|
Name |
Accession |
Description |
Interval |
E-value |
| CHGN |
pfam05679 |
Chondroitin N-acetylgalactosaminyltransferase; |
330-868 |
0e+00 |
|
Chondroitin N-acetylgalactosaminyltransferase;
Pssm-ID: 461712 [Multi-domain] Cd Length: 500 Bit Score: 751.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 330 HIGECLREMYTTHEDVEVGRCVRRFGGTQCVWSYEMQQLFHENYEHNRKGYIQDLHNSKIHAAITLHPNKRPAYQYRLHN 409
Cdd:pfam05679 1 HLDWCLKNLYSTHEDVELGRCIQKFAGIPCTWSYEGQRYFYFNYSSGKKGFIGNLKSKEFHSAITLHPVKDPADMYRLHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 410 YMLSRKISELRYRTIQLHRESALMSKLSNSEVSKEDQQLGMMPSFNHfqPQERNEVMEWEFLTGKLLYSAAENQPpRQSI 489
Cdd:pfam05679 81 YFLSLELQKLRQEIIKLQREIKNMSELLPEGIDSLSWPLGIPPPLNR--PKSRFDVLRWDYFTETHLYSADDGQP-RRRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 490 NSILRSALDDTVLQVMEMINENAKSRGRLIDFKEIQYGYRRVDPMHGVEYILDLLLLYKRHKGRklTVPVRRHAYLQQPF 569
Cdd:pfam05679 158 DGADKEDLDDVINTAMEEINRNYRPRGRVLEFKQLLNGYRRFDPLRGMEYILDLLLEYKKYRGR--TVPVRRRVYLQRPF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 570 SKPFFREMEELDinslvesinsgtpatgfsfisnslkilsslqepkeigghNEKKVHILVPLVGRYDIFLRFMENFESTC 649
Cdd:pfam05679 236 SKVEIIPMPYVT---------------------------------------ESTRVHIILPLSGRYETFERFLENYERVC 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 650 IIPKQNV-KLVIILFSRDSGQE--SIKHIELIQEYQNRYPSAEMTLIPMKGEFSRGLGLEMGSSQFDNDTLLLFCDVDLI 726
Cdd:pfam05679 277 LETGENVvLLLVVLYDPDEGQNdvFAEIKELIEELEKKYPKAKIPWISVKGEFSRGKALDLGAKKFPPDSLLFFCDVDMV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 727 FRGDFLQRCRDNTVQGQQVYYPIIFSQYDPKVTRMGNSPTEGD--FVFSKETGFWRDYGYGITCIYKSDLLGAGGFDTSI 804
Cdd:pfam05679 357 FTPEFLNRCRMNTIQGKQVYFPIVFSQYDPEVVYYDKPVPTSDdnFDISKDTGHWRRYGFGIVCFYKSDYMAVGGFRTSI 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2780850327 805 QGWGLEDVDLYNKVIQSGLRPFRSQEVGVVHIFHPVHCDPNLDPKQYKMCLGSKASTFASTMKL 868
Cdd:pfam05679 437 QGWGLEDVDLYDKFVKSGLHVFRAVEPGLVHRYHPRHCDPRLSEKQYHMCLGSKAEGLASRTQL 500
|
|
| Fringe |
pfam02434 |
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ... |
170-400 |
3.25e-14 |
|
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls the response of the Notch receptor to specific ligands. FNG is localized to the Golgi apparatus (not secreted as previously thought). Modification of Notch occurs through glycosylation by FNG. The xenopus homolog, lunatic fringe, has been implicated in a variety of functions.
