|
Name |
Accession |
Description |
Interval |
E-value |
| Ufd2P_core |
pfam10408 |
Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ... |
747-1367 |
0e+00 |
|
Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ubiquitin elongating factor or E4, running from helix alpha-11 to alpha-38. It consists of 31 helices of variable length connected by loops of variable size forming a compact unit; the helical packing pattern of the compact unit consists of five structural repeats that resemble tandem Armadillo (ARM) repeats. This domain is involved in ubiquitination as it binds Cdc48p and escorts ubiquitinated proteins from Cdc48p to the proteasome for degradation. The core is structurally similar to the nuclear transporter protein importin-alpha. The core is associated with the U-box at the C-terminus, pfam04564, which has ligase activity.
Pssm-ID: 463080 Cd Length: 594 Bit Score: 738.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 747 LGAFFSFSVFAeDDAKVVEKYFSGPAITLENTRVVSQ-SLQHYLELGRQELFKILHSILLNG-ETREAALSYMAALVNAN 824
Cdd:pfam10408 1 LGPFLRLSPLP-DDPEVAKKYFSNPKTRSPADIESSQsSLRQELKTLQEQLFQIVNKLLRASpESRERVLDWFAQIINLN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 825 MKKAQMQADDRLVSTDGFMLNLLWVLQQLS------TKIKLETVDPTYIFHPRCRITLPnDETRINATMEDVNERltelY 898
Cdd:pfam10408 80 HKRRKMQVDPNTVSSDGFMLNLTAVLLRLCepfldaTFSKIDKIDPDYLLPRSSRIDIS-DETRLNADQEEADEF----Y 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 899 GDQPPFSEPKFPTECFFLTLHAHHLSILPSCRRYIRRLRAIRELNRTvedlknnesqwkdsplatrhremlkrcktqlkk 978
Cdd:pfam10408 155 EQKAKEGEPNFITECFFLTLAALHLGILPAISKYKRLARELKRLQAE--------------------------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 979 lvrcKACADAGLLDESFLRRCLNFYGLLIQLMLRILDP--AYPD--VTLPLNSEVPKVFAALPEFYVEDVAEFLFFIVQY 1054
Cdd:pfam10408 202 ----KLAYEAVLLDPSLLQRSLQFLRFVATWLLRVADPkhQYPKkpLKLPLPAEPPEPFKYLPEYFIEDIVDFLLFVTRF 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 1055 SPQVLY-EPCTQDIVMFLVVMLCNQNYIRNPYLVAKLVEVMFMTNPSVQ-PRTQKFFEMIENHPLSTKLLVPSLMKFYTD 1132
Cdd:pfam10408 278 APDILEsLSQLDELITFCIVFLRSPEYIKNPHLKAKLVEVLFYGTPPRQnGRPGVLGDILESHPLALKHLLPALMKFYID 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 1133 VEHTGATSEFYDKFTIRYHISTIFKSLWQNIAHHGTFMEEFNSGKQ-FVRYINMLINDTTFLLDESLESLKRIHEVQEEM 1211
Cdd:pfam10408 358 VEKTGASSQFYDKFNIRYNISQILKYLWKNPSYREQLKKEAKENEDfFVRFVNLLLNDVTFLLDESLSKLKEIHELQEEM 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 1212 KNKEQWDQLPRDQQQARQSQLAQDERVSRSYLALATETVDMFHLLTKQVQKPFLRPELGPRLAAMLNFNLQQLCGPKCRD 1291
Cdd:pfam10408 438 ADAAEWEALPEEERQEREEQLRSLERQAKSYLQLANETVKLLKLFTKEIPEPFLMPEIVDRLAAMLNYNLDQLVGPKCKN 517
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907156787 1292 LKVENPEKYGFEPKKLLDQLTDIYLQLDCA-RFAKAIADDQRSYSKELFEEVISKMRKAGIKSTIAIEKFKLLAEKV 1367
Cdd:pfam10408 518 LKVKNPEKYGFNPKELLSDIVDIYLNLSDQpEFVRAVARDGRSYSPELFEKAARILRRKGLKSPEEIEKFEELAQKV 594
|
|
| UFD2 |
COG5113 |
Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, ... |
652-1453 |
4.10e-131 |
|
Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227444 [Multi-domain] Cd Length: 929 Bit Score: 429.40 E-value: 4.10e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 652 NLPYGFIQELVRTTHQDEEVFKQIFIPILQglALAAKECSLESDYFKYPLMALGELcetkFGKTHPMCNLVASLPLWLPk 731
Cdd:COG5113 129 LLPMIFLSSFKQRQLDEASNLDNLFTSALE--ALTGLHGVLEEDTVLKNVMEIYWG----LVNTKPIADVILKFPIYSG- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 732 SLSPGsgrELQRLSYLGAFFSFSVFAEDdakVVEKYFSGPAI-TLENTRVVSQSLQHYLELGRQELFKILHSILLNG-ET 809
Cdd:COG5113 202 TNFPC---GFEYKTLLGFIESLSYKKCD---VAARALDYLGIrSRQVVEKSRRSLRLTLSDHSDKLFQIIHSLVRSSkEL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 810 REAALSYMAALVNANMKKAQMQADDRLVSTDGFMLNLLWVLQQLSTKI------KLETVDPTYIFHPRCRITlpnDETRI 883
Cdd:COG5113 276 RANFMKYFAKVINVNHERSKTIFSWRENISDGFMYNMSMVLSRFSRPFldigcsKIDMVDKIYFNNPRVDIK---EETKL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 884 NatmedVNERLTELYGDQPPFSEPKFPTECFFLTLHAHHLSI---LPSCRRYIRRLRAIRELNRTVEDLKNNESQwkdsp 960
Cdd:COG5113 353 N-----VDEKSLDSFYTKPAEGSNNFISDIFFLYLTKIHYGVnatFTSCEKFGEYIRKLKESLEYECRLLDGSFQ----- 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 961 lATRHREMLKRCKTQLKKLVRCKACADAGLLDESFLRRCLNFYGLLIQLMLRILDP--AYP--DVTLPLNSEVPKVFAAL 1036
Cdd:COG5113 423 -ATRLTAQLSRMEAYLKGIDSKMSALNGFLFMTSLFADEFPFTDFMTEYLARVEDPwpTYPfyYKTLPWMENAPMTFKLI 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 1037 PEFYVEDVAEFLFFIVQYSPQVLYEPCTQDIVMFLVVMLCNQNYIRNPYLVAKLVEVMFMTNPSVQPRTQKFF-EMIENH 1115
Cdd:COG5113 502 PEATIENALNYVLESIKDWRSPIFKKELEPLCEFVKIVLHRSSAIKNPMLNRKLDYYLSLGRDEMRMESRSIIhDIFKEG 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 1116 PLSTKLLVPSLMKFYTDVEHTGATSEFYDKFTIRYHISTIFKSLWQNIAHHGTFM-EEFNSGKQFVRYINMLINDTTFLL 1194
Cdd:COG5113 582 KVFSRWLLPALMAFYIEIESTGQSTQFYDKFNIRFIICMMKDFEYKQPSYSEGLSsIKDTNLPFFVKFDAKMLNDLTRLL 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 1195 DESLESLKRIHEVQEEMKNKEQWDQLPRDQQQArQSQLAQDERVSRSYLALATETVDMFHLLTKQVQKPFLRPELGPRLA 1274
Cdd:COG5113 662 DEALKELVEEHNIQSLLADAISNSNISERIGEL-QKSLAFAKRQARNSCLLVDGCFDLFTHILDEIPDAFLVDEIVSRLA 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 1275 AMLNFNLQQLCGPKCRDLKVENPEKYGFEPKKLLDQLTDIYLQL-DCARFAKAIADDQRSYSKELFEEVISKMRKAGIKS 1353
Cdd:COG5113 741 RMLNYNLKILTGPKCTDLKVKDPEQYGFNAKNLLRRMVMVYINLrSESKFVEAVASDKRSFDIDFFRRALRICENKYLIS 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 1354 TIAIEKFKLLAEKVEEIVAKNARAEIDYSDAPDEFRDPLMDTLMTDPVRLP-SGTVMDRSIILRHLLNSPTDPFNRQMLT 1432
Cdd:COG5113 821 ESQIEELRSFINRLEKVRVIEAVEEEDMGDVPDEFLDPLMFTIMKDPVKLPtSRITIDRSTIKAHLLSDGTDPFNRMPLT 900
|
810 820
....*....|....*....|.
gi 1907156787 1433 ESMLEPVPELKEQIQAWMREK 1453
Cdd:COG5113 901 LDDVTPNAELREKINRFYKCK 921
|
|
| RING-Ubox_UBE4B |
cd16658 |
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and ... |
1381-1454 |
2.16e-48 |
|
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and similar proteins; UBE4B, also known as UFD2a, is a U-box-type ubiquitin-protein ligase that functions as an E3 ubiquitin ligase and an E4 polyubiquitin chain elongation factor, which catalyzes formation of Lys27- and Lys33-linked polyubiquitin chains rather than the Lys48-linked chain. It is a mammalian homolog of yeast UFD2 ubiquitination factor and it participates in the proteasomal degradation of misfolded or damaged proteins through association with chaperones. It is located in common neuroblastoma deletion regions and may be subject to mutations in tumors. UBE4B has contradictory functions upon tumorigenesis as an oncogene or tumor suppressor in different types of cancers. It is essential for Hdm2 (also known as Mdm2)-mediated p53 degradation. It mediates p53 polyubiquitination and degradation, as well as inhibits p53-dependent transactivation and apoptosis, and thus plays an important role in regulating phosphorylated p53 following DNA damage. UBE4B is also associated with other pathways independent of the p53 family, such as polyglutamine aggregation and Wallerian degeneration, both of which are critical in neurodegenerative diseases. Moreover, UBE4B acts as a regulator of epidermal growth factor receptor (EGFR) degradation. It is recruited to endosomes in response to EGFR activation by binding to Hrs, a key component of endosomal sorting complex required for transport (ESCRT) 0, and then regulates endosomal sorting, affecting cellular levels of the EGFR and its downstream signaling. UBE4B contains a ubiquitin elongating factor core and a RING-like U-box domain at the C-terminus.
Pssm-ID: 438320 Cd Length: 74 Bit Score: 166.30 E-value: 2.16e-48
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907156787 1381 YSDAPDEFRDPLMDTLMTDPVRLPSGTVMDRSIILRHLLNSPTDPFNRQMLTESMLEPVPELKEQIQAWMREKQ 1454
Cdd:cd16658 1 LGDAPDEFLDPLMDTLMTDPVILPSGTIMDRSIILRHLLNSQTDPFNRQPLTEDMLEPVPELKERIQAWIREKQ 74
|
|
| U-box |
pfam04564 |
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ... |
1384-1454 |
1.19e-32 |
|
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues.
Pssm-ID: 398320 [Multi-domain] Cd Length: 73 Bit Score: 121.26 E-value: 1.19e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907156787 1384 APDEFRDPLMDTLMTDPVRLPSGTVMDRSIILRHLLN-SPTDPFNRQMLTESMLEPVPELKEQIQAWMREKQ 1454
Cdd:pfam04564 1 IPDEFLDPITFELMTDPVILPSGITYDRSTIERHLLSvDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEKR 72
|
|
| Ubox |
smart00504 |
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ... |
1387-1449 |
3.45e-22 |
|
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.
