcribed mRNAs are cryptic and encode multiple subunits for the electron transport chain following maturation through a uridine insertion/deletion process called RNA editing. KREPAs participate in the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. The editosome, a high molecular mass enzyme complex, carries out the reaction with the help of critical enzymes and structural proteins. Five related editosome proteins KREPA1 (TbMP81), KREPA2 (TbMP63), KREPA3 (TbMP42), KREPA4 (TbMP24), KREPA5 (TbMP19), and KREPA6 (TbMP18) play critical roles in the structure and auxiliary functions of the editing process without any predicted catalytic function. The KREPA1, KREPA2, and KREPA3 proteins contain C2H2 zinc finger motifs and KREPA4 and KREPA6, contain RNA-binding domains but all have a conserved C-terminal sequences that resemble an oligonucleotide-binding (OB)-fold domain. Thus, this group of five proteins is likely to be involved in protein-protein and/or protein-RNA interactions. RNA editing is crucial for the parasite's survival in both its bloodstream and procyclic form life cycle stages which allows the parasite to adapt to its environment and maintain its viability.


The actual alignment was detected with superfamily member cd23959:

Pssm-ID: 483960 [Multi-domain]  Cd Length: 424  Bit Score: 52.18  E-value: 9.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778959 335 VPPTPTGGTPQPG-PALPSLGLPVSTASATASSDPAAVSSgPSATPATPATSTDGNTTPAAPPGVAMPPSATTGGDGPFA 413
Cdd:cd23959   145 APVTPFGQLPMFGqHPPPAKPLPAAAAAQQSSASPGEVAS-PFASGTVSASPFATATDTAPSSGAPDGFPAEASAPSPFA 223

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039778959 414 CSLCWKVFKKPSHLHQHQIihtgEKPFSCSVCSKSFNRRESLKRHVKT-HSADLLR 468
Cdd:cd23959   224 APASAASFPAAPVANGEAA----TPTHACTICGKAFSTHEGLRMHSKAkHGVELEK 275
PHA03378 super family cl33729
EBNA-3B; Provisional
 225-411 4.97e-04

EBNA-3B; Provisional


The actual alignment was detected with superfamily member PHA03378:

Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.90  E-value: 4.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778959 225 PTPGPG--------------VASGLGTPTGTPGPLTTPSQTPPGPAVGAACDPTKDDKGYFRRLKYLMERrfPCGVCQKS 290
Cdd:PHA03378  565 PAPGLGplqiqpltspttsqLASSAPSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMR--PLRMQPIT 642

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778959 291 F------------KQSSHLVQHMLVHSGERPYEcgicGRTYNHVSSLIRHRRCHKDVPPtPTGGTPQPGPALPSLGLPVS 358
Cdd:PHA03378  643 FnvlvfptphqppQVEITPYKPTWTQIGHIPYQ----PSPTGANTMLPIQWAPGTMQPP-PRAPTPMRPPAAPPGRAQRP 717

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039778959 359 TASATASSDPAAVSSG---PSATPA---TPATSTDGNTTPAAPPGVAMPPSATTGGDGP 411
Cdd:PHA03378  718 AAATGRARPPAAAPGRarpPAAAPGrarPPAAAPGRARPPAAAPGRARPPAAAPGAPTP 776
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 632-683 2.72e-03

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


The actual alignment was detected with superfamily member COG5189:

Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.86  E-value: 2.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039778959 632 GEKPHQCPV--CGKRFRESFHLsKHHVVH--------------------TRERPYKCELCGKVFGYPQSLTRHR 683
Cdd:COG5189   346 DGKPYKCPVegCNKKYKNQNGL-KYHMLHghqnqklhenpspekmnifsAKDKPYRCEVCDKRYKNLNGLKYHR 418
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
623-645 9.30e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.83  E-value: 9.30e-07
                          10        20
                  ....*....|....*....|...
gi 1039778959 623 LKRHERIHTGEKPHQCPVCGKRF 645
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 335-468 9.37e-07

