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Conserved domains on  [gi|1993776359|ref|NP_001380571|]
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DDB1- and CUL4-associated factor 15 isoform 7 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DCAF15_WD40 pfam14939
DDB1-and CUL4-substrate receptor 15, WD repeat; DCAFs, Ddb1- and Cul4-associated factors, are ...
 48-259 4.65e-118

DDB1-and CUL4-substrate receptor 15, WD repeat; DCAFs, Ddb1- and Cul4-associated factors, are substrate receptors for the Cul4-Ddb1 Ubiquitin Ligase. There are 18 different factors, the majority of which are WD40-repeat-proteins.


:

Pssm-ID: 464387  Cd Length: 206  Bit Score: 347.79  E-value: 4.65e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359  48 QLSPRLFRKLPPRVCVSLKNIVDEDFLYAGHIFLGFSKCGRYVLSYTSSSGDDD---FSFYIYHLYWWEFNVHSKLKLVR 124
Cdd:pfam14939   1 QKSQRLFRKLPPRLCLSLKDIVPESFLQAGHIFLGFTKCGQFLLSYTSDCDDEDslsFGNYKYHLYWWEFNPHSKLRKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 125 QVRLFQDEEIYSDLYLTVCEWPSDASKVIVFGFNTRSAngmlmnmmmMSDENHRDIYVSTVAVPPPGRCAACQDASRAHP 204
Cdd:pfam14939  81 EVRLFGDEEIYSDLYLTICQWPSDSSKLVVHGFNTTSS---------MSDEEHRDIYITIVTVPSLSPCKDCKRVADSHP 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1993776359 205 GDPNAQCLRHGFMLHTKYQVVYPFPTFQPAFQLKKDQVVLLNTSYSLVACAVSVH 259
Cdd:pfam14939 152 EEDNALCLRHGLTIHTKYEVVYPYPTFQPSVSLKCDNVVLLNTGNFLHALAVDVD 206
DCAF15-CTD cd20913
C-terminal domain of DDB1- and CUL4-associated factor 15; This model represents the C-terminal ...
 387-564 7.13e-55

C-terminal domain of DDB1- and CUL4-associated factor 15; This model represents the C-terminal domain of DCAF15 (DDB1- and CUL4-associated factor 15), the cullin RING ligase substrate receptor/adaptor that forms a complex with CUL4A or CUL4B, as part of the Rbx-Cul4-DDA1-DDB1-DCAF15 E3 ubiquitin ligase that is responsible for the proteasome degradation of certain proteins. Aryl sulfonamide anticancer agents such as indisulam, tasisulam, E7820, and chloroquinoxaline have been shown to recruit the essential mRNA-splicing factor RBM39 to DCAF15. These agents appear to promote binding of DCAF15 to the RNA-recognition motif (RRM) of RBM39, which suggests that derivatives of the aryl-sulfonamides may be used to target other RRM-containing proteins. Cell proliferation is inhibited by these aryl sulfonamides by causing degradation of RBM39, which leads to aberrant processing of pre-mRNA in hundreds of genes, primarily reflected by intron retention and exon skipping, thus collectively referred to as splicing inhibitor sulfonamides, or SPLAMs.


:

Pssm-ID: 411023  Cd Length: 224  Bit Score: 184.80  E-value: 7.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 387 VNYTKLYYVLESGEG--TEPEDELEDDK--ISLPFVVTDLRGRNLRPMRERTA--VQGQYLTVEQLTLDFEYVINEVIRH 460
Cdd:cd20913     1 VKKVVRRYSEVDDEIviTDIEDDSLLSGqhIELPLEVHGLGYQQLQMVSNAKAdkLTEPQVIVTQRSLDIEQFINEVAQK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 461 D-ATWGHQFCSFSDYDIVILEVCPETNQVLINIGLLLLAFPSPTEEGQLR------------------------------ 509
Cdd:cd20913    81 LcAEWGKKFWSCSDYDIEIVDVCPLSGDVICLLVILIQALESPEESKLDCsnrrklyetsclftwnistgqyrtldvgdl 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993776359 510 ---------GSVWSSYRKSCVDMVMKWLVPESSGRYVNRMTNEALHKGCSLKVLADSERYTWIV 564
Cdd:cd20913   161 tevppeqtsSQEWNPARKEASRLRKKWLVPQSSKRSVRVLTNESVFKGRSLDNLIDPFHYSAIV 224
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 274-381 5.66e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 5.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359  274 STCPLAPASPPEPQSPELPPALPSFCPEAAPARSSGSPEPSPAIAKAKEFVADIFRRAKEAKGGVPEEARPALCPGPSgs 353
Cdd:PHA03247  2769 PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPP-- 2846