Pssm-ID: 128780 [Multi-domain] Cd Length: 63 Bit Score: 91.14 E-value: 3.45e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907156787 1387 EFRDPLMDTLMTDPVRLPSGTVMDRSIILRHLLNSPTDPFNRQMLTESMLEPVPELKEQIQAW 1449
Cdd:smart00504 1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLLSHGTDPVTGQPLTHEDLIPNLALKSAIQEW 63
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
289-514 |
2.54e-11 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 68.81 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 289 PSHPAPQAAMPSQSLSPHGVAPQA---AVPSQSLSPhGVAPQAAVPSQSLSPHGVAPQVAVPSQSL-STHGVAPQAAVPS 364
Cdd:PHA03247 2554 PLPPAAPPAAPDRSVPPPRPAPRPsepAVTSRARRP-DAPPQSARPRAPVDDRGDPRGPAPPSPLPpDTHAPDPPPPSPS 2632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 365 QSLSTHGVAPQAAVPSQSLSTHGVAPQVAVPSQSLSTHGVAPQAAvpSPPLSPHSTASGNAAGS-----QPSSPRYRPYT 439
Cdd:PHA03247 2633 PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQAS--SPPQRPRRRAARPTVGSltslaDPPPPPPTPEP 2710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 440 VTHPWGSS-PCPTPRSSILASSPGFPShASSPRAVPASSSRQRPRSRVPAFP-------------PAS-PSAASRRPSSL 504
Cdd:PHA03247 2711 APHALVSAtPLPPGPAAARQASPALPA-APAPPAVPAGPATPGGPARPARPPttagppapappaaPAAgPPRRLTRPAVA 2789
|
250
....*....|
gi 1907156787 505 RISPSMSNSP 514
Cdd:PHA03247 2790 SLSESRESLP 2799
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
267-496 |
3.59e-09 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 61.47 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 267 TSPAPS-ASLWSFVPALSPSFALPSHPAPQAA-MPSQSLSPHGVAPQAAVPSQSlsPHGVAPQAAVPSQSlsPHGVAPQV 344
Cdd:pfam05109 464 TGPTVStADVTSPTPAGTTSGASPVTPSPSPRdNGTESKAPDMTSPTSAVTTPT--PNATSPTPAVTTPT--PNATSPTL 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 345 AVPSQSLSTHGVAPQAAVPSQSLSTHgvAPQAAVPSQSLSTHGVAPQVAVPSQSLSTHG-VAPQA--------------A 409
Cdd:pfam05109 540 GKTSPTSAVTTPTPNATSPTPAVTTP--TPNATIPTLGKTSPTSAVTTPTPNATSPTVGeTSPQAnttnhtlggtsstpV 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 410 VPSPP---LSPHSTASGNAAGSQPSSPRYRPYTVT---------------------HPWG-------------------S 446
Cdd:pfam05109 618 VTSPPknaTSAVTTGQHNITSSSTSSMSLRPSSISetlspstsdnstshmplltsaHPTGgenitqvtpaststhhvstS 697
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1907156787 447 SPCPTPRSSILASSPGFPSHASSPRAVPASSSRQRPRSRVPAFPPASPSA 496
Cdd:pfam05109 698 SPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTA 747
|
|
| KLF10_11_N |
cd21974 |
N-terminal domain of Kruppel-like factor (KLF) 10, KLF11, and similar proteins; This subfamily ... |
283-438 |
3.54e-03 |
|
N-terminal domain of Kruppel-like factor (KLF) 10, KLF11, and similar proteins; This subfamily is composed of Kruppel-like factor or Krueppel-like factor (KLF) 10, KLF11, and similar proteins. KLF10 was first identified in human osteoblasts and plays a role in mediating estrogen (E2) signaling in bone and skeletal homeostasis and a regulatory role in tumor formation and metastasis. KLF11 is involved in cell growth, apoptosis, cellular inflammation and differentiation, endometriosis, and cholesterol, prostaglandin, neurotransmitter, fat, and sugar metabolism. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF10/11 belong 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 KLF10, KLF11, and similar proteins.
Pssm-ID: 409243 [Multi-domain] Cd Length: 229 Bit Score: 40.69 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 283 SPSFALPSHPAPQAampsqslSPHGVAPQAAVPSQSLSPHGVAPQAAVPSQSLS-------PHGVAPqVAVPSQSLSthg 355
Cdd:cd21974 63 SPPFFEASHSPSVA-------SLHPPSAASSQPPPEPESSEPPAASPQRAQATSvirhtadPVPVSP-PPVLCQMLP--- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 356 VAPQAAVPSQSLSTHGVAPQAAVPSQSLSTHGVAPQVAVPsqslstHG----VAPQAAVPSPPLS--------------- 416
Cdd:cd21974 132 VSSSSGVIVAFLKAPQQPSPQPQKPALPQPQVVLVGGQVP------QGpvmlVVPQPAVPQPYVQptvvtpggtkllpia 205
|
170 180
....*....|....*....|....
gi 1907156787 417 --PHSTASGNAAGSQPSSPRYRPY 438
Cdd:cd21974 206 paPGFIPSGQSSAPQPDFSRRRNH 229
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
289-475 |
3.94e-03 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 41.66 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 289 PSHPAPQAAMPSQS-LSPHGVAPQAAVPSQSLSPHGVAPQAAVPSQSLSPHGVAPQVAVPSQSLSTHGVAPqAAVPSQSL 367
Cdd:COG3469 11 TAGGASATAVTLLGaAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTAT-ATAAAAAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 368 STHGVAPQAAVPSQSLSTHGVAPQVAVPSQSLSTHGVAPQAAVPSPPLSPHSTASGnAAGSQPSSPRYR------PYTVT 441
Cdd:COG3469 90 TSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAG-STTTTTTVSGTEtatggtTTTST 168
|
170 180 190
....*....|....*....|....*....|....
gi 1907156787 442 HPWGSSPCPTPRSSILASSPGFPSHASSPRAVPA 475
Cdd:COG3469 169 TTTTTSASTTPSATTTATATTASGATTPSATTTA 202
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
266-434 |
8.46e-03 |
|
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: 40.52 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 266 ETSPAPSASlwsfVPALSPSfalPSHPAPQAAMPSQSLSPHgVAPQAAVPSQSLSPHGVAPQAAVPSQSLSPH------- 338
Cdd:NF033839 287 PGNKKPSAP----KPGMQPS---PQPEKKEVKPEPETPKPE-VKPQLEKPKPEVKPQPEKPKPEVKPQLETPKpevkpqp 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 339 -----GVAPQVAVPSQSlsthgVAPQAAVPSQSLSTHGVAPQAAV-PSQSLSTHGVAPQVAVPSQSLS------THGVAP 406
Cdd:NF033839 359 ekpkpEVKPQPEKPKPE-----VKPQPETPKPEVKPQPEKPKPEVkPQPEKPKPEVKPQPEKPKPEVKpqpekpKPEVKP 433
|
170 180
....*....|....*....|....*...
gi 1907156787 407 QAAVPSPPLSPHSTASGNAAGSQPSSPR 434
Cdd:NF033839 434 QPEKPKPEVKPQPEKPKPEVKPQPETPK 461
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Ufd2P_core |
pfam10408 |
Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ... |
747-1367 |
0e+00 |
|
Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ubiquitin elongating factor or E4, running from helix alpha-11 to alpha-38. It consists of 31 helices of variable length connected by loops of variable size forming a compact unit; the helical packing pattern of the compact unit consists of five structural repeats that resemble tandem Armadillo (ARM) repeats. This domain is involved in ubiquitination as it binds Cdc48p and escorts ubiquitinated proteins from Cdc48p to the proteasome for degradation. The core is structurally similar to the nuclear transporter protein importin-alpha. The core is associated with the U-box at the C-terminus, pfam04564, which has ligase activity.
Pssm-ID: 463080 Cd Length: 594 Bit Score: 738.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 747 LGAFFSFSVFAeDDAKVVEKYFSGPAITLENTRVVSQ-SLQHYLELGRQELFKILHSILLNG-ETREAALSYMAALVNAN 824
Cdd:pfam10408 1 LGPFLRLSPLP-DDPEVAKKYFSNPKTRSPADIESSQsSLRQELKTLQEQLFQIVNKLLRASpESRERVLDWFAQIINLN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 825 MKKAQMQADDRLVSTDGFMLNLLWVLQQLS------TKIKLETVDPTYIFHPRCRITLPnDETRINATMEDVNERltelY 898
Cdd:pfam10408 80 HKRRKMQVDPNTVSSDGFMLNLTAVLLRLCepfldaTFSKIDKIDPDYLLPRSSRIDIS-DETRLNADQEEADEF----Y 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 899 GDQPPFSEPKFPTECFFLTLHAHHLSILPSCRRYIRRLRAIRELNRTvedlknnesqwkdsplatrhremlkrcktqlkk 978
Cdd:pfam10408 155 EQKAKEGEPNFITECFFLTLAALHLGILPAISKYKRLARELKRLQAE--------------------------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 979 lvrcKACADAGLLDESFLRRCLNFYGLLIQLMLRILDP--AYPD--VTLPLNSEVPKVFAALPEFYVEDVAEFLFFIVQY 1054
Cdd:pfam10408 202 ----KLAYEAVLLDPSLLQRSLQFLRFVATWLLRVADPkhQYPKkpLKLPLPAEPPEPFKYLPEYFIEDIVDFLLFVTRF 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 1055 SPQVLY-EPCTQDIVMFLVVMLCNQNYIRNPYLVAKLVEVMFMTNPSVQ-PRTQKFFEMIENHPLSTKLLVPSLMKFYTD 1132
Cdd:pfam10408 278 APDILEsLSQLDELITFCIVFLRSPEYIKNPHLKAKLVEVLFYGTPPRQnGRPGVLGDILESHPLALKHLLPALMKFYID 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 1133 VEHTGATSEFYDKFTIRYHISTIFKSLWQNIAHHGTFMEEFNSGKQ-FVRYINMLINDTTFLLDESLESLKRIHEVQEEM 1211
Cdd:pfam10408 358 VEKTGASSQFYDKFNIRYNISQILKYLWKNPSYREQLKKEAKENEDfFVRFVNLLLNDVTFLLDESLSKLKEIHELQEEM 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 1212 KNKEQWDQLPRDQQQARQSQLAQDERVSRSYLALATETVDMFHLLTKQVQKPFLRPELGPRLAAMLNFNLQQLCGPKCRD 1291
Cdd:pfam10408 438 ADAAEWEALPEEERQEREEQLRSLERQAKSYLQLANETVKLLKLFTKEIPEPFLMPEIVDRLAAMLNYNLDQLVGPKCKN 517
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907156787 1292 LKVENPEKYGFEPKKLLDQLTDIYLQLDCA-RFAKAIADDQRSYSKELFEEVISKMRKAGIKSTIAIEKFKLLAEKV 1367
Cdd:pfam10408 518 LKVKNPEKYGFNPKELLSDIVDIYLNLSDQpEFVRAVARDGRSYSPELFEKAARILRRKGLKSPEEIEKFEELAQKV 594
|
|
| UFD2 |
COG5113 |
Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, ... |
652-1453 |
4.10e-131 |
|
Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227444 [Multi-domain] Cd Length: 929 Bit Score: 429.40 E-value: 4.10e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 652 NLPYGFIQELVRTTHQDEEVFKQIFIPILQglALAAKECSLESDYFKYPLMALGELcetkFGKTHPMCNLVASLPLWLPk 731
Cdd:COG5113 129 LLPMIFLSSFKQRQLDEASNLDNLFTSALE--ALTGLHGVLEEDTVLKNVMEIYWG----LVNTKPIADVILKFPIYSG- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 732 SLSPGsgrELQRLSYLGAFFSFSVFAEDdakVVEKYFSGPAI-TLENTRVVSQSLQHYLELGRQELFKILHSILLNG-ET 809
Cdd:COG5113 202 TNFPC---GFEYKTLLGFIESLSYKKCD---VAARALDYLGIrSRQVVEKSRRSLRLTLSDHSDKLFQIIHSLVRSSkEL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 810 REAALSYMAALVNANMKKAQMQADDRLVSTDGFMLNLLWVLQQLSTKI------KLETVDPTYIFHPRCRITlpnDETRI 883
Cdd:COG5113 276 RANFMKYFAKVINVNHERSKTIFSWRENISDGFMYNMSMVLSRFSRPFldigcsKIDMVDKIYFNNPRVDIK---EETKL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 884 NatmedVNERLTELYGDQPPFSEPKFPTECFFLTLHAHHLSI---LPSCRRYIRRLRAIRELNRTVEDLKNNESQwkdsp 960
Cdd:COG5113 353 N-----VDEKSLDSFYTKPAEGSNNFISDIFFLYLTKIHYGVnatFTSCEKFGEYIRKLKESLEYECRLLDGSFQ----- 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 961 lATRHREMLKRCKTQLKKLVRCKACADAGLLDESFLRRCLNFYGLLIQLMLRILDP--AYP--DVTLPLNSEVPKVFAAL 1036
Cdd:COG5113 423 -ATRLTAQLSRMEAYLKGIDSKMSALNGFLFMTSLFADEFPFTDFMTEYLARVEDPwpTYPfyYKTLPWMENAPMTFKLI 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 1037 PEFYVEDVAEFLFFIVQYSPQVLYEPCTQDIVMFLVVMLCNQNYIRNPYLVAKLVEVMFMTNPSVQPRTQKFF-EMIENH 1115
Cdd:COG5113 502 PEATIENALNYVLESIKDWRSPIFKKELEPLCEFVKIVLHRSSAIKNPMLNRKLDYYLSLGRDEMRMESRSIIhDIFKEG 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 1116 PLSTKLLVPSLMKFYTDVEHTGATSEFYDKFTIRYHISTIFKSLWQNIAHHGTFM-EEFNSGKQFVRYINMLINDTTFLL 1194
Cdd:COG5113 582 KVFSRWLLPALMAFYIEIESTGQSTQFYDKFNIRFIICMMKDFEYKQPSYSEGLSsIKDTNLPFFVKFDAKMLNDLTRLL 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 1195 DESLESLKRIHEVQEEMKNKEQWDQLPRDQQQArQSQLAQDERVSRSYLALATETVDMFHLLTKQVQKPFLRPELGPRLA 1274
Cdd:COG5113 662 DEALKELVEEHNIQSLLADAISNSNISERIGEL-QKSLAFAKRQARNSCLLVDGCFDLFTHILDEIPDAFLVDEIVSRLA 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 1275 AMLNFNLQQLCGPKCRDLKVENPEKYGFEPKKLLDQLTDIYLQL-DCARFAKAIADDQRSYSKELFEEVISKMRKAGIKS 1353
Cdd:COG5113 741 RMLNYNLKILTGPKCTDLKVKDPEQYGFNAKNLLRRMVMVYINLrSESKFVEAVASDKRSFDIDFFRRALRICENKYLIS 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 1354 TIAIEKFKLLAEKVEEIVAKNARAEIDYSDAPDEFRDPLMDTLMTDPVRLP-SGTVMDRSIILRHLLNSPTDPFNRQMLT 1432
Cdd:COG5113 821 ESQIEELRSFINRLEKVRVIEAVEEEDMGDVPDEFLDPLMFTIMKDPVKLPtSRITIDRSTIKAHLLSDGTDPFNRMPLT 900
|
810 820
....*....|....*....|.
