|
Name |
Accession |
Description |
Interval |
E-value |
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
421-1035 |
1.78e-23 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 106.32 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 421 ASPATLAGATAVSEWTEYKTADGKTYYYNNRTLESTWEKPQElkekekleekikepIKEPSEEPLPMEteeedpkeepik 500
Cdd:COG5104 3 AALLGMASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPKE--------------LLKGSEEDLDVD------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 501 eikeepkeeemteeekaaqkakpvatapipgtPWCVVWTGDERVFFYNPTTRLSMWDRpddligradvdkiiqePPHKKG 580
Cdd:COG5104 57 --------------------------------PWKECRTADGKVYYYNSITRESRWKI----------------PPERKK 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 581 MEELKKLRHPTPTMLSIQKWQFSMSAIkEEQELMEEINEDepvkakkrkrmskksfmwiaraslfrrddnkdidsEKEAA 660
Cdd:COG5104 89 VEPIAEQKHDERSMIGGNGNDMAITDH-ETSEPKYLLGRL-----------------------------------MSQYG 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 661 MEAEIKAARERAivpLEARMKQFKDMLLERGVSAFSTWEKELHKIVfDPRYLLL--NPKERKQVFDQYVKTRAEEERREK 738
Cdd:COG5104 133 ITSTKDAVYRLT---KEEAEKEFITMLKENQVDSTWPIFRAIEELR-DPRYWMVdtDPLWRKDLFKKYFENQEKDQREEE 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 739 KNKIMQAKEDFKKMME-EAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEKEDSKTRGEKIKSDFF 817
Cdd:COG5104 209 ENKQRKYINEFCKMLAgNSHIKYYTDWFTFKSIFSKHPYYSSVVNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLE 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 818 ELLSNHHLDSQSRWSKVKDKVESDPRYKAvdSSSM----REDLFKQYIeKIAKNLdsekekelerqarieaslrerEREV 893
Cdd:COG5104 289 EVLRSLGSETFIIWLLNHYVFDSVVRYLK--NKEMkpldRKDILFSFI-RYVRRL---------------------EKEL 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 894 QKARSEQTKEIDReREQHKREeaiqNFKALLSDMVRSSDVS----WSDTRRTLRKDHRWESGSLLEREEKEKLFNEHIEA 969
Cdd:COG5104 345 LSAIEERKAAAAQ-NARHHRD----EFRTLLRKLYSEGKIYyrmkWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVD 419
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841659210 970 LTKKKREHFRQLLDETSaITLTSTW--KEVKKIIKEDPRciKFSSSDRKKQREFEE---YIRDKYITAKAD 1035
Cdd:COG5104 420 LENMYGFARRSYERETR-TGQISPTdrRAVDEIFEAIAE--KKEEGEIKFDKVDKEdisLIVDGLIKQRNE 487
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
811-860 |
4.24e-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: 67.48 E-value: 4.24e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1841659210 811 KIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQY 860
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
972-1027 |
2.81e-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: 56.81 E-value: 2.81e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1841659210 972 KKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCiKFSSSDRKKQREFEEYIRD 1027
Cdd:smart00441 1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRY-KALLSESEREQLFEDHIEE 55
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
433-460 |
2.71e-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: 50.60 E-value: 2.71e-08
10 20
....*....|....*....|....*...
gi 1841659210 433 SEWTEYKTADGKTYYYNNRTLESTWEKP 460
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 |
7.56e-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: 7.56e-08
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
132-164 |
7.89e-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: 7.89e-08
10 20 30
....*....|....*....|....*....|...
gi 1841659210 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 |
1.99e-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: 1.99e-07
10 20
....*....|....*....|....*...