Pssm-ID: 367085 Cd Length: 248 Bit Score: 73.51 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 170 GDFLYVGVMTAQKYLGSRALAAHRTWARFIPGRVEFFSSQQPPsaalGQPPPPLPVIALPGVDDSYPPQKKSFMM-IKYm 248
Cdd:pfam02434 3 LDDIFIAVKTTKKFHKTRLPLLLKTWISRAKHQTYIFTDGEDE----GLPTRTGGHLINTNCSAGHCRKALSCKMaVEY- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 249 hDHYL-DKYEWFMRADDDVYIKGDKLEEFLRSLNSSKPLYLGQT---GLGNTEELGKLGLEPGENFCMGGPGMIFSREVL 324
Cdd:pfam02434 78 -DRFLeSGKKWFCHVDDDNYVNVPRLVRLLSCYNHTQDVYLGKPslyRPIEATERVKGNRKVGFWFATGGAGFCISRGLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 325 RRMVPHIGEClrEMYTT------HEDVEVGRCVRRFGGTQCVWSyemqQLFHENYEHnrkgyIQDLHNSKIHAAITL--- 395
Cdd:pfam02434 157 LKMSPWASGG--RFMSTsekirlPDDCTLGYIIENLLGVPLTHS----PLFHSHLEN-----LQDLPPETLHEQVTLsyg 225
|
....*.
gi 2780850327 396 -HPNKR 400
Cdd:pfam02434 226 kFWNKR 231
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
76-238 |
3.37e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.56 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 76 PPPASHQLPGPLRPEVAPGGPSLRSSPWQQPAPlPQRRRGHKPEGATALPGAPAAKGEPEEEDGGAAGPRKGGRPRSSQN 155
Cdd:PHA03247 2560 PPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAP-PQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEP 2638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 156 GSGDGGAAAPTSGPGDFLYVGVM-----TAQKYLGSRALAAHRTW----ARFIPGRVEFFSSQQPPsaalGQPPPPLPVI 226
Cdd:PHA03247 2639 DPHPPPTVPPPERPRDDPAPGRVsrprrARRLGRAAQASSPPQRPrrraARPTVGSLTSLADPPPP----PPTPEPAPHA 2714
|
170
....*....|..
gi 2780850327 227 ALPGVDDSYPPQ 238
Cdd:PHA03247 2715 LVSATPLPPGPA 2726
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
51-238 |
4.56e-07 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 53.53 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 51 SATGPRADAQQLLPQPQSQPRLQQSPPPAshQLPGPLRPEVAPGGPSLRSSPWQQPAPLPQRRRG------HKPEGATAL 124
Cdd:COG5180 285 AGSEPQSDAPEAETARPIDVKGVASAPPA--TRPVRPPGGARDPGTPRPGQPTERPAGVPEAASDagqppsAYPPAEEAV 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 125 PGAPAAKGEPEEEDGGAAGPRKGGRPRSSQNGSGDGGAAAPTSGPGDflyvgvmtaqkyLGSRALaahrtwarfiPGRVE 204
Cdd:COG5180 363 PGKPLEQGAPRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGAGD------------LVQAAL----------DGGGR 420
|
170 180 190
....*....|....*....|....*....|....
gi 2780850327 205 FFSSQQPPSAALGQPPPPLPViALPGVDDSYPPQ 238
Cdd:COG5180 421 ETASLGGAAGGAGQGPKADFV-PGDAESVSGPAG 453
|
|
| KLF14_N |
cd21576 |
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ... |
84-167 |
1.84e-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: 43.27 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 84 PGP-LRPEVAPGGPSLRSSPWQQPAPLPQRRRGHKPE-----GATALPGAPAAKGEPEEEDGGAAGPrKGGRPRSsqngs 157
Cdd:cd21576 103 SGEaPRASSGSSDPARGSSPTLGSEPAPASGEDAVSGpessfGAPAIPSAPAAPGAPAVSGEVPGGA-PGAGPAP----- 176
|
90
....*....|
gi 2780850327 158 gdggAAAPTS 167
Cdd:cd21576 177 ----AAGPAP 182
|
|
| GT2_Chondriotin_Pol_N |
cd06420 |
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ... |
790-838 |
1.01e-03 |
|
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.