gi 1907156787 1433 ESMLEPVPELKEQIQAWMREK 1453
Cdd:COG5113 901 LDDVTPNAELREKINRFYKCK 921
|
|
| RING-Ubox_UBE4B |
cd16658 |
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and ... |
1381-1454 |
2.16e-48 |
|
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and similar proteins; UBE4B, also known as UFD2a, is a U-box-type ubiquitin-protein ligase that functions as an E3 ubiquitin ligase and an E4 polyubiquitin chain elongation factor, which catalyzes formation of Lys27- and Lys33-linked polyubiquitin chains rather than the Lys48-linked chain. It is a mammalian homolog of yeast UFD2 ubiquitination factor and it participates in the proteasomal degradation of misfolded or damaged proteins through association with chaperones. It is located in common neuroblastoma deletion regions and may be subject to mutations in tumors. UBE4B has contradictory functions upon tumorigenesis as an oncogene or tumor suppressor in different types of cancers. It is essential for Hdm2 (also known as Mdm2)-mediated p53 degradation. It mediates p53 polyubiquitination and degradation, as well as inhibits p53-dependent transactivation and apoptosis, and thus plays an important role in regulating phosphorylated p53 following DNA damage. UBE4B is also associated with other pathways independent of the p53 family, such as polyglutamine aggregation and Wallerian degeneration, both of which are critical in neurodegenerative diseases. Moreover, UBE4B acts as a regulator of epidermal growth factor receptor (EGFR) degradation. It is recruited to endosomes in response to EGFR activation by binding to Hrs, a key component of endosomal sorting complex required for transport (ESCRT) 0, and then regulates endosomal sorting, affecting cellular levels of the EGFR and its downstream signaling. UBE4B contains a ubiquitin elongating factor core and a RING-like U-box domain at the C-terminus.
Pssm-ID: 438320 Cd Length: 74 Bit Score: 166.30 E-value: 2.16e-48
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907156787 1381 YSDAPDEFRDPLMDTLMTDPVRLPSGTVMDRSIILRHLLNSPTDPFNRQMLTESMLEPVPELKEQIQAWMREKQ 1454
Cdd:cd16658 1 LGDAPDEFLDPLMDTLMTDPVILPSGTIMDRSIILRHLLNSQTDPFNRQPLTEDMLEPVPELKERIQAWIREKQ 74
|
|
| U-box |
pfam04564 |
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ... |
1384-1454 |
1.19e-32 |
|
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues.
Pssm-ID: 398320 [Multi-domain] Cd Length: 73 Bit Score: 121.26 E-value: 1.19e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907156787 1384 APDEFRDPLMDTLMTDPVRLPSGTVMDRSIILRHLLN-SPTDPFNRQMLTESMLEPVPELKEQIQAWMREKQ 1454
Cdd:pfam04564 1 IPDEFLDPITFELMTDPVILPSGITYDRSTIERHLLSvDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEKR 72
|
|
| RING-Ubox_UBE4A |
cd16657 |
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 A (UBE4A) and ... |
1386-1454 |
2.46e-28 |
|
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 A (UBE4A) and similar proteins; This subfamily includes yeast ubiquitin fusion degradation protein 2 (UFD2p) and its mammalian homolog, UBE4A. Yeast UFD2p, also known as ubiquitin conjugation factor E4 or UB fusion protein 2, is a polyubiquitin chain conjugation factor (E4) in the ubiquitin fusion degradation (UFD) pathway which catalyzes elongation of the ubiquitin chain through Lys48 linkage. It binds to substrates conjugated with one to three ubiquitin molecules and catalyzes the addition of further ubiquitin moieties in the presence of ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2) and ubiquitin ligase (E3), yielding multiubiquitylated substrates that are targets for the 26S proteasome. UFD2p is implicated in cell survival under stress conditions and is essential for homoeostasis of unsaturated fatty acids. It interacts with UBL-UBA proteins Rad23 and Dsk2, which are involved in the endoplasmic reticulum-associated degradation, ubiquitin fusion degradation, and OLE-1 gene induction pathways. UBE4A is a U-box-type ubiquitin-protein ligase that is located in common neuroblastoma deletion regions and may be subject to mutations in tumors. It may have a specific role in different biochemical processes other than ubiquitination, including growth or differentiation. Members of this family contain an N-terminal ubiquitin elongating factor core and a RING-like U-box domain at the C-terminus.
Pssm-ID: 438319 Cd Length: 70 Bit Score: 108.90 E-value: 2.46e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 1386 DEFRDPLMDTLMTDPVRLP-SGTVMDRSIILRHLLNSPTDPFNRQMLTESMLEPVPELKEQIQAWMREKQ 1454
Cdd:cd16657 1 DEFLDPIMYTLMKDPVILPsSKVTVDRSTIKRHLLSDQTDPFNRSPLTLDMVIPNEELKQKIEEFLAEKK 70
|
|
| Ubox |
smart00504 |
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ... |
1387-1449 |
3.45e-22 |
|
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.
Pssm-ID: 128780 [Multi-domain] Cd Length: 63 Bit Score: 91.14 E-value: 3.45e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907156787 1387 EFRDPLMDTLMTDPVRLPSGTVMDRSIILRHLLNSPTDPFNRQMLTESMLEPVPELKEQIQAW 1449
Cdd:smart00504 1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLLSHGTDPVTGQPLTHEDLIPNLALKSAIQEW 63
|
|
| RING-Ubox |
cd16453 |
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ... |
1388-1431 |
3.07e-15 |
|
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that also includes the HECT family and the RING finger family. The E3 enzyme is ubiquitin-protein ligase that cooperates with a ubiquitin-activating enzyme (E1) and a ubiquitin-conjugating enzyme (E2), and plays a central role in determining the specificity of the ubiquitination system. It removes the ubiquitin molecule from the E2 enzyme and attaches it to the target substrate, forming a covalent bond between ubiquitin and the target. U-box proteins are characterized by the presence of a U-box domain of approximately 70 amino acids. The U-box is a modified form of the RING finger domain that lacks metal chelating cysteines and histidines. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms.
Pssm-ID: 438117 [Multi-domain] Cd Length: 44 Bit Score: 70.66 E-value: 3.07e-15
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1907156787 1388 FRDPLMDTLMTDPVRLPSGTVMDRSIILRHLLNSPTDPFNRQML 1431
Cdd:cd16453 1 FLCPISGELMKDPVITPSGITYDRSAIERWLLSDNTDPFTREPL 44
|
|
| RING-Ubox_CHIP |
cd16654 |
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ... |
1384-1452 |
7.37e-12 |
|
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein (CHIP) and similar proteins; CHIP, also known as STIP1 homology and U box-containing protein 1 (STUB1), CLL-associated antigen KW-8, or Antigen NY-CO-7, is a multifunctional protein that functions both as a co-chaperone and an E3 ubiquitin-protein ligase. It couples protein folding and proteasome mediated degradation by interacting with heat shock proteins (e.g. HSC70) and ubiquitinating their misfolded client proteins, thereby targeting them for proteasomal degradation. It is also important for cellular differentiation and survival (or apoptosis), as well as susceptibility to stress. It targets a wide range of proteins, such as expanded ataxin-1, ataxin-3, huntingtin, and androgen receptor, which play roles in glucocorticoid response, tau degradation, and both p53 and cAMP signaling. CHIP contains an N-terminal tetratricopeptide repeat (TPR) domain responsible for protein-protein interaction, a highly charged middle coiled-coil (CC), and a C-terminal RING-like U-box domain acting as an ubiquitin ligase.
Pssm-ID: 438316 [Multi-domain] Cd Length: 71 Bit Score: 62.21 E-value: 7.37e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 1384 APDEFRDPLMDTLMTDPVRLPSGTVMDRSIILRHLL-NSPTDPFNRQMLTESMLEPVPELKEQIQAWMRE 1452
Cdd:cd16654 1 VPDYLCCKISFELMRDPVITPSGITYERKDIEEHLQrVGHFDPITREPLTQDQLIPNLALKEAIEAFLEE 70
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
289-514 |
2.54e-11 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 68.81 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 289 PSHPAPQAAMPSQSLSPHGVAPQA---AVPSQSLSPhGVAPQAAVPSQSLSPHGVAPQVAVPSQSL-STHGVAPQAAVPS 364
Cdd:PHA03247 2554 PLPPAAPPAAPDRSVPPPRPAPRPsepAVTSRARRP-DAPPQSARPRAPVDDRGDPRGPAPPSPLPpDTHAPDPPPPSPS 2632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 365 QSLSTHGVAPQAAVPSQSLSTHGVAPQVAVPSQSLSTHGVAPQAAvpSPPLSPHSTASGNAAGS-----QPSSPRYRPYT 439
Cdd:PHA03247 2633 PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQAS--SPPQRPRRRAARPTVGSltslaDPPPPPPTPEP 2710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 440 VTHPWGSS-PCPTPRSSILASSPGFPShASSPRAVPASSSRQRPRSRVPAFP-------------PAS-PSAASRRPSSL 504
Cdd:PHA03247 2711 APHALVSAtPLPPGPAAARQASPALPA-APAPPAVPAGPATPGGPARPARPPttagppapappaaPAAgPPRRLTRPAVA 2789
|
250
....*....|
gi 1907156787 505 RISPSMSNSP 514
Cdd:PHA03247 2790 SLSESRESLP 2799
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
268-517 |
1.80e-10 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 65.96 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 268 SPAPSAslwsfVPALSPSF--ALPSHPAPQAAMP------SQSLSPHGVAPQAAVPSQSLSPH---GVAPQAAVPSQSlS 336
Cdd:PHA03307 125 SPPPSP-----APDLSEMLrpVGSPGPPPAASPPaagaspAAVASDAASSRQAALPLSSPEETaraPSSPPAEPPPST-P 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 337 PHGVAPQVAVPSQSLSTHGVAPQA---------AVPSQSLSTHGVAPQAAVPSQSLSTHGVAPQVAVPSQSLSTHGVAPQ 407
Cdd:PHA03307 199 PAAASPRPPRRSSPISASASSPAPapgrsaaddAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGP 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 408 AAVPSPPlSPHSTASGNAAGSQPSSPRYRPYTVTHP----WGSSP----------CPTPRSSILASSPGFPSHASSPRAV 473
Cdd:PHA03307 279 SSRPGPA-SSSSSPRERSPSPSPSSPGSGPAPSSPRasssSSSSRessssstsssSESSRGAAVSPGPSPSRSPSPSRPP 357
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1907156787 474 PASSSRQRPRSRVPAFPPASPSAASRRPSSLRISPS------MSNSPFSF 517
Cdd:PHA03307 358 PPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAvagrarRRDATGRF 407
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
296-508 |
1.18e-09 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 62.97 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 296 AAMPSQSLSPHGVAPQAAVPSQSLSPHGVAPQAAVPSQSLSPhgvAPQVAVPSQSLSTHGVAPQAAVPSQSLSTHGVAPQ 375
Cdd:PRK12323 362 AFRPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPP---AAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQ 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 376 AAVPSQSLSTHGVAPQVAVPsqslsthgVAPQAAVPSPPLSPHSTASGNAAGSQPSSPRYRPYTVTHPWGSSPCPTPRSS 455
Cdd:PRK12323 439 ASARGPGGAPAPAPAPAAAP--------AAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPA 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907156787 456 ILASSPGFPSHASSPRAVPASSSRQRPRSRVPAFPPASPSAASRRPSSLRISP 508
Cdd:PRK12323 511 PAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAP 563
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
272-514 |
3.20e-09 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 61.73 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 272 SASLWSFVPALSpsFALPSHPAPQAAMPSqSLSPHGVAPQAAVPSQSLSPHGVAPQAAVPSQSLSPHGVAPQV-AVPSQS 350
Cdd:PHA03307 86 STPTWSLSTLAP--ASPAREGSPTPPGPS-SPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAgASPAAV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 351 LSTHGVAPQAAVPSQSLSTH---GVAPQAAVPSQSLSTHGvAPQVAVPSQSLSthgvapQAAVPSPPLSPHSTASGNAAG 427
Cdd:PHA03307 163 ASDAASSRQAALPLSSPEETaraPSSPPAEPPPSTPPAAA-SPRPPRRSSPIS------ASASSPAPAPGRSAADDAGAS 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 428 SQPSSPRYRPYTVTHPWGSSPCPTPRSSILASSP--GFPSHASSPRAVPASSSRQRPRSRVPAFPPASPSAASrrPSSLR 505
Cdd:PHA03307 236 SSDSSSSESSGCGWGPENECPLPRPAPITLPTRIweASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPA--PSSPR 313
|
....*....