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1993776359  354 rcrahSEPLALCGETAP----RDSPPASEAPA 381
Cdd:PHA03247  2847 -----PPSLPLGGSVAPggdvRRRPPSRSPAA 2873
 
Name Accession Description Interval E-value
DCAF15_WD40 pfam14939
DDB1-and CUL4-substrate receptor 15, WD repeat; DCAFs, Ddb1- and Cul4-associated factors, are ...
 48-259 4.65e-118

DDB1-and CUL4-substrate receptor 15, WD repeat; DCAFs, Ddb1- and Cul4-associated factors, are substrate receptors for the Cul4-Ddb1 Ubiquitin Ligase. There are 18 different factors, the majority of which are WD40-repeat-proteins.


Pssm-ID: 464387  Cd Length: 206  Bit Score: 347.79  E-value: 4.65e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359  48 QLSPRLFRKLPPRVCVSLKNIVDEDFLYAGHIFLGFSKCGRYVLSYTSSSGDDD---FSFYIYHLYWWEFNVHSKLKLVR 124
Cdd:pfam14939   1 QKSQRLFRKLPPRLCLSLKDIVPESFLQAGHIFLGFTKCGQFLLSYTSDCDDEDslsFGNYKYHLYWWEFNPHSKLRKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 125 QVRLFQDEEIYSDLYLTVCEWPSDASKVIVFGFNTRSAngmlmnmmmMSDENHRDIYVSTVAVPPPGRCAACQDASRAHP 204
Cdd:pfam14939  81 EVRLFGDEEIYSDLYLTICQWPSDSSKLVVHGFNTTSS---------MSDEEHRDIYITIVTVPSLSPCKDCKRVADSHP 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1993776359 205 GDPNAQCLRHGFMLHTKYQVVYPFPTFQPAFQLKKDQVVLLNTSYSLVACAVSVH 259
Cdd:pfam14939 152 EEDNALCLRHGLTIHTKYEVVYPYPTFQPSVSLKCDNVVLLNTGNFLHALAVDVD 206
DCAF15-NTD cd20917
N-terminal domain of DDB1- and CUL4-associated factor 15; This model represents the N-terminal ...
 35-259 1.27e-93

N-terminal domain of DDB1- and CUL4-associated factor 15; This model represents the N-terminal domain of DCAF15 (DDB1- and CUL4-associated factor 15), the cullin RING ligase substrate receptor/adaptor that forms a complex with CUL4A or CUL4B, as part of the Rbx-Cul4-DDA1-DDB1-DCAF15 E3 ubiquitin ligase that is responsible for the proteasome degradation of certain proteins. Aryl sulfonamide anticancer agents such as indisulam, tasisulam, E7820, and chloroquinoxaline have been shown to recruit the essential mRNA-splicing factor RBM39 to DCAF15. These agents appear to promote binding of DCAF15 to the RNA-recognition motif (RRM) of RBM39, which suggests that derivatives of the aryl-sulfonamides may be used to target other RRM-containing proteins. Cell proliferation is inhibited by these aryl sulfonamides by causing degradation of RBM39, which leads to aberrant processing of pre-mRNA in hundreds of genes, primarily reflected by intron retention and exon skipping, thus collectively referred to as splicing inhibitor sulfonamides, or SPLAMs.