Pssm-ID: 133042 [Multi-domain] Cd Length: 182 Bit Score: 41.02 E-value: 1.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2780850327 790 YKSDLLGAGGFDTSIQGWGLEDVDLYNKVIQSGLRPFRSQEVGVVhiFH 838
Cdd:cd06420 134 WKKDLLAVNGFDEEFTGWGGEDSELVARLLNSGIKFRKLKFAAIV--FH 180
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CHGN |
pfam05679 |
Chondroitin N-acetylgalactosaminyltransferase; |
330-868 |
0e+00 |
|
Chondroitin N-acetylgalactosaminyltransferase;
Pssm-ID: 461712 [Multi-domain] Cd Length: 500 Bit Score: 751.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 330 HIGECLREMYTTHEDVEVGRCVRRFGGTQCVWSYEMQQLFHENYEHNRKGYIQDLHNSKIHAAITLHPNKRPAYQYRLHN 409
Cdd:pfam05679 1 HLDWCLKNLYSTHEDVELGRCIQKFAGIPCTWSYEGQRYFYFNYSSGKKGFIGNLKSKEFHSAITLHPVKDPADMYRLHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 410 YMLSRKISELRYRTIQLHRESALMSKLSNSEVSKEDQQLGMMPSFNHfqPQERNEVMEWEFLTGKLLYSAAENQPpRQSI 489
Cdd:pfam05679 81 YFLSLELQKLRQEIIKLQREIKNMSELLPEGIDSLSWPLGIPPPLNR--PKSRFDVLRWDYFTETHLYSADDGQP-RRRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 490 NSILRSALDDTVLQVMEMINENAKSRGRLIDFKEIQYGYRRVDPMHGVEYILDLLLLYKRHKGRklTVPVRRHAYLQQPF 569
Cdd:pfam05679 158 DGADKEDLDDVINTAMEEINRNYRPRGRVLEFKQLLNGYRRFDPLRGMEYILDLLLEYKKYRGR--TVPVRRRVYLQRPF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 570 SKPFFREMEELDinslvesinsgtpatgfsfisnslkilsslqepkeigghNEKKVHILVPLVGRYDIFLRFMENFESTC 649
Cdd:pfam05679 236 SKVEIIPMPYVT---------------------------------------ESTRVHIILPLSGRYETFERFLENYERVC 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 650 IIPKQNV-KLVIILFSRDSGQE--SIKHIELIQEYQNRYPSAEMTLIPMKGEFSRGLGLEMGSSQFDNDTLLLFCDVDLI 726
Cdd:pfam05679 277 LETGENVvLLLVVLYDPDEGQNdvFAEIKELIEELEKKYPKAKIPWISVKGEFSRGKALDLGAKKFPPDSLLFFCDVDMV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 727 FRGDFLQRCRDNTVQGQQVYYPIIFSQYDPKVTRMGNSPTEGD--FVFSKETGFWRDYGYGITCIYKSDLLGAGGFDTSI 804
Cdd:pfam05679 357 FTPEFLNRCRMNTIQGKQVYFPIVFSQYDPEVVYYDKPVPTSDdnFDISKDTGHWRRYGFGIVCFYKSDYMAVGGFRTSI 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2780850327 805 QGWGLEDVDLYNKVIQSGLRPFRSQEVGVVHIFHPVHCDPNLDPKQYKMCLGSKASTFASTMKL 868
Cdd:pfam05679 437 QGWGLEDVDLYDKFVKSGLHVFRAVEPGLVHRYHPRHCDPRLSEKQYHMCLGSKAEGLASRTQL 500
|
|
| Fringe |
pfam02434 |
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ... |
170-400 |
3.25e-14 |
|
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls the response of the Notch receptor to specific ligands. FNG is localized to the Golgi apparatus (not secreted as previously thought). Modification of Notch occurs through glycosylation by FNG. The xenopus homolog, lunatic fringe, has been implicated in a variety of functions.
