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Conserved domains on  [gi|594190882|ref|NP_001277355|]
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zinc finger protein 865 isoform 2 [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
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
349-421 8.47e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 8.47e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 594190882 349 PFACSLCWKVFKKPSHLHQHQIIHTGEKPFSCSV--CSKSFNRRESLKRHVKTHSADLLRLPCGICGKVFRDASY 421
Cdd:COG5048   33 PDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASS 107
zf-H2C2_2 pfam13465
Zinc-finger double domain;
561-583 8.61e-07

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.83  E-value: 8.61e-07
                          10        20
                  ....*....|....*....|...
gi 594190882  561 LKRHERIHTGEKPHQCPVCGKRF 583
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, ...
 273-406 1.44e-06

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: 51.41  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882 273 VPPTPTGGTPQPG-PALPSLGLPVSTASATASSDPAAVSSgPSATPATPATSTDGNTTPAAPPGVAMPPSATTGGDGPFA 351
Cdd:cd23959  145 APVTPFGQLPMFGqHPPPAKPLPAAAAAQQSSASPGEVAS-PFASGTVSASPFATATDTAPSSGAPDGFPAEASAPSPFA 223

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 594190882 352 CSLCWKVFKKPSHLHQHQIihtgEKPFSCSVCSKSFNRRESLKRHVKT-HSADLLR 406
Cdd:cd23959  224 APASAASFPAAPVANGEAA----TPTHACTICGKAFSTHEGLRMHSKAkHGVELEK 275
PHA03378 super family cl33729
EBNA-3B; Provisional
 163-349 8.31e-04

EBNA-3B; Provisional


The actual alignment was detected with superfamily member PHA03378:

Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.13  E-value: 8.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882 163 PTPGPG--------------VASGLGTPTGTPGPLTTPSQTPPGPAVGAACDPTKDDKGYFRRLKYLMERrfPCGVCQKS 228
Cdd:PHA03378 565 PAPGLGplqiqpltspttsqLASSAPSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMR--PLRMQPIT 642

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882 229 F------------KQSSHLVQHMLVHSGERPYEcgicGRTYNHVSSLIRHRRCHKDVPPtPTGGTPQPGPALPSLGLPVS 296
Cdd:PHA03378 643 FnvlvfptphqppQVEITPYKPTWTQIGHIPYQ----PSPTGANTMLPIQWAPGTMQPP-PRAPTPMRPPAAPPGRAQRP 717

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 594190882 297 TASATASSDPAAVSSG---PSATPA---TPATSTDGNTTPAAPPGVAMPPSATTGGDGP 349
Cdd:PHA03378 718 AAATGRARPPAAAPGRarpPAAAPGrarPPAAAPGRARPPAAAPGRARPPAAAPGAPTP 776
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 570-621 3.56e-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: 40.47  E-value: 3.56e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 594190882 570 GEKPHQCPV--CGKRFRESFHLsKHHVVH--------------------TRERPYKCELCGKVFGYPQSLTRHR 621
Cdd:COG5189  346 DGKPYKCPVegCNKKYKNQNGL-KYHMLHghqnqklhenpspekmnifsAKDKPYRCEVCDKRYKNLNGLKYHR 418
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
349-421 8.47e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 8.47e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 594190882 349 PFACSLCWKVFKKPSHLHQHQIIHTGEKPFSCSV--CSKSFNRRESLKRHVKTHSADLLRLPCGICGKVFRDASY 421
Cdd:COG5048   33 PDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASS 107
zf-H2C2_2 pfam13465
Zinc-finger double domain;
561-583 8.61e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.83  E-value: 8.61e-07
                          10        20
                  ....*....|....*....|...
gi 594190882  561 LKRHERIHTGEKPHQCPVCGKRF 583
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 273-406 1.44e-06

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: 51.41  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882 273 VPPTPTGGTPQPG-PALPSLGLPVSTASATASSDPAAVSSgPSATPATPATSTDGNTTPAAPPGVAMPPSATTGGDGPFA 351
Cdd:cd23959  145 APVTPFGQLPMFGqHPPPAKPLPAAAAAQQSSASPGEVAS-PFASGTVSASPFATATDTAPSSGAPDGFPAEASAPSPFA 223

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 594190882 352 CSLCWKVFKKPSHLHQHQIihtgEKPFSCSVCSKSFNRRESLKRHVKT-HSADLLR 406
Cdd:cd23959  224 APASAASFPAAPVANGEAA----TPTHACTICGKAFSTHEGLRMHSKAkHGVELEK 275
PHA03247 PHA03247
large tegument protein UL36; Provisional
 272-343 1.89e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.86  E-value: 1.89e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 594190882  272 DVPPTPTGGTPQPGPALPSLGLPVSTASATASSDPAAVSSGPSATPATPATSTdGNTTPAAPPGVAMPPSAT 343
Cdd:PHA03247 2700 DPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPG-GPARPARPPTTAGPPAPA 2770
zf-H2C2_2 pfam13465
Zinc-finger double domain;
367-389 4.88e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.88e-04
                          10        20
                  ....*....|....*....|...
gi 594190882  367 QHQIIHTGEKPFSCSVCSKSFNR 389
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
PHA03378 PHA03378
EBNA-3B; Provisional
 163-349 8.31e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.13  E-value: 8.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882 163 PTPGPG--------------VASGLGTPTGTPGPLTTPSQTPPGPAVGAACDPTKDDKGYFRRLKYLMERrfPCGVCQKS 228
Cdd:PHA03378 565 PAPGLGplqiqpltspttsqLASSAPSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMR--PLRMQPIT 642

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882 229 F------------KQSSHLVQHMLVHSGERPYEcgicGRTYNHVSSLIRHRRCHKDVPPtPTGGTPQPGPALPSLGLPVS 296
Cdd:PHA03378 643 FnvlvfptphqppQVEITPYKPTWTQIGHIPYQ----PSPTGANTMLPIQWAPGTMQPP-PRAPTPMRPPAAPPGRAQRP 717

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 594190882 297 TASATASSDPAAVSSG---PSATPA---TPATSTDGNTTPAAPPGVAMPPSATTGGDGP 349
Cdd:PHA03378 718 AAATGRARPPAAAPGRarpPAAAPGrarPPAAAPGRARPPAAAPGRARPPAAAPGAPTP 776
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 275-351 8.40e-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: 42.98  E-value: 8.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882  275 PTPTGGTPQPGPALPSLGlPVSTASATASSDPAAVSSGPSATPATPATS--TDGNTTPAAPPGVAMP--PSATTGGDGPF 350
Cdd:pfam05109 523 PTPAVTTPTPNATSPTLG-KTSPTSAVTTPTPNATSPTPAVTTPTPNATipTLGKTSPTSAVTTPTPnaTSPTVGETSPQ 601


                  .
gi 594190882  351 A 351
Cdd:pfam05109 602 A 602
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
 275-353 1.19e-03

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 41.80  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882  275 PTPTGGTPQPGPALPSLglpvstASATASSDPAAVSSGPSATPAtpATSTDGNTTPAAPPGVAM-PPSATTGGDGPFACS 353
Cdd:TIGR00601  77 PKTGTGKVAPPAATPTS------APTPTPSPPASPASGMSAAPA--SAVEEKSPSEESATATAPeSPSTSVPSSGSDAAS 148
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 220-242 1.98e-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: 1.98e-03
                          10        20
                  ....*....|....*....|...
gi 594190882  220 FPCGVCQKSFKQSSHLVQHMLVH 242
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 570-621 3.56e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 3.56e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 594190882 570 GEKPHQCPV--CGKRFRESFHLsKHHVVH--------------------TRERPYKCELCGKVFGYPQSLTRHR 621
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 ...
 602-624 6.75e-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: 6.75e-03
                          10        20
                  ....*....|....*....|...
gi 594190882  602 YKCELCGKVFGYPQSLTRHRQVH 624
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
273-349 8.50e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 39.35  E-value: 8.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882 273 VPPTPTGGTPQPGPALPSLGLPVSTAS-----------ATASSDPAAVSSGPSATPATPAT--STDGNTTPAAPPGVAMP 339
Cdd:COG3469  122 VTSTTSSTAGSTTTSGASATSSAGSTTttttvsgtetaTGGTTTTSTTTTTTSASTTPSATttATATTASGATTPSATTT 201

                         90
                 ....*....|
gi 594190882 340 PSATTGGDGP 349
Cdd:COG3469  202 ATTTGPPTPG 211
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
349-421 8.47e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 8.47e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 594190882 349 PFACSLCWKVFKKPSHLHQHQIIHTGEKPFSCSV--CSKSFNRRESLKRHVKTHSADLLRLPCGICGKVFRDASY 421
Cdd:COG5048   33 PDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASS 107
zf-H2C2_2 pfam13465
Zinc-finger double domain;
561-583 8.61e-07

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 45.83  E-value: 8.61e-07
                          10        20
                  ....*....|....*....|...
gi 594190882  561 LKRHERIHTGEKPHQCPVCGKRF 583
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 273-406 1.44e-06

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: 51.41  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882 273 VPPTPTGGTPQPG-PALPSLGLPVSTASATASSDPAAVSSgPSATPATPATSTDGNTTPAAPPGVAMPPSATTGGDGPFA 351
Cdd:cd23959  145 APVTPFGQLPMFGqHPPPAKPLPAAAAAQQSSASPGEVAS-PFASGTVSASPFATATDTAPSSGAPDGFPAEASAPSPFA 223

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 594190882 352 CSLCWKVFKKPSHLHQHQIihtgEKPFSCSVCSKSFNRRESLKRHVKT-HSADLLR 406
Cdd:cd23959  224 APASAASFPAAPVANGEAA----TPTHACTICGKAFSTHEGLRMHSKAkHGVELEK 275
PHA03247 PHA03247
large tegument protein UL36; Provisional
 272-343 1.89e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.86  E-value: 1.89e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 594190882  272 DVPPTPTGGTPQPGPALPSLGLPVSTASATASSDPAAVSSGPSATPATPATSTdGNTTPAAPPGVAMPPSAT 343
Cdd:PHA03247 2700 DPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPG-GPARPARPPTTAGPPAPA 2770
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
219-396 2.45e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.38  E-value: 2.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882 219 RFPCGVCQKSFKQSSHLVQHM--LVHSGE--RPYECGI--CGRTYNHVSSLIRHRRCHKDVPPTPTggTPQPGPAL---P 289
Cdd:COG5048  289 PIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKE--KLLNSSSKfspL 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882 290 SLGLPVSTASATASSDPAAVSSGPSatPATPATSTDGNTtpaappgvAMPPSATTGGDGP--FACSLCWKVFKKPSHLHQ 367
Cdd:COG5048  367 LNNEPPQSLQQYKDLKNDKKSETLS--NSCIRNFKRDSN--------LSLHIITHLSFRPynCKNPPCSKSFNRHYNLIP 436

                        170       180
                 ....*....|....*....|....*....
gi 594190882 368 HQIIHTGEKPFSCSvCSKSFNRRESLKRH 396
Cdd:COG5048  437 HKKIHTNHAPLLCS-ILKSFRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
367-389 4.88e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.88e-04
                          10        20
                  ....*....|....*....|...
gi 594190882  367 QHQIIHTGEKPFSCSVCSKSFNR 389
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
PRK10856 PRK10856
cytoskeleton protein RodZ;
272-343 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 594190882 272 DVPPTPTGgTPQPGPALPSLGLPVSTASATASSDPAAVSSGPSATPATPATSTDGNTTPAAPPGVAMPPSAT 343
Cdd:PRK10856 181 PVDTTPTN-SQTPAVATAPAPAVDPQQNAVVAPSQANVDTAATPAPAAPATPDGAAPLPTDQAGVSTPAADP 251
PHA03378 PHA03378
EBNA-3B; Provisional
 163-349 8.31e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.13  E-value: 8.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882 163 PTPGPG--------------VASGLGTPTGTPGPLTTPSQTPPGPAVGAACDPTKDDKGYFRRLKYLMERrfPCGVCQKS 228
Cdd:PHA03378 565 PAPGLGplqiqpltspttsqLASSAPSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMR--PLRMQPIT 642

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882 229 F------------KQSSHLVQHMLVHSGERPYEcgicGRTYNHVSSLIRHRRCHKDVPPtPTGGTPQPGPALPSLGLPVS 296
Cdd:PHA03378 643 FnvlvfptphqppQVEITPYKPTWTQIGHIPYQ----PSPTGANTMLPIQWAPGTMQPP-PRAPTPMRPPAAPPGRAQRP 717

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 594190882 297 TASATASSDPAAVSSG---PSATPA---TPATSTDGNTTPAAPPGVAMPPSATTGGDGP 349
Cdd:PHA03378 718 AAATGRARPPAAAPGRarpPAAAPGrarPPAAAPGRARPPAAAPGRARPPAAAPGAPTP 776
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 275-351 8.40e-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: 42.98  E-value: 8.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882  275 PTPTGGTPQPGPALPSLGlPVSTASATASSDPAAVSSGPSATPATPATS--TDGNTTPAAPPGVAMP--PSATTGGDGPF 350
Cdd:pfam05109 523 PTPAVTTPTPNATSPTLG-KTSPTSAVTTPTPNATSPTPAVTTPTPNATipTLGKTSPTSAVTTPTPnaTSPTVGETSPQ 601


                  .
gi 594190882  351 A 351
Cdd:pfam05109 602 A 602
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 276-344 9.39e-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: 42.64  E-value: 9.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882  276 TPTGGTPQPGPALPSLGLPVSTASATASSDPAAVSSGPSATPATP-ATSTDGNTTPAAPPGVAMPPSATT 344
Cdd:pfam17823 167 APHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGiSTAATATGHPAAGTALAAVGNSSP 236
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
 275-353 1.19e-03

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 41.80  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882  275 PTPTGGTPQPGPALPSLglpvstASATASSDPAAVSSGPSATPAtpATSTDGNTTPAAPPGVAM-PPSATTGGDGPFACS 353
Cdd:TIGR00601  77 PKTGTGKVAPPAATPTS------APTPTPSPPASPASGMSAAPA--SAVEEKSPSEESATATAPeSPSTSVPSSGSDAAS 148
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
229-429 1.41e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.99  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882 229 FKQSSHLVQHMLVHSGERPYECgICGRTYNHVSSLIRHRRCHKDVPPTPTGgTPQPGPALPSLGLPVSTASATASSdpaa 308
Cdd:COG5048  181 SSNLSLLISSNVSTSIPSSSEN-SPLSSSYSIPSSSSDQNLENSSSSLPLT-TNSQLSPKSLLSQSPSSLSSSDSS---- 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882 309 vssgpsATPATPATSTDGNTTPAAPPGVAMPPSATTGGDGPFACSLCWKVFKKPSHL--HQHQIIHTGE--KPFSC--SV 382
Cdd:COG5048  255 ------SSASESPRSSLPTASSQSSSPNESDSSSEKGFSLPIKSKQCNISFSRSSPLtrHLRSVNHSGEslKPFSCpySL 328

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 594190882 383 CSKSFNRRESLKRHVKTHSADLLRLPC-GICGKVFRDASYLLKHQAAH 429
Cdd:COG5048  329 CGKLFSRNDALKRHILLHTSISPAKEKlLNSSSKFSPLLNNEPPQSLQ 376
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
548-593 1.44e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.99  E-value: 1.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 594190882 548 CGICGRAFGRRETLKRHERIHTGEKPHQCPVCGKRFRES------FHLSKHH 593
Cdd:COG5048   36 CPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrplelsRHLRTHH 87
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 378-400 1.52e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 1.52e-03
                          10        20
                  ....*....|....*....|...
gi 594190882  378 FSCSVCSKSFNRRESLKRHVKTH 400
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 220-242 1.98e-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: 1.98e-03
                          10        20
                  ....*....|....*....|...
gi 594190882  220 FPCGVCQKSFKQSSHLVQHMLVH 242
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
273-351 2.46e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 41.37  E-value: 2.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594190882 273 VPPTPTGGTPQPGPAlpslglPVSTASATASSDPAAVSSGPSATPATPATSTDGNTTPAAPPGVAMPPSATTGGDGPFA 351
Cdd:PRK07003 372 VPARVAGAVPAPGAR------AAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAAD 444
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 570-621 3.56e-03

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 40.47  E-value: 3.56e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 594190882 570 GEKPHQCPV--CGKRFRESFHLsKHHVVH--------------------TRERPYKCELCGKVFGYPQSLTRHR 621
Cdd:COG5189  346 DGKPYKCPVegCNKKYKNQNGL-KYHMLHghqnqklhenpspekmnifsAKDKPYRCEVCDKRYKNLNGLKYHR 418
PRK10856 PRK10856
cytoskeleton protein RodZ;
276-344 3.76e-03

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 40.01  E-value: 3.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594190882 276 TPTGGTPQPGPALPSLGLPVSTASATASSDPAAVSSGPSATPATPATSTdgNTTPAAPPGVAMPPSATT 344
Cdd:PRK10856 170 TDPATTPAPAAPVDTTPTNSQTPAVATAPAPAVDPQQNAVVAPSQANVD--TAATPAPAAPATPDGAAP 236
PHA03247 PHA03247
large tegument protein UL36; Provisional
 265-344 3.85e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882  265 RHRRCHKDVPPTPTGGTPQpGPALPSLglPVSTASATASSDPAAVSSGP--------SATPATPATSTDGNTTPAAPPGV 336
Cdd:PHA03247 2663 RPRRARRLGRAAQASSPPQ-RPRRRAA--RPTVGSLTSLADPPPPPPTPepaphalvSATPLPPGPAAARQASPALPAAP 2739


                  ....*...
gi 594190882  337 AMPPSATT 344
Cdd:PHA03247 2740 APPAVPAG 2747
zf-H2C2_2 pfam13465
Zinc-finger double domain;
234-259 4.41e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.41e-03
                          10        20
                  ....*....|....*....|....*.
gi 594190882  234 HLVQHMLVHSGERPYECGICGRTYNH 259
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 272-322 6.56e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 40.05  E-value: 6.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 594190882 272 DVPPTP--TGGTPQPGPALPSL----GLPVSTASATASSDPAAVSSGPSA-TPATPAT 322
Cdd:PRK14959 438 DAPPAPprSGIPPRPAPRMPEAspvpGAPDSVASASDAPPTLGDPSDTAEhTPSGPRT 495
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 602-624 6.75e-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: 6.75e-03
                          10        20
                  ....*....|....*....|...
gi 594190882  602 YKCELCGKVFGYPQSLTRHRQVH 624
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
273-349 8.50e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 39.35  E-value: 8.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882 273 VPPTPTGGTPQPGPALPSLGLPVSTAS-----------ATASSDPAAVSSGPSATPATPAT--STDGNTTPAAPPGVAMP 339
Cdd:COG3469  122 VTSTTSSTAGSTTTSGASATSSAGSTTttttvsgtetaTGGTTTTSTTTTTTSASTTPSATttATATTASGATTPSATTT 201

                         90
                 ....*....|
gi 594190882 340 PSATTGGDGP 349
Cdd:COG3469  202 ATTTGPPTPG 211
PHA03247 PHA03247
large tegument protein UL36; Provisional
 274-354 8.52e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 8.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594190882  274 PPTPTGGTPQPGPALPSLGLPVSTASATASSDPAAVSSgpSATPATPATSTDGNTTPAAPPGVAMPPSATTGGDGPFACS 353
Cdd:PHA03247 2772 PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPA--AVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPS 2849


                  .
gi 594190882  354 L 354
Cdd:PHA03247 2850 L 2850
PRK12495 PRK12495
hypothetical protein; Provisional
 274-342 8.61e-03

hypothetical protein; Provisional


Pssm-ID: 183558 [Multi-domain]  Cd Length: 226  Bit Score: 38.70  E-value: 8.61e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594190882 274 PPTPTGGTPQPGPALPSlglPVSTASATASSDPAAVSSGPSATPATPATSTdgNTTPAAPPGVAMPPSA 342
Cdd:PRK12495 102 PAAEAEAADQSAPPEAS---STSATDEAATDPPATAAARDGPTPDPTAQPA--TPDERRSPRQRPPVSG 165
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 274-348 9.63e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 9.63e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 594190882 274 PPTPTGGTPQPGPALPSLGLPVSTASATASSDPAAVSSGPSATPATPATSTDGNTTPAAPPGVAMPPSATTGGDG 348
Cdd:PRK07764 434 APAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADD 508
 
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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