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: 52.18  E-value: 9.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778959 335 VPPTPTGGTPQPG-PALPSLGLPVSTASATASSDPAAVSSgPSATPATPATSTDGNTTPAAPPGVAMPPSATTGGDGPFA 413
Cdd:cd23959   145 APVTPFGQLPMFGqHPPPAKPLPAAAAAQQSSASPGEVAS-PFASGTVSASPFATATDTAPSSGAPDGFPAEASAPSPFA 223

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039778959 414 CSLCWKVFKKPSHLHQHQIihtgEKPFSCSVCSKSFNRRESLKRHVKT-HSADLLR 468
Cdd:cd23959   224 APASAASFPAAPVANGEAA----TPTHACTICGKAFSTHEGLRMHSKAkHGVELEK 275
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
411-483 9.40e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 9.40e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039778959 411 PFACSLCWKVFKKPSHLHQHQIIHTGEKPFSCSV--CSKSFNRRESLKRHVKTHSADLLRLPCGICGKVFRDASY 483
Cdd:COG5048    33 PDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASS 107
PHA03247 PHA03247
large tegument protein UL36; Provisional
 334-405 1.50e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 1.50e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039778959  334 DVPPTPTGGTPQPGPALPSLGLPVSTASATASSDPAAVSSGPSATPATPATSTdGNTTPAAPPGVAMPPSAT 405
Cdd:PHA03247  2700 DPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPG-GPARPARPPTTAGPPAPA 2770
PHA03378 PHA03378
EBNA-3B; Provisional
 225-411 4.97e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.90  E-value: 4.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778959 225 PTPGPG--------------VASGLGTPTGTPGPLTTPSQTPPGPAVGAACDPTKDDKGYFRRLKYLMERrfPCGVCQKS 290
Cdd:PHA03378  565 PAPGLGplqiqpltspttsqLASSAPSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMR--PLRMQPIT 642

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778959 291 F------------KQSSHLVQHMLVHSGERPYEcgicGRTYNHVSSLIRHRRCHKDVPPtPTGGTPQPGPALPSLGLPVS 358
Cdd:PHA03378  643 FnvlvfptphqppQVEITPYKPTWTQIGHIPYQ----PSPTGANTMLPIQWAPGTMQPP-PRAPTPMRPPAAPPGRAQRP 717

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039778959 359 TASATASSDPAAVSSG---PSATPA---TPATSTDGNTTPAAPPGVAMPPSATTGGDGP 411
Cdd:PHA03378  718 AAATGRARPPAAAPGRarpPAAAPGrarPPAAAPGRARPPAAAPGRARPPAAAPGAPTP 776
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 337-413 5.11e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 43.75  E-value: 5.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778959 337 PTPTGGTPQPGPALPSLGlPVSTASATASSDPAAVSSGPSATPATPATS--TDGNTTPAAPPGVAMP--PSATTGGDGPF 412
Cdd:pfam05109 523 PTPAVTTPTPNATSPTLG-KTSPTSAVTTPTPNATSPTPAVTTPTPNATipTLGKTSPTSAVTTPTPnaTSPTVGETSPQ 601


                  .
gi 1039778959 413 A 413
Cdd:pfam05109 602 A 602
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
610-655 1.59e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.99  E-value: 1.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039778959 610 CGICGRAFGRRETLKRHERIHTGEKPHQCPVCGKRFRES------FHLSKHH 655
Cdd:COG5048    36 CPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrplelsRHLRTHH 87
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 282-304 2.14e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 2.14e-03
                          10        20
                  ....*....|....*....|...
gi 1039778959 282 FPCGVCQKSFKQSSHLVQHMLVH 304
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 632-683 2.72e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.86  E-value: 2.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039778959 632 GEKPHQCPV--CGKRFRESFHLsKHHVVH--------------------TRERPYKCELCGKVFGYPQSLTRHR 683
Cdd:COG5189   346 DGKPYKCPVegCNKKYKNQNGL-KYHMLHghqnqklhenpspekmnifsAKDKPYRCEVCDKRYKNLNGLKYHR 418
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 664-686 7.29e-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: 34.58  E-value: 7.29e-03
                          10        20
                  ....*....|....*....|...
gi 1039778959 664 YKCELCGKVFGYPQSLTRHRQVH 686
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
623-645 9.30e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.83  E-value: 9.30e-07
                          10        20
                  ....*....|....*....|...
gi 1039778959 623 LKRHERIHTGEKPHQCPVCGKRF 645
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 335-468 9.37e-07