Pssm-ID: 411024  Cd Length: 225  Bit Score: 285.75  E-value: 1.27e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359  35 HVLKQLERVKISGQLSP-------RLFRKLPPRVCVSLKNIVDEDFLYAGHIFLGFSKCGRYVLSYTSSSGDDDFSF--- 104
Cdd:cd20917     1 NLLQKLLNREITGSFSRhrrskseRLFRKIPPRLCFPLKDILPDEGLLLGHVFLGFTKCGQFLLSYTLSSDDDDSSLfpl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 105 YIYHLYWWEFNVHSKLKLVRQVRLFQDEEIYSDLYLTVCEWPSDASKVIVFGFNTRSangmlmnmmmmSDENHRDIYVST 184
Cdd:cd20917    81 YKYRLHWWLFVPGQPLRKVSEVRLFGDEGIYDDLKITVCQWPDDPSKLVVYGYSAES-----------SPEESRDCYITI 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993776359 185 VAVPPPGRCAACQDASRAH-PGDPNAQCLRHGFMLHTKYQVVYPFPTFQPAFQLKKDQVVLLNTSYSLVACAVSVH 259
Cdd:cd20917   150 TAVPSLSNCPDCKQLALSNwDSCSRFRCLKHGFTVHTKYELVPPFPPFDPSVSLKLPGVVVLNTGNFLHVLSVSLE 225
DCAF15-CTD cd20913
C-terminal domain of DDB1- and CUL4-associated factor 15; This model represents the C-terminal ...
 387-564 7.13e-55

C-terminal domain of DDB1- and CUL4-associated factor 15; This model represents the C-terminal domain of DCAF15 (DDB1- and CUL4-associated factor 15), the cullin RING ligase substrate receptor/adaptor that forms a complex with CUL4A or CUL4B, as part of the Rbx-Cul4-DDA1-DDB1-DCAF15 E3 ubiquitin ligase that is responsible for the proteasome degradation of certain proteins. Aryl sulfonamide anticancer agents such as indisulam, tasisulam, E7820, and chloroquinoxaline have been shown to recruit the essential mRNA-splicing factor RBM39 to DCAF15. These agents appear to promote binding of DCAF15 to the RNA-recognition motif (RRM) of RBM39, which suggests that derivatives of the aryl-sulfonamides may be used to target other RRM-containing proteins. Cell proliferation is inhibited by these aryl sulfonamides by causing degradation of RBM39, which leads to aberrant processing of pre-mRNA in hundreds of genes, primarily reflected by intron retention and exon skipping, thus collectively referred to as splicing inhibitor sulfonamides, or SPLAMs.


Pssm-ID: 411023  Cd Length: 224  Bit Score: 184.80  E-value: 7.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 387 VNYTKLYYVLESGEG--TEPEDELEDDK--ISLPFVVTDLRGRNLRPMRERTA--VQGQYLTVEQLTLDFEYVINEVIRH 460
Cdd:cd20913     1 VKKVVRRYSEVDDEIviTDIEDDSLLSGqhIELPLEVHGLGYQQLQMVSNAKAdkLTEPQVIVTQRSLDIEQFINEVAQK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 461 D-ATWGHQFCSFSDYDIVILEVCPETNQVLINIGLLLLAFPSPTEEGQLR------------------------------ 509
Cdd:cd20913    81 LcAEWGKKFWSCSDYDIEIVDVCPLSGDVICLLVILIQALESPEESKLDCsnrrklyetsclftwnistgqyrtldvgdl 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993776359 510 ---------GSVWSSYRKSCVDMVMKWLVPESSGRYVNRMTNEALHKGCSLKVLADSERYTWIV 564
Cdd:cd20913   161 tevppeqtsSQEWNPARKEASRLRKKWLVPQSSKRSVRVLTNESVFKGRSLDNLIDPFHYSAIV 224
PHA03247 PHA03247
large tegument protein UL36; Provisional
 274-381 5.66e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 5.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359  274 STCPLAPASPPEPQSPELPPALPSFCPEAAPARSSGSPEPSPAIAKAKEFVADIFRRAKEAKGGVPEEARPALCPGPSgs 353
Cdd:PHA03247  2769 PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPP-- 2846

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1993776359  354 rcrahSEPLALCGETAP----RDSPPASEAPA 381
Cdd:PHA03247  2847 -----PPSLPLGGSVAPggdvRRRPPSRSPAA 2873
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 280-383 3.54e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 43.22  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 280 PASPPEPQS--PELPPALPSFCPEAAPARSSGSPEPSPAIAKAKEFVADIFRRAKEAKGGVPEEARPALCPGPSGSRCRA 357
Cdd:NF033839  374 PEVKPQPETpkPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEV 453