gi 1841659210 137 WVENKTPDGKVYYYNARTRESAWTKPDG 164
Cdd:cd00201 4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
260-365 |
3.98e-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: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 260 TPTTSSPAPAVSTStssstpssttsttttatsvAQTVSTPTTQDQTPSSAVSVATP-----TVSVSTPAPTAT------- 327
Cdd:pfam05109 517 TPNATSPTPAVTTP-------------------TPNATSPTLGKTSPTSAVTTPTPnatspTPAVTTPTPNATiptlgkt 577
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1841659210 328 -PVQTVPQPHPQTLPPAVPHSVPQPTT------AIPAFPPVMVPP 365
Cdd:pfam05109 578 sPTSAVTTPTPNATSPTVGETSPQANTtnhtlgGTSSTPVVTSPP 622
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
727-1067 |
5.23e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 727 VKTRAEEERR--EKKNKIMQAK--EDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREAlfNEFVAAARKKEK 802
Cdd:PTZ00121 1423 AKKKAEEKKKadEAKKKAEEAKkaDEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA--KKKAEEAKKKAD 1500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 803 EDSKTRGEKIKSDffELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEKIAKNLDSEKEKELERQARI 882
Cdd:PTZ00121 1501 EAKKAAEAKKKAD--EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 883 EASLREREREVQKARSEQTKEIDREREQHKREEAiqnfKALLSDMVRSSDVSWSDTRRtlRKDHRWESGSLLEREEKEKL 962
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEELKKAEEEK--KKVEQLKKKEAEEKKKAEEL 1652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 963 FNEHIEALTKKKREHFRQLLDETSAitltstwKEVKKIIKEDPRCIKFSSSDRKKQREFEEyIRDKYITAKADFRTLLKE 1042
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKKA-------EEAKKAEEDEKKAAEALKKEAEEAKKAEE-LKKKEAEEKKKAEELKKA 1724
|
330 340
....*....|....*....|....*
gi 1841659210 1043 TKFITYRSKKLIQESDQHLKDVEKI 1067
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEEA 1749
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
136-173 |
1.24e-05 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 49.31 E-value: 1.24e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1841659210 136 IWVENKTPDGKVYYYNARTRESAWTKPDgvKVIQQSEL 173
Cdd:COG5104 16 EWEELKAPDGRIYYYNKRTGKSSWEKPK--ELLKGSEE 51
|
|
| PRK13729 |
PRK13729 |
conjugal transfer pilus assembly protein TraB; Provisional |
323-413 |
2.91e-05 |
|
conjugal transfer pilus assembly protein TraB; Provisional
Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 47.90 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 323 APTATPVQTVPQPHPQT-LPPAVPHSVPQPTTAIPAFPP---VMVPPFRVPLPGMPIPLPGVamMQIVSCPYVKTVATTK 398
Cdd:PRK13729 122 ALGANPVTATGEPVPQMpASPPGPEGEPQPGNTPVSFPPqgsVAVPPPTAFYPGNGVTPPPQ--VTYQSVPVPNRIQRKT 199
|
90
....*....|....*
gi 1841659210 399 TGVLPGMAPPIVPMI 413
Cdd:PRK13729 200 FTYNEGKKGPSLPYI 214
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
258-434 |
3.13e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 47.95 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 258 ASTPTTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPTATP--VQTVPQP 335
Cdd:PRK12323 394 AAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPaaAGPRPVA 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 336 HPQTLPPAVPHSVPQPTTAIPAFPPVMVPPFRVPLPGMPIPLPGVAMMQIVSCPYVKTVATTKTGVLPGMAPPIVPMihP 415
Cdd:PRK12323 474 AAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPA--P 551
|
170
....*....|....*....
gi 1841659210 416 QVAIAASPATLAGATAVSE 434
Cdd:PRK12323 552 RAAAATEPVVAPRPPRASA 570
|
|
| KLF3_N |
cd21577 |
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ... |
306-390 |
5.86e-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: 45.41 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 306 PSSAVSVATPTVSVSTPAPTATPvqtvPQPHPQTLPPAvPHSVPQPTTAIPaFPPVMVPPFRVPL--PGMPIPLPGVaMM 383
Cdd:cd21577 33 PSSSSSSSSSSSSSSSPSSRASP----PSPYSKSSPPS-PPQQRPLSPPLS-LPPPVAPPPLSPGsvPGGLPVISPV-MV 105
|
....*..