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: 52.18  E-value: 9.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778959 335 VPPTPTGGTPQPG-PALPSLGLPVSTASATASSDPAAVSSgPSATPATPATSTDGNTTPAAPPGVAMPPSATTGGDGPFA 413
Cdd:cd23959   145 APVTPFGQLPMFGqHPPPAKPLPAAAAAQQSSASPGEVAS-PFASGTVSASPFATATDTAPSSGAPDGFPAEASAPSPFA 223

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039778959 414 CSLCWKVFKKPSHLHQHQIihtgEKPFSCSVCSKSFNRRESLKRHVKT-HSADLLR 468
Cdd:cd23959   224 APASAASFPAAPVANGEAA----TPTHACTICGKAFSTHEGLRMHSKAkHGVELEK 275
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
411-483 9.40e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 9.40e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039778959 411 PFACSLCWKVFKKPSHLHQHQIIHTGEKPFSCSV--CSKSFNRRESLKRHVKTHSADLLRLPCGICGKVFRDASY 483
Cdd:COG5048    33 PDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASS 107
PHA03247 PHA03247
large tegument protein UL36; Provisional
 334-405 1.50e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 1.50e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039778959  334 DVPPTPTGGTPQPGPALPSLGLPVSTASATASSDPAAVSSGPSATPATPATSTdGNTTPAAPPGVAMPPSAT 405
Cdd:PHA03247  2700 DPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPG-GPARPARPPTTAGPPAPA 2770
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
281-458 2.71e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.38  E-value: 2.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778959 281 RFPCGVCQKSFKQSSHLVQHM--LVHSGE--RPYECGI--CGRTYNHVSSLIRHRRCHKDVPPTPTggTPQPGPAL---P 351
Cdd:COG5048   289 PIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKE--KLLNSSSKfspL 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778959 352 SLGLPVSTASATASSDPAAVSSGPSatPATPATSTDGNTtpaappgvAMPPSATTGGDGP--FACSLCWKVFKKPSHLHQ 429
Cdd:COG5048   367 LNNEPPQSLQQYKDLKNDKKSETLS--NSCIRNFKRDSN--------LSLHIITHLSFRPynCKNPPCSKSFNRHYNLIP 436

                         170       180
                  ....*....|....*....|....*....
gi 1039778959 430 HQIIHTGEKPFSCSvCSKSFNRRESLKRH 458
Cdd:COG5048   437 HKKIHTNHAPLLCS-ILKSFRRDLDLSNH 464
PHA03378 PHA03378
EBNA-3B; Provisional
 225-411 4.97e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.90  E-value: 4.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778959 225 PTPGPG--------------VASGLGTPTGTPGPLTTPSQTPPGPAVGAACDPTKDDKGYFRRLKYLMERrfPCGVCQKS 290
Cdd:PHA03378  565 PAPGLGplqiqpltspttsqLASSAPSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMR--PLRMQPIT 642

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778959 291 F------------KQSSHLVQHMLVHSGERPYEcgicGRTYNHVSSLIRHRRCHKDVPPtPTGGTPQPGPALPSLGLPVS 358
Cdd:PHA03378  643 FnvlvfptphqppQVEITPYKPTWTQIGHIPYQ----PSPTGANTMLPIQWAPGTMQPP-PRAPTPMRPPAAPPGRAQRP 717

