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Conserved domains on  [gi|530417514|ref|XP_005259440|]
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zinc finger protein 835 isoform X1 [Homo sapiens]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 11472214)

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
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];
136-487 1.54e-14

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 75.89  E-value: 1.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417514 136 KPFACPECGKAFSQSVHLTLHQRTHTGEKPYACHECGKAFSQGSYLAS--HWRTHTGEKPHRCAD--------------- 198
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELsrHLRTHHNNPSDLNSKslplsnskassssls 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417514 199 -CGKAFTRVTHLTQH-------------------------RRVHTGERPYACA-----------QCAKAFRNRSSLIEHQ 241
Cdd:COG5048  112 sSSSNSNDNNLLSSHslppssrdpqlpdllsisnlrnnplPGNNSSSVNTPQSnslhpplpansLSKDPSSNLSLLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417514 242 RIHTGEKPYECSACAKAFRFSSALIRHQRIHTEEkPYRCGQCAKAFAQiaHLTQHRRVHTGEK--PYTCQDCGALFSQSA 319
Cdd:COG5048  192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSS-SLPLTTNSQLSPK--SLLSQSPSSLSSSdsSSSASESPRSSLPTA 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417514 320 SLAEHRRIHTGE-------KPYACGQCAKAFTQVSHLTQHQRT--HTGE--RPYPC--HDCGKRFSNRSHLLQHRLVHTG 386
Cdd:COG5048  269 SSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTS 348

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417514 387 ERPYRCLQCGAAFSHVSSLIE-------HQKIHTGERPYKC--GECGKAFSQGSSLALHQRTHTGERP--YTCPECGKAF 455
Cdd:COG5048  349 ISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSF 428

                        410       420       430
                 ....*....|....*....|....*....|..
gi 530417514 456 SNRSYLIQHHIVHTGEKPYECSGCGKAFSFSS 487
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
136-487 1.54e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 75.89  E-value: 1.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417514 136 KPFACPECGKAFSQSVHLTLHQRTHTGEKPYACHECGKAFSQGSYLAS--HWRTHTGEKPHRCAD--------------- 198
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELsrHLRTHHNNPSDLNSKslplsnskassssls 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417514 199 -CGKAFTRVTHLTQH-------------------------RRVHTGERPYACA-----------QCAKAFRNRSSLIEHQ 241
Cdd:COG5048  112 sSSSNSNDNNLLSSHslppssrdpqlpdllsisnlrnnplPGNNSSSVNTPQSnslhpplpansLSKDPSSNLSLLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417514 242 RIHTGEKPYECSACAKAFRFSSALIRHQRIHTEEkPYRCGQCAKAFAQiaHLTQHRRVHTGEK--PYTCQDCGALFSQSA 319
Cdd:COG5048  192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSS-SLPLTTNSQLSPK--SLLSQSPSSLSSSdsSSSASESPRSSLPTA 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417514 320 SLAEHRRIHTGE-------KPYACGQCAKAFTQVSHLTQHQRT--HTGE--RPYPC--HDCGKRFSNRSHLLQHRLVHTG 386
Cdd:COG5048  269 SSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTS 348

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417514 387 ERPYRCLQCGAAFSHVSSLIE-------HQKIHTGERPYKC--GECGKAFSQGSSLALHQRTHTGERP--YTCPECGKAF 455
Cdd:COG5048  349 ISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSF 428

                        410       420       430
                 ....*....|....*....|....*....|..
gi 530417514 456 SNRSYLIQHHIVHTGEKPYECSGCGKAFSFSS 487
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
zf-H2C2_2 pfam13465
Zinc-finger double domain;
348-373 1.90e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.90e-04
                          10        20
                  ....*....|....*....|....*.
gi 530417514  348 HLTQHQRTHTGERPYPCHDCGKRFSN 373
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PRK10426 PRK10426
alpha-glucosidase; Provisional
 178-277 4.85e-03

alpha-glucosidase; Provisional


Pssm-ID: 236691 [Multi-domain]  Cd Length: 635  Bit Score: 39.59  E-value: 4.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417514 178 GSYLASHWRTHTGEKPHRCADCGkAFTRVThltqhrRVHTGERPYACAQcakaFRNRSSLIEH----QRIHTGEKPYECS 253
Cdd:PRK10426 461 GGYTTLFGMKRTKELLLRWCEFS-AFTPVM------RTHEGNRPGDNWQ----FDSDAETIAHfarmTRVFTTLKPYLKE 529