                          90       100
                  ....*....|....*....|....*.
gi 1993776359 358 HSEPlalcgETAPRDSPPASEAPASE 383
Cdd:NF033839  454 KPQP-----ETPKPEVKPQPEKPKPE 474
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 284-383 5.35e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.83  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 284 PEPQSPELPPALPSFCPEAAPARSSGSPEPSPAIAKAKEFVADIFRRAKEAKGGVPEEARPALCPGPSGSRCRAHSEPla 363
Cdd:NF033839  303 PQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQP-- 380

                          90       100
                  ....*....|....*....|
gi 1993776359 364 lcgETAPRDSPPASEAPASE 383
Cdd:NF033839  381 ---ETPKPEVKPQPEKPKPE 397
KLF14_N cd21576
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ...
 277-382 8.41e-04

N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as Krueppel-like factor 14 or basic transcription element-binding protein 5/BTEB5) is a protein that in humans is encoded by the KLF14 gene. KLF14 regulates the transcription of various genes, including TGFbetaRII (the type II receptor for TGFbeta). KLF14 is expressed in many tissues, lacks introns, and is subject to parent-specific expression. It also appears to be a master regulator of gene expression in adipose tissue. KLF14 is associated with coronary artery disease, hypercholesterolemia, and type 2 diabetes. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF14 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF14.


Pssm-ID: 409238 [Multi-domain]  Cd Length: 195  Bit Score: 40.96  E-value: 8.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 277 PLAPASP-PEPQSPELPPALPsfcpeAAPARSSGSPEPSPAIAKAkEFVADIFRRAKEAKGGVPEEA--------RPALC 347
Cdd:cd21576    46 PPESALPgPGPPGPAWVPPLL-----QVPAPSPGAGGAAPHLLAA-SVLADLRGGAGEGSREDSGEAprassgssDPARG 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1993776359 348 PGPSG-------SRCRAHSEPLALCGETAPRDSPPASEAPAS 382
Cdd:cd21576   120 SSPTLgsepapaSGEDAVSGPESSFGAPAIPSAPAAPGAPAV 161
 
Name Accession Description Interval E-value
DCAF15_WD40 pfam14939
DDB1-and CUL4-substrate receptor 15, WD repeat; DCAFs, Ddb1- and Cul4-associated factors, are ...
 48-259 4.65e-118

DDB1-and CUL4-substrate receptor 15, WD repeat; DCAFs, Ddb1- and Cul4-associated factors, are substrate receptors for the Cul4-Ddb1 Ubiquitin Ligase. There are 18 different factors, the majority of which are WD40-repeat-proteins.


Pssm-ID: 464387  Cd Length: 206  Bit Score: 347.79  E-value: 4.65e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359  48 QLSPRLFRKLPPRVCVSLKNIVDEDFLYAGHIFLGFSKCGRYVLSYTSSSGDDD---FSFYIYHLYWWEFNVHSKLKLVR 124
Cdd:pfam14939   1 QKSQRLFRKLPPRLCLSLKDIVPESFLQAGHIFLGFTKCGQFLLSYTSDCDDEDslsFGNYKYHLYWWEFNPHSKLRKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 125 QVRLFQDEEIYSDLYLTVCEWPSDASKVIVFGFNTRSAngmlmnmmmMSDENHRDIYVSTVAVPPPGRCAACQDASRAHP 204
Cdd:pfam14939  81 EVRLFGDEEIYSDLYLTICQWPSDSSKLVVHGFNTTSS---------MSDEEHRDIYITIVTVPSLSPCKDCKRVADSHP 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1993776359 205 GDPNAQCLRHGFMLHTKYQVVYPFPTFQPAFQLKKDQVVLLNTSYSLVACAVSVH 259
Cdd:pfam14939 152 EEDNALCLRHGLTIHTKYEVVYPYPTFQPSVSLKCDNVVLLNTGNFLHALAVDVD 206
DCAF15-NTD cd20917
N-terminal domain of DDB1- and CUL4-associated factor 15; This model represents the N-terminal ...
 35-259 1.27e-93