Pssm-ID: 367085 Cd Length: 248 Bit Score: 73.51 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 170 GDFLYVGVMTAQKYLGSRALAAHRTWARFIPGRVEFFSSQQPPsaalGQPPPPLPVIALPGVDDSYPPQKKSFMM-IKYm 248
Cdd:pfam02434 3 LDDIFIAVKTTKKFHKTRLPLLLKTWISRAKHQTYIFTDGEDE----GLPTRTGGHLINTNCSAGHCRKALSCKMaVEY- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 249 hDHYL-DKYEWFMRADDDVYIKGDKLEEFLRSLNSSKPLYLGQT---GLGNTEELGKLGLEPGENFCMGGPGMIFSREVL 324
Cdd:pfam02434 78 -DRFLeSGKKWFCHVDDDNYVNVPRLVRLLSCYNHTQDVYLGKPslyRPIEATERVKGNRKVGFWFATGGAGFCISRGLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 325 RRMVPHIGEClrEMYTT------HEDVEVGRCVRRFGGTQCVWSyemqQLFHENYEHnrkgyIQDLHNSKIHAAITL--- 395
Cdd:pfam02434 157 LKMSPWASGG--RFMSTsekirlPDDCTLGYIIENLLGVPLTHS----PLFHSHLEN-----LQDLPPETLHEQVTLsyg 225
|
....*.
gi 2780850327 396 -HPNKR 400
Cdd:pfam02434 226 kFWNKR 231
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
76-238 |
3.37e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.56 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 76 PPPASHQLPGPLRPEVAPGGPSLRSSPWQQPAPlPQRRRGHKPEGATALPGAPAAKGEPEEEDGGAAGPRKGGRPRSSQN 155
Cdd:PHA03247 2560 PPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAP-PQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEP 2638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 156 GSGDGGAAAPTSGPGDFLYVGVM-----TAQKYLGSRALAAHRTW----ARFIPGRVEFFSSQQPPsaalGQPPPPLPVI 226
Cdd:PHA03247 2639 DPHPPPTVPPPERPRDDPAPGRVsrprrARRLGRAAQASSPPQRPrrraARPTVGSLTSLADPPPP----PPTPEPAPHA 2714
|
170
....*....|..
gi 2780850327 227 ALPGVDDSYPPQ 238
Cdd:PHA03247 2715 LVSATPLPPGPA 2726
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
51-238 |
4.56e-07 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 53.53 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 51 SATGPRADAQQLLPQPQSQPRLQQSPPPAshQLPGPLRPEVAPGGPSLRSSPWQQPAPLPQRRRG------HKPEGATAL 124
Cdd:COG5180 285 AGSEPQSDAPEAETARPIDVKGVASAPPA--TRPVRPPGGARDPGTPRPGQPTERPAGVPEAASDagqppsAYPPAEEAV 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 125 PGAPAAKGEPEEEDGGAAGPRKGGRPRSSQNGSGDGGAAAPTSGPGDflyvgvmtaqkyLGSRALaahrtwarfiPGRVE 204
Cdd:COG5180 363 PGKPLEQGAPRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGAGD------------LVQAAL----------DGGGR 420
|
170 180 190
....*....|....*....|....*....|....