gi 1841659210 384 QIVSCPY 390
Cdd:cd21577 106 QPVPVLY 112
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
1030-1094 |
7.03e-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: 41.41 E-value: 7.03e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1841659210 1030 ITAKADFRTLLKETKFITYrskkliqesDQHLKDVEKILQNDKRYLVLDcVPEERRKLIVAYVDD 1094
Cdd:smart00441 1 EEAKEAFKELLKEHEVITP---------DTTWSEARKKLKNDPRYKALL-SESEREQLFEDHIEE 55
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
1032-1091 |
7.63e-05 |
|
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: 41.29 E-value: 7.63e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 1032 AKADFRTLLKETKfITYRSkkliqesdqHLKDVEKILQNDKRYLVLDcVPEERRKLIVAY 1091
Cdd:pfam01846 2 AREAFKELLKEHK-ITPYS---------TWSEIKKKIENDPRYKALL-DGSEREELFEDY 50
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
861-1070 |
2.49e-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: 41.98 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 861 IEKIAKNLDSEKEKELERQARIEASLREREREVQKARSEQT---KEIDREREQ-HKREEAIQNFKALLSD-MVRSSDVSW 935
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleARIEELEEDlHKLEEALNDLEARLSHsRIPEIQAEL 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 936 SDtrrtLRKDHRWESGSL--LEREEKEKLFNEHIEaltKKKREHFRQLLDEtsaitLTSTWKEVKKIIKEDPRCIKFSSS 1013
Cdd:TIGR02169 801 SK----LEEEVSRIEARLreIEQKLNRLTLEKEYL---EKEIQELQEQRID-----LKEQIKSIEKEIENLNGKKEELEE 868
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 1014 DRKKQREFEEYIRDKYITAKADFRTLLKETKFITYRSKKL---IQESDQHLKDVEKILQN 1070
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELeaqIEKKRKRLSELKAKLEA 928
|
|
| half-pint |
TIGR01645 |
poly-U binding splicing factor, half-pint family; The proteins represented by this model ... |
297-434 |
5.21e-03 |
|
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: 40.82 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 297 STPTTQDQTPSSAVSvATPTvSVSTPaPTATPVQTVPQPHPqTLPPAVPHSVPqpttaipafPPVMVPPFRVPLPGMPIP 376
Cdd:TIGR01645 322 AVLGPRAQSPATPSS-SLPT-DIGNK-AVVSSAKKEAEEVP-PLPQAAPAVVK---------PGPMEIPTPVPPPGLAIP 388
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841659210 377 LpGVAMMQIVScpyvktvattKTGVLPG-MAPPIVPMIHPQVAIAASP--ATLAGATAVSE 434
Cdd:TIGR01645 389 S-LVAPPGLVA----------PTEINPSfLASPRKKMKREKLPVTFGAldDTLAWKEPSKE 438
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
421-1035 |
1.78e-23 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 106.32 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 421 ASPATLAGATAVSEWTEYKTADGKTYYYNNRTLESTWEKPQElkekekleekikepIKEPSEEPLPMEteeedpkeepik 500
Cdd:COG5104 3 AALLGMASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPKE--------------LLKGSEEDLDVD------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 501 eikeepkeeemteeekaaqkakpvatapipgtPWCVVWTGDERVFFYNPTTRLSMWDRpddligradvdkiiqePPHKKG 580
Cdd:COG5104 57 --------------------------------PWKECRTADGKVYYYNSITRESRWKI----------------PPERKK 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 581 MEELKKLRHPTPTMLSIQKWQFSMSAIkEEQELMEEINEDepvkakkrkrmskksfmwiaraslfrrddnkdidsEKEAA 660
Cdd:COG5104 89 VEPIAEQKHDERSMIGGNGNDMAITDH-ETSEPKYLLGRL-----------------------------------MSQYG 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 661 MEAEIKAARERAivpLEARMKQFKDMLLERGVSAFSTWEKELHKIVfDPRYLLL--NPKERKQVFDQYVKTRAEEERREK 738
Cdd:COG5104 133 ITSTKDAVYRLT---KEEAEKEFITMLKENQVDSTWPIFRAIEELR-DPRYWMVdtDPLWRKDLFKKYFENQEKDQREEE 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 739 KNKIMQAKEDFKKMME-EAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEKEDSKTRGEKIKSDFF 817
Cdd:COG5104 209 ENKQRKYINEFCKMLAgNSHIKYYTDWFTFKSIFSKHPYYSSVVNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLE 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 818 ELLSNHHLDSQSRWSKVKDKVESDPRYKAvdSSSM----REDLFKQYIeKIAKNLdsekekelerqarieaslrerEREV 893