gi 1907156787 506 ISPSMSNSP 514
Cdd:PHA03307 314 ASSSSSSSR 322
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
267-496 |
3.59e-09 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 61.47 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 267 TSPAPS-ASLWSFVPALSPSFALPSHPAPQAA-MPSQSLSPHGVAPQAAVPSQSlsPHGVAPQAAVPSQSlsPHGVAPQV 344
Cdd:pfam05109 464 TGPTVStADVTSPTPAGTTSGASPVTPSPSPRdNGTESKAPDMTSPTSAVTTPT--PNATSPTPAVTTPT--PNATSPTL 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 345 AVPSQSLSTHGVAPQAAVPSQSLSTHgvAPQAAVPSQSLSTHGVAPQVAVPSQSLSTHG-VAPQA--------------A 409
Cdd:pfam05109 540 GKTSPTSAVTTPTPNATSPTPAVTTP--TPNATIPTLGKTSPTSAVTTPTPNATSPTVGeTSPQAnttnhtlggtsstpV 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 410 VPSPP---LSPHSTASGNAAGSQPSSPRYRPYTVT---------------------HPWG-------------------S 446
Cdd:pfam05109 618 VTSPPknaTSAVTTGQHNITSSSTSSMSLRPSSISetlspstsdnstshmplltsaHPTGgenitqvtpaststhhvstS 697
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1907156787 447 SPCPTPRSSILASSPGFPSHASSPRAVPASSSRQRPRSRVPAFPPASPSA 496
Cdd:pfam05109 698 SPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTA 747
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
266-502 |
3.64e-09 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 61.43 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 266 ETSPAPSAS--LWSFVPALSPSFALPSHPAPQAAMPSQSLSPHGVAPQAAVPSQSLSPHGVAPQAAVPSQSLSPHGVAPQ 343
Cdd:PRK12323 371 GAGPATAAAapVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAP 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 344 VAVPsqslsthgvapqAAVPsqslsthgvAPQAAVPSQSLSThgvAPQVAVPSQSLSTHGVAPQAAVPSPPLSPHSTASG 423
Cdd:PRK12323 451 APAP------------AAAP---------AAAARPAAAGPRP---VAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEF 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907156787 424 NAAGSQPSSPRYRPYTVThpwgsspcPTPRSSILASSPGFPSHASSPRAVPASSSRQRPRSRVPAFPPAspSAASRRPS 502
Cdd:PRK12323 507 ASPAPAQPDAAPAGWVAE--------SIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPR--ASASGLPD 575
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
269-516 |
4.31e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 61.49 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 269 PAPSASlwsfVPALSPSFALPSHPaPQAAMPSQSLSPHGVAPQAAVPSQSL-SPHGVAPQAAVPSQSLSPHGVAPQVAVP 347
Cdd:PHA03247 2573 PAPRPS----EPAVTSRARRPDAP-PQSARPRAPVDDRGDPRGPAPPSPLPpDTHAPDPPPPSPSPAANEPDPHPPPTVP 2647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 348 SQSLSTHGVAPQAAVPSQSLSTHGVAPQAAVPSQSLSTHGVAPQV------AVPSQSLSTHGVAPQAAVPSPPLSPHSTA 421
Cdd:PHA03247 2648 PPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVgsltslADPPPPPPTPEPAPHALVSATPLPPGPAA 2727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 422 SGNAAGSQPSSP--RYRPYTVTHPWGSSPCPTPRSSilaSSPGFPSHASSPRAVPASSSRQrprsrvpafPPASPSAASR 499
Cdd:PHA03247 2728 ARQASPALPAAPapPAVPAGPATPGGPARPARPPTT---AGPPAPAPPAAPAAGPPRRLTR---------PAVASLSESR 2795
|
250
....*....|....*..
gi 1907156787 500 RPSSLRISPSMSNSPFS 516
Cdd:PHA03247 2796 ESLPSPWDPADPPAAVL 2812
|
|
| RING-Ubox_RNF37 |
cd16660 |
U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37); RNF37, also ... |
1385-1426 |
4.92e-09 |
|
U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37); RNF37, also known as KIAA0860, U-box domain-containing protein 5 (UBOX5), UbcM4-interacting protein 5 (UIP5), or ubiquitin-conjugating enzyme 7-interacting protein 5, is an E3 ubiquitin-protein ligase found exclusively in the nucleus as part of a nuclear dot-like structure. It interacts with the molecular chaperone VCP/p97 protein. RNF37 contains a U-box domain followed by a potential nuclear location signal (NLS), and a C-terminal C3HC4-type RING-HC finger. The U-box domain is a modified RING finger domain that lacks the hallmark metal-chelating cysteines and histidines of the latter, but is likely to adopt a RING finger-like conformation. The presence of the U-box, but not of the RING finger, is required for the E3 activity. The U-box domain can directly interact with several E2 enzymes, including UbcM2, UbcM3, UbcM4, UbcH5, and UbcH8, suggesting a similar function as the RING finger in the ubiquitination pathway. This model corresponds to the U-box domain.
Pssm-ID: 438322 Cd Length: 53 Bit Score: 53.47 E-value: 4.92e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1907156787 1385 PDEFRDPLMDTLMTDPVRLPSGTVMDRSIILRHLLNS------PTDPF 1426
Cdd:cd16660 1 PEEFLDPITCELMTLPVLLPSGKVVDQSTLEKYIKEEatwgrlPSDPF 48
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
268-515 |
5.68e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 61.11 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 268 SPAPSASLWSFVPALSPSFALPSHPAPQ-AAMPSQSLSPHGVAPQAAVPSQSLSPHGVAPQAAVPSQSLSPHGVAPQVAv 346
Cdd:PHA03247 2615 SPLPPDTHAPDPPPPSPSPAANEPDPHPpPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVG- 2693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 347 psqSLSTHGVAPQAAVPSQSlsthgvAPQAAVPSQSLSTHGVAPQVAVPSqslsthgvAPQAAVPSPPLSPHSTASGNAA 426
Cdd:PHA03247 2694 ---SLTSLADPPPPPPTPEP------APHALVSATPLPPGPAAARQASPA--------LPAAPAPPAVPAGPATPGGPAR 2756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 427 GSQPSSPRyRPYTVTHPWGSSPCPTPRSSILASSPGFPSHASSPRAVPASSSRQRPRSRVPAFPPASPSAASRRP--SSL 504
Cdd:PHA03247 2757 PARPPTTA-GPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPptSAQ 2835
|
250
....*....|.
gi 1907156787 505 RISPSMSNSPF 515
Cdd:PHA03247 2836 PTAPPPPPGPP 2846
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
323-509 |
8.17e-09 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 60.25 E-value: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 323 GVAPQAAVPSQSlsPHGVAPQVAVPSQSLSTHGVAPQAAVPSQSLSThgVAPQAAVPSQSlsTHGVAPQVAV-PSQS--L 399
Cdd:PRK07003 365 GGAPGGGVPARV--AGAVPAPGARAAAAVGASAVPAVTAVTGAAGAA--LAPKAAAAAAA--TRAEAPPAAPaPPATadR 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 400 STHGVAPQAAVPSPPLSPHSTASgnAAGSQPSSPRYRPYTVTHPWGSSPCPTPRSSilASSPGFPSHASSPRAVPASSSR 479
Cdd:PRK07003 439 GDDAADGDAPVPAKANARASADS--RCDERDAQPPADSGSASAPASDAPPDAAFEP--APRAAAPSAATPAAVPDARAPA 514
|
170 180 190
....*....|....*....|....*....|
gi 1907156787 480 QRPRSRVPAfPPASPSAASRRPSSLRISPS 509
Cdd:PRK07003 515 AASREDAPA-AAAPPAPEARPPTPAAAAPA 543
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
269-502 |
1.86e-08 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 59.09 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 269 PAPSASLWSFVPALSPSFALPSHPAPQAAMPSQSLS----PHGVAPQAA-----------VPSQSLSPHGVAPQAAVPSQ 333
Cdd:PRK07003 387 AAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRaeapPAAPAPPATadrgddaadgdAPVPAKANARASADSRCDER 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 334 SLSPHGVAPQVAVPSQSlsthgvAPQAAVPSQSLSTHGVAPQAAVPSQSLSTHGVAPQVAVPSQSLSthgVAPQAAVPSP 413
Cdd:PRK07003 467 DAQPPADSGSASAPASD------APPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAP---PAPEARPPTP 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 414 PL-SPHSTASGNA--------AGSQPSSPRYR-----PYTVTHPWGSSPCPTPRSSILASSPGFPSHASSPRAVPASssr 479
Cdd:PRK07003 538 AAaAPAARAGGAAaaldvlrnAGMRVSSDRGAraaaaAKPAAAPAAAPKPAAPRVAVQVPTPRARAATGDAPPNGAA--- 614
|
250 260
....*....|....*....|...
gi 1907156787 480 qrprsrvpafpPASPSAASRRPS 502
Cdd:PRK07003 615 -----------RAEQAAESRGAP 626
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
269-517 |
2.88e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.80 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 269 PAPSASLWSFvpALSPSFALPSHPAPQAAMPSQSLSPHGVAPQAAVPSQSLSPhgVAPqaAVPSQSLSPHGVAPQVAVPS 348
Cdd:PHA03247 2689 RPTVGSLTSL--ADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAP--APP--AVPAGPATPGGPARPARPPT 2762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 349 QSLSTHGVAPQ--AAVPSQSLSTHGVAPQA-AVPSQSLSTHGVAPQVAVPSQSLSThgvaPQAAVPSPPLSPHSTAsgna 425
Cdd:PHA03247 2763 TAGPPAPAPPAapAAGPPRRLTRPAVASLSeSRESLPSPWDPADPPAAVLAPAAAL----PPAASPAGPLPPPTSA---- 2834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 426 agsQPSSPryrpytvthPWGSSPCPTPRSSILASSPGFP-SHASSPRAVPAsssrqrprsrvpafPPASPsaasRRPSSL 504
Cdd:PHA03247 2835 ---QPTAP---------PPPPGPPPPSLPLGGSVAPGGDvRRRPPSRSPAA--------------KPAAP----ARPPVR 2884
|
250
....*....|....