gi 2780850327 205 FFSSQQPPSAALGQPPPPLPViALPGVDDSYPPQ 238
Cdd:COG5180 421 ETASLGGAAGGAGQGPKADFV-PGDAESVSGPAG 453
|
|
| PRK14959 |
PRK14959 |
DNA polymerase III subunits gamma and tau; Provisional |
6-198 |
5.08e-06 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 50.06 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 6 RRPWVSVALGLVLGFTAASWLIAPRVAELSEKRRRGSSLCSYYGRSATGPrADAQQLLPQPQSQPRLQQSPPPA----SH 81
Cdd:PRK14959 340 RRVLTSLEPAMALELLLLNLAMLPRLMPVESLRPSGGGASAPSGSAAEGP-ASGGAATIPTPGTQGPQGTAPAAgmtpSS 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 82 QLPGPLRPEVAPGgPSLrssPWQQPAPLPQRRrGHKPEGATALPGAPAAKGEPEE-----------EDGGAAGPRKGGRP 150
Cdd:PRK14959 419 AAPATPAPSAAPS-PRV---PWDDAPPAPPRS-GIPPRPAPRMPEASPVPGAPDSvasasdapptlGDPSDTAEHTPSGP 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2780850327 151 RS-------SQNGSGDGGA-------AAPTSGPGdFLYVGVMTAQKY-----LGSRALAAHRTWARF 198
Cdd:PRK14959 494 RTwdgflefCQGRNGQGGRlatvlrqATPEHADG-RLRLATMSSVQYerltdAATETTLAGLVRDYF 559
|
|
| Glyco_transf_7C |
pfam02709 |
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ... |
779-839 |
1.02e-05 |
|
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of galactosyltransferases from a wide range of Metazoa with three related galactosyltransferases activities, all three of which are possessed by one sequence in some cases. EC:2.4.1.90, N-acetyllactosamine synthase; EC:2.4.1.38, Beta-N-acetylglucosaminyl-glycopeptide beta-1,4- galactosyltransferase; and EC:2.4.1.22 Lactose synthase. Note that N-acetyllactosamine synthase is a component of Lactose synthase along with alpha-lactalbumin, in the absence of alpha-lactalbumin EC:2.4.1.90 is the catalyzed reaction.
Pssm-ID: 460659 [Multi-domain] Cd Length: 78 Bit Score: 44.14 E-value: 1.02e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2780850327 779 WRDYGYGITCIYKSDLLGAGGFDTSIQGWGLEDVDLYNKVIQSGLRPFR-SQEVG-VVHIFHP 839
Cdd:pfam02709 16 YKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERpPGDIGrYYMLYHK 78
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
72-231 |
1.04e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.55 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 72 LQQSPPPASHQLPGPLRPE--VAPGGPSLRSSPWQQPAPLPQRRR------------------------GHKPEGATALP 125
Cdd:PHA03247 2835 QPTAPPPPPGPPPPSLPLGgsVAPGGDVRRRPPSRSPAAKPAAPArppvrrlarpavsrstesfalppdQPERPPQPQAP 2914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 126 GAPAAKGEPEEEDGGAAGPRKGGRPRSSqngsgdggaAAPTSGPGdflyvGVMTAQKYLGSRALAAhrtwarFIPGRVEF 205
Cdd:PHA03247 2915 PPPQPQPQPPPPPQPQPPPPPPPRPQPP---------LAPTTDPA-----GAGEPSGAVPQPWLGA------LVPGRVAV 2974
|
170 180 190
....*....|....*....|....*....|
gi 2780850327 206 FSSQQPPSA----ALGQPPPPLPVIALPGV 231
Cdd:PHA03247 2975 PRFRVPQPApsreAPASSTPPLTGHSLSRV 3004
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
76-229 |
8.19e-05 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 46.60 E-value: 8.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 76 PPPAShqlPGPLRPEVAPGGPSLRSSPWQQPAPLPQRRRGHKPEGATALPGAPAAKGEPEEEDGGAAGPRKGGRPrssqn 155
Cdd:PHA03378 696 PPPRA---PTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPP----- 767
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2780850327 156 gSGDGGAAAPTSGPGdflyvGVMTAQkylgsralaahrtwarfipgrveffssQQPPSAALGQPPP---PLPVIALP 229
Cdd:PHA03378 768 -AAAPGAPTPQPPPQ-----APPAPQ---------------------------QRPRGAPTPQPPPqagPTSMQLMP 811
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
75-169 |
1.44e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.93 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 75 SPPPASHQLPGPLRPEVAPGGPSLRSSPWQQPAPLPQRRRGHKPEGATAlpgapAAKGEPEEEDGGAA-----------G 143
Cdd:PHA03307 331 SSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPA-----ASAGRPTRRRARAAvagrarrrdatG 405
|
90 100
....*....|....*....|....*.