Cdd:COG5104 289 EVLRSLGSETFIIWLLNHYVFDSVVRYLK--NKEMkpldRKDILFSFI-RYVRRL---------------------EKEL 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 894 QKARSEQTKEIDReREQHKREeaiqNFKALLSDMVRSSDVS----WSDTRRTLRKDHRWESGSLLEREEKEKLFNEHIEA 969
Cdd:COG5104 345 LSAIEERKAAAAQ-NARHHRD----EFRTLLRKLYSEGKIYyrmkWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVD 419
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841659210 970 LTKKKREHFRQLLDETSaITLTSTW--KEVKKIIKEDPRciKFSSSDRKKQREFEE---YIRDKYITAKAD 1035
Cdd:COG5104 420 LENMYGFARRSYERETR-TGQISPTdrRAVDEIFEAIAE--KKEEGEIKFDKVDKEdisLIVDGLIKQRNE 487
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
811-860 |
4.24e-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: 67.48 E-value: 4.24e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1841659210 811 KIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQY 860
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
744-793 |
4.74e-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: 61.70 E-value: 4.74e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1841659210 744 QAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEF 793
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
972-1027 |
2.81e-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: 56.81 E-value: 2.81e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1841659210 972 KKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCiKFSSSDRKKQREFEEYIRD 1027
Cdd:smart00441 1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRY-KALLSESEREQLFEDHIEE 55
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
679-726 |
3.33e-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: 56.31 E-value: 3.33e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1841659210 679 RMKQFKDMLLERGVSAFSTWEKELHKIVFDPRYL-LLNPKERKQVFDQY 726
Cdd:pfam01846 2 AREAFKELLKEHKITPYSTWSEIKKKIENDPRYKaLLDGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
810-863 |
6.03e-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: 55.66 E-value: 6.03e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1841659210 810 EKIKSDFFELLSNHHLD-SQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEK 863
Cdd:smart00441 1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
915-966 |
1.19e-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: 54.77 E-value: 1.19e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1841659210 915 EAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWEsgSLLEREEKEKLFNEH 966
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYK--ALLDGSEREELFEDY 50
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
433-460 |
2.71e-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: 50.60 E-value: 2.71e-08
10 20
....*....|....*....|....*...
gi 1841659210 433 SEWTEYKTADGKTYYYNNRTLESTWEKP 460
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDP 29
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
433-460 |
4.41e-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: 4.41e-08
10 20
....*....|....*....|....*...
gi 1841659210 433 SEWTEYKTADGKTYYYNNRTLESTWEKP 460
Cdd:pfam00397 3 PGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
743-796 |
5.50e-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: 50.26 E-value: 5.50e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1841659210 743 MQAKEDFKKMMEEAKFN-PRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAA 796
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 |
7.56e-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: 7.56e-08
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
132-164 |
7.89e-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: 7.89e-08
10 20 30
....*....|....*....|....*....|...