N-terminal domain of DDB1- and CUL4-associated factor 15; This model represents the N-terminal domain of DCAF15 (DDB1- and CUL4-associated factor 15), the cullin RING ligase substrate receptor/adaptor that forms a complex with CUL4A or CUL4B, as part of the Rbx-Cul4-DDA1-DDB1-DCAF15 E3 ubiquitin ligase that is responsible for the proteasome degradation of certain proteins. Aryl sulfonamide anticancer agents such as indisulam, tasisulam, E7820, and chloroquinoxaline have been shown to recruit the essential mRNA-splicing factor RBM39 to DCAF15. These agents appear to promote binding of DCAF15 to the RNA-recognition motif (RRM) of RBM39, which suggests that derivatives of the aryl-sulfonamides may be used to target other RRM-containing proteins. Cell proliferation is inhibited by these aryl sulfonamides by causing degradation of RBM39, which leads to aberrant processing of pre-mRNA in hundreds of genes, primarily reflected by intron retention and exon skipping, thus collectively referred to as splicing inhibitor sulfonamides, or SPLAMs.


Pssm-ID: 411024  Cd Length: 225  Bit Score: 285.75  E-value: 1.27e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359  35 HVLKQLERVKISGQLSP-------RLFRKLPPRVCVSLKNIVDEDFLYAGHIFLGFSKCGRYVLSYTSSSGDDDFSF--- 104
Cdd:cd20917     1 NLLQKLLNREITGSFSRhrrskseRLFRKIPPRLCFPLKDILPDEGLLLGHVFLGFTKCGQFLLSYTLSSDDDDSSLfpl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 105 YIYHLYWWEFNVHSKLKLVRQVRLFQDEEIYSDLYLTVCEWPSDASKVIVFGFNTRSangmlmnmmmmSDENHRDIYVST 184
Cdd:cd20917    81 YKYRLHWWLFVPGQPLRKVSEVRLFGDEGIYDDLKITVCQWPDDPSKLVVYGYSAES-----------SPEESRDCYITI 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993776359 185 VAVPPPGRCAACQDASRAH-PGDPNAQCLRHGFMLHTKYQVVYPFPTFQPAFQLKKDQVVLLNTSYSLVACAVSVH 259
Cdd:cd20917   150 TAVPSLSNCPDCKQLALSNwDSCSRFRCLKHGFTVHTKYELVPPFPPFDPSVSLKLPGVVVLNTGNFLHVLSVSLE 225
DCAF15-CTD cd20913
C-terminal domain of DDB1- and CUL4-associated factor 15; This model represents the C-terminal ...
 387-564 7.13e-55

C-terminal domain of DDB1- and CUL4-associated factor 15; This model represents the C-terminal domain of DCAF15 (DDB1- and CUL4-associated factor 15), the cullin RING ligase substrate receptor/adaptor that forms a complex with CUL4A or CUL4B, as part of the Rbx-Cul4-DDA1-DDB1-DCAF15 E3 ubiquitin ligase that is responsible for the proteasome degradation of certain proteins. Aryl sulfonamide anticancer agents such as indisulam, tasisulam, E7820, and chloroquinoxaline have been shown to recruit the essential mRNA-splicing factor RBM39 to DCAF15. These agents appear to promote binding of DCAF15 to the RNA-recognition motif (RRM) of RBM39, which suggests that derivatives of the aryl-sulfonamides may be used to target other RRM-containing proteins. Cell proliferation is inhibited by these aryl sulfonamides by causing degradation of RBM39, which leads to aberrant processing of pre-mRNA in hundreds of genes, primarily reflected by intron retention and exon skipping, thus collectively referred to as splicing inhibitor sulfonamides, or SPLAMs.