                         90       100
                 ....*....|....*....|....
gi 530417514 254 ACAKAFRFSSALIRHQRIHTEEKP 277
Cdd:PRK10426 530 LVAEAAKTGLPVMRPLFLHYEDDA 553
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 388-436 7.98e-03

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 35.61  E-value: 7.98e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530417514 388 RPYrCLQCGAAFSHVSSLIEHQKIHTgerpYKCGECGKAFSQGSSLALH 436
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
136-487 1.54e-14

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 75.89  E-value: 1.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417514 136 KPFACPECGKAFSQSVHLTLHQRTHTGEKPYACHECGKAFSQGSYLAS--HWRTHTGEKPHRCAD--------------- 198
Cdd:COG5048   32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELsrHLRTHHNNPSDLNSKslplsnskassssls 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417514 199 -CGKAFTRVTHLTQH-------------------------RRVHTGERPYACA-----------QCAKAFRNRSSLIEHQ 241
Cdd:COG5048  112 sSSSNSNDNNLLSSHslppssrdpqlpdllsisnlrnnplPGNNSSSVNTPQSnslhpplpansLSKDPSSNLSLLISSN 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417514 242 RIHTGEKPYECSACAKAFRFSSALIRHQRIHTEEkPYRCGQCAKAFAQiaHLTQHRRVHTGEK--PYTCQDCGALFSQSA 319
Cdd:COG5048  192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSS-SLPLTTNSQLSPK--SLLSQSPSSLSSSdsSSSASESPRSSLPTA 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417514 320 SLAEHRRIHTGE-------KPYACGQCAKAFTQVSHLTQHQRT--HTGE--RPYPC--HDCGKRFSNRSHLLQHRLVHTG 386
Cdd:COG5048  269 SSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCpySLCGKLFSRNDALKRHILLHTS 348

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417514 387 ERPYRCLQCGAAFSHVSSLIE-------HQKIHTGERPYKC--GECGKAFSQGSSLALHQRTHTGERP--YTCPECGKAF 455
Cdd:COG5048  349 ISPAKEKLLNSSSKFSPLLNNeppqslqQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSF 428

                        410       420       430
                 ....*....|....*....|....*....|..
gi 530417514 456 SNRSYLIQHHIVHTGEKPYECSGCGKAFSFSS 487
Cdd:COG5048  429 NRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
64-268 5.55e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.01  E-value: 5.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417514  64 ISSPAATQASVPDDSSSRRCSAPGES--PKERHPDSRQRERGGGPKKPW----KCGDCGKAFSYCSAFILHQR--IHTGE 135
Cdd:COG5048  238 KSLLSQSPSSLSSSDSSSSASESPRSslPTASSQSSSPNESDSSSEKGFslpiKSKQCNISFSRSSPLTRHLRsvNHSGE 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417514 136 --KPFACPE--CGKAFSQSVHLTLHQRTHTGEKPYACH--ECGKAFSQGSYLASHWRTH-----TGEKPHRCAD--CGKA 202
Cdd:COG5048  318 slKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETLSnsCIRN 397

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530417514 203 FTRVTHLTQHRRVHTGERPYAC--AQCAKAFRNRSSLIEHQRIHTGEKPYECSACaKAFRFSSALIRH 268
Cdd:COG5048  398 FKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSIL-KSFRRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
348-373 1.90e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 1.90e-04
                          10        20
                  ....*....|....*....|....*.
gi 530417514  348 HLTQHQRTHTGERPYPCHDCGKRFSN 373
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
152-177 2.16e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.16e-04
                          10        20
                  ....*....|....*....|....*.
gi 530417514  152 HLTLHQRTHTGEKPYACHECGKAFSQ 177
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
432-457 2.50e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.50e-04
                          10        20
                  ....*....|....*....|....*.
gi 530417514  432 SLALHQRTHTGERPYTCPECGKAFSN 457
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
128-149 3.39e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 3.39e-04
                          10        20
                  ....*....|....*....|..
gi 530417514  128 HQRIHTGEKPFACPECGKAFSQ 149
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 213-297 4.91e-04

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


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 42.78  E-value: 4.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417514 213 RRVHTGERPYACA--QCAKAFRNRSSLIEHqRIHtgekpyecSACAKAFRFSSALIRHQRIHTEEKPYRCGQCAKAFAQI 290
Cdd:COG5189  341 MLKVKDGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNL 411


                 ....*..
gi 530417514 291 AHLTQHR 297
Cdd:COG5189  412 NGLKYHR 418
zf-H2C2_2 pfam13465
Zinc-finger double domain;
404-429 7.88e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 7.88e-04
                          10        20
                  ....*....|....*....|....*.
gi 530417514  404 SLIEHQKIHTGERPYKCGECGKAFSQ 429
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 474-496 2.68e-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: 35.35  E-value: 2.68e-03
                          10        20
                  ....*....|....*....|...
gi 530417514  474 YECSGCGKAFSFSSALIRHQRTH 496
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
264-289 2.77e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.42  E-value: 2.77e-03
                          10        20
                  ....*....|....*....|....*.
gi 530417514  264 ALIRHQRIHTEEKPYRCGQCAKAFAQ 289
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
180-205 3.37e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 3.37e-03
                          10        20
                  ....*....|....*....|....*.
gi 530417514  180 YLASHWRTHTGEKPHRCADCGKAFTR 205
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 362-384 3.97e-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: 3.97e-03
                          10        20
                  ....*....|....*....|...
gi 530417514  362 YPCHDCGKRFSNRSHLLQHRLVH 384
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 138-160 4.29e-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: 4.29e-03
                          10        20
                  ....*....|....*....|...
gi 530417514  138 FACPECGKAFSQSVHLTLHQRTH 160
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
320-345 4.31e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 4.31e-03
                          10        20
                  ....*....|....*....|....*.
gi 530417514  320 SLAEHRRIHTGEKPYACGQCAKAFTQ 345
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PRK10426 PRK10426
alpha-glucosidase; Provisional
 178-277 4.85e-03

alpha-glucosidase; Provisional


Pssm-ID: 236691 [Multi-domain]  Cd Length: 635  Bit Score: 39.59  E-value: 4.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530417514 178 GSYLASHWRTHTGEKPHRCADCGkAFTRVThltqhrRVHTGERPYACAQcakaFRNRSSLIEH----QRIHTGEKPYECS 253
Cdd:PRK10426 461 GGYTTLFGMKRTKELLLRWCEFS-AFTPVM------RTHEGNRPGDNWQ----FDSDAETIAHfarmTRVFTTLKPYLKE 529

                         90       100
                 ....*....|....*....|....
gi 530417514 254 ACAKAFRFSSALIRHQRIHTEEKP 277
Cdd:PRK10426 530 LVAEAAKTGLPVMRPLFLHYEDDA 553
zf-H2C2_2 pfam13465
Zinc-finger double domain;
236-259 6.08e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.27  E-value: 6.08e-03
                          10        20
                  ....*....|....*....|....
gi 530417514  236 SLIEHQRIHTGEKPYECSACAKAF 259
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
292-317 7.93e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 33.88  E-value: 7.93e-03
                          10        20
                  ....*....|....*....|....*.
gi 530417514  292 HLTQHRRVHTGEKPYTCQDCGALFSQ 317
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
 388-436 7.98e-03

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 35.61  E-value: 7.98e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530417514 388 RPYrCLQCGAAFSHVSSLIEHQKIHTgerpYKCGECGKAFSQGSSLALH 436
Cdd:cd20908    1 KPW-CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44
PTZ00074 PTZ00074
60S ribosomal protein L34; Provisional
 178-243 9.78e-03

60S ribosomal protein L34; Provisional


Pssm-ID: 185429  Cd Length: 135  Bit Score: 36.59  E-value: 9.78e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530417514 178 GSYLASHWRTHTGEKPHrCADCGKAFTRVTHLTQH------RRVHTGERPYACAQCAKAFRN---RSSLIEHQRI 243
Cdd:PTZ00074  27 GGRLVVQKRKKKSSGPK-CGDCGKVLAGIKALRPTeykqlsRRERTVSRAYGGVLCHKCVRDrivRAFLVEEQKI 100
 
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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