gi 2780850327 144 PRKGGRPRSSQNGSGDGGAAAPTSGP 169
Cdd:PHA03307 406 RFPAGRPRPSPLDAGAASGAFYARYP 431
|
|
| KLF14_N |
cd21576 |
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ... |
84-167 |
1.84e-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: 43.27 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 84 PGP-LRPEVAPGGPSLRSSPWQQPAPLPQRRRGHKPE-----GATALPGAPAAKGEPEEEDGGAAGPrKGGRPRSsqngs 157
Cdd:cd21576 103 SGEaPRASSGSSDPARGSSPTLGSEPAPASGEDAVSGpessfGAPAIPSAPAAPGAPAVSGEVPGGA-PGAGPAP----- 176
|
90
....*....|
gi 2780850327 158 gdggAAAPTS 167
Cdd:cd21576 177 ----AAGPAP 182
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
55-237 |
2.35e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.31 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 55 PRADAQQLLPQPQSQPRLQQSPPPASHQLPGPLRPEVAPGGPSLRSSPWQQPAPLPQRRRGHKPEGATALPGAPAAKGE- 133
Cdd:PHA03247 2652 PRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQa 2731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 134 ----------PEEEDGGA--AGPRKGGRPRSSQNGSGDGGAAAPTSGPGDFLYVgvmTAQKYLGSRALAAHRTW-ARFIP 200
Cdd:PHA03247 2732 spalpaapapPAVPAGPAtpGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTR---PAVASLSESRESLPSPWdPADPP 2808
|
170 180 190
....*....|....*....|....*....|....*....
gi 2780850327 201 GRVEFFSSQQPPSA--ALGQPPPPLPVIALPGVDDSYPP 237
Cdd:PHA03247 2809 AAVLAPAAALPPAAspAGPLPPPTSAQPTAPPPPPGPPP 2847
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
51-238 |
3.94e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.21 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 51 SATGPRADAQQLLPQPQSQPRLQQSPPPAShqlPGPLRPEVAPGGPSLRSSPWQQPAPLPQRRRGHKPEGATALPGAPAA 130
Cdd:PRK07764 594 AAGGEGPPAPASSGPPEEAARPAAPAAPAA---PAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWP 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 131 KGEPEEEDGGAAGPRKGGRPRSSQNGSGDGGAAAPTSGPGdflyvgvmtaqkylGSRALAAHRTWARFIPGrveffSSQQ 210
Cdd:PRK07764 671 AKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPP--------------AGQADDPAAQPPQAAQG-----ASAP 731
|
170 180
....*....|....*....|....*...
gi 2780850327 211 PPSAALGQPPPPLPVIALPGVDDSYPPQ 238
Cdd:PRK07764 732 SPAADDPVPLPPEPDDPPDPAGAPAQPP 759
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
74-169 |
6.91e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 74 QSPPPASHQLPGPLRPEVAPGGPSLRSSPWQQPAPLPQRRRGHK-----------------------PEGATALPGAP-- 128
Cdd:PHA03307 184 RAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSaaddagasssdssssessgcgwgPENECPLPRPApi 263
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2780850327 129 --------AAKGEPEEEDGGAAGPRKGGRPRSSQNGSGDGGAAAPTSGP 169
Cdd:PHA03307 264 tlptriweASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSP 312
|
|
| GT2_Chondriotin_Pol_N |
cd06420 |
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ... |
790-838 |
1.01e-03 |
|
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.
Pssm-ID: 133042 [Multi-domain] Cd Length: 182 Bit Score: 41.02 E-value: 1.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2780850327 790 YKSDLLGAGGFDTSIQGWGLEDVDLYNKVIQSGLRPFRSQEVGVVhiFH 838
Cdd:cd06420 134 WKKDLLAVNGFDEEFTGWGGEDSELVARLLNSGIKFRKLKFAAIV--FH 180
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
73-170 |
1.34e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.67 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 73 QQSPPPASHQLPGPLRPEVAPGGPSLRSS-----PWQQPAPLPQRRRGHKPEGATALPG-APAAKGEPEEEDGGAAGPRK 146
Cdd:PRK07764 397 AAPSAAAAAPAAAPAPAAAAPAAAAAPAPaaapqPAPAPAPAPAPPSPAGNAPAGGAPSpPPAAAPSAQPAPAPAAAPEP 476
|
90 100
....*....|....*....|....*
gi 2780850327 147 GGRPRSSQNGSG-DGGAAAPTSGPG 170
Cdd:PRK07764 477 TAAPAPAPPAAPaPAAAPAAPAAPA 501
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
50-237 |
2.29e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.79 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 50 RSATGPRADAQQLLPQPQSQPRLQQSPPPASHQLPGPLRPEVAPGGPSLRSSPWQQPAPLPQRRRGHKPEGATALPGAPA 129
Cdd:PRK12323 376 TAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPA 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 130 AKGEPEEEDGGAAGPRKGGRPRSSQNGSGDGGAAAPTSG---PGDFLYVGVMTAQKYLGSRALAAHRTWARFIPGRVEFF 206
Cdd:PRK12323 456 AAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDdppPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPD 535
|
170 180 190
....*....|....*....|....*....|.
gi 2780850327 207 SSQQPPSAALGQPPPPLPVIALPGVDDSYPP 237
Cdd:PRK12323 536 DAFETLAPAPAAAPAPRAAAATEPVVAPRPP 566
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
73-145 |
3.31e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.12 E-value: 3.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2780850327 73 QQSPPPASHQLPGPLRPEVAPGGPSLRSSPWQQPAPLPQRRRGHKPEGATALPGAPAAKGEPEEEDGG--AAGPR 145
Cdd:PRK07764 439 PAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGAddAATLR 513
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
76-170 |
3.41e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 41.21 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 76 PPPASHQLPGPLRPEVAPggPSLRSSPWQQPAPLPQRRRGhkPEGATALPGAPAAKGEPEEE--DGGAAGPRKGGRPRSS 153
Cdd:PHA03378 766 PPAAAPGAPTPQPPPQAP--PAPQQRPRGAPTPQPPPQAG--PTSMQLMPRAAPGQQGPTKQilRQLLTGGVKRGRPSLK 841
|
90
....*....|....*...
gi 2780850327 154 QNGSGDGGAAA-PTSGPG 170
Cdd:PHA03378 842 KPAALERQAAAgPTPSPG 859
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
76-170 |
3.99e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 40.92 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 76 PPPASHQLPGPLRPEVAPGGPSLRSSPWQQPAPLPQRR----RGHKPEGATALPGAPAAKGEPEEEDGGAAGPRKGGRPR 151
Cdd:PHA03307 258 PRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSpspsPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSR 337
|
90
....*....|....*....
gi 2780850327 152 SSQNGSGDGGAAAPTSGPG 170
Cdd:PHA03307 338 GAAVSPGPSPSRSPSPSRP 356
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
2-237 |
5.33e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 40.60 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 2 AVRSRRPWVSVALGLVLGFTAAswliAPRVAELSEKRRRGSSLcSYYGRSATGPRADAQQLLPQPQSQPRLQQSPPPASH 81
Cdd:PRK07003 394 SAVPAVTAVTGAAGAALAPKAA----AAAAATRAEAPPAAPAP-PATADRGDDAADGDAPVPAKANARASADSRCDERDA 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 82 QLPGPLRPEVAPGGPSLRSSPWQ-----------------QPAPLPQRRRGHKPEGAT-----ALPGAPAAkGEPEEEDG 139
Cdd:PRK07003 469 QPPADSGSASAPASDAPPDAAFEpapraaapsaatpaavpDARAPAAASREDAPAAAAppapeARPPTPAA-AAPAARAG 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 140 GAAGP----RKGGRPRSSQNGSGDGGAAAPTSGPGdflyvgvmTAQKYLGSRALAAHRT--WARFIPGRVEFFSSQQPPS 213
Cdd:PRK07003 548 GAAAAldvlRNAGMRVSSDRGARAAAAAKPAAAPA--------AAPKPAAPRVAVQVPTprARAATGDAPPNGAARAEQA 619
|
250 260 270
....*....|....*....|....*....|....*.