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039778959 359 TASATASSDPAAVSSG---PSATPA---TPATSTDGNTTPAAPPGVAMPPSATTGGDGP 411
Cdd:PHA03378  718 AAATGRARPPAAAPGRarpPAAAPGrarPPAAAPGRARPPAAAPGRARPPAAAPGAPTP 776
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 337-413 5.11e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 43.75  E-value: 5.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778959 337 PTPTGGTPQPGPALPSLGlPVSTASATASSDPAAVSSGPSATPATPATS--TDGNTTPAAPPGVAMP--PSATTGGDGPF 412
Cdd:pfam05109 523 PTPAVTTPTPNATSPTLG-KTSPTSAVTTPTPNATSPTPAVTTPTPNATipTLGKTSPTSAVTTPTPnaTSPTVGETSPQ 601


                  .
gi 1039778959 413 A 413
Cdd:pfam05109 602 A 602
zf-H2C2_2 pfam13465
Zinc-finger double domain;
429-451 5.28e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 5.28e-04
                          10        20
                  ....*....|....*....|...
gi 1039778959 429 QHQIIHTGEKPFSCSVCSKSFNR 451
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
PRK10856 PRK10856
cytoskeleton protein RodZ;
334-405 5.81e-04

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 42.71  E-value: 5.81e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039778959 334 DVPPTPTGgTPQPGPALPSLGLPVSTASATASSDPAAVSSGPSATPATPATSTDGNTTPAAPPGVAMPPSAT 405
Cdd:PRK10856  181 PVDTTPTN-SQTPAVATAPAPAVDPQQNAVVAPSQANVDTAATPAPAAPATPDGAAPLPTDQAGVSTPAADP 251
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 338-406 5.82e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 43.41  E-value: 5.82e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778959 338 TPTGGTPQPGPALPSLGLPVSTASATASSDPAAVSSGPSATPATP-ATSTDGNTTPAAPPGVAMPPSATT 406
Cdd:pfam17823 167 APHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGiSTAATATGHPAAGTALAAVGNSSP 236
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
291-491 1.55e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.99  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778959 291 FKQSSHLVQHMLVHSGERPYECgICGRTYNHVSSLIRHRRCHKDVPPTPTGgTPQPGPALPSLGLPVSTASATASSdpaa 370
Cdd:COG5048   181 SSNLSLLISSNVSTSIPSSSEN-SPLSSSYSIPSSSSDQNLENSSSSLPLT-TNSQLSPKSLLSQSPSSLSSSDSS---- 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778959 371 vssgpsATPATPATSTDGNTTPAAPPGVAMPPSATTGGDGPFACSLCWKVFKKPSHL--HQHQIIHTGE--KPFSC--SV 444
Cdd:COG5048   255 ------SSASESPRSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLtrHLRSVNHSGEslKPFSCpySL 328

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1039778959 445 CSKSFNRRESLKRHVKTHSADLLRLPC-GICGKVFRDASYLLKHQAAH 491
Cdd:COG5048   329 CGKLFSRNDALKRHILLHTSISPAKEKlLNSSSKFSPLLNNEPPQSLQ 376
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
610-655 1.59e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.99  E-value: 1.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039778959 610 CGICGRAFGRRETLKRHERIHTGEKPHQCPVCGKRFRES------FHLSKHH 655
Cdd:COG5048    36 CPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrplelsRHLRTHH 87
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 440-462 1.64e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 1.64e-03
                          10        20
                  ....*....|....*....|...
gi 1039778959 440 FSCSVCSKSFNRRESLKRHVKTH 462
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
335-413 1.95e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 41.76  E-value: 1.95e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039778959 335 VPPTPTGGTPQPGPAlpslglPVSTASATASSDPAAVSSGPSATPATPATSTDGNTTPAAPPGVAMPPSATTGGDGPFA 413
Cdd:PRK07003  372 VPARVAGAVPAPGAR------AAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAAD 444
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 282-304 2.14e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 2.14e-03
                          10        20
                  ....*....|....*....|...
gi 1039778959 282 FPCGVCQKSFKQSSHLVQHMLVH 304
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 632-683 2.72e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.86  E-value: 2.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039778959 632 GEKPHQCPV--CGKRFRESFHLsKHHVVH--------------------TRERPYKCELCGKVFGYPQSLTRHR 683
Cdd:COG5189   346 DGKPYKCPVegCNKKYKNQNGL-KYHMLHghqnqklhenpspekmnifsAKDKPYRCEVCDKRYKNLNGLKYHR 418
PHA03247 PHA03247
large tegument protein UL36; Provisional
 327-406 3.02e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 3.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778959  327 RHRRCHKDVPPTPTGGTPQpGPALPSLglPVSTASATASSDPAAVSSGP--------SATPATPATSTDGNTTPAAPPGV 398
Cdd:PHA03247  2663 RPRRARRLGRAAQASSPPQ-RPRRRAA--RPTVGSLTSLADPPPPPPTPepaphalvSATPLPPGPAAARQASPALPAAP 2739


