|
Name |
Accession |
Description |
Interval |
E-value |
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
400-1014 |
6.39e-23 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 104.78 E-value: 6.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 400 ASPATLAGATAVSEWTEYKTADGKTYYYNNRTLESTWEKPQElkekekleekikepIKEPSEEPLPMEteeedpkeepik 479
Cdd:COG5104 3 AALLGMASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPKE--------------LLKGSEEDLDVD------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 480 eikeepkeeemteeekaaqkakpvatapipgtPWCVVWTGDERVFFYNPTTRLSMWDRpddligradvdkiiqePPHKKG 559
Cdd:COG5104 57 --------------------------------PWKECRTADGKVYYYNSITRESRWKI----------------PPERKK 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 560 MEELKKLRHPTPTMLSIQKWQFSMSAIkEEQELMEEINEDepvkakkrkrmskksfmwiaraslfrrddnkdidsEKEAA 639
Cdd:COG5104 89 VEPIAEQKHDERSMIGGNGNDMAITDH-ETSEPKYLLGRL-----------------------------------MSQYG 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 640 MEAEIKAARERAivpLEARMKQFKDMLLERGVSAFSTWEKELHKIVfDPRYLLL--NPKERKQVFDQYVKTRAEEERREK 717
Cdd:COG5104 133 ITSTKDAVYRLT---KEEAEKEFITMLKENQVDSTWPIFRAIEELR-DPRYWMVdtDPLWRKDLFKKYFENQEKDQREEE 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 718 KNKIMQAKEDFKKMME-EAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEKEDSKTRGEKIKSDFF 796
Cdd:COG5104 209 ENKQRKYINEFCKMLAgNSHIKYYTDWFTFKSIFSKHPYYSSVVNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLE 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 797 ELLSNHHLDSQSRWSKVKDKVESDPRYKAvdSSSM----REDLFKQYIeKIAKNLdsekekelerqarieaslrerEREV 872
Cdd:COG5104 289 EVLRSLGSETFIIWLLNHYVFDSVVRYLK--NKEMkpldRKDILFSFI-RYVRRL---------------------EKEL 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 873 QKARSEQTKEIDReREQHKREeaiqNFKALLSDMVRSSDVS----WSDTRRTLRKDHRWESGSLLEREEKEKLFNEHIEA 948
Cdd:COG5104 345 LSAIEERKAAAAQ-NARHHRD----EFRTLLRKLYSEGKIYyrmkWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVD 419
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181405734 949 LTKKKREHFRQLLDETSaITLTSTW--KEVKKIIKEDPRciKFSSSDRKKQREFEE---YIRDKYITAKAD 1014
Cdd:COG5104 420 LENMYGFARRSYERETR-TGQISPTdrRAVDEIFEAIAE--KKEEGEIKFDKVDKEdisLIVDGLIKQRNE 487
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
790-839 |
6.27e-14 |
|
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.
Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 66.71 E-value: 6.27e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2181405734 790 KIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQY 839
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
951-1006 |
3.88e-10 |
|
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.
Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 56.43 E-value: 3.88e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2181405734 951 KKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCiKFSSSDRKKQREFEEYIRD 1006
Cdd:smart00441 1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRY-KALLSESEREQLFEDHIEE 55
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
412-439 |
2.84e-08 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 50.22 E-value: 2.84e-08
10 20
....*....|....*....|....*...
gi 2181405734 412 SEWTEYKTADGKTYYYNNRTLESTWEKP 439
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDP 29
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
137-162 |
8.02e-08 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 49.04 E-value: 8.02e-08
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
132-164 |
8.13e-08 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 49.14 E-value: 8.13e-08
10 20 30
....*....|....*....|....*....|...
gi 2181405734 132 PTEEIWVENKTPDGKVYYYNARTRESAWTKPDG 164
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
137-164 |
2.09e-07 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 47.91 E-value: 2.09e-07
10 20
....*....|....*....|....*...
gi 2181405734 137 WVENKTPDGKVYYYNARTRESAWTKPDG 164
Cdd:cd00201 4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
292-421 |
3.62e-06 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 49.86 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 292 VAQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPtATPVQTVPqphpqTLPPavPHSVPQPTTAIPAFPP--VMVPPfRVP 369
Cdd:PHA02682 82 LAPSPACAAPAPACPACAPAAPAPAVTCPAPAP-ACPPATAP-----TCPP--PAVCPAPARPAPACPPstRQCPP-APP 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2181405734 370 LPgMPIPLPGVLP-----GMAPPIVPmihpqvaiAASPATLAGATAVSEWTEYKTAD 421
Cdd:PHA02682 153 LP-TPKPAPAAKPiflhnQLPPPDYP--------AASCPTIETAPAASPVLEPRIPD 200
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
260-365 |
3.92e-06 |
|
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: 51.07 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 260 TPTTSSPAPAVSTStssstpssttsttttatsvAQTVSTPTTQDQTPSSAVSVATP-----TVSVSTPAPTAT------- 327
Cdd:pfam05109 517 TPNATSPTPAVTTP-------------------TPNATSPTLGKTSPTSAVTTPTPnatspTPAVTTPTPNATiptlgkt 577
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2181405734 328 -PVQTVPQPHPQTLPPAVPHSVPQPTT------AIPAFPPVMVPP 365
Cdd:pfam05109 578 sPTSAVTTPTPNATSPTVGETSPQANTtnhtlgGTSSTPVVTSPP 622
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
706-1046 |
8.33e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 8.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 706 VKTRAEEERR--EKKNKIMQAK--EDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREAlfNEFVAAARKKEK 781
Cdd:PTZ00121 1423 AKKKAEEKKKadEAKKKAEEAKkaDEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA--KKKAEEAKKKAD 1500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 782 EDSKTRGEKIKSDffELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEKIAKNLDSEKEKELERQARI 861
Cdd:PTZ00121 1501 EAKKAAEAKKKAD--EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 862 EASLREREREVQKARSEQTKEIDREREQHKREEAiqnfKALLSDMVRSSDVSWSDTRRtlRKDHRWESGSLLEREEKEKL 941
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEELKKAEEEK--KKVEQLKKKEAEEKKKAEEL 1652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 942 FNEHIEALTKKKREHFRQLLDETSAitltstwKEVKKIIKEDPRCIKFSSSDRKKQREFEEyIRDKYITAKADFRTLLKE 1021
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKKA-------EEAKKAEEDEKKAAEALKKEAEEAKKAEE-LKKKEAEEKKKAEELKKA 1724
|
330 340
....*....|....*....|....*
gi 2181405734 1022 TKFITYRSKKLIQESDQHLKDVEKI 1046
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEEA 1749
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
136-173 |
1.52e-05 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 48.92 E-value: 1.52e-05
10 20 30
....*....|....*....|....*....|....*...
gi 2181405734 136 IWVENKTPDGKVYYYNARTRESAWTKPDgvKVIQQSEL 173
Cdd:COG5104 16 EWEELKAPDGRIYYYNKRTGKSSWEKPK--ELLKGSEE 51
|
|
| KLF3_N |
cd21577 |
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ... |
306-394 |
3.09e-05 |
|
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called Krueppel-like factor 3 and originally called Basic Kruppel-like Factor/BKLF), was the third member of the KLF family of zinc finger transcription factors to be discovered. KLF3 possesses a wide range of biological impacts on regulating apoptosis, differentiation, and proliferation in various tissues during the entire progression process. It has been proposed as a tumor suppressor in colorectal cancer. It appears to function predominantly as a repressor of transcription, turning genes off by recruiting the C-terminal Binding Protein co-repressors CtBP1 and CtBP2. CtBP docks onto a short motif (residues 61-65) in the N-terminus of KLF3, through the Proline-X-Aspartate-Leucine-Serine (PXDLS) motif. CtBP in turn recruits histone modifying enzymes to alter chromatin and repress gene expression. KLF3 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 KLF3.