gi 2780850327 214 AALGQPPPP---------LPVIA---LPGVDDSYPP 237
Cdd:PRK07003 620 AESRGAPPPwedippddyVPLSAdegFGGPDDGFVP 655
|
|
| GINS_A_psf1 |
cd11710 |
Alpha-helical domain of GINS complex protein Psf1; Psf1 is a component of the GINS tetrameric ... |
364-441 |
5.55e-03 |
|
Alpha-helical domain of GINS complex protein Psf1; Psf1 is a component of the GINS tetrameric protein complex. Psf1 is mainly expressed in highly proliferative tissues, such as blastocysts, adult bone marrow, and testis, in which the stem cell system is active. Loss of Psf1 causes embryonic lethality. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) that is involved in both initiation and elongation stages of eukaryotic chromosome replication. Besides being essential for the maintenance of genomic integrity, GINS plays a central role in coordinating DNA replication with cell cycle checkpoints and is involved in cell growth. The eukaryotic GINS subunits are homologous and homologs are also found in the archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3.
Pssm-ID: 212548 Cd Length: 129 Bit Score: 38.00 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 364 EMQQLFHENYEHNRKGYIQDLHNS-----KIHAAITLHpNKRP--AYQY-RLhnymlsRKISELRYRTIQlHRESALMSK 435
Cdd:cd11710 33 EIRDLYEENQALLEEAQEEEEDPGlipglLVRHLSILR-NKRCllAYLYeRL------DRIRELRWENGS-VLPEDIKEN 104
|
....*.
gi 2780850327 436 LSNSEV 441
Cdd:cd11710 105 LSPAEK 110
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
28-171 |
5.76e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.35 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 28 APRVAELSEKRRRGSSLCSYYGRSATGPRADAQQLLPQPQSQPRLQQSPPPASHQLPGPL----RPEVAPGGPSLRSSPW 103
Cdd:PRK07764 635 APAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAgaapAQPAPAPAATPPAGQA 714
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2780850327 104 QQPAPLPQRRRGHKPEGATALPGAPAAKGEPEEEDGGAAGPRKGGRPRSSQNGSGDGGAAAPTSGPGD 171
Cdd:PRK07764 715 DDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
28-236 |
8.66e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 39.92 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 28 APRVAE---LSEKRRRGSSLCSYYGRSATGPRADAQQLLPQPqsqprlqqSPPPASHQLPGPL-----RPEVAPGGPSLR 99
Cdd:PHA03247 2574 APRPSEpavTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPS--------PLPPDTHAPDPPPpspspAANEPDPHPPPT 2645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2780850327 100 SSPWQQPAPLPQRRRGHKPEGATALPGAPAAKGEPEEEDGGAAGPRKGG----------------RPRSSQNGSGDGGAA 163
Cdd:PHA03247 2646 VPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSltsladpppppptpepAPHALVSATPLPPGP 2725
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2780850327 164 APTSGPGDFLYVGVMTAQKYLGSRALAAHRTWARfiPGRVEFFSSQQPPSAALGQPPPPLPVIALPGVDDSYP 236
Cdd:PHA03247 2726 AAARQASPALPAAPAPPAVPAGPATPGGPARPAR--PPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRE 2796
|
|
| |