gi 1841659210 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 ... |
973-1024 |
1.22e-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: 48.99 E-value: 1.22e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1841659210 973 KKREHFRQLLDETSaITLTSTWKEVKKIIKEDPRCIKFSSSDRKKQrEFEEY 1024
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 ... |
435-461 |
1.61e-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: 1.61e-07
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
137-164 |
1.99e-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: 1.99e-07
10 20
....*....|....*....|....*...
gi 1841659210 137 WVENKTPDGKVYYYNARTRESAWTKPDG 164
Cdd:cd00201 4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
914-969 |
9.91e-07 |
|
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: 46.80 E-value: 9.91e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1841659210 914 EEAIQNFKALLSDMVRS-SDVSWSDTRRTLRKDHRWESgsLLEREEKEKLFNEHIEA 969
Cdd:smart00441 1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKA--LLSESEREQLFEDHIEE 55
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
677-728 |
2.70e-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: 45.64 E-value: 2.70e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1841659210 677 EARMKQFKDMLLERGVS-AFSTWEKELHKIVFDPRY-LLLNPKERKQVFDQYVK 728
Cdd:smart00441 1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYkALLSESEREQLFEDHIE 54
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
260-365 |
3.98e-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: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 260 TPTTSSPAPAVSTStssstpssttsttttatsvAQTVSTPTTQDQTPSSAVSVATP-----TVSVSTPAPTAT------- 327
Cdd:pfam05109 517 TPNATSPTPAVTTP-------------------TPNATSPTLGKTSPTSAVTTPTPnatspTPAVTTPTPNATiptlgkt 577
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1841659210 328 -PVQTVPQPHPQTLPPAVPHSVPQPTT------AIPAFPPVMVPP 365
Cdd:pfam05109 578 sPTSAVTTPTPNATSPTVGETSPQANTtnhtlgGTSSTPVVTSPP 622
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
727-1067 |
5.23e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 727 VKTRAEEERR--EKKNKIMQAK--EDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREAlfNEFVAAARKKEK 802
Cdd:PTZ00121 1423 AKKKAEEKKKadEAKKKAEEAKkaDEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA--KKKAEEAKKKAD 1500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 803 EDSKTRGEKIKSDffELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEKIAKNLDSEKEKELERQARI 882
Cdd:PTZ00121 1501 EAKKAAEAKKKAD--EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 883 EASLREREREVQKARSEQTKEIDREREQHKREEAiqnfKALLSDMVRSSDVSWSDTRRtlRKDHRWESGSLLEREEKEKL 962
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEELKKAEEEK--KKVEQLKKKEAEEKKKAEEL 1652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 963 FNEHIEALTKKKREHFRQLLDETSAitltstwKEVKKIIKEDPRCIKFSSSDRKKQREFEEyIRDKYITAKADFRTLLKE 1042
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKKA-------EEAKKAEEDEKKAAEALKKEAEEAKKAEE-LKKKEAEEKKKAEELKKA 1724
|
330 340
....*....|....*....|....*
gi 1841659210 1043 TKFITYRSKKLIQESDQHLKDVEKI 1067
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEEA 1749
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
718-968 |
8.31e-06 |
|
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: 50.12 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 718 ERKQVfDQYVKTRAEEERREKKNKIMQAKEdfKKMMEEAKFNPRATFSEFAAKHAKDSRFkAIEKMKDREALFNEfvaaa 797
Cdd:pfam17380 286 ERQQQ-EKFEKMEQERLRQEKEEKAREVER--RRKLEEAEKARQAEMDRQAAIYAEQERM-AMERERELERIRQE----- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 798 rKKEKEDSKTRGEKIKSDFFEL--LSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMRE-DLFKQYIEKIaknldsEKEK 874
Cdd:pfam17380 357 -ERKRELERIRQEEIAMEISRMreLERLQMERQQKNERVRQELEAARKVKILEEERQRKiQQQKVEMEQI------RAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 875 ELERQARIEASLREREREVQKARSEQ---TKEIDREREQhkrEEAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWESG 951
Cdd:pfam17380 430 EEARQREVRRLEEERAREMERVRLEEqerQQQVERLRQQ---EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQ 506
|
250
....*....|....*..