Pssm-ID: 410554 [Multi-domain] Cd Length: 214 Bit Score: 46.19 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 306 PSSAVSVATPTVSVSTPAPTATPvqtvPQPH--------PQTLPPAVPHSVPQPTTAIPAFPPVMVPPFRVPLPGMPIPL 377
Cdd:cd21577 33 PSSSSSSSSSSSSSSSPSSRASP----PSPYskssppspPQQRPLSPPLSLPPPVAPPPLSPGSVPGGLPVISPVMVQPV 108
|
90
....*....|....*....
gi 2181405734 378 PGVLPG--MAPPIVPMIHP 394
Cdd:cd21577 109 PVLYPPhlHQPIMVSSSPP 127
|
|
| half-pint |
TIGR01645 |
poly-U binding splicing factor, half-pint family; The proteins represented by this model ... |
297-413 |
8.18e-05 |
|
poly-U binding splicing factor, half-pint family; The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA.
Pssm-ID: 130706 [Multi-domain] Cd Length: 612 Bit Score: 46.60 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 297 STPTTQDQTPSSAVSvATPTvSVSTPaPTATPVQTVPQPHPqTLPPAVPHSV-PQPTTAI-PAFPPVMVPPFRVPLPGMP 374
Cdd:TIGR01645 322 AVLGPRAQSPATPSS-SLPT-DIGNK-AVVSSAKKEAEEVP-PLPQAAPAVVkPGPMEIPtPVPPPGLAIPSLVAPPGLV 397
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2181405734 375 IPLPGVLPGMAPPIVPMIHPQVAIAASP--ATLAGATAVSE 413
Cdd:TIGR01645 398 APTEINPSFLASPRKKMKREKLPVTFGAldDTLAWKEPSKE 438
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
1009-1073 |
9.92e-05 |
|
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.
Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 41.02 E-value: 9.92e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181405734 1009 ITAKADFRTLLKETKFITYrskkliqesDQHLKDVEKILQNDKRYLVLDcVPEERRKLIVAYVDD 1073
Cdd:smart00441 1 EEAKEAFKELLKEHEVITP---------DTTWSEARKKLKNDPRYKALL-SESEREQLFEDHIEE 55
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
1011-1070 |
1.07e-04 |
|
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.
Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 40.90 E-value: 1.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 1011 AKADFRTLLKETKfITYRSkkliqesdqHLKDVEKILQNDKRYLVLDcVPEERRKLIVAY 1070
Cdd:pfam01846 2 AREAFKELLKEHK-ITPYS---------TWSEIKKKIENDPRYKALL-DGSEREELFEDY 50
|
|
| Amelogenin |
smart00818 |
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
299-404 |
3.57e-04 |
|
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.
Pssm-ID: 197891 [Multi-domain] Cd Length: 165 Bit Score: 42.47 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 299 PTTQDQTPSSAVSV--ATPTVSVSTPAPTATPVQTVPQPHPQT--------LPPAVPHSVpQPTTAIPAFPPVMVPPFRV 368
Cdd:smart00818 41 PVSQQHPPTHTLQPhhHIPVLPAQQPVVPQQPLMPVPGQHSMTptqhhqpnLPQPAQQPF-QPQPLQPPQPQQPMQPQPP 119
|
90 100 110
....*....|....*....|....*....|....*...
gi 2181405734 369 PLPGMPIPLPGVLPGMAP--PIVPMIhPQVAIAASPAT 404
Cdd:smart00818 120 VHPIPPLPPQPPLPPMFPmqPLPPLL-PDLPLEAWPAT 156
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
840-1049 |
3.91e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 840 IEKIAKNLDSEKEKELERQARIEASLREREREVQKARSEQT---KEIDREREQ-HKREEAIQNFKALLSD-MVRSSDVSW 914
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleARIEELEEDlHKLEEALNDLEARLSHsRIPEIQAEL 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 915 SDtrrtLRKDHRWESGSL--LEREEKEKLFNEHIEaltKKKREHFRQLLDEtsaitLTSTWKEVKKIIKEDPRCIKFSSS 992
Cdd:TIGR02169 801 SK----LEEEVSRIEARLreIEQKLNRLTLEKEYL---EKEIQELQEQRID-----LKEQIKSIEKEIENLNGKKEELEE 868
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 993 DRKKQREFEEYIRDKYITAKADFRTLLKETKFITYRSKKL---IQESDQHLKDVEKILQN 1049
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELeaqIEKKRKRLSELKAKLEA 928
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
400-1014 |
6.39e-23 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 104.78 E-value: 6.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 400 ASPATLAGATAVSEWTEYKTADGKTYYYNNRTLESTWEKPQElkekekleekikepIKEPSEEPLPMEteeedpkeepik 479
Cdd:COG5104 3 AALLGMASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPKE--------------LLKGSEEDLDVD------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 480 eikeepkeeemteeekaaqkakpvatapipgtPWCVVWTGDERVFFYNPTTRLSMWDRpddligradvdkiiqePPHKKG 559
Cdd:COG5104 57 --------------------------------PWKECRTADGKVYYYNSITRESRWKI----------------PPERKK 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 560 MEELKKLRHPTPTMLSIQKWQFSMSAIkEEQELMEEINEDepvkakkrkrmskksfmwiaraslfrrddnkdidsEKEAA 639
Cdd:COG5104 89 VEPIAEQKHDERSMIGGNGNDMAITDH-ETSEPKYLLGRL-----------------------------------MSQYG 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 640 MEAEIKAARERAivpLEARMKQFKDMLLERGVSAFSTWEKELHKIVfDPRYLLL--NPKERKQVFDQYVKTRAEEERREK 717
Cdd:COG5104 133 ITSTKDAVYRLT---KEEAEKEFITMLKENQVDSTWPIFRAIEELR-DPRYWMVdtDPLWRKDLFKKYFENQEKDQREEE 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 718 KNKIMQAKEDFKKMME-EAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEKEDSKTRGEKIKSDFF 796
Cdd:COG5104 209 ENKQRKYINEFCKMLAgNSHIKYYTDWFTFKSIFSKHPYYSSVVNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLE 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 797 ELLSNHHLDSQSRWSKVKDKVESDPRYKAvdSSSM----REDLFKQYIeKIAKNLdsekekelerqarieaslrerEREV 872
Cdd:COG5104 289 EVLRSLGSETFIIWLLNHYVFDSVVRYLK--NKEMkpldRKDILFSFI-RYVRRL---------------------EKEL 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 873 QKARSEQTKEIDReREQHKREeaiqNFKALLSDMVRSSDVS----WSDTRRTLRKDHRWESGSLLEREEKEKLFNEHIEA 948
Cdd:COG5104 345 LSAIEERKAAAAQ-NARHHRD----EFRTLLRKLYSEGKIYyrmkWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVD 419
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181405734 949 LTKKKREHFRQLLDETSaITLTSTW--KEVKKIIKEDPRciKFSSSDRKKQREFEE---YIRDKYITAKAD 1014
Cdd:COG5104 420 LENMYGFARRSYERETR-TGQISPTdrRAVDEIFEAIAE--KKEEGEIKFDKVDKEdisLIVDGLIKQRNE 487
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
790-839 |
6.27e-14 |
|
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.
Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 66.71 E-value: 6.27e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2181405734 790 KIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQY 839
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
723-772 |
7.01e-12 |
|
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.
Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 60.93 E-value: 7.01e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2181405734 723 QAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEF 772
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
951-1006 |
3.88e-10 |
|
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.
Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 56.43 E-value: 3.88e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2181405734 951 KKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCiKFSSSDRKKQREFEEYIRD 1006
Cdd:smart00441 1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRY-KALLSESEREQLFEDHIEE 55
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
658-705 |
4.60e-10 |
|
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.
Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 55.93 E-value: 4.60e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2181405734 658 RMKQFKDMLLERGVSAFSTWEKELHKIVFDPRYL-LLNPKERKQVFDQY 705
Cdd:pfam01846 2 AREAFKELLKEHKITPYSTWSEIKKKIENDPRYKaLLDGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
789-842 |
8.75e-10 |
|
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.
Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 55.27 E-value: 8.75e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2181405734 789 EKIKSDFFELLSNHHLD-SQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEK 842
Cdd:smart00441 1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
894-945 |
1.63e-09 |
|
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.
Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 54.39 E-value: 1.63e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2181405734 894 EAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWEsgSLLEREEKEKLFNEH 945
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYK--ALLDGSEREELFEDY 50
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
412-439 |
2.84e-08 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 50.22 E-value: 2.84e-08
10 20
....*....|....*....|....*...
gi 2181405734 412 SEWTEYKTADGKTYYYNNRTLESTWEKP 439
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDP 29
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
412-439 |
4.73e-08 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 49.81 E-value: 4.73e-08
10 20
....*....|....*....|....*...
gi 2181405734 412 SEWTEYKTADGKTYYYNNRTLESTWEKP 439
Cdd:pfam00397 3 PGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
722-775 |
7.53e-08 |
|
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.
Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 49.88 E-value: 7.53e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2181405734 722 MQAKEDFKKMMEEAKFN-PRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAA 775
Cdd:smart00441 1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
137-162 |
8.02e-08 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 49.04 E-value: 8.02e-08
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
132-164 |
8.13e-08 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 49.14 E-value: 8.13e-08
10 20 30
....*....|....*....|....*....|...
gi 2181405734 132 PTEEIWVENKTPDGKVYYYNARTRESAWTKPDG 164
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
952-1003 |
1.67e-07 |
|
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.
Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 48.61 E-value: 1.67e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2181405734 952 KKREHFRQLLDETSaITLTSTWKEVKKIIKEDPRCIKFSSSDRKKQrEFEEY 1003
Cdd:pfam01846 1 KAREAFKELLKEHK-ITPYSTWSEIKKKIENDPRYKALLDGSEREE-LFEDY 50
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
414-440 |
1.71e-07 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 48.37 E-value: 1.71e-07
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
137-164 |
2.09e-07 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 47.91 E-value: 2.09e-07
10 20
....*....|....*....|....*...
gi 2181405734 137 WVENKTPDGKVYYYNARTRESAWTKPDG 164
Cdd:cd00201 4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
893-948 |
1.41e-06 |
|
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.
Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 46.41 E-value: 1.41e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2181405734 893 EEAIQNFKALLSDMVRS-SDVSWSDTRRTLRKDHRWESgsLLEREEKEKLFNEHIEA 948
Cdd:smart00441 1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKA--LLSESEREQLFEDHIEE 55
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
292-421 |
3.62e-06 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 49.86 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 292 VAQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPtATPVQTVPqphpqTLPPavPHSVPQPTTAIPAFPP--VMVPPfRVP 369
Cdd:PHA02682 82 LAPSPACAAPAPACPACAPAAPAPAVTCPAPAP-ACPPATAP-----TCPP--PAVCPAPARPAPACPPstRQCPP-APP 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2181405734 370 LPgMPIPLPGVLP-----GMAPPIVPmihpqvaiAASPATLAGATAVSEWTEYKTAD 421
Cdd:PHA02682 153 LP-TPKPAPAAKPiflhnQLPPPDYP--------AASCPTIETAPAASPVLEPRIPD 200
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
656-707 |
3.88e-06 |
|
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.
Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 44.87 E-value: 3.88e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2181405734 656 EARMKQFKDMLLERGVS-AFSTWEKELHKIVFDPRY-LLLNPKERKQVFDQYVK 707
Cdd:smart00441 1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYkALLSESEREQLFEDHIE 54
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
260-365 |
3.92e-06 |
|
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: 51.07 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 260 TPTTSSPAPAVSTStssstpssttsttttatsvAQTVSTPTTQDQTPSSAVSVATP-----TVSVSTPAPTAT------- 327
Cdd:pfam05109 517 TPNATSPTPAVTTP-------------------TPNATSPTLGKTSPTSAVTTPTPnatspTPAVTTPTPNATiptlgkt 577
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2181405734 328 -PVQTVPQPHPQTLPPAVPHSVPQPTT------AIPAFPPVMVPP 365
Cdd:pfam05109 578 sPTSAVTTPTPNATSPTVGETSPQANTtnhtlgGTSSTPVVTSPP 622
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
706-1046 |
8.33e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 8.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 706 VKTRAEEERR--EKKNKIMQAK--EDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREAlfNEFVAAARKKEK 781
Cdd:PTZ00121 1423 AKKKAEEKKKadEAKKKAEEAKkaDEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA--KKKAEEAKKKAD 1500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 782 EDSKTRGEKIKSDffELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEKIAKNLDSEKEKELERQARI 861
Cdd:PTZ00121 1501 EAKKAAEAKKKAD--EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 862 EASLREREREVQKARSEQTKEIDREREQHKREEAiqnfKALLSDMVRSSDVSWSDTRRtlRKDHRWESGSLLEREEKEKL 941
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEELKKAEEEK--KKVEQLKKKEAEEKKKAEEL 1652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 942 FNEHIEALTKKKREHFRQLLDETSAitltstwKEVKKIIKEDPRCIKFSSSDRKKQREFEEyIRDKYITAKADFRTLLKE 1021
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKKA-------EEAKKAEEDEKKAAEALKKEAEEAKKAEE-LKKKEAEEKKKAEELKKA 1724
|
330 340
....*....|....*....|....*
gi 2181405734 1022 TKFITYRSKKLIQESDQHLKDVEKI 1046
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEEA 1749
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
697-947 |
1.11e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.74 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 697 ERKQVfDQYVKTRAEEERREKKNKIMQAKEdfKKMMEEAKFNPRATFSEFAAKHAKDSRFkAIEKMKDREALFNEfvaaa 776
Cdd:pfam17380 286 ERQQQ-EKFEKMEQERLRQEKEEKAREVER--RRKLEEAEKARQAEMDRQAAIYAEQERM-AMERERELERIRQE----- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 777 rKKEKEDSKTRGEKIKSDFFEL--LSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMRE-DLFKQYIEKIaknldsEKEK 853
Cdd:pfam17380 357 -ERKRELERIRQEEIAMEISRMreLERLQMERQQKNERVRQELEAARKVKILEEERQRKiQQQKVEMEQI------RAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 854 ELERQARIEASLREREREVQKARSEQ---TKEIDREREQhkrEEAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWESG 930
Cdd:pfam17380 430 EEARQREVRRLEEERAREMERVRLEEqerQQQVERLRQQ---EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQ 506
|
250
....*....|....*..