                   ....*...
gi 1039778959  399 AMPPSATT 406
Cdd:PHA03247  2740 APPAVPAG 2747
PRK10856 PRK10856
cytoskeleton protein RodZ;
338-406 3.82e-03

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 40.39  E-value: 3.82e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039778959 338 TPTGGTPQPGPALPSLGLPVSTASATASSDPAAVSSGPSATPATPATSTdgNTTPAAPPGVAMPPSATT 406
Cdd:PRK10856  170 TDPATTPAPAAPVDTTPTNSQTPAVATAPAPAVDPQQNAVVAPSQANVD--TAATPAPAAPATPDGAAP 236
zf-H2C2_2 pfam13465
Zinc-finger double domain;
296-321 4.76e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.76e-03
                          10        20
                  ....*....|....*....|....*.
gi 1039778959 296 HLVQHMLVHSGERPYECGICGRTYNH 321
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
335-411 6.04e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 40.12  E-value: 6.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778959 335 VPPTPTGGTPQPGPALPSLGLPVSTAS-----------ATASSDPAAVSSGPSATPATPAT--STDGNTTPAAPPGVAMP 401
Cdd:COG3469   122 VTSTTSSTAGSTTTSGASATSSAGSTTttttvsgtetaTGGTTTTSTTTTTTSASTTPSATttATATTASGATTPSATTT 201

                          90
                  ....*....|
gi 1039778959 402 PSATTGGDGP 411
Cdd:COG3469   202 ATTTGPPTPG 211
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 334-384 6.14e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 40.05  E-value: 6.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039778959 334 DVPPTP--TGGTPQPGPALPSL----GLPVSTASATASSDPAAVSSGPSA-TPATPAT 384
Cdd:PRK14959  438 DAPPAPprSGIPPRPAPRMPEAspvpGAPDSVASASDAPPTLGDPSDTAEhTPSGPRT 495
PHA03247 PHA03247
large tegument protein UL36; Provisional
 336-416 7.16e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 7.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778959  336 PPTPTGGTPQPGPALPSLGLPVSTASATASSDPAAVSSgpSATPATPATSTDGNTTPAAPPGVAMPPSATTGGDGPFACS 415
Cdd:PHA03247  2772 PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPA--AVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPS 2849


                   .
gi 1039778959  416 L 416
Cdd:PHA03247  2850 L 2850
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 664-686 7.29e-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: 34.58  E-value: 7.29e-03
                          10        20
                  ....*....|....*....|...
gi 1039778959 664 YKCELCGKVFGYPQSLTRHRQVH 686
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 336-410 8.21e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.97  E-value: 8.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039778959 336 PPTPTGGTPQPGPALPSLGLPVSTASATASSDPAAVSSGPSATPATPATSTDGNTTPAAPPGVAMPPSATTGGDG 410
Cdd:PRK07764  434 APAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADD 508
PHA03247 PHA03247
large tegument protein UL36; Provisional
 336-416 9.71e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 9.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039778959  336 PPTPTGGTPQP-GPALPSLGLPVSTASATASSDPA--AVSSGPSATPATPATSTDGNTTPAAPPGVAMPPSATTGGDGPF 412
Cdd:PHA03247  2712 PHALVSATPLPpGPAAARQASPALPAAPAPPAVPAgpATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASL 2791


                   ....
gi 1039778959  413 ACSL 416
Cdd:PHA03247  2792 SESR 2795
 
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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