Pssm-ID: 411023  Cd Length: 224  Bit Score: 184.80  E-value: 7.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 387 VNYTKLYYVLESGEG--TEPEDELEDDK--ISLPFVVTDLRGRNLRPMRERTA--VQGQYLTVEQLTLDFEYVINEVIRH 460
Cdd:cd20913     1 VKKVVRRYSEVDDEIviTDIEDDSLLSGqhIELPLEVHGLGYQQLQMVSNAKAdkLTEPQVIVTQRSLDIEQFINEVAQK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 461 D-ATWGHQFCSFSDYDIVILEVCPETNQVLINIGLLLLAFPSPTEEGQLR------------------------------ 509
Cdd:cd20913    81 LcAEWGKKFWSCSDYDIEIVDVCPLSGDVICLLVILIQALESPEESKLDCsnrrklyetsclftwnistgqyrtldvgdl 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993776359 510 ---------GSVWSSYRKSCVDMVMKWLVPESSGRYVNRMTNEALHKGCSLKVLADSERYTWIV 564
Cdd:cd20913   161 tevppeqtsSQEWNPARKEASRLRKKWLVPQSSKRSVRVLTNESVFKGRSLDNLIDPFHYSAIV 224
PHA03247 PHA03247
large tegument protein UL36; Provisional
 274-381 5.66e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 5.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359  274 STCPLAPASPPEPQSPELPPALPSFCPEAAPARSSGSPEPSPAIAKAKEFVADIFRRAKEAKGGVPEEARPALCPGPSgs 353
Cdd:PHA03247  2769 PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPP-- 2846

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1993776359  354 rcrahSEPLALCGETAP----RDSPPASEAPA 381
Cdd:PHA03247  2847 -----PPSLPLGGSVAPggdvRRRPPSRSPAA 2873
PHA03247 PHA03247
large tegument protein UL36; Provisional
 292-438 9.05e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 9.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359  292 PPALPSFCPEAAPARSSGSPEPSPaiaKAKEFVAdifrRAKEAKGGVP-EEARPALCPGPSGSRcRAHSEPLALCGETAP 370
Cdd:PHA03247  2552 PPPLPPAAPPAAPDRSVPPPRPAP---RPSEPAV----TSRARRPDAPpQSARPRAPVDDRGDP-RGPAPPSPLPPDTHA 2623

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359  371 RDSPPASEAP-ASEPGyvnytklyyvlESGEGTEPEDELEDDKISLPFVVTDLRGRNL-RPMRERTAVQG 438
Cdd:PHA03247  2624 PDPPPPSPSPaANEPD-----------PHPPPTVPPPERPRDDPAPGRVSRPRRARRLgRAAQASSPPQR 2682
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
279-384 5.59e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.02  E-value: 5.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 279 APASPPEPQSPELPPALPSFCPEAAPARSSGSPEPSPAIAKAkefvadifrRAKEAKGGVPEEARPALCPGPSGSRCRAH 358
Cdd:PRK12323  398 APAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQA---------SARGPGGAPAPAPAPAAAPAAAARPAAAG 468

                          90       100
                  ....*....|....*....|....*.
gi 1993776359 359 SEPLAlcgetAPRDSPPASEAPASEP 384
Cdd:PRK12323  469 PRPVA-----AAAAAAPARAAPAAAP 489
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 277-385 9.27e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.55  E-value: 9.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359  277 PLAPASPPEPQSPElpPALPSFCPEAAPARSSGSPEPSPAIAKAKEFVadifRRAKEAKGGVPEEARPALCPGPSGS--- 353
Cdd:PHA03307    94 TLAPASPAREGSPT--PPGPSSPDPPPPTPPPASPPPSPAPDLSEMLR----PVGSPGPPPAASPPAAGASPAAVASdaa 167

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1993776359  354 RCRAHSEPLALCGETAPRDSPPASEAPASEPG 385
Cdd:PHA03307   168 SSRQAALPLSSPEETARAPSSPPAEPPPSTPP 199
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 257-385 1.14e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359  257 SVHSAGDRSFCQILYDHSTCPLAPASPPEPQSPelPPALPSFCPEAAPARSSGSPEPSPAIAKAKEF-------VADIFR 329
Cdd:PHA03307   166 AASSRQAALPLSSPEETARAPSSPPAEPPPSTP--PAAASPRPPRRSSPISASASSPAPAPGRSAADdagasssDSSSSE 243

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1993776359  330 RAKEAKGGVPEEARPALCPGPSGSRCRAHSEPlalcGETAPRDSPPASEAPASEPG 385
Cdd:PHA03307   244 SSGCGWGPENECPLPRPAPITLPTRIWEASGW----NGPSSRPGPASSSSSPRERS 295
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 280-383 3.54e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 43.22  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 280 PASPPEPQS--PELPPALPSFCPEAAPARSSGSPEPSPAIAKAKEFVADIFRRAKEAKGGVPEEARPALCPGPSGSRCRA 357
Cdd:NF033839  374 PEVKPQPETpkPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEV 453