gi 2181405734 931 SLLEREEKEKLFNEHIE 947
Cdd:pfam17380 507 AMIEEERKRKLLEKEME 523
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
512-540 |
1.41e-05 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 42.97 E-value: 1.41e-05
10 20
....*....|....*....|....*....
gi 2181405734 512 PWCVVWTGDERVFFYNPTTRLSMWDRPDD 540
Cdd:smart00456 5 GWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
136-173 |
1.52e-05 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 48.92 E-value: 1.52e-05
10 20 30
....*....|....*....|....*....|....*...
gi 2181405734 136 IWVENKTPDGKVYYYNARTRESAWTKPDgvKVIQQSEL 173
Cdd:COG5104 16 EWEELKAPDGRIYYYNKRTGKSSWEKPK--ELLKGSEE 51
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
259-410 |
1.70e-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: 49.14 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 259 STPTTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQDQTPSSavSVATPTVSVSTPAPTAT--------PVQ 330
Cdd:pfam05109 469 STADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTP--NATSPTPAVTTPTPNATsptlgktsPTS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 331 TVPQPHPQTLPPAVPHSVPQPTTAIPAFPPVMvppfrvPLPGMPIPLPGVlpgmAPPIVPMIHPQVaiAASPATLAGATA 410
Cdd:pfam05109 547 AVTTPTPNATSPTPAVTTPTPNATIPTLGKTS------PTSAVTTPTPNA----TSPTVGETSPQA--NTTNHTLGGTSS 614
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
511-540 |
2.38e-05 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 42.13 E-value: 2.38e-05
10 20 30
....*....|....*....|....*....|
gi 2181405734 511 TPWCVVWTGDERVFFYNPTTRLSMWDRPDD 540
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| KLF3_N |
cd21577 |
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ... |
306-394 |
3.09e-05 |
|
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called Krueppel-like factor 3 and originally called Basic Kruppel-like Factor/BKLF), was the third member of the KLF family of zinc finger transcription factors to be discovered. KLF3 possesses a wide range of biological impacts on regulating apoptosis, differentiation, and proliferation in various tissues during the entire progression process. It has been proposed as a tumor suppressor in colorectal cancer. It appears to function predominantly as a repressor of transcription, turning genes off by recruiting the C-terminal Binding Protein co-repressors CtBP1 and CtBP2. CtBP docks onto a short motif (residues 61-65) in the N-terminus of KLF3, through the Proline-X-Aspartate-Leucine-Serine (PXDLS) motif. CtBP in turn recruits histone modifying enzymes to alter chromatin and repress gene expression. KLF3 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 KLF3.
Pssm-ID: 410554 [Multi-domain] Cd Length: 214 Bit Score: 46.19 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 306 PSSAVSVATPTVSVSTPAPTATPvqtvPQPH--------PQTLPPAVPHSVPQPTTAIPAFPPVMVPPFRVPLPGMPIPL 377
Cdd:cd21577 33 PSSSSSSSSSSSSSSSPSSRASP----PSPYskssppspPQQRPLSPPLSLPPPVAPPPLSPGSVPGGLPVISPVMVQPV 108
|
90
....*....|....*....
gi 2181405734 378 PGVLPG--MAPPIVPMIHP 394
Cdd:cd21577 109 PVLYPPhlHQPIMVSSSPP 127
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
258-395 |
3.26e-05 |
|
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: 48.22 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 258 ASTPTTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQDQTPSSAVSVATPTVSVSTP------------APT 325
Cdd:pfam03154 176 AQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQrlpsphpplqpmTQP 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 326 ATPVQTVPQPHP---------------QTLPPAVPHSVPQ-----------------PTTAIP-------------AFPP 360
Cdd:pfam03154 256 PPPSQVSPQPLPqpslhgqmppmphslQTGPSHMQHPVPPqpfpltpqssqsqvppgPSPAAPgqsqqrihtppsqSQLQ 335
|
170 180 190
....*....|....*....|....*....|....*
gi 2181405734 361 VMVPPFRVPLPGMPIPLPGVLPGMAPPIVPMIHPQ 395
Cdd:pfam03154 336 SQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQ 370
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
709-978 |
5.11e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 709 RAEEERR--EKKNKIMQAK--EDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEKEDS 784
Cdd:PTZ00121 1297 KAEEKKKadEAKKKAEEAKkaDEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 785 KTRGEKIKSDFFELLSNHHLDSQSRwskvKDKVESDPRYKAVDSSSMREDLfKQYIEKIAKNLDSEKEKELERQARieaS 864
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAE----EDKKKADELKKAAAAKKKADEA-KKKAEEKKKADEAKKKAEEAKKAD---E 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 865 LREREREVQKARSEQTKEIDREREQHKREEAIQNFKAllSDMVRSSDVSWSDTRRTLRKDHRWESGSLLEREEKEKLFNE 944
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA--DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
250 260 270
....*....|....*....|....*....|....
gi 2181405734 945 HIEALTKKKREHFRQLLDETSAITLTSTwKEVKK 978
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELKKA-EELKK 1559
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
258-466 |
6.34e-05 |
|
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: 46.88 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 258 ASTPTTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQDQTPSSAVSVATPTVSVSTPA-PTATPVQTVPQPH 336
Cdd:pfam17823 165 ASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGISTAATATGHPAAGTALAAvGNSSPAAGTVTAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 337 PQTLPPAVPHSVPQP--TTAIPAFPPVMVPPF-RVPLPGMPIPlpgvLPGMAPPIVPMIHPQVAIAASPATlagatavSE 413
Cdd:pfam17823 245 VGTVTPAALATLAAAagTVASAAGTINMGDPHaRRLSPAKHMP----SDTMARNPAAPMGAQAQGPIIQVS-------TD 313
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2181405734 414 WTEYKTADGKTYYYNNRTLESTWEKPQELKEKEKLEEKIKEPiKEPSEEPLPM 466
Cdd:pfam17823 314 QPVHNTAGEPTPSPSNTTLEPNTPKSVASTNLAVVTTTKAQA-KEPSASPVPV 365
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
137-172 |
6.40e-05 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 47.00 E-value: 6.40e-05
10 20 30
....*....|....*....|....*....|....*.
gi 2181405734 137 WVENKTPDGKVYYYNARTRESAWTKPDGVKVIQQSE 172
Cdd:COG5104 58 WKECRTADGKVYYYNSITRESRWKIPPERKKVEPIA 93
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
293-402 |
7.92e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 46.63 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 293 AQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPTATPVQTVP-QPHPQTLPPAVPHSVPQPtTAIPAFPPVMVPPFRVPLP 371
Cdd:PRK14951 385 EAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPvAAPAAAAPAAAPAAAPAA-VALAPAPPAQAAPETVAIP 463
|
90 100 110
....*....|....*....|....*....|.
gi 2181405734 372 GMPIPLPGVLPgmAPPIVPMIHPQVAIAASP 402
Cdd:PRK14951 464 VRVAPEPAVAS--AAPAPAAAPAAARLTPTE 492
|
|
| half-pint |
TIGR01645 |
poly-U binding splicing factor, half-pint family; The proteins represented by this model ... |
297-413 |
8.18e-05 |
|
poly-U binding splicing factor, half-pint family; The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA.
Pssm-ID: 130706 [Multi-domain] Cd Length: 612 Bit Score: 46.60 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 297 STPTTQDQTPSSAVSvATPTvSVSTPaPTATPVQTVPQPHPqTLPPAVPHSV-PQPTTAI-PAFPPVMVPPFRVPLPGMP 374
Cdd:TIGR01645 322 AVLGPRAQSPATPSS-SLPT-DIGNK-AVVSSAKKEAEEVP-PLPQAAPAVVkPGPMEIPtPVPPPGLAIPSLVAPPGLV 397
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2181405734 375 IPLPGVLPGMAPPIVPMIHPQVAIAASP--ATLAGATAVSE 413
Cdd:TIGR01645 398 APTEINPSFLASPRKKMKREKLPVTFGAldDTLAWKEPSKE 438
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
1009-1073 |
9.92e-05 |
|
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.
Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 41.02 E-value: 9.92e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181405734 1009 ITAKADFRTLLKETKFITYrskkliqesDQHLKDVEKILQNDKRYLVLDcVPEERRKLIVAYVDD 1073
Cdd:smart00441 1 EEAKEAFKELLKEHEVITP---------DTTWSEARKKLKNDPRYKALL-SESEREQLFEDHIEE 55
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
1011-1070 |
1.07e-04 |
|
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.
Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 40.90 E-value: 1.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 1011 AKADFRTLLKETKfITYRSkkliqesdqHLKDVEKILQNDKRYLVLDcVPEERRKLIVAY 1070
Cdd:pfam01846 2 AREAFKELLKEHK-ITPYS---------TWSEIKKKIENDPRYKALL-DGSEREELFEDY 50
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
712-1066 |
1.16e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 712 EERREKKNKIMQAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSRF-----KAIEKMKDREALFNEFVAAARKKEKEDSKT 786
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELreeleKLEKEVKELEELKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 787 RGEKIKsdffelLSNhhldSQSRWSKVKDKVEsDPRYKAVDSSSMREDLfKQYIEkiaknLDSEKEKELERQARIE---A 863
Cdd:PRK03918 255 RKLEEK------IRE----LEERIEELKKEIE-ELEEKVKELKELKEKA-EEYIK-----LSEFYEEYLDELREIEkrlS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 864 SLREREREVQKARSEQTKEIDREREQHKREEAIQNFKALLSDMVRSSDvswsDTRRTLRKDHRWESGslLEREEKEKLFN 943
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE----EAKAKKEELERLKKR--LTGLTPEKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 944 EhIEALTKKKREHFRQLLdetsaiTLTSTWKEVKKIIKEDPRCIKFSSSDRKK----QREFEEYIRDKYITA-KADFRTL 1018
Cdd:PRK03918 392 E-LEELEKAKEEIEEEIS------KITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELLEEyTAELKRI 464
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2181405734 1019 LKETKFITYRSKKLIQEsdqhLKDVEKILQNDKRYLVLDCVPEERRKL 1066
Cdd:PRK03918 465 EKELKEIEEKERKLRKE----LRELEKVLKKESELIKLKELAEQLKEL 508
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
293-407 |
1.16e-04 |
|
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.
Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 46.18 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 293 AQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPTATPVQTVPQPHPQTLPPAVPHSVPQPTTAIPAFPPVMV--------- 363
Cdd:pfam09770 227 AQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVqptqilqnp 306
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2181405734 364 ---PPFRVPLPGMPIPLPGVLPG-MAPPIVPMIHPQVAIAASPATLAG 407
Cdd:pfam09770 307 nrlSAARVGYPQNPQPGVQPAPAhQAHRQQGSFGRQAPIITHPQQLAQ 354
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
295-411 |
1.27e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 45.86 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 295 TVSTPTTQDQTPSSAVSVATPTVSVSTPAPTATPVQTVP---QPHPQTLPPAVPHSVPQPTTAIPAFP------PVMVPP 365
Cdd:PRK14951 385 EAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPapvAAPAAAAPAAAPAAAPAAVALAPAPPaqaapeTVAIPV 464
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2181405734 366 FRVPLPGMPIPLPGVLPGMAPPIVPMIHPQVAIAASPATLAGATAV 411
Cdd:PRK14951 465 RVAPEPAVASAAPAPAAAPAAARLTPTEEGDVWHATVQQLAAAEAI 510
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
693-1065 |
1.88e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 693 LNPKERKQVFDQYVKTRAEEERREKKNKIMQAKEDFKKMMEEAKfnpratFSEFAAKHAKDSRfKAIEKMKDREALFNEf 772
Cdd:PTZ00121 1072 LKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEAR------KAEEAKKKAEDAR-KAEEARKAEDARKAE- 1143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 773 vaAARKKEkEDSKTRGEKIKSDFFELLSNHHLDSQSRWSKVKDKVE---SDPRYKAVDSSSMREDLFKQYIEKIAKNLDS 849
Cdd:PTZ00121 1144 --EARKAE-DAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEvrkAEELRKAEDARKAEAARKAEEERKAEEARKA 1220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 850 EKEKELERQARIEaSLREREREVQKARSEQTKEIDREREQHKREEAIQNFKALLSDMVRSSDvswsdtrrTLRK-DHRWE 928
Cdd:PTZ00121 1221 EDAKKAEAVKKAE-EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAD--------ELKKaEEKKK 1291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 929 SGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDET--SAITLTSTWKEVKKIIKEDPRCIKFSSSDRKKQREFEEYIRD 1006
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181405734 1007 KYITAKADFRTLLK--ETKFITYRSKKLIQESDQHLKDVEKILQNDKRYLVLDCVPEERRK 1065
Cdd:PTZ00121 1372 KKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK 1432
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
292-400 |
2.04e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 45.19 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 292 VAQTVSTPTTQDQTPSSAVsvATPTVSVSTPAPTATPVQTVPQPHPQTlpPAVPHSVPQPTTAIP--AFPPVMVPPFRVP 369
Cdd:PRK14950 355 VIEALLVPVPAPQPAKPTA--AAPSPVRPTPAPSTRPKAAAAANIPPK--EPVRETATPPPVPPRpvAPPVPHTPESAPK 430
|
90 100 110
....*....|....*....|....*....|.
gi 2181405734 370 LPGMPIPLPgVLPGMAPPIVPMIHPQVAIAA 400
Cdd:PRK14950 431 LTRAAIPVD-EKPKYTPPAPPKEEEKALIAD 460
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
694-1086 |
2.38e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.35 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 694 NPKERKQVFDQYVKTRAEEERREKKNKIMQAKEDfkkmmeeakfnpratfsefaakhakdsrfKAIEKMKDREALFNEFV 773
Cdd:pfam02463 151 KPERRLEIEEEAAGSRLKRKKKEALKKLIEETEN-----------------------------LAELIIDLEELKLQELK 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 774 AAARKKEKEDSKTRGEKIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKavDSSSMREDLFKQYIEKIAKNLDSEKEK 853
Cdd:pfam02463 202 LKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEE--IESSKQEIEKEEEKLAQVLKENKEEEK 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 854 ELERQARIEASLREREREVQKAR--SEQTKEIDREREQHKREEAIQNFKALLSDMVRSSDvswsdtRRTLRKDHRWESGS 931
Cdd:pfam02463 280 EKKLQEEELKLLAKEEEELKSELlkLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEE------LEKELKELEIKREA 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 932 LLEREE----KEKLFNEHIEALTKKKREHFRQLLDETSAITLTSTWKEVKKIIkedprcikfsSSDRKKQREFEEYIRDK 1007
Cdd:pfam02463 354 EEEEEEelekLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE----------AQLLLELARQLEDLLKE 423
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181405734 1008 YITAKADFrtLLKETKFITYRSKKLIQESDqHLKDVEKILQNDKRYLVLDCVPEERRKLIVAYVDDLDRRGPPPPPTAS 1086
Cdd:pfam02463 424 EKKEELEI--LEEEEESIELKQGKLTEEKE-ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERS 499
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
296-397 |
2.48e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 45.15 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 296 VSTPTTQDQTPSSAVSVATPTVSVSTPAPTATPVQTVPQPHPQT--LPPAVPHSVPQPTTAIPAFPPVMVPPFRvplpgm 373
Cdd:PRK14971 383 FTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTvsVDPPAAVPVNPPSTAPQAVRPAQFKEEK------ 456
|
90 100
....*....|....*....|....
gi 2181405734 374 PIPLPGVlPGMAPPIVPMIHPQVA 397
Cdd:PRK14971 457 KIPVSKV-SSLGPSTLRPIQEKAE 479
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
511-538 |
2.63e-04 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 39.03 E-value: 2.63e-04
10 20
....*....|....*....|....*...
gi 2181405734 511 TPWCVVWTGDERVFFYNPTTRLSMWDRP 538
Cdd:pfam00397 3 PGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| Amelogenin |
smart00818 |
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
299-404 |
3.57e-04 |
|
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.
Pssm-ID: 197891 [Multi-domain] Cd Length: 165 Bit Score: 42.47 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 299 PTTQDQTPSSAVSV--ATPTVSVSTPAPTATPVQTVPQPHPQT--------LPPAVPHSVpQPTTAIPAFPPVMVPPFRV 368
Cdd:smart00818 41 PVSQQHPPTHTLQPhhHIPVLPAQQPVVPQQPLMPVPGQHSMTptqhhqpnLPQPAQQPF-QPQPLQPPQPQQPMQPQPP 119
|
90 100 110
....*....|....*....|....*....|....*...
gi 2181405734 369 PLPGMPIPLPGVLPGMAP--PIVPMIhPQVAIAASPAT 404
Cdd:smart00818 120 VHPIPPLPPQPPLPPMFPmqPLPPLL-PDLPLEAWPAT 156
|
|
| motB |
PRK12799 |
flagellar motor protein MotB; Reviewed |
258-365 |
4.00e-04 |
|
flagellar motor protein MotB; Reviewed
Pssm-ID: 183756 [Multi-domain] Cd Length: 421 Bit Score: 44.32 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 258 ASTPTTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQdqTPSSAVSVATPTVSVSTPAPTATPVQTVPQPH- 336
Cdd:PRK12799 303 AVTPSSAVTQSSAITPSSAAIPSPAVIPSSVTTQSATTTQASAVA--LSSAGVLPSDVTLPGTVALPAAEPVNMQPQPMs 380
|
90 100 110
....*....|....*....|....*....|...
gi 2181405734 337 -PQTLPPAVPHSVP---QPTTAIPAFPPVMVPP 365
Cdd:PRK12799 381 tTETQQSSTGNITStanGPTTSLPAAPASNIPV 413
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
313-423 |
6.93e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 43.55 E-value: 6.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 313 ATPTVSVSTPAPTATPVQTVPQPHPQTLPPAVPHSVPQPTTAIPafPPVMVPPFRVPLPGMPiplpgvlPGMAPPIVPMI 392
Cdd:PRK14951 369 AAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAAS--APAAPPAAAPPAPVAA-------PAAAAPAAAPA 439
|
90 100 110
....*....|....*....|....*....|.
gi 2181405734 393 HPQVAIAASPATLAGATAVSEWTEYKTADGK 423
Cdd:PRK14951 440 AAPAAVALAPAPPAQAAPETVAIPVRVAPEP 470
|
|
| PRK10856 |
PRK10856 |
cytoskeleton protein RodZ; |
293-371 |
7.00e-04 |
|
cytoskeleton protein RodZ;
Pssm-ID: 236776 [Multi-domain] Cd Length: 331 Bit Score: 43.09 E-value: 7.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181405734 293 AQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPTATPVQTvPQPHPQTLPPAVPHSVPQPTTAIPAFPPVMVPPFRVPLP 371
Cdd:PRK10856 161 SVPLDTSTTTDPATTPAPAAPVDTTPTNSQTPAVATAPA-PAVDPQQNAVVAPSQANVDTAATPAPAAPATPDGAAPLP 238
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
262-408 |
7.05e-04 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 43.44 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 262 TTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQDQTpSSAVSVATPtVSVSTPAPTATPVQTVPQPHP---Q 338
Cdd:PRK12727 65 TAAAPAPAPQAPTKPAAPVHAPLKLSANANMSQRQRVASAAEDM-IAAMALRQP-VSVPRQAPAAAPVRAASIPSPaaqA 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 339 TLPPAVPHSVPQPTTAIPAFPPVMvppFRVPLPGMPIPLPGVLPGMAPPIVPMihpQVAIAASPATLAGA 408
Cdd:PRK12727 143 LAHAAAVRTAPRQEHALSAVPEQL---FADFLTTAPVPRAPVQAPVVAAPAPV---PAIAAALAAHAAYA 206
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
709-991 |
8.05e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.41 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 709 RAEEERREKKNKIMQAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSrfKAIEKMKDREALFNEFVAAARKKEKEDSKTRG 788
Cdd:COG5185 257 KLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYT--KSIDIKKATESLEEQLAAAEAEQELEESKRET 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 789 EKIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEKIAKNLDSekekelerqarIEASLRER 868
Cdd:COG5185 335 ETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDE-----------IPQNQRGY 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 869 EREVQKARSEQTKEIDREREQHKR---------EEAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWESGSLLEREEKE 939
Cdd:COG5185 404 AQEILATLEDTLKAADRQIEELQRqieqatssnEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDL 483
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181405734 940 --------------KLFNEHIEALTKKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCIKFSS 991
Cdd:COG5185 484 neeltqiesrvstlKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASE 549
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
292-418 |
1.27e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 43.10 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 292 VAQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPTATPVQTVPQPHPQTLPPAVPHSVPQPTTAIPAFPPVMVPPFRVPLP 371
Cdd:PRK10811 887 VVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETA 966
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2181405734 372 GMPIPLPGVLPGMAPPIVPMIHPQVAIAASPATLAGATAVSEWTEYK 418
Cdd:PRK10811 967 EVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATVEH 1013
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
258-403 |
1.34e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.94 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 258 ASTPTTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPTATP--VQTVPQP 335
Cdd:PRK12323 394 AAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPaaAGPRPVA 473
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2181405734 336 HPQTLPPAVPHSVPQPTTAIPAFPP--VMVPPFRVPLPGMPIPLP-------GVLPGMAPPIVPMIHPQVAIAASPA 403
Cdd:PRK12323 474 AAAAAAPARAAPAAAPAPADDDPPPweELPPEFASPAPAQPDAAPagwvaesIPDPATADPDDAFETLAPAPAAAPA 550
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
266-410 |
1.50e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 42.76 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 266 PAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQdQTPSSAVSVATPTVSVSTPAPTATPVQTVPQPHPQTLPPAVP 345
Cdd:PRK10263 403 PQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPE-QPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQP 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 346 HSVPQPTTAIPAFPPVMVPPFRVPLPGM-------------------PIPLPGVLPgmaPPIVPMIHPQVAIAASPATLA 406
Cdd:PRK10263 482 QPVEQQPVVEPEPVVEETKPARPPLYYFeeveekrarereqlaawyqPIPEPVKEP---EPIKSSLKAPSVAAVPPVEAA 558
|
....
gi 2181405734 407 GATA 410
Cdd:PRK10263 559 AAVS 562
|
|
| PRK13729 |
PRK13729 |
conjugal transfer pilus assembly protein TraB; Provisional |
323-392 |
1.54e-03 |
|
conjugal transfer pilus assembly protein TraB; Provisional
Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 42.50 E-value: 1.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181405734 323 APTATPVQTVPQPHPQT-LPPAVPHSVPQPTTAIPAFPP---VMVPPFRVPLPGMPIPLPgvlPGMAPPIVPMI 392
Cdd:PRK13729 122 ALGANPVTATGEPVPQMpASPPGPEGEPQPGNTPVSFPPqgsVAVPPPTAFYPGNGVTPP---PQVTYQSVPVP 192
|
|
| DUF3729 |
pfam12526 |
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ... |
306-379 |
1.61e-03 |
|
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important.
Pssm-ID: 372164 [Multi-domain] Cd Length: 115 Bit Score: 39.29 E-value: 1.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181405734 306 PSSAVSVATPTVSVSTPAPTATPVQTVPQPHPqtlpPAVPHSVPQPTTAIPAFPPVMVPPfRVPLPGMPIPLPG 379
Cdd:pfam12526 37 PDPPPPVGDPRPPVVDTPPPVSAVWVLPPPSE----PAAPEPDLVPPVTGPAGPPSPLAP-PAPAQKPPLPPPR 105
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
257-424 |
2.32e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.17 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 257 GASTPTTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPTATPVQTVPQPH 336
Cdd:PRK12323 370 GGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 337 PQTLPPAVPHSVPQPTTAIPAFPPV---MVPPFRVPlPGMPIPLPGVLPGM--APPIVPMIHPqVAIAASPATLAGATAV 411
Cdd:PRK12323 450 PAPAPAAAPAAAARPAAAGPRPVAAaaaAAPARAAP-AAAPAPADDDPPPWeeLPPEFASPAP-AQPDAAPAGWVAESIP 527
|
170
....*....|...
gi 2181405734 412 SEWTEYKTADGKT 424
Cdd:PRK12323 528 DPATADPDDAFET 540
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
295-413 |
2.32e-03 |
|
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: 42.21 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 295 TVSTPTTQDQTPSSAVSVATPTVSVSTP--------APTAT-PVQTVPQPHPQTLPPAVPHSVPQPTTAIPAFPPVM-VP 364
Cdd:pfam05109 467 TVSTADVTSPTPAGTTSGASPVTPSPSPrdngteskAPDMTsPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSpTS 546
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2181405734 365 PFRVPLPGMPIPLPGV---LPGMAPPIVPMIHPQVAIaASPATLAGATAVSE 413
Cdd:pfam05109 547 AVTTPTPNATSPTPAVttpTPNATIPTLGKTSPTSAV-TTPTPNATSPTVGE 597
|
|
| Drf_FH1 |
pfam06346 |
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ... |
299-391 |
2.84e-03 |
|
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.
Pssm-ID: 461881 [Multi-domain] Cd Length: 157 Bit Score: 39.47 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 299 PTTQDQTPSSAVSVATPTV-SVSTPAPTATP-VQTVPQPHPQTLPPAVPHSVPQP-TTAIPAFPPVMVPPfRVPLPgmPI 375
Cdd:pfam06346 22 PTPPPLPGGGGPPPPPPLPgSAAIPPPPPLPgGTSIPPPPPLPGAASIPPPPPLPgSTGIPPPPPLPGGA-GIPPP--PP 98
|
90
....*....|....*.
gi 2181405734 376 PLPGVlPGMAPPIVPM 391
Cdd:pfam06346 99 PLPGG-AGVPPPPPPL 113
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
304-403 |
2.91e-03 |
|
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: 41.68 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 304 QTPSSAVSVATPTVSVSTPAPTATPvqtvpqphpqtlPPAVPHSVPQPTtaipafPPVMVPPFRVPLPGMPIPLPGVLPG 383
Cdd:pfam03154 175 QAQSGAASPPSPPPPGTTQAATAGP------------TPSAPSVPPQGS------PATSQPPNQTQSTAAPHTLIQQTPT 236
|
90 100
....*....|....*....|
gi 2181405734 384 MAPPIVPMIHPQVAIAASPA 403
Cdd:pfam03154 237 LHPQRLPSPHPPLQPMTQPP 256
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
299-411 |
3.42e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 41.59 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 299 PTTQdQTPSSAVSVATPTVSVSTPA--PTATPVQTVP---QPHPQTLPPAVPHSVPQPTTAIPAFPPVMVPPFRVP---- 369
Cdd:PHA03378 691 PGTM-QPPPRAPTPMRPPAAPPGRAqrPAAATGRARPpaaAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARppaa 769
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2181405734 370 LPGMPIPLPgvlPGMAPPiVPMIHPQVAIAASPATLAGATAV 411
Cdd:PHA03378 770 APGAPTPQP---PPQAPP-APQQRPRGAPTPQPPPQAGPTSM 807
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
306-410 |
3.66e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 41.24 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 306 PSSAVSVATPTVSVSTPAPTATPvqtVPQPHPQTLPPAVPHSVPQPTTAIPAFPPVMVPPFRVPLPGM--PIPLPGVLPG 383
Cdd:PRK14951 367 AAAAEAAAPAEKKTPARPEAAAP---AAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAaaPAAAPAAAPA 443
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2181405734 384 MAPP--------------IVPMIHPQVAIAASPATLAGATA 410
Cdd:PRK14951 444 AVALapappaqaapetvaIPVRVAPEPAVASAAPAPAAAPA 484
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
712-1046 |
3.69e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 712 EERREKKNKIMQAKEDFKKMMEE-AKFNPRA-TFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEK--EDSKTR 787
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRlEELEERHeLYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEieEEISKI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 788 GEKIKSdfFELLSNHHLDSQSRWSKVKDKVesdPRYKAVDSSSMREDLFKQYIEKIAKnldseKEKELERQARIEASLRE 867
Cdd:PRK03918 411 TARIGE--LKKEIKELKKAIEELKKAKGKC---PVCGRELTEEHRKELLEEYTAELKR-----IEKELKEIEEKERKLRK 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 868 REREVQKARS------------EQTKEIDREREQHKREEAIQNFKALLSDMVRSsdvswsdtrRTLRKDHRwesgSLLER 935
Cdd:PRK03918 481 ELRELEKVLKkeseliklkelaEQLKELEEKLKKYNLEELEKKAEEYEKLKEKL---------IKLKGEIK----SLKKE 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 936 EEKEKLFNEHIEALTKKKREHFRQLldetsaitltstwKEVKKIIKEdprcIKFSSSD--RKKQREFEEYIRdKYIT--- 1010
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELEEEL-------------AELLKELEE----LGFESVEelEERLKELEPFYN-EYLElkd 609
|
330 340 350
....*....|....*....|....*....|....*.
gi 2181405734 1011 AKADFRTLLKETKFITYRSKKLIQESDQHLKDVEKI 1046
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
840-1049 |
3.91e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 840 IEKIAKNLDSEKEKELERQARIEASLREREREVQKARSEQT---KEIDREREQ-HKREEAIQNFKALLSD-MVRSSDVSW 914
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleARIEELEEDlHKLEEALNDLEARLSHsRIPEIQAEL 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 915 SDtrrtLRKDHRWESGSL--LEREEKEKLFNEHIEaltKKKREHFRQLLDEtsaitLTSTWKEVKKIIKEDPRCIKFSSS 992
Cdd:TIGR02169 801 SK----LEEEVSRIEARLreIEQKLNRLTLEKEYL---EKEIQELQEQRID-----LKEQIKSIEKEIENLNGKKEELEE 868
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 993 DRKKQREFEEYIRDKYITAKADFRTLLKETKFITYRSKKL---IQESDQHLKDVEKILQN 1049
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELeaqIEKKRKRLSELKAKLEA 928
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
832-963 |
4.26e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 832 REDLFKQYIEKIAKNLDSEKEKELERQARIEAsLREREREVQKARSEQ--------TKEIDR-EREQHKREEAIQNFKAL 902
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDA-LREELDELEAQIRGNggdrleqlEREIERlERELEERERRRARLEAL 367
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181405734 903 LSDMvrssDVSWSDTRRTLRKDHRwESGSLLER--EEKEKLFNEHIEALTKKK--REHFRQLLDE 963
Cdd:COG4913 368 LAAL----GLPLPASAEEFAALRA-EAAALLEAleEELEALEEALAEAEAALRdlRRELRELEAE 427
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
532-908 |
4.37e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 532 LSMWDR----PDDLIGRADVDKiiqepphkKGMEELKKLRHPTPTMLSIQ-------------KWQFSmSAIKEEQELME 594
Cdd:pfam02463 148 AMMKPErrleIEEEAAGSRLKR--------KKKEALKKLIEETENLAELIidleelklqelklKEQAK-KALEYYQLKEK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 595 EINEDEpvkAKKRKRMSKKSFMWIARASLFRRDDNKDIDSEKEAAMEAEIKAARERAIVPLEARMKQFKDMLLERGVSAF 674
Cdd:pfam02463 219 LELEEE---YLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 675 STWEKELHKIVfdpryLLLNPKERKQVFDQYVKTRAEEErrekKNKIMQAKEDFKKMMEE--AKFNPRATFSEFAAKHAK 752
Cdd:pfam02463 296 EELKSELLKLE-----RRKVDDEEKLKESEKEKKKAEKE----LKKEKEEIEELEKELKEleIKREAEEEEEEELEKLQE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 753 DSRFKAIEKMKDREALFNEFVAAARKKEKEDS-KTRGEKIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSssm 831
Cdd:pfam02463 367 KLEQLEEELLAKKKLESERLSSAAKLKEEELElKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ--- 443
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2181405734 832 REDLFKQYIEKIAKNLDSEKEKELERQARIEAslREREREVQKARSEQTKEIDREREQHKREEAIQNFKALLSDMVR 908
Cdd:pfam02463 444 GKLTEEKEELEKQELKLLKDELELKKSEDLLK--ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKD 518
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
292-410 |
4.91e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.12 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 292 VAQTVSTPTTQDQTPSSAVSVATPTvsvstPAPTATPVQTVPQPHPQTLPPAVPHSVPQPTTAIPAFPPVMVPPFRVPLP 371
Cdd:PRK07764 387 VAGGAGAPAAAAPSAAAAAPAAAPA-----PAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAA 461
|
90 100 110
....*....|....*....|....*....|....*....
gi 2181405734 372 GMPIPLPGVLPGMAPPIVPMIHPQVAIAASPATLAGATA 410
Cdd:PRK07764 462 PSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAP 500
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
293-416 |
7.51e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.35 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 293 AQTVSTPTTQDQTPSSAvSVATPTVSVSTPAPTATPvQTVPQPHPQTLPPAVPHS----VPQPTTAIPAFPPVMVPPFRV 368
Cdd:PRK07764 395 AAAAPSAAAAAPAAAPA-PAAAAPAAAAAPAPAAAP-QPAPAPAPAPAPPSPAGNapagGAPSPPPAAAPSAQPAPAPAA 472
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2181405734 369 PLPGMPIPLPGVLPGMAPPIVPMIhPQVAiAASPATLAGATAVSEWTE 416
Cdd:PRK07764 473 APEPTAAPAPAPPAAPAPAAAPAA-PAAP-AAPAGADDAATLRERWPE 518
|
|
| PRK14959 |
PRK14959 |
DNA polymerase III subunits gamma and tau; Provisional |
293-374 |
8.01e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 40.05 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 293 AQTVSTPTTQ-DQTPSSAVSVATPTVSVSTPAPTATPVQTVPQphpQTLPPAVPHSvpqpttAIPAFPPVMVPPfRVPLP 371
Cdd:PRK14959 394 AATIPTPGTQgPQGTAPAAGMTPSSAAPATPAPSAAPSPRVPW---DDAPPAPPRS------GIPPRPAPRMPE-ASPVP 463
|
...
gi 2181405734 372 GMP 374
Cdd:PRK14959 464 GAP 466
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
293-375 |
8.29e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 40.14 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 293 AQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPTATPVQ-TVPQPHPQTLPPavPHSVPQPTTAIPAFPPVMVPPFRVPLP 371
Cdd:PRK14971 389 APQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTvSVDPPAAVPVNP--PSTAPQAVRPAQFKEEKKIPVSKVSSL 466
|
....
gi 2181405734 372 GMPI 375
Cdd:PRK14971 467 GPST 470
|
|
| Drf_FH1 |
pfam06346 |
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ... |
315-387 |
8.31e-03 |
|
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.
Pssm-ID: 461881 [Multi-domain] Cd Length: 157 Bit Score: 38.31 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 315 PTVSVSTPAPTATPVQTVPQPHPQTLPPAVPHSVPQPTTA-IPAFPP-----VMVPPFRVPLPG-----MPIPLPGVlPG 383
Cdd:pfam06346 52 PGGTSIPPPPPLPGAASIPPPPPLPGSTGIPPPPPLPGGAgIPPPPPplpggAGVPPPPPPLPGgpgipPPPPFPGG-PG 130
|
....
gi 2181405734 384 MAPP 387
Cdd:pfam06346 131 IPPP 134
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
829-914 |
8.69e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 40.24 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181405734 829 SSMREDLFKQYiekiaknLDSEKEKELERQARIEASlREREREVQKARSEQTKEIDREREQHKREEAIQNFKA--LLSDM 906
Cdd:PLN02316 239 GGMDEHSFEDF-------LLEEKRRELEKLAKEEAE-RERQAEEQRRREEEKAAMEADRAQAKAEVEKRREKLqnLLKKA 310
|
....*...
gi 2181405734 907 VRSSDVSW 914
Cdd:PLN02316 311 SRSADNVW 318
|
|
| |