gi 1907156787 505 RIS-PSMSNSPFSF 517
Cdd:PHA03247 2885 RLArPAVSRSTESF 2898
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
266-503 |
3.23e-08 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 58.46 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 266 ETSPAPSASLWSFVPALSPSFALPSHPAPQAAM-PSQSLSPHGVAPQAAVPSQSLSPHGVAPQAAVPSQSLSPHGvaPQV 344
Cdd:PRK07764 442 PSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPePTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERW--PEI 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 345 --AVPSQSLSTHG-VAPQAAVPS---QSLS-THGVAPQAA---------VPSQSL-----STHGVAPQVAVPSQSLSTHG 403
Cdd:PRK07764 520 laAVPKRSRKTWAiLLPEATVLGvrgDTLVlGFSTGGLARrfaspgnaeVLVTALaeelgGDWQVEAVVGPAPGAAGGEG 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 404 VAPQAAVPSPPLSPHSTASGNAAGSQPSSPRYRPYTVTHPWGSSPCPTPRSSILASSPGFPSHASSPRAVPASSSRQRPR 483
Cdd:PRK07764 600 PPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPA 679
|
250 260
....*....|....*....|
gi 1907156787 484 SRVPAFPPASPSAASRRPSS 503
Cdd:PRK07764 680 APPPAPAPAAPAAPAGAAPA 699
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
266-471 |
3.84e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.41 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 266 ETSPAPSASLWSFVPALSPSFALPSH-------PAPQAAMPSQSLSPHGVAPQAAVPSQSLSPHG-----VAPQAAVPSQ 333
Cdd:PHA03247 2796 ESLPSPWDPADPPAAVLAPAAALPPAaspagplPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGdvrrrPPSRSPAAKP 2875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 334 SLSPHGVAPQVAVPSQSLSTHGVaPQAAVPSQSLSThgvaPQAAVPSQSLSTHGVAPQVAVPsqslsthgvAPQAAVPSP 413
Cdd:PHA03247 2876 AAPARPPVRRLARPAVSRSTESF-ALPPDQPERPPQ----PQAPPPPQPQPQPPPPPQPQPP---------PPPPPRPQP 2941
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907156787 414 PLSPHSTASGnAAGSQPSSPRYR-----PYTVTHPWGSSPCPTPRSSILASSPGFPSHASSPR 471
Cdd:PHA03247 2942 PLAPTTDPAG-AGEPSGAVPQPWlgalvPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSR 3003
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
266-514 |
5.75e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.03 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 266 ETSPAPSASLWSFVPALSPSFALPSHPAPQA-----AMPSQSLSPHGVAPQAAVPSQSLSPHGVAPqaAVPSQSLSPHGV 340
Cdd:PHA03247 2707 TPEPAPHALVSATPLPPGPAAARQASPALPAapappAVPAGPATPGGPARPARPPTTAGPPAPAPP--AAPAAGPPRRLT 2784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 341 APQVAVPSQSLSTHGVAPQAAVPSQSLSthgvAPQAAVPSQSLSTHGVAPqvavPSQSLSThgvAPqaAVPSPPLSPHST 420
Cdd:PHA03247 2785 RPAVASLSESRESLPSPWDPADPPAAVL----APAAALPPAASPAGPLPP----PTSAQPT---AP--PPPPGPPPPSLP 2851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 421 ASGNAAgsqPSSP-RYRPYTVTHPWGSSPCPTPRSSILASSPGFPSHASSPRAVPASSSRQRPRSRVPAFPPASPSAASR 499
Cdd:PHA03247 2852 LGGSVA---PGGDvRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ 2928
|
250
....*....|....*
gi 1907156787 500 RPSSLRiSPSMSNSP 514
Cdd:PHA03247 2929 PQPPPP-PPPRPQPP 2942
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
266-454 |
1.35e-07 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 56.53 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 266 ETSPAPSASLWSFV---PALSPSFALPSHPAPQAAMPSQSLSPHGVAPQAAVPSQSLSPHGVAPQAAVPSQSLSPHGVAP 342
Cdd:PRK07764 598 EGPPAPASSGPPEEaarPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAA 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 343 QVAVPSQSLSTHGVAPQAAVPSQSLSThgvAPQAAVPSQSLSTHGVAPQVAVPSQSLSThgvAPQAAVPSPPLSPHSTAS 422
Cdd:PRK07764 678 PAAPPPAPAPAAPAAPAGAAPAQPAPA---PAATPPAGQADDPAAQPPQAAQGASAPSP---AADDPVPLPPEPDDPPDP 751
|
170 180 190
....*....|....*....|....*....|..
gi 1907156787 423 GNAAGSQPSSPRYRPYTvthPWGSSPCPTPRS 454
Cdd:PRK07764 752 AGAPAQPPPPPAPAPAA---APAAAPPPSPPS 780
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
269-470 |
1.75e-07 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 56.15 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 269 PAPSASLWSFVPALSPSFALPSHPAPQAampsqslSPHGVAPQAAVPSQSlSPHGVAPQAAVPSQSLSPHGVAPQVAVPS 348
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAA-------PAAPAAPAAPAPAGA-AAAPAEASAAPAPGVAAPEHHPKHVAVPD 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 349 QSLSTHGVAPQAAVPSQSLSTHGVAPQAAVPSQslsthGVAPQVAVPSQSLSTHGVAPQAAVPSPPLSPHSTASGNAAGS 428
Cdd:PRK07764 662 ASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPA-----GAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAAD 736
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907156787 429 Q----PSSPRYRPYTVTHPWGSSPCPTPRSSILASSPGFPSHASSP 470
Cdd:PRK07764 737 DpvplPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
|
|
| RING-Ubox_LubX-like_rpt1 |
cd23149 |
first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX ... |
1391-1442 |
2.68e-07 |
|
first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX and similar proteins; LubX, also called RING-type E3 ubiquitin transferase LubX, is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. LubX acts as an E3 ubiquitin-protein ligase (EC 2.3.2.27) that interferes with the host's ubiquitination pathway. LubX contains two RING-like U-box domains. U-box 1 is critical to the ubiquitin ligase activity, and U-box 2 mediates interaction with host target. This model corresponds to the first one.
Pssm-ID: 438511 [Multi-domain] Cd Length: 55 Bit Score: 48.63 E-value: 2.68e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907156787 1391 PLMDTLMTDPVRLPSGTVMDRSIILRHLLNSPTDPFNRQMLTESMLEPVPEL 1442
Cdd:cd23149 4 PITSGFMEDPVITPSGFSYERSAIERWLETKPEDPQTREPLTAKDLQPNREL 55
|
|
| GGN |
pfam15685 |
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ... |
294-514 |
4.44e-07 |
|
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the maturation of sperm and is expressed virtually only in the testis. It is found to be associated with the intracellular membrane, binds with GGNBP1 and may be involved in vesicular trafficking.
Pssm-ID: 434857 [Multi-domain] Cd Length: 668 Bit Score: 54.39 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 294 PQAA---MPSQSLSPHGVAPQAAVPSQSLSPhgVAPQAA---VPSQSLSPHGVAPQVAVPSQSLSTHGVAPQAAVPSQSL 367
Cdd:pfam15685 225 PQAGegeMARFAASESGLSLLCKVTFKSAAP--LCPAAAsgpLAAKASLGGGGGGGLFAASGAISCAEVLKQGPLAPGAA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 368 STHGVAPQAAVPSQSLSTHG-------VAPQV---AVPSQSLSTH-GVAPQAAVPSPPLSPHSTASGNAAGSQPSSPRYR 436
Cdd:pfam15685 303 RPLGEVPRAALETEGGEGDGegcsggpAAPASharALPPPAYTTFpGSKPKFDWVSPPDGPERHFRFNGAGGGIGAPRRR 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 437 PYTVTHPWGSS--------PCPTPR--SSILASSPGFPSHASS-----------PRAVPASSSRQRPRSRVPAFPPASPS 495
Cdd:pfam15685 383 AAALSGPWGSPppppgkahPIPGPRrpAPALLAPPMFIFPAPTngepvrpgppaPQALLPRPPPPTPPATPPPVPPPIPQ 462
|
250
....*....|....*....
gi 1907156787 496 AASRRPSSLRISPSMSNSP 514
Cdd:pfam15685 463 LPALQPMPLAAARPPTPRP 481
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
210-514 |
5.77e-07 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 54.41 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 210 RDENPFASLTATSQPiATAARSPDRNLMLNTGSSSGTSPmfcnmgsfstsslsslyeTSPAPSASLWSFVPALSPSFALP 289
Cdd:PHA03307 149 AASPPAAGASPAAVA-SDAASSRQAALPLSSPEETARAP------------------SSPPAEPPPSTPPAAASPRPPRR 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 290 SHPAPQAAMPSQSLSPHGVApQAAVPSQSLSPHGVAPQAAVPSQSLSPHGVAPQVAVPSQSLSTHGVAPQAAVPSQSLST 369
Cdd:PHA03307 210 SSPISASASSPAPAPGRSAA-DDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSS 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 370 HGVAPQAAVPSQSLSTHGVAPqvavPSQSLSTHGVAPQAAVPSPPLSPHSTASGnaAGSQPSSPRYRPYTVTHPWGSSPC 449
Cdd:PHA03307 289 SSPRERSPSPSPSSPGSGPAP----SSPRASSSSSSSRESSSSSTSSSSESSRG--AAVSPGPSPSRSPSPSRPPPPADP 362
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907156787 450 PTPRSSILASSPGFPSHASSPRAVPASSSRQRPRSRVPAFPPaSPSAASRRPSSLRISPSMSNSP 514
Cdd:PHA03307 363 SSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDAT-GRFPAGRPRPSPLDAGAASGAF 426
|
|
| PLN03131 |
PLN03131 |
hypothetical protein; Provisional |
267-518 |
6.46e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 178677 [Multi-domain] Cd Length: 705 Bit Score: 54.01 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 267 TSPAPSASLWSfVPALSPSFALPSHPAPQAAMPSQSLSPHGVAPQAAVPS-QSLSPH-------------GVAPQAAVP- 331
Cdd:PLN03131 370 TSPAPPVDLFE-IPPLDPAPAINAYQPPQTSLPSSIDLFGGITQQQSINSlDEKSPElsipknegwatfdGIQPIASTPg 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 332 SQSLSPHGVAPQVA-------VPSQSLSTHGVAPQAAVPSQSLS--------THGVAPQAAVPSQSLSTHGVAPQVAvps 396
Cdd:PLN03131 449 NENLTPFSIGPSMAgsanfdqVPSLDKGMQWPPFQNSSDEESASgpapwlgdLHNVEAPDNTSAQNWNAFEFDDSVA--- 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 397 qSLSTHGVApQAAVPSPPLSPHSTA--SGNAAGSQPSSPRYRPYTVTHPWGSSPCPTPRSSILASSPGFPShaSSPRAVP 474
Cdd:PLN03131 526 -GIPLEGIK-QSSEPQTAANMPPTAdqLIGCKALEDFNKDGIKRTAPHGQGELPGLDEPSDILAEPSYTPP--AHPIMEH 601
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1907156787 475 ASSSRQRPRSRVPAFPP----ASPSAASRRPSSLRISPSMSNSPFSFL 518
Cdd:PLN03131 602 AQSHANDHKSINPFDLPydsdLEPGNMFLDMSSLEAALPDAHLPSAFL 649
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
220-514 |
6.82e-07 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 53.81 E-value: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 220 ATSQPIATAARSPDRNLMLNTGSSSGTSPMfcnmgsfstsslsslyETSPAPSASLWSFVPALSPSFALPSHPAPQAAMP 299
Cdd:pfam17823 110 AASRALAAAASSSPSSAAQSLPAAIAALPS----------------EAFSAPRAAACRANASAAPRAAIAAASAPHAASP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 300 SQSLSPHGVAPQAAVPSQSLSPHG---VAPQAAVPSQSLSPHGVApqVAVPSQSLSTHGVAPQAAVPSQSLSTHGVAPQA 376
Cdd:pfam17823 174 APRTAASSTTAASSTTAASSAPTTaasSAPATLTPARGISTAATA--TGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 377 AVpsQSLSTHgvAPQVAVPSQSLSTHgvAPQAAVPSPPLS-PHSTASGNAA---GSQPSSPRYRpYTVTHP-WGSSPCPT 451
Cdd:pfam17823 252 AL--ATLAAA--AGTVASAAGTINMG--DPHARRLSPAKHmPSDTMARNPAapmGAQAQGPIIQ-VSTDQPvHNTAGEPT 324
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907156787 452 PRSSILASSPGFPSHASSPRAvpASSSRQRPRSRVPAFPPASPSAASRRPSSLRISPSMSNSP 514
Cdd:pfam17823 325 PSPSNTTLEPNTPKSVASTNL--AVVTTTKAQAKEPSASPVPVLHTSMIPEVEATSPTTQPSP 385
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
269-501 |
1.79e-06 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 52.54 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 269 PAPSA-SLWSFVPALSPSFALPShPAPQAAMPSQSLSPHGVAPQAAVPSQSLSPHGVAPQAAVPSQSLSPHGVAPQVAVP 347
Cdd:PRK07003 360 PAVTGgGAPGGGVPARVAGAVPA-PGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADR 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 348 SQSLSTHGVAPQAAVPSQSLSTHGVAPQAAVPSQSLSTHGVAPQVAVPS----QSLSTHGVAPQAAVPSPPLSPHSTASG 423
Cdd:PRK07003 439 GDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDaafePAPRAAAPSAATPAAVPDARAPAAASR 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 424 NAAGSQPSSPRYRpytvthpwgsSPCPTPRSSILASSPGFPSHA-----------SSPRAVPASSSRQRprsrvPAFPPA 492
Cdd:PRK07003 519 EDAPAAAAPPAPE----------ARPPTPAAAAPAARAGGAAAAldvlrnagmrvSSDRGARAAAAAKP-----AAAPAA 583
|
....*....
gi 1907156787 493 SPSAASRRP 501
Cdd:PRK07003 584 APKPAAPRV 592
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
280-468 |
4.27e-06 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 51.69 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 280 PALSPSFALPSHPAPQAAMPSQSLSPHgvapqaavpSQSLSPHGVAPQAAVPSQSLSPhgvaPQVAVPSQSlSTHGVAPQ 359
Cdd:pfam03154 394 PALKPLSSLSTHHPPSAHPPPLQLMPQ---------SQQLPPPPAQPPVLTQSQSLPP----PAASHPPTS-GLHQVPSQ 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 360 AAVPSQSLSTHG----VAPQAAVPSQSLSTHGVAPQVAVPSQSLSTHGVAPQAAVPSPPLSPHSTASGNAAGSQPSSPRy 435
Cdd:pfam03154 460 SPFPQHPFVPGGpppiTPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPR- 538
|
170 180 190
....*....|....*....|....*....|...
gi 1907156787 436 rpytvthpwgsSPCPTPrsSILASspgfPSHAS 468
Cdd:pfam03154 539 -----------SPSPEP--TVVNT----PSHAS 554
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
266-514 |
5.10e-06 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 51.31 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 266 ETSPAPSASLWSFVPALSPSFALPSHPAPQAAMPSQSLSPHGVAPQAAVPSQSLSPHGVAPQaavPSQSLSPHGV---AP 342
Cdd:pfam03154 177 QSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLH---PQRLPSPHPPlqpMT 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 343 QVAVPSQslsthgVAPQaavPSQSLSTHGVAPQAAVPSQSLSTHGVAPqvaVPSQSLSTHGVAPQAAVPSPP---LSPHS 419
Cdd:pfam03154 254 QPPPPSQ------VSPQ---PLPQPSLHGQMPPMPHSLQTGPSHMQHP---VPPQPFPLTPQSSQSQVPPGPspaAPGQS 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 420 TASGNAAGSQPSS-----PRYRPY---TVTHPWGSSPCPTPRSSI-LASSPGFPSHASSPRAV---------PASSSRQR 481
Cdd:pfam03154 322 QQRIHTPPSQSQLqsqqpPREQPLppaPLSMPHIKPPPTTPIPQLpNPQSHKHPPHLSGPSPFqmnsnlpppPALKPLSS 401
|
250 260 270
....*....|....*....|....*....|...
gi 1907156787 482 PRSRVPafPPASPSAASRRPSSLRISPSMSNSP 514
Cdd:pfam03154 402 LSTHHP--PSAHPPPLQLMPQSQQLPPPPAQPP 432
|
|
| RING-Ubox_WDSUB1-like |
cd16655 |
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ... |
1385-1438 |
1.01e-05 |
|
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing protein 1 (WDSUB1) and similar proteins; WDSUB1 is an uncharacterized protein containing seven WD40 repeats and a SAM domain in addition to the U-box. Its biological role remains unclear. This subfamily also includes many uncharacterized kinase domain-containing U-box (AtPUB) proteins and several MIF4G motif-containing AtPUB proteins from Arabidopsis.
Pssm-ID: 438317 [Multi-domain] Cd Length: 55 Bit Score: 44.03 E-value: 1.01e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907156787 1385 PDEFRDPLMDTLMTDPVRLPSGTVMDRSIILRHLLNSPTDPFNRQMLTESMLEP 1438
Cdd:cd16655 1 PDEFLCPITQELMRDPVVAADGHTYERSAIEEWLETHNTSPMTRLPLSSTDLVP 54
|
|
| RING-Ubox_PUB |
cd16664 |
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ... |
1385-1436 |
1.32e-05 |
|
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and similar proteins; The plant PUB proteins, also known as U-box domain-containing proteins, are much more numerous in Arabidopsis which has 62 in comparison with the typical 6 in most animals. The majority of AtPUBs in this subfamily are known as ARM domain-containing PUB proteins, containing a C-terminally-located, tandem ARM (armadillo) repeat protein-interaction region in addition to the U-box domain. They have been implicated in the regulation of cell death and defense. They also play important roles in other plant-specific pathways, such as controlling both self-incompatibility and pseudo-self-incompatibility, as well as acting in abiotic stress. A subgroup of ARM domain-containing PUB proteins harbors a plant-specific U-box N-terminal domain.
Pssm-ID: 438326 [Multi-domain] Cd Length: 53 Bit Score: 43.71 E-value: 1.32e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907156787 1385 PDEFRDPLMDTLMTDPVRLPSGTVMDRSIILRHL-LNSPTDPFNRQMLTESML 1436
Cdd:cd16664 1 PEEFICPISLELMKDPVILATGQTYERAAIEKWLdSGNNTCPITGQPLTHTDL 53
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
302-513 |
1.35e-05 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 49.91 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 302 SLSPHGVAPQAAVPSQS-----LSPHGV----APQAAVPSQSLSPHGVAP---QVAVPSQS-LSTHGVAPQAAVPSQSLS 368
Cdd:pfam05109 392 TVSGLGTAPKTLIITRTatnatTTTHKVifskAPESTTTSPTLNTTGFAApntTTGLPSSThVPTNLTAPASTGPTVSTA 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 369 thgvapQAAVPSQSLSTHGVAPqvAVPSQSLSTHGVAPQAAVPSPPLSPHSTASGNAAGSQPSspryrpytVTHPWGSSP 448
Cdd:pfam05109 472 ------DVTSPTPAGTTSGASP--VTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPA--------VTTPTPNAT 535
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 449 CPT-----PRSSILASSPgfpsHASSPraVPASSSRQRPRSrVPAFPPASPSAASRRPSSLRISPSMSNS 513
Cdd:pfam05109 536 SPTlgktsPTSAVTTPTP----NATSP--TPAVTTPTPNAT-IPTLGKTSPTSAVTTPTPNATSPTVGET 598
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
271-508 |
1.89e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.55 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 271 PSASLWSFVPALSPSFALPSHPAPQAAMPSQSLSPhGVAPQA----AVPSQSLS-PHGV----APQAAVPSQSLSPhgvA 341
Cdd:PHA03247 2483 PAEARFPFAAGAAPDPGGGGPPDPDAPPAPSRLAP-AILPDEpvgePVHPRMLTwIRGLeelaSDDAGDPPPPLPP---A 2558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 342 PQVAVPSQSLSTHGVAPQAAVPSQSLSTH--GVAPQAAVPSQSLSTHGVAPQVAVPSQSlsthgvAPQAAVPSPPLSPHS 419
Cdd:PHA03247 2559 APPAAPDRSVPPPRPAPRPSEPAVTSRARrpDAPPQSARPRAPVDDRGDPRGPAPPSPL------PPDTHAPDPPPPSPS 2632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 420 TASGNAAGSQPSSPRYRPYTVTHPWGSSPCPTPRssilASSPGFPSHASS------PRAVPASSSRQRPRSRVPAfPPAS 493
Cdd:PHA03247 2633 PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR----ARRLGRAAQASSppqrprRRAARPTVGSLTSLADPPP-PPPT 2707
|
250
....*....|....*
gi 1907156787 494 PSAASRRPSSLRISP 508
Cdd:PHA03247 2708 PEPAPHALVSATPLP 2722
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
330-498 |
2.05e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 49.21 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 330 VPSQSLSPHGVAPQVAVPSQSLST--HGVAPQAAVPSQslstHGVAPQAAVPsqslsthgvAPQVAVPSQSLSTHGVAPQ 407
Cdd:PRK07764 364 LPSASDDERGLLARLERLERRLGVagGAGAPAAAAPSA----AAAAPAAAPA---------PAAAAPAAAAAPAPAAAPQ 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 408 AAVPSPPLSPHSTASGNAAGSQPSSPRYRPytvthpwGSSPCPTPRSSilASSPGFPSHASSPRAVPAsssrqrprsrvP 487
Cdd:PRK07764 431 PAPAPAPAPAPPSPAGNAPAGGAPSPPPAA-------APSAQPAPAPA--AAPEPTAAPAPAPPAAPA-----------P 490
|
170
....*....|.
gi 1907156787 488 AFPPASPSAAS 498
Cdd:PRK07764 491 AAAPAAPAAPA 501
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
216-460 |
5.73e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.01 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 216 ASLTATSQPIATAARSPDRNLMLNTGSS-SGTSPmfcnmgsFSTSSLSSLYETSPAPSASLWSFVPALSPSFALPSHPAP 294
Cdd:PHA03247 2796 ESLPSPWDPADPPAAVLAPAAALPPAASpAGPLP-------PPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPS 2868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 295 QAAMPSQSLSPHGVAPQAAVPSQSLSPHgvaPQAAVPSQSLSPhgvaPQVAVPSQSLSThgvaPQAAVPSQslsthgvaP 374
Cdd:PHA03247 2869 RSPAAKPAAPARPPVRRLARPAVSRSTE---SFALPPDQPERP----PQPQAPPPPQPQ----PQPPPPPQ--------P 2929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 375 QAAVPSQSLSTHGVAPQVAVPSQSlsthgvAPQAAVPSP---PLSPHSTASGNAAGSQPSSPRYRPYTVTHPWGSSpcPT 451
Cdd:PHA03247 2930 QPPPPPPPRPQPPLAPTTDPAGAG------EPSGAVPQPwlgALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGH--SL 3001
|
....*....
gi 1907156787 452 PRSSILASS 460
Cdd:PHA03247 3002 SRVSSWASS 3010
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
266-412 |
7.04e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 47.40 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 266 ETSPAPSASLWSFVPALSPSFALPSHPAPQAAMPSQSLSPHGVAPQAAVPSQSLSPHGVAP--QAAVPSQSLSPHGVAPQ 343
Cdd:PRK14951 379 KTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAaaPAAVALAPAPPAQAAPE 458
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907156787 344 -VAVPSQslsthgVAPQAAVPSQSLSTHGVAPQAAVPSQSLST--HGVAPQVAvpsQSLSTHGVAPQAAVPS 412
Cdd:PRK14951 459 tVAIPVR------VAPEPAVASAAPAPAAAPAAARLTPTEEGDvwHATVQQLA---AAEAITALARELALQS 521
|
|
| RING-Ubox_LubX-like_rpt2 |
cd23150 |
second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein ... |
1385-1453 |
7.58e-05 |
|
second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX and similar proteins; LubX, also called RING-type E3 ubiquitin transferase LubX, is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. LubX acts as an E3 ubiquitin-protein ligase (EC 2.3.2.27) that interferes with the host's ubiquitination pathway. LubX contains two RING-like U-box domains. U-box 1 is critical to the ubiquitin ligase activity, and U-box 2 mediates interaction with host target. This model corresponds to the second one.
Pssm-ID: 438512 [Multi-domain] Cd Length: 69 Bit Score: 42.07 E-value: 7.58e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907156787 1385 PDEFRDPLMDTLMTDPVRLPSGTVMDRSIILRHLLNSPTDPFNRQMLTESMLEPVPELKEQIQAWMREK 1453
Cdd:cd23150 1 PDIFLCPISKTLIKTPVITAQGKVYDQEALSNFLIATGNKDETGKKLSIDDVVVFDELYQQIKVYNFYR 69
|
|
| PHA03379 |
PHA03379 |
EBNA-3A; Provisional |
284-510 |
9.14e-05 |
|
EBNA-3A; Provisional
Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 47.36 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 284 PSFALPSHPAPQ------AAMPSQSLSP---HGVAPQAAVPSQSLSPHGVAPQAAVPSQSLSPHGVAPQV-------AVP 347
Cdd:PHA03379 418 PPVEKPRPEVPQsletatSHGSAQVPEPppvHDLEPGPLHDQHSMAPCPVAQLPPGPLQDLEPGDQLPGVvqdgrpaCAP 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 348 SQSLSTHGVAPQAAVPSQS----LSTHGVAPQAAVPSQSLSTHGVAPQVAVPSQSL-----STHGV-------APQAAVP 411
Cdd:PHA03379 498 VPAPAGPIVRPWEASLSQVpgvaFAPVMPQPMPVEPVPVPTVALERPVCPAPPLIAmqgpgETSGIvrvrerwRPAPWTP 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 412 SPPLSPhstaSGNAAGSQPSSPRYRPYTVTHPWGSSPCPTPRSSILA--SSPGFPSHASSPRAVPASSSRQRPRSRVPAF 489
Cdd:PHA03379 578 NPPRSP----SQMSVRDRLARLRAEAQPYQASVEVQPPQLTQVSPQQpmEYPLEPEQQMFPGSPFSQVADVMRAGGVPAM 653
|
250 260
....*....|....*....|.
gi 1907156787 490 PPASPSAASRRPSSLRISPSM 510
Cdd:PHA03379 654 QPQYFDLPLQQPISQGAPLAP 674
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
271-424 |
9.17e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 47.02 E-value: 9.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 271 PSASLWSFVPALSPSFALPSHPAPQAAMPSQSLSPHgvAPQAAVPSQSLSPhgVAPQAAVPSQSLSPHGVAPQVAVPSqs 350
Cdd:PRK14951 366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAP--APAAAPAAAASAP--AAPPAAAPPAPVAAPAAAAPAAAPA-- 439
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907156787 351 lsthgvAPQAAVPSQSLSTHGVAPQ-AAVPSQslsthgVAPQVAVPSQSlsTHGVAPQAAVPSPPLSPHSTASGN 424
Cdd:PRK14951 440 ------AAPAAVALAPAPPAQAAPEtVAIPVR------VAPEPAVASAA--PAPAAAPAAARLTPTEEGDVWHAT 500
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
306-433 |
1.16e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 46.90 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 306 HGVAPQAAVPSQSLSPHGVAPQAAVPSQSlSPHGVAPQVAVPSqslsthgVAPQAAVPSQSLSthgvAPQAAVPSQSLST 385
Cdd:PRK07764 385 LGVAGGAGAPAAAAPSAAAAAPAAAPAPA-AAAPAAAAAPAPA-------AAPQPAPAPAPAP----APPSPAGNAPAGG 452
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1907156787 386 HGVAPQVAVPSQSLSTHGVAPQAAVPSPPLSPHSTASGNAAGSQPSSP 433
Cdd:PRK07764 453 APSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAP 500
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
267-509 |
1.73e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 46.13 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 267 TSPAPSASLWSFVPALSP-SFALPSHPAPQAAMPSQSLSPHGVAPQAAVPSQSLSPHGVAPQAAVPSQSLSPHGVAPQVA 345
Cdd:PRK07764 395 AAAAPSAAAAAPAAAPAPaAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAP 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 346 VPSQSLSTHGVAPQAAVPSQSLSTHGVAPQAAVPSQSLSTHGvaPQV--AVPSQSLSTHG-VAPQAAV------------ 410
Cdd:PRK07764 475 EPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERW--PEIlaAVPKRSRKTWAiLLPEATVlgvrgdtlvlgf 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 411 PSPPL-----SPHST--------------------ASGNAAGSQPSSPRYRPYTVTHPWGSSPCPTPRssilASSPGFPS 465
Cdd:PRK07764 553 STGGLarrfaSPGNAevlvtalaeelggdwqveavVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAA----PAAPAAPA 628
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907156787 466 HASSPRAvPASSSRQRPRSRVPafPPASPSAASRRPSSLRISPS 509
Cdd:PRK07764 629 PAGAAAA-PAEASAAPAPGVAA--PEHHPKHVAVPDASDGGDGW 669
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
360-514 |
1.79e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 46.02 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 360 AAVPSQSLSTHGVAPQAAVPSQSLSTHGVAPQVAVPsqslsthgvAPQAAVPSPPLSPHSTASGNAAGSQPSSPRYRPyt 439
Cdd:PRK12323 362 AFRPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAP---------APAAPPAAPAAAPAAAAAARAVAAAPARRSPAP-- 430
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907156787 440 vthpwgsSPCPTPRSSILASSPGFPSHASSPRAVPASSSRqrprsrvPAFPPASPSAASRRPSSLRISPSMSNSP 514
Cdd:PRK12323 431 -------EALAAARQASARGPGGAPAPAPAPAAAPAAAAR-------PAAAGPRPVAAAAAAAPARAAPAAAPAP 491
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
281-434 |
2.29e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 45.63 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 281 ALSPSFALPSHPAPQAAMPSQSLSPHGVAPQAAVPSQSLSPHGVAPQAAVPSQSlsphgvAPQVAVPSQSLSthGVAPQA 360
Cdd:PRK07994 358 AFHPAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAP------AVPLPETTSQLL--AARQQL 429
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907156787 361 AVPSQSLSTHGVAPQAAVPSQSLSThgVAPQVAVPSQSLSTHGVAPQAAVPSPPLSPHSTASGNAAGSQPSSPR 434
Cdd:PRK07994 430 QRAQGATKAKKSEPAAASRARPVNS--ALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALK 501
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
337-470 |
2.80e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 45.48 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 337 PHGVAPQVAVPSQSLSTHGVAPQAAVPSQSLSTHGVAPQAAVPSQSLSThgVAPQVAVPSQSlsthgVAPQAAVPSPPLS 416
Cdd:PRK14951 366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAP--AAPPAAAPPAP-----VAAPAAAAPAAAP 438
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1907156787 417 PHSTASgnAAGSQPSSPRYRPYTVTHPWGSSPCPTPRSSILASSPGFPSHASSP 470
Cdd:PRK14951 439 AAAPAA--VALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTP 490
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
281-437 |
3.24e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 45.09 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 281 ALSPSFALPSHPAPQAAmpsqSLSPHGVAPQAAVPsQSLSPHGVAPQAAVPSQSlsphgvAPQVAVPSqslsthgvapqA 360
Cdd:PRK14951 363 AFKPAAAAEAAAPAEKK----TPARPEAAAPAAAP-VAQAAAAPAPAAAPAAAA------SAPAAPPA-----------A 420
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907156787 361 AVPSQSLSTHGVAPQAAVPsqslsthgvAPQVAVPSQSLSTHGVAPQAAVPSPPLSP--HSTASGNAAGSQPSSPRYRP 437
Cdd:PRK14951 421 APPAPVAAPAAAAPAAAPA---------AAPAAVALAPAPPAQAAPETVAIPVRVAPepAVASAAPAPAAAPAAARLTP 490
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
266-391 |
3.93e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 44.77 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 266 ETSPAPSASLWSFVPALSPSFALPSHPAPQAAMPSQSLSphGVAPQAAVPSQSLSPHGVAPQAAVP---SQSLSPHGVAP 342
Cdd:PRK14971 367 DDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQS--SAAAQPSAPQSATQPAGTPPTVSVDppaAVPVNPPSTAP 444
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1907156787 343 QVAVPSQSLSTHGVAPqAAVPSQSLST-HGVAPQAAVPSQSLSTHGVAPQ 391
Cdd:PRK14971 445 QAVRPAQFKEEKKIPV-SKVSSLGPSTlRPIQEKAEQATGNIKEAPTGTQ 493
|
|
| PLN02217 |
PLN02217 |
probable pectinesterase/pectinesterase inhibitor |
395-511 |
4.07e-04 |
|
probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 215130 [Multi-domain] Cd Length: 670 Bit Score: 45.08 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 395 PSQSLSTHGVAPQAAVP-SPPLSPHSTASGNAAGSQPSSPRYRPYTVTHPWGS-SPCPTPRSSILASSPGFPSHASSPRA 472
Cdd:PLN02217 540 PAQYIQGDAWIPGKGVPyIPGLFAGNPGSTNSTPTGSAASSNTTFSSDSPSTVvAPSTSPPAGHLGSPPATPSKIVSPST 619
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907156787 473 VPAsssrqRPRSRVPAFPPASPSAASRRPSSLRISPSMS 511
Cdd:PLN02217 620 SPP-----ASHLGSPSTTPSSPESSIKVASTETASPESS 653
|
|
| PRK10672 |
PRK10672 |
endolytic peptidoglycan transglycosylase RlpA; |
285-398 |
4.44e-04 |
|
endolytic peptidoglycan transglycosylase RlpA;
Pssm-ID: 236733 [Multi-domain] Cd Length: 361 Bit Score: 44.28 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 285 SFALPSHPAPQAAMPSQSLSPhGVAPQAAVPSQSLSPHGVAPQAAVPSQSlSPHGVAPQvAVPSQSLSTHGVAPQAAVPS 364
Cdd:PRK10672 191 SYALPARPDLSGGMGTPSVQP-APAPQGDVLPVSNSTLKSEDPTGAPVTS-SGFLGAPT-TLAPGVLEGSEPTPTAPSSA 267
|
90 100 110
....*....|....*....|....*....|....*
gi 1907156787 365 QSLSTHGVAPQAAVPSQSLSTHGVApQV-AVPSQS 398
Cdd:PRK10672 268 PATAPAAAAPQAAATSSSASGNFVV-QVgAVSDQQ 301
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
335-501 |
5.28e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.78 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 335 LSPHGVAPQVAVPSQSLSTHGVAPQAAVPSQSLSTHGVAPQAAVPSQSLSTHGVAPQVAVPSQSlSTHGVAPQAAVPSPP 414
Cdd:PHA03307 758 FSNPSLVPAKLAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTASKRKS-RSHTPDGGSESSGPA 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 415 LSPHSTASGNAAGSQPSSPRYRPYTVTHPWGSSPC-----PTPRSSILASSPGFPSHASSPRAVPASSSRQRPRSRVPAF 489
Cdd:PHA03307 837 RPPGAAARPPPARSSESSKSKPAAAGGRARGKNGRrrprpPEPRARPGAAAPPKAAAAAPPAGAPAPRPRPAPRVKLGPM 916
|
170
....*....|....
gi 1907156787 490 PPASPS--AASRRP 501
Cdd:PHA03307 917 PPGGPDprGGFRRV 930
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
289-443 |
5.53e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 44.38 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 289 PSHPApQAAMPSQSLSPHGVAPQAA-VPSQSLSPHGVAPQAAVPSQSLSPHGVAPQVavpsqslSTHGVAPQAAVPSQSl 367
Cdd:PRK14971 372 GRGPK-QHIKPVFTQPAAAPQPSAAaAASPSPSQSSAAAQPSAPQSATQPAGTPPTV-------SVDPPAAVPVNPPST- 442
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907156787 368 sthgvAPQAAVPSQSLSTHGVAPqVAVPSQSLST-HGVAPQAAVPSPPLSPHSTASGNAAGSQPSSPRY-RPYTVTHP 443
Cdd:PRK14971 443 -----APQAVRPAQFKEEKKIPV-SKVSSLGPSTlRPIQEKAEQATGNIKEAPTGTQKEIFTEEDLQYYwQEFAGTRP 514
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
323-514 |
5.72e-04 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 44.18 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 323 GVAPQAAVPSQSLSPHGVApqvavpsQSLSTHGVAPqaavPSQSLSThgvaPQAAVPSqslsthgvAPQVAVPSQSLSTh 402
Cdd:pfam17823 109 GAASRALAAAASSSPSSAA-------QSLPAAIAAL----PSEAFSA----PRAAACR--------ANASAAPRAAIAA- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 403 GVAPQAAVPSPPLSPHSTASGNAAGSQPSSPryRPYTVTHPwgSSPCPTPRSSILASSPGFPSHASSPRAVP-ASSSRQR 481
Cdd:pfam17823 165 ASAPHAASPAPRTAASSTTAASSTTAASSAP--TTAASSAP--ATLTPARGISTAATATGHPAAGTALAAVGnSSPAAGT 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907156787 482 PRSRVPAFPPAS-----------PSAA---------SRRPSSLRISPS--MSNSP 514
Cdd:pfam17823 241 VTAAVGTVTPAAlatlaaaagtvASAAgtinmgdphARRLSPAKHMPSdtMARNP 295
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
321-452 |
7.15e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 43.93 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 321 PHGVAPQAAVPSQSLSPHGVAPQVAVPSQSLSTHGVAPQAAVPSQSLSThgVAPQAAVPSQSLSTHGVAPQVAVPSqsls 400
Cdd:PRK14951 366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAP--AAPPAAAPPAPVAAPAAAAPAAAPA---- 439
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907156787 401 thgvAPQAAVPSPPLSPHSTASGNAA-----GSQPSSPRYRPYTVTHPWGSSPCPTP 452
Cdd:PRK14951 440 ----AAPAAVALAPAPPAQAAPETVAipvrvAPEPAVASAAPAPAAAPAAARLTPTE 492
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
283-501 |
1.00e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 43.90 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 283 SPSFALPSHPAPQAAMPSQSLSPHGVAPQAAVPSQSLSPHGVAPQAAVPSQSLS-PHGVAPQVAVPSQSLSTHGVAPQAA 361
Cdd:PHA03378 589 APSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITfNVLVFPTPHQPPQVEITPYKPTWTQ 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 362 VPSQSLSTHGVAPQAAVPSQSlsthgvAPQVAVPSqslsthgvaPQAAVP-SPPLSPHSTASGNAAGSQPSSPRYRPYTV 440
Cdd:PHA03378 669 IGHIPYQPSPTGANTMLPIQW------APGTMQPP---------PRAPTPmRPPAAPPGRAQRPAAATGRARPPAAAPGR 733
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907156787 441 THPWGSSPCPTPRSSILASSPGFPSHASSPRAVPAsssrQRPRSRVPAFPPASPSAASRRP 501
Cdd:PHA03378 734 ARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPA----AAPGAPTPQPPPQAPPAPQQRP 790
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
321-494 |
1.34e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.44 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 321 PHGVAPQAAVPSQSLSPhGVAPQVAVPSQSlsTHGVAPQAAVPSQSLSTHGVAPQAAVPSQSLSTHGVAPqVAVPSQSLS 400
Cdd:PRK07764 590 PAPGAAGGEGPPAPASS-GPPEEAARPAAP--AAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKH-VAVPDASDG 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 401 THGVAPQAAVPSPPLSPHSTASGNAAGSQPSSPRyrpytvthpwgsSPCPTPRSSilASSPGFPSHASSPRAVPASSSRQ 480
Cdd:PRK07764 666 GDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPA------------QPAPAPAAT--PPAGQADDPAAQPPQAAQGASAP 731
|
170
....*....|....
gi 1907156787 481 RPRSRVPAFPPASP 494
Cdd:PRK07764 732 SPAADDPVPLPPEP 745
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
309-414 |
1.82e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 42.84 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 309 APQAAVPSQSLSPHGVAPQAAVPSQSlsphgvapqVAVPSQSLSTHGVAPQAAVPSQslsthgvAPQAAVPSQSLSTHGV 388
Cdd:PRK14971 369 ASGGRGPKQHIKPVFTQPAAAPQPSA---------AAAASPSPSQSSAAAQPSAPQS-------ATQPAGTPPTVSVDPP 432
|
90 100
....*....|....*....|....*.
gi 1907156787 389 APQVAVPSQSLSTHGVAPQAAVPSPP 414
Cdd:PRK14971 433 AAVPVNPPSTAPQAVRPAQFKEEKKI 458
|
|
| SAP130_C |
pfam16014 |
Histone deacetylase complex subunit SAP130 C-terminus; |
339-474 |
2.66e-03 |
|
Histone deacetylase complex subunit SAP130 C-terminus;
Pssm-ID: 464973 [Multi-domain] Cd Length: 371 Bit Score: 41.84 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 339 GVAPQVAVPSQSLSTHGvAPQAAVPSQSLSTHgvaPQAAVPSqslsthgVAPQVAVPSQSLSTHGVAPqAAVPSPPLSPH 418
Cdd:pfam16014 29 AVAPPVTVAVEALPGQN-SEQQTASASPPSQH---PAQAIPT-------ILAPAAPPSQPSVVLSTLP-AAMAVTPPIPA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 419 STASGNAAGSQP--SSPRYRPYTVTHP----------------------WGSSPCPTPRSSILASSPGFPSHASSPRAVP 474
Cdd:pfam16014 97 SMANVVAPPTQPaaSSTAACAVSSVLPeikikqeaepmdtsqsvppltpTSISPALTSLANNLSVPAGDLLPGASPRKKP 176
|
|
| KLF10_11_N |
cd21974 |
N-terminal domain of Kruppel-like factor (KLF) 10, KLF11, and similar proteins; This subfamily ... |
283-438 |
3.54e-03 |
|
N-terminal domain of Kruppel-like factor (KLF) 10, KLF11, and similar proteins; This subfamily is composed of Kruppel-like factor or Krueppel-like factor (KLF) 10, KLF11, and similar proteins. KLF10 was first identified in human osteoblasts and plays a role in mediating estrogen (E2) signaling in bone and skeletal homeostasis and a regulatory role in tumor formation and metastasis. KLF11 is involved in cell growth, apoptosis, cellular inflammation and differentiation, endometriosis, and cholesterol, prostaglandin, neurotransmitter, fat, and sugar metabolism. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF10/11 belong 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 KLF10, KLF11, and similar proteins.
Pssm-ID: 409243 [Multi-domain] Cd Length: 229 Bit Score: 40.69 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 283 SPSFALPSHPAPQAampsqslSPHGVAPQAAVPSQSLSPHGVAPQAAVPSQSLS-------PHGVAPqVAVPSQSLSthg 355
Cdd:cd21974 63 SPPFFEASHSPSVA-------SLHPPSAASSQPPPEPESSEPPAASPQRAQATSvirhtadPVPVSP-PPVLCQMLP--- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 356 VAPQAAVPSQSLSTHGVAPQAAVPSQSLSTHGVAPQVAVPsqslstHG----VAPQAAVPSPPLS--------------- 416
Cdd:cd21974 132 VSSSSGVIVAFLKAPQQPSPQPQKPALPQPQVVLVGGQVP------QGpvmlVVPQPAVPQPYVQptvvtpggtkllpia 205
|
170 180
....*....|....*....|....
gi 1907156787 417 --PHSTASGNAAGSQPSSPRYRPY 438
Cdd:cd21974 206 paPGFIPSGQSSAPQPDFSRRRNH 229
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
289-475 |
3.94e-03 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 41.66 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 289 PSHPAPQAAMPSQS-LSPHGVAPQAAVPSQSLSPHGVAPQAAVPSQSLSPHGVAPQVAVPSQSLSTHGVAPqAAVPSQSL 367
Cdd:COG3469 11 TAGGASATAVTLLGaAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTAT-ATAAAAAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 368 STHGVAPQAAVPSQSLSTHGVAPQVAVPSQSLSTHGVAPQAAVPSPPLSPHSTASGnAAGSQPSSPRYR------PYTVT 441
Cdd:COG3469 90 TSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAG-STTTTTTVSGTEtatggtTTTST 168
|
170 180 190
....*....|....*....|....*....|....
gi 1907156787 442 HPWGSSPCPTPRSSILASSPGFPSHASSPRAVPA 475
Cdd:COG3469 169 TTTTTSASTTPSATTTATATTASGATTPSATTTA 202
|
|
| KLF10_N |
cd21572 |
N-terminal domain of Kruppel-like factor 10; Kruppel-like factor 10 (KLF10; also known as ... |
267-437 |
4.04e-03 |
|
N-terminal domain of Kruppel-like factor 10; Kruppel-like factor 10 (KLF10; also known as Krueppel-like factor 10; early growth response(EGR)-alpha/EGRA; TGFbeta inducible early gene-1/TIEG1) is a protein that in humans is encoded by the KLF10 gene. KLF10 was first identified in human osteoblasts and plays a role in mediating estrogen (E2) signaling in bone and skeletal homeostasis and a regulatory role in tumor formation and metastasis. It may also play a role in adipocyte differentiation and adipose tissue function. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF10 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 KLF10.
Pssm-ID: 409241 [Multi-domain] Cd Length: 245 Bit Score: 40.74 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 267 TSPAPSASLWSFVPALSPSFALPSHPAPQAAmpsqslsPHGVAPQAAVPSQSLSPHGVAPQ-----------AAVPSQSL 335
Cdd:cd21572 47 PADFHDSPPFCMTPPYSPPHFEATHPPSAAT-------LHPPAAQPPEEQHLSAETAASQQrfqctsvirhtADAQPCSC 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 336 SPHgVAPQVAVPSQSLSTHGVAPQAA----VPSQSLSTHGVAPQAAVPSQSLSThGVAPQVAVPSQSLSTHGV---APQA 408
Cdd:cd21572 120 SSC-PSSPSVVPSVPAGVAGVSPVPVycqiLPVSSSSTTVVAAQAPLPQPQQQA-ASPAQVFLMGGQVPKGPVmflVPQP 197
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907156787 409 AVPSPPLSPHSTASGN--------AAGSQPSSPRYRP 437
Cdd:cd21572 198 VVPTLYVQPTLVTPGGtklaaiapAPGHTPSEQRKSP 234
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
214-416 |
4.08e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.79 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 214 PFASLTATSQPIATAARSPDRNLMLNTGSSSGTSPmfcnmgsFSTSSLSSLYETSPAPSASLwSFVPALSPSFALPSHPA 293
Cdd:PRK12323 410 PAAAAAARAVAAAPARRSPAPEALAAARQASARGP-------GGAPAPAPAPAAAPAAAARP-AAAGPRPVAAAAAAAPA 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 294 PQAAMPSQSLSPHGVAPQAAVPSQSLSPhGVAPQAAVPSQSLSPHGVAPQVAVPSQSLSTHGVAPQAA-VPSQSLSTHGV 372
Cdd:PRK12323 482 RAAPAAAPAPADDDPPPWEELPPEFASP-APAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAApAPRAAAATEPV 560
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907156787 373 APQAAvPSQS------------------LSTHGVAPQVAVPSQSLSTHGVAPQAAVPSPPLS 416
Cdd:PRK12323 561 VAPRP-PRASasglpdmfdgdwpalaarLPVRGLAQQLARQSELAGVEGDTVRLRVPVPALA 621
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
292-503 |
4.59e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 41.59 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 292 PAPQAAMPSQSLSPHGVAPQAAVPSQSLSPHGVAPQAavPSQSLSPHGVaPQVAVPSQSLSTHGVAPQAAVPSQSLSTHG 371
Cdd:PHA03378 553 PASTEPVHDQLLPAPGLGPLQIQPLTSPTTSQLASSA--PSYAQTPWPV-PHPSQTPEPPTTQSHIPETSAPRQWPMPLR 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 372 VAPQAAVPSQSLS-THGVAPQVAVPSQSLSTHGVAPQAAVPSPPLSPHSTasgNAAGSQPssPRYRPYTV-THPWGSSPC 449
Cdd:PHA03378 630 PIPMRPLRMQPITfNVLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPT---GANTMLP--IQWAPGTMqPPPRAPTPM 704
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907156787 450 PTPRSSILASSP--GFPSHASSPRAVPASSSRQRPRSRvPAFPPASPSAASRRPSS 503
Cdd:PHA03378 705 RPPAAPPGRAQRpaAATGRARPPAAAPGRARPPAAAPG-RARPPAAAPGRARPPAA 759
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
267-414 |
6.58e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 40.99 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 267 TSPAPSASLWSFVPALSPSFALPSHPAPQAAMPSQSLSPHGVAPQAAVPSQSLSPhgvAPQAAVPSQSLSPHGVAPQV-- 344
Cdd:PRK07003 481 ASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPP---TPAAAAPAARAGGAAAALDVlr 557
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907156787 345 ----AVPSQSLSTHGVAPQAAVPsQSLSTHGVAPQAAVPSQSLSTHGVAPQvavpsQSLSTHGVAPQAA---VPSPP 414
Cdd:PRK07003 558 nagmRVSSDRGARAAAAAKPAAA-PAAAPKPAAPRVAVQVPTPRARAATGD-----APPNGAARAEQAAesrGAPPP 628
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
298-471 |
6.70e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.12 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 298 MPSQSLSPHGVAPQAAVPSQSLSP--HGVAPQAAVPSQslspHGVAPQVAVPSQslsthGVAPQAAVPSQSLSTHGVAPQ 375
Cdd:PRK07764 364 LPSASDDERGLLARLERLERRLGVagGAGAPAAAAPSA----AAAAPAAAPAPA-----AAAPAAAAAPAPAAAPQPAPA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 376 AAVPSQSLSTHGVAPQVAVPSQSLSTHGVAPQAAVPSPPLSPhstasgnAAGSQPSSPryrpytvthPWGSSPcPTPRSS 455
Cdd:PRK07764 435 PAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEP-------TAAPAPAPP---------AAPAPA-AAPAAP 497
|
170
....*....|....*.
gi 1907156787 456 ILASSPGFPSHASSPR 471
Cdd:PRK07764 498 AAPAAPAGADDAATLR 513
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
266-434 |
8.46e-03 |
|
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: 40.52 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 266 ETSPAPSASlwsfVPALSPSfalPSHPAPQAAMPSQSLSPHgVAPQAAVPSQSLSPHGVAPQAAVPSQSLSPH------- 338
Cdd:NF033839 287 PGNKKPSAP----KPGMQPS---PQPEKKEVKPEPETPKPE-VKPQLEKPKPEVKPQPEKPKPEVKPQLETPKpevkpqp 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156787 339 -----GVAPQVAVPSQSlsthgVAPQAAVPSQSLSTHGVAPQAAV-PSQSLSTHGVAPQVAVPSQSLS------THGVAP 406
Cdd:NF033839 359 ekpkpEVKPQPEKPKPE-----VKPQPETPKPEVKPQPEKPKPEVkPQPEKPKPEVKPQPEKPKPEVKpqpekpKPEVKP 433
|
170 180
....*....|....*....|....*...
gi 1907156787 407 QAAVPSPPLSPHSTASGNAAGSQPSSPR 434
Cdd:NF033839 434 QPEKPKPEVKPQPEKPKPEVKPQPETPK 461
|
|
| |