gi 1841659210 952 SLLEREEKEKLFNEHIE 968
Cdd:pfam17380 507 AMIEEERKRKLLEKEME 523
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
298-431 |
1.10e-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: 49.53 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 298 TPTTQDQ-TPSSAVSVATPTVSVSTPAPTAT-PVQTVPQPHPQTLPPAVPHSVPQPTTAIPafppvmVPPFRVPLPGMPI 375
Cdd:pfam05109 491 SPSPRDNgTESKAPDMTSPTSAVTTPTPNATsPTPAVTTPTPNATSPTLGKTSPTSAVTTP------TPNATSPTPAVTT 564
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1841659210 376 PLPGvAMMQIVSCPYVKTVATTKTgvlPGMAPPIVPMIHPQVaiAASPATLAGATA 431
Cdd:pfam05109 565 PTPN-ATIPTLGKTSPTSAVTTPT---PNATSPTVGETSPQA--NTTNHTLGGTSS 614
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
136-173 |
1.24e-05 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 49.31 E-value: 1.24e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1841659210 136 IWVENKTPDGKVYYYNARTRESAWTKPDgvKVIQQSEL 173
Cdd:COG5104 16 EWEELKAPDGRIYYYNKRTGKSSWEKPK--ELLKGSEE 51
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
533-561 |
1.34e-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: 1.34e-05
10 20
....*....|....*....|....*....
gi 1841659210 533 PWCVVWTGDERVFFYNPTTRLSMWDRPDD 561
Cdd:smart00456 5 GWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
532-561 |
2.29e-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: 2.29e-05
10 20 30
....*....|....*....|....*....|
gi 1841659210 532 TPWCVVWTGDERVFFYNPTTRLSMWDRPDD 561
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| PRK13729 |
PRK13729 |
conjugal transfer pilus assembly protein TraB; Provisional |
323-413 |
2.91e-05 |
|
conjugal transfer pilus assembly protein TraB; Provisional
Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 47.90 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 323 APTATPVQTVPQPHPQT-LPPAVPHSVPQPTTAIPAFPP---VMVPPFRVPLPGMPIPLPGVamMQIVSCPYVKTVATTK 398
Cdd:PRK13729 122 ALGANPVTATGEPVPQMpASPPGPEGEPQPGNTPVSFPPqgsVAVPPPTAFYPGNGVTPPPQ--VTYQSVPVPNRIQRKT 199
|
90
....*....|....*
gi 1841659210 399 TGVLPGMAPPIVPMI 413
Cdd:PRK13729 200 FTYNEGKKGPSLPYI 214
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
258-434 |
3.13e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 47.95 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 258 ASTPTTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPTATP--VQTVPQP 335
Cdd:PRK12323 394 AAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPaaAGPRPVA 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 336 HPQTLPPAVPHSVPQPTTAIPAFPPVMVPPFRVPLPGMPIPLPGVAMMQIVSCPYVKTVATTKTGVLPGMAPPIVPMihP 415
Cdd:PRK12323 474 AAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPA--P 551
|
170
....*....|....*....
gi 1841659210 416 QVAIAASPATLAGATAVSE 434
Cdd:PRK12323 552 RAAAATEPVVAPRPPRASA 570
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
258-425 |
3.55e-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: 47.65 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 258 ASTPTTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQDQTPSSAVSVATPTVSV-------STPAP------ 324
Cdd:pfam17823 165 ASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGISTAATATGHPAAGTalaavgnSSPAAgtvtaa 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 325 -----------TATPVQTVP---------QPHPQTLPPAvpHSVPQPTTAIPAFPP-----------VMVPPFRVPLPGM 373
Cdd:pfam17823 245 vgtvtpaalatLAAAAGTVAsaagtinmgDPHARRLSPA--KHMPSDTMARNPAAPmgaqaqgpiiqVSTDQPVHNTAGE 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841659210 374 PIPLPGVAMMQIVSCPYVKT-----VATTKTGVLPGMAPPiVPMIH----PQVAiAASPAT 425
Cdd:pfam17823 323 PTPSPSNTTLEPNTPKSVAStnlavVTTTKAQAKEPSASP-VPVLHtsmiPEVE-ATSPTT 381
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
730-999 |
3.61e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 730 RAEEERR--EKKNKIMQAK--EDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEKEDS 805
Cdd:PTZ00121 1297 KAEEKKKadEAKKKAEEAKkaDEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 806 KTRGEKIKSDFFELLSNHHLDSQSRwskvKDKVESDPRYKAVDSSSMREDLfKQYIEKIAKNLDSEKEKELERQARieaS 885
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAE----EDKKKADELKKAAAAKKKADEA-KKKAEEKKKADEAKKKAEEAKKAD---E 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 886 LREREREVQKARSEQTKEIDREREQHKREEAIQNFKAllSDMVRSSDVSWSDTRRTLRKDHRWESGSLLEREEKEKLFNE 965
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA--DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
250 260 270
....*....|....*....|....*....|....
gi 1841659210 966 HIEALTKKKREHFRQLLDETSAITLTSTwKEVKK 999
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELKKA-EELKK 1559
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
137-172 |
5.38e-05 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 47.38 E-value: 5.38e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1841659210 137 WVENKTPDGKVYYYNARTRESAWTKPDGVKVIQQSE 172
Cdd:COG5104 58 WKECRTADGKVYYYNSITRESRWKIPPERKKVEPIA 93
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
733-1087 |
5.51e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 733 EERREKKNKIMQAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSRF-----KAIEKMKDREALFNEFVAAARKKEKEDSKT 807
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELreeleKLEKEVKELEELKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 808 RGEKIKsdffelLSNhhldSQSRWSKVKDKVEsDPRYKAVDSSSMREDLfKQYIEkiaknLDSEKEKELERQARIE---A 884
Cdd:PRK03918 255 RKLEEK------IRE----LEERIEELKKEIE-ELEEKVKELKELKEKA-EEYIK-----LSEFYEEYLDELREIEkrlS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 885 SLREREREVQKARSEQTKEIDREREQHKREEAIQNFKALLSDMVRSSDvswsDTRRTLRKDHRWESGslLEREEKEKLFN 964
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE----EAKAKKEELERLKKR--LTGLTPEKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 965 EhIEALTKKKREHFRQLLdetsaiTLTSTWKEVKKIIKEDPRCIKFSSSDRKK----QREFEEYIRDKYITA-KADFRTL 1039
Cdd:PRK03918 392 E-LEELEKAKEEIEEEIS------KITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELLEEyTAELKRI 464
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1841659210 1040 LKETKFITYRSKKLIQEsdqhLKDVEKILQNDKRYLVLDCVPEERRKL 1087
Cdd:PRK03918 465 EKELKEIEEKERKLRKE----LRELEKVLKKESELIKLKELAEQLKEL 508
|
|
| KLF3_N |
cd21577 |
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ... |
306-390 |
5.86e-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: 45.41 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 306 PSSAVSVATPTVSVSTPAPTATPvqtvPQPHPQTLPPAvPHSVPQPTTAIPaFPPVMVPPFRVPL--PGMPIPLPGVaMM 383
Cdd:cd21577 33 PSSSSSSSSSSSSSSSPSSRASP----PSPYSKSSPPS-PPQQRPLSPPLS-LPPPVAPPPLSPGsvPGGLPVISPV-MV 105
|
....*..
gi 1841659210 384 QIVSCPY 390
Cdd:cd21577 106 QPVPVLY 112
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
1030-1094 |
7.03e-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: 41.41 E-value: 7.03e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1841659210 1030 ITAKADFRTLLKETKFITYrskkliqesDQHLKDVEKILQNDKRYLVