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Conserved domains on  [gi|1046845297|ref|XP_017445450|]
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zinc finger protein 865 isoform X1 [Rattus norvegicus]

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 3.75e-07

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.93  E-value: 3.75e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046845297  349 PFACSLCWKVFKKPSHLHQHQIIHTGEKPFSCSV--CSKSFNRRESLKRHVKTHSADLLRLPCGICGKVFRDASY 421
Cdd:COG5048     33 PDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASS 107
KREPA super family cl49620
Kinetoplastid RNA Editing Protein A (KREPA); The KREPA 1-6 (TbMP81, 63, 42, 24, 19, and 18, ...
 273-406 6.31e-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: 52.95  E-value: 6.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046845297  273 VPSTPTGSTSQPG-PALPSLGLPVPTASATASSDPAAVSSgPSATPATPATSTDGNTTPAAPPGVamPPSATTGGEGPFA 351
Cdd:cd23959    145 APVTPFGQLPMFGqHPPPAKPLPAAAAAQQSSASPGEVAS-PFASGTVSASPFATATDTAPSSGA--PDGFPAEASAPSP 221

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046845297  352 CSLCWKVFKKPSHLHQHQIIHTGEKpfSCSVCSKSFNRRESLKRHVKT-HSADLLR 406
Cdd:cd23959    222 FAAPASAASFPAAPVANGEAATPTH--ACTICGKAFSTHEGLRMHSKAkHGVELEK 275
PHA03378 super family cl33729
EBNA-3B; Provisional
 163-349 9.50e-07

EBNA-3B; Provisional


The actual alignment was detected with superfamily member PHA03378:

Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 53.15  E-value: 9.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046845297  163 PTPGPG--------------VASGLGTPTGTPGPLPTPSQTPPGPTVGAACDPTKDDKGYFRRLKYLMERrfPCGVCQKS 228
Cdd:PHA03378   565 PAPGLGplqiqpltspttsqLASSAPSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMR--PLRMQPIT 642

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046845297  229 F------------KQSSHLVQHMLVHSGERPYEcgicGRTYNHVSSLIRHRrchkdVPSTPTGSTSQPGPALPSLGLPV- 295
Cdd:PHA03378   643 FnvlvfptphqppQVEITPYKPTWTQIGHIPYQ----PSPTGANTMLPIQW-----APGTMQPPPRAPTPMRPPAAPPGr 713

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046845297  296 --PTASATASSDPAAVSSGPSATPAT-------PATSTDGNTTPAAPPGVAMPPSATTGGEGP 349
Cdd:PHA03378   714 aqRPAAATGRARPPAAAPGRARPPAAapgrarpPAAAPGRARPPAAAPGRARPPAAAPGAPTP 776
zf-H2C2_2 pfam13465
Zinc-finger double domain;
561-583 4.37e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.90  E-value: 4.37e-06
                           10        20
                   ....*....|....*....|...
gi 1046845297  561 LKRHERIHTGEKPHQCPVCGKRF 583
Cdd:pfam13465    2 LKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
863-887 9.02e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 9.02e-03
                           10        20
                   ....*....|....*....|....*
gi 1046845297  863 LMRHQRCHTEQRPYRCGVCGRGFLR 887
Cdd:pfam13465    2 LKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
349-421 3.75e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.93  E-value: 3.75e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046845297  349 PFACSLCWKVFKKPSHLHQHQIIHTGEKPFSCSV--CSKSFNRRESLKRHVKTHSADLLRLPCGICGKVFRDASY 421
Cdd:COG5048     33 PDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASS 107
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 273-406 6.31e-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: 52.95  E-value: 6.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046845297  273 VPSTPTGSTSQPG-PALPSLGLPVPTASATASSDPAAVSSgPSATPATPATSTDGNTTPAAPPGVamPPSATTGGEGPFA 351
Cdd:cd23959    145 APVTPFGQLPMFGqHPPPAKPLPAAAAAQQSSASPGEVAS-PFASGTVSASPFATATDTAPSSGA--PDGFPAEASAPSP 221