                          90       100
                  ....*....|....*....|....*.
gi 1993776359 358 HSEPlalcgETAPRDSPPASEAPASE 383
Cdd:NF033839  454 KPQP-----ETPKPEVKPQPEKPKPE 474
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 284-383 5.35e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.83  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 284 PEPQSPELPPALPSFCPEAAPARSSGSPEPSPAIAKAKEFVADIFRRAKEAKGGVPEEARPALCPGPSGSRCRAHSEPla 363
Cdd:NF033839  303 PQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQP-- 380

                          90       100
                  ....*....|....*....|
gi 1993776359 364 lcgETAPRDSPPASEAPASE 383
Cdd:NF033839  381 ---ETPKPEVKPQPEKPKPE 397
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 277-385 7.19e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 7.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 277 PLAPASPPEPQSPELPPALPSFCPEAAPARSSGSPEPSPAIAKAKEFVADIFRRAKEAKGGVPEEARPAlcPGPSGSRCR 356
Cdd:PRK07764  399 PSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPA--PAPAAAPEP 476

                          90       100
                  ....*....|....*....|....*....
gi 1993776359 357 AHSEPLALCGETAPRDSPPASEAPASEPG 385
Cdd:PRK07764  477 TAAPAPAPPAAPAPAAAPAAPAAPAAPAG 505
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 280-405 7.39e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 7.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359  280 PASPPEPQSPELPPALPSFCPEAAPARSSGSPEPSPAIAKAKE--------FVADIFRRAKEAKGGVPEEARPALCPGPS 351
Cdd:PHA03307   123 PASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDaassrqaaLPLSSPEETARAPSSPPAEPPPSTPPAAA 202

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1993776359  352 GSRCRAHSEPLALCGETAPRDSPPASEAPASEPGYVNYTklYYVLESGEGTEPE 405
Cdd:PHA03307   203 SPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSS--SESSGCGWGPENE 254
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 279-360 8.36e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.39  E-value: 8.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 279 APASPPEPQSPELPPALPSFCPEAAPARSSGS--PEPSPAIAKAKEFVADIFRRAKEAKGGVPEEARPalcPGPSGSRCR 356
Cdd:PRK14951  413 APAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAvaLAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPA---AAPAAARLT 489


                  ....
gi 1993776359 357 AHSE 360
Cdd:PRK14951  490 PTEE 493
KLF14_N cd21576
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ...
 277-382 8.41e-04

N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as Krueppel-like factor 14 or basic transcription element-binding protein 5/BTEB5) is a protein that in humans is encoded by the KLF14 gene. KLF14 regulates the transcription of various genes, including TGFbetaRII (the type II receptor for TGFbeta). KLF14 is expressed in many tissues, lacks introns, and is subject to parent-specific expression. It also appears to be a master regulator of gene expression in adipose tissue. KLF14 is associated with coronary artery disease, hypercholesterolemia, and type 2 diabetes. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF14 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF14.


Pssm-ID: 409238 [Multi-domain]  Cd Length: 195  Bit Score: 40.96  E-value: 8.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 277 PLAPASP-PEPQSPELPPALPsfcpeAAPARSSGSPEPSPAIAKAkEFVADIFRRAKEAKGGVPEEA--------RPALC 347
Cdd:cd21576    46 PPESALPgPGPPGPAWVPPLL-----QVPAPSPGAGGAAPHLLAA-SVLADLRGGAGEGSREDSGEAprassgssDPARG 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1993776359 348 PGPSG-------SRCRAHSEPLALCGETAPRDSPPASEAPAS 382
Cdd:cd21576   120 SSPTLgsepapaSGEDAVSGPESSFGAPAIPSAPAAPGAPAV 161
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 277-384 9.76e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.01  E-value: 9.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 277 PLAPASPPEP-QSPELPPALPSFCPEAAPARSSGSPEPSPAIAKAKEfvadifRRAKEAKGGVPEEARPALCPGPSGSRC 355
Cdd:PRK14951  380 TPARPEAAAPaAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPV------AAPAAAAPAAAPAAAPAAVALAPAPPA 453

                          90       100       110
                  ....*....|....*....|....*....|
gi 1993776359 356 RAHSEPLALCGETAPRDSPP-ASEAPASEP 384
Cdd:PRK14951  454 QAAPETVAIPVRVAPEPAVAsAAPAPAAAP 483
PHA03247 PHA03247
large tegument protein UL36; Provisional
 277-384 1.02e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359  277 PLAPASPPEPQSPELPPALPSfCPEAAPARSSGSPEP----SPAIAKAKEFVADIFRRAKEAKGGVPEEARPALCP--GP 350
Cdd:PHA03247  2701 PPPPPPTPEPAPHALVSATPL-PPGPAAARQASPALPaapaPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPaaGP 2779

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1993776359  351 SGSRCRAHSEPLALCGETAPRDSPPASEAPASEP 384
Cdd:PHA03247  2780 PRRLTRPAVASLSESRESLPSPWDPADPPAAVLA 2813
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
274-411 1.26e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.79  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 274 STCPLAPASPPEPQSPELPPALPSFCPEA-APARSSGSPEPSPAIAKAKEFVADIFRRAKEAKGGVPEEARPALCPGPSG 352
Cdd:PRK12323  404 AAPAAAPAAAAAARAVAAAPARRSPAPEAlAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARA 483

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993776359 353 SRCRAHSeplalcgeTAPRDSPPASEAPA--SEPGYVNYTKLYYVLESGEGTEPEDELEDD 411
Cdd:PRK12323  484 APAAAPA--------PADDDPPPWEELPPefASPAPAQPDAAPAGWVAESIPDPATADPDD 536
PHA03247 PHA03247
large tegument protein UL36; Provisional
 277-384 1.27e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359  277 PLAPASPPEPQSPELPPAlPSFCPEAAPARSSGSPEPSPAIAKAKEFVADIFRRAKEAKGGVPEEARPALCPGPSG-SRC 355
Cdd:PHA03247  2899 ALPPDQPERPPQPQAPPP-PQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAvPRF 2977

                           90       100
                   ....*....|....*....|....*....
gi 1993776359  356 RAHSeplalcgetaPRDSPPASEAPASEP 384
Cdd:PHA03247  2978 RVPQ----------PAPSREAPASSTPPL 2996
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 277-385 2.96e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.47  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 277 PLAPASPPEPQSPELPPALPSFCPEAAPARSSGSPEPSPAIAKAKEFVADIFRRAKEakggvPEEARPALCPGPSGSRCR 356
Cdd:PRK14951  391 AAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVAL-----APAPPAQAAPETVAIPVR 465

                          90       100
                  ....*....|....*....|....*....
gi 1993776359 357 AHSEPLALCGETAPRDSPPASEAPASEPG 385
Cdd:PRK14951  466 VAPEPAVASAAPAPAAAPAAARLTPTEEG 494
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
281-385 4.67e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.86  E-value: 4.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359 281 ASPPEPQSPELPPALPSFCPEAAPARSSGSPEPSPAIAKAKEFVADIFRRAKEAKGGVP--EEARPALcPGPSGSRCRAH 358
Cdd:PRK12323  439 ASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPpwEELPPEF-ASPAPAQPDAA 517

                          90       100
                  ....*....|....*....|....*..
gi 1993776359 359 SEPLALCGETAPRDSPPASEAPASEPG 385
Cdd:PRK12323  518 PAGWVAESIPDPATADPDDAFETLAPA 544
PHA03247 PHA03247
large tegument protein UL36; Provisional
 277-384 4.84e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 4.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993776359  277 PLAPASPPE-PQSPELPPALPSFCPEAAPARSSGSPEPSPAIAKAKEFVADIFRRAKEAKGGVPeeARPALCPGPSGSRC 355
Cdd:PHA03247  2673 AAQASSPPQrPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALP--AAPAPPAVPAGPAT 2750

                           90       100
                   ....*....|....*....|....*....
gi 1993776359  356 RAHSEPLALCGETAPRDSPPASEAPASEP 384
Cdd:PHA03247  2751 PGGPARPARPPTTAGPPAPAPPAAPAAGP 2779
 
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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