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046845297  352 CSLCWKVFKKPSHLHQHQIIHTGEKpfSCSVCSKSFNRRESLKRHVKT-HSADLLR 406
Cdd:cd23959    222 FAAPASAASFPAAPVANGEAATPTH--ACTICGKAFSTHEGLRMHSKAkHGVELEK 275
PHA03378 PHA03378
EBNA-3B; Provisional
 163-349 9.50e-07

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 53.15  E-value: 9.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046845297  163 PTPGPG--------------VASGLGTPTGTPGPLPTPSQTPPGPTVGAACDPTKDDKGYFRRLKYLMERrfPCGVCQKS 228
Cdd:PHA03378   565 PAPGLGplqiqpltspttsqLASSAPSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMR--PLRMQPIT 642

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046845297  229 F------------KQSSHLVQHMLVHSGERPYEcgicGRTYNHVSSLIRHRrchkdVPSTPTGSTSQPGPALPSLGLPV- 295
Cdd:PHA03378   643 FnvlvfptphqppQVEITPYKPTWTQIGHIPYQ----PSPTGANTMLPIQW-----APGTMQPPPRAPTPMRPPAAPPGr 713

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046845297  296 --PTASATASSDPAAVSSGPSATPAT-------PATSTDGNTTPAAPPGVAMPPSATTGGEGP 349
Cdd:PHA03378   714 aqRPAAATGRARPPAAAPGRARPPAAapgrarpPAAAPGRARPPAAAPGRARPPAAAPGAPTP 776
zf-H2C2_2 pfam13465
Zinc-finger double domain;
561-583 4.37e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.90  E-value: 4.37e-06
                           10        20
                   ....*....|....*....|...
gi 1046845297  561 LKRHERIHTGEKPHQCPVCGKRF 583
Cdd:pfam13465    2 LKRHMRTHTGEKPYKCPECGKSF 24
PHA03247 PHA03247
large tegument protein UL36; Provisional
 272-343 2.45e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 2.45e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046845297  272 DVPSTPTGSTSQPGPALPSLGLPVPTASATASSDPAAVSSGPSATPATPATSTdGNTTPAAPPGVAMPPSAT 343
Cdd:PHA03247  2700 DPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPG-GPARPARPPTTAGPPAPA 2770
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
 274-353 2.88e-04

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: 44.50  E-value: 2.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046845297  274 PSTPTGSTSQPgPALPSLGlPVPTASAtassdPAAVSSGPSATPAtpATSTDGNTTPAAPPGVAM-PPSATTGGEGPFAC 352
Cdd:TIGR00601   77 PKTGTGKVAPP-AATPTSA-PTPTPSP-----PASPASGMSAAPA--SAVEEKSPSEESATATAPeSPSTSVPSSGSDAA 147


                   .
gi 1046845297  353 S 353
Cdd:TIGR00601  148 S 148
zf-H2C2_2 pfam13465
Zinc-finger double domain;
367-389 2.00e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 2.00e-03
                           10        20
                   ....*....|....*....|...
gi 1046845297  367 QHQIIHTGEKPFSCSVCSKSFNR 389
Cdd:pfam13465    4 RHMRTHTGEKPYKCPECGKSFKS 26
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
273-349 7.33e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 40.12  E-value: 7.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046845297  273 VPSTPTGSTSQPGPALPSLGLPVPTAS-----------ATASSDPAAVSSGPSATPATPAT--STDGNTTPAAPPGVAMP 339
Cdd:COG3469    122 VTSTTSSTAGSTTTSGASATSSAGSTTttttvsgtetaTGGTTTTSTTTTTTSASTTPSATttATATTASGATTPSATTT 201

                           90
                   ....*....|
gi 1046845297  340 PSATTGGEGP 349
Cdd:COG3469    202 ATTTGPPTPG 211
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 220-242 8.28e-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: 8.28e-03
                           10        20
                   ....*....|....*....|...
gi 1046845297  220 FPCGVCQKSFKQSSHLVQHMLVH 242
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
863-887 9.02e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 9.02e-03
                           10        20
                   ....*....|....*....|....*
gi 1046845297  863 LMRHQRCHTEQRPYRCGVCGRGFLR 887
Cdd:pfam13465    2 LKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
349-421 3.75e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.93  E-value: 3.75e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046845297  349 PFACSLCWKVFKKPSHLHQHQIIHTGEKPFSCSV--CSKSFNRRESLKRHVKTHSADLLRLPCGICGKVFRDASY 421
Cdd:COG5048     33 PDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASS 107
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 273-406 6.31e-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: 52.95  E-value: 6.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046845297  273 VPSTPTGSTSQPG-PALPSLGLPVPTASATASSDPAAVSSgPSATPATPATSTDGNTTPAAPPGVamPPSATTGGEGPFA 351
Cdd:cd23959    145 APVTPFGQLPMFGqHPPPAKPLPAAAAAQQSSASPGEVAS-PFASGTVSASPFATATDTAPSSGA--PDGFPAEASAPSP 221

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046845297  352 CSLCWKVFKKPSHLHQHQIIHTGEKpfSCSVCSKSFNRRESLKRHVKT-HSADLLR 406
Cdd:cd23959    222 FAAPASAASFPAAPVANGEAATPTH--ACTICGKAFSTHEGLRMHSKAkHGVELEK 275
PHA03378 PHA03378
EBNA-3B; Provisional
 163-349 9.50e-07

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 53.15  E-value: 9.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046845297  163 PTPGPG--------------VASGLGTPTGTPGPLPTPSQTPPGPTVGAACDPTKDDKGYFRRLKYLMERrfPCGVCQKS 228
Cdd:PHA03378   565 PAPGLGplqiqpltspttsqLASSAPSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMR--PLRMQPIT 642

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046845297  229 F------------KQSSHLVQHMLVHSGERPYEcgicGRTYNHVSSLIRHRrchkdVPSTPTGSTSQPGPALPSLGLPV- 295
Cdd:PHA03378   643 FnvlvfptphqppQVEITPYKPTWTQIGHIPYQ----PSPTGANTMLPIQW-----APGTMQPPPRAPTPMRPPAAPPGr 713

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046845297  296 --PTASATASSDPAAVSSGPSATPAT-------PATSTDGNTTPAAPPGVAMPPSATTGGEGP 349
Cdd:PHA03378   714 aqRPAAATGRARPPAAAPGRARPPAAapgrarpPAAAPGRARPPAAAPGRARPPAAAPGAPTP 776
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
219-396 2.11e-06

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 51.62  E-value: 2.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046845297  219 RFPCGVCQKSFKQSSHLVQHM--LVHSGE--RPYECGI--CGRTYNHVSSLIRHRRCHKDVPSTPTgSTSQPGPALPSLG 292
Cdd:COG5048    289 PIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKE-KLLNSSSKFSPLL 367

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046845297  293 LPVPTASATASSDPAavssgPSATPATPATSTDGNTTpaAPPGVAMPPS-ATTGGEGPFACSLCWKVFKKPSHLHQHQII 371
Cdd:COG5048    368 NNEPPQSLQQYKDLK-----NDKKSETLSNSCIRNFK--RDSNLSLHIItHLSFRPYNCKNPPCSKSFNRHYNLIPHKKI 440

                          170       180
                   ....*....|....*....|....*
gi 1046845297  372 HTGEKPFSCSvCSKSFNRRESLKRH 396
Cdd:COG5048    441 HTNHAPLLCS-ILKSFRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
561-583 4.37e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 43.90  E-value: 4.37e-06
                           10        20
                   ....*....|....*....|...
gi 1046845297  561 LKRHERIHTGEKPHQCPVCGKRF 583
Cdd:pfam13465    2 LKRHMRTHTGEKPYKCPECGKSF 24
PHA03247 PHA03247
large tegument protein UL36; Provisional
 272-343 2.45e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 2.45e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046845297  272 DVPSTPTGSTSQPGPALPSLGLPVPTASATASSDPAAVSSGPSATPATPATSTdGNTTPAAPPGVAMPPSAT 343
Cdd:PHA03247  2700 DPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPG-GPARPARPPTTAGPPAPA 2770
PRK10856 PRK10856
cytoskeleton protein RodZ;
272-343 8.98e-05

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 45.79  E-value: 8.98e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046845297  272 DVPSTPTgSTSQPGPALPSLGLPVPTASATASSDPAAVSSGPSATPATPATSTDGNTTPAAPPGVAMPPSAT 343
Cdd:PRK10856   181 PVDTTPT-NSQTPAVATAPAPAVDPQQNAVVAPSQANVDTAATPAPAAPATPDGAAPLPTDQAGVSTPAADP 251
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
 274-353 2.88e-04

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: 44.50  E-value: 2.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046845297  274 PSTPTGSTSQPgPALPSLGlPVPTASAtassdPAAVSSGPSATPAtpATSTDGNTTPAAPPGVAM-PPSATTGGEGPFAC 352
Cdd:TIGR00601   77 PKTGTGKVAPP-AATPTSA-PTPTPSP-----PASPASGMSAAPA--SAVEEKSPSEESATATAPeSPSTSVPSSGSDAA 147


                   .
gi 1046845297  353 S 353
Cdd:TIGR00601  148 S 148
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
232-429 3.29e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.30  E-value: 3.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046845297  232 SSHLVQHMLVHSGERPYECGICGRTYNHVSSLIRHRRCHKDVPSTP---TGSTSQPGPALPSLGLPVPTASATASSDPAA 308
Cdd:COG5048    165 NSLHPPLPANSLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSipsSSSDQNLENSSSSLPLTTNSQLSPKSLLSQS 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046845297  309 VSSGPSATPATPATSTDGNTTPAAPPGVAMP----PSATTGGEGPFACSLCWKVFKKPSHL--HQHQIIHTGE--KPFSC 380
Cdd:COG5048    245 PSSLSSSDSSSSASESPRSSLPTASSQSSSPnesdSSSEKGFSLPIKSKQCNISFSRSSPLtrHLRSVNHSGEslKPFSC 324

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1046845297  381 --SVCSKSFNRRESLKRHVKTHSADLLRLPC-GICGKVFRDASYLLKHQAAH 429
Cdd:COG5048    325 pySLCGKLFSRNDALKRHILLHTSISPAKEKlLNSSSKFSPLLNNEPPQSLQ 376
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
548-593 7.84e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.15  E-value: 7.84e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1046845297  548 CGICGRAFGRRETLKRHERIHTGEKPHQCPVCGKRFRES------FHLSKHH 593
Cdd:COG5048     36 CPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSrplelsRHLRTHH 87
PHA03247 PHA03247
large tegument protein UL36; Provisional
 175-344 9.44e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 9.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046845297  175 TPTGTPGPLPTPSQTPPGPTVGAACDPtkddkgyfrrlkylmerrfpcgvcqKSFKQSSHLVQHMLVHSGERPYECGicG 254
Cdd:PHA03247  2600 APVDDRGDPRGPAPPSPLPPDTHAPDP-------------------------PPPSPSPAANEPDPHPPPTVPPPER--P 2652

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046845297  255 RTYNHVSSLIRHRRCHKdvPSTPTGSTSQP-GPALPSLglPVPTASATASSDPAAVSSGP--------SATPATPATSTD 325
Cdd:PHA03247  2653 RDDPAPGRVSRPRRARR--LGRAAQASSPPqRPRRRAA--RPTVGSLTSLADPPPPPPTPepaphalvSATPLPPGPAAA 2728

                          170
                   ....*....|....*....
gi 1046845297  326 GNTTPAAPPGVAMPPSATT 344
Cdd:PHA03247  2729 RQASPALPAAPAPPAVPAG 2747
PHA03247 PHA03247
large tegument protein UL36; Provisional
 274-349 1.88e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.88e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046845297  274 PSTPTGSTSQPGPALPSLGLPVPTASATASSDPAAVSSGPSATPAT--PATSTDGNTTPAAPPGVAMPPSATTGGEGP 349
Cdd:PHA03247  2781 RRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGplPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858
zf-H2C2_2 pfam13465
Zinc-finger double domain;
367-389 2.00e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 2.00e-03
                           10        20
                   ....*....|....*....|...
gi 1046845297  367 QHQIIHTGEKPFSCSVCSKSFNR 389
Cdd:pfam13465    4 RHMRTHTGEKPYKCPECGKSFKS 26
PHA03247 PHA03247
large tegument protein UL36; Provisional
 268-356 3.49e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 3.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046845297  268 RCHKDVPSTPT----GSTSQPGPALPSLglPVPTASATASSDPAAVSSGPS-ATPATPATSTDGNTTPAAPPGVAMPPSA 342
Cdd:PHA03247  2711 APHALVSATPLppgpAAARQASPALPAA--PAPPAVPAGPATPGGPARPARpPTTAGPPAPAPPAAPAAGPPRRLTRPAV 2788

                           90
                   ....*....|....
gi 1046845297  343 TTGGEGPFACSLCW 356
Cdd:PHA03247  2789 ASLSESRESLPSPW 2802
PHA03247 PHA03247
large tegument protein UL36; Provisional
 274-343 3.73e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 3.73e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046845297  274 PSTPTGSTSQPGPALPSlGLPVPTASATASSDPAAVSSGPSATPATPAT-STDGNTTPAAPPGVAMPPSAT 343
Cdd:PHA03247  2748 PATPGGPARPARPPTTA-GPPAPAPPAAPAAGPPRRLTRPAVASLSESReSLPSPWDPADPPAAVLAPAAA 2817
PRK10856 PRK10856
cytoskeleton protein RodZ;
272-344 4.53e-03

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 40.39  E-value: 4.53e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046845297  272 DVPSTPTGSTSQPGPALPSLGLPVPTASATASSDPAAVSSGPSATPATPATSTdgNTTPAAPPGVAMPPSATT 344
Cdd:PRK10856   166 TSTTTDPATTPAPAAPVDTTPTNSQTPAVATAPAPAVDPQQNAVVAPSQANVD--TAATPAPAAPATPDGAAP 236
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 378-400 6.29e-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: 34.97  E-value: 6.29e-03
                           10        20
                   ....*....|....*....|...
gi 1046845297  378 FSCSVCSKSFNRRESLKRHVKTH 400
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
273-349 7.33e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 40.12  E-value: 7.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046845297  273 VPSTPTGSTSQPGPALPSLGLPVPTAS-----------ATASSDPAAVSSGPSATPATPAT--STDGNTTPAAPPGVAMP 339
Cdd:COG3469    122 VTSTTSSTAGSTTTSGASATSSAGSTTttttvsgtetaTGGTTTTSTTTTTTSASTTPSATttATATTASGATTPSATTT 201

                           90
                   ....*....|
gi 1046845297  340 PSATTGGEGP 349
Cdd:COG3469    202 ATTTGPPTPG 211
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 220-242 8.28e-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: 8.28e-03
                           10        20
                   ....*....|....*....|...
gi 1046845297  220 FPCGVCQKSFKQSSHLVQHMLVH 242
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
863-887 9.02e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 9.02e-03
                           10        20
                   ....*....|....*....|....*
gi 1046845297  863 LMRHQRCHTEQRPYRCGVCGRGFLR 887
Cdd:pfam13465    2 LKRHMRTHTGEKPYKCPECGKSFKS 26
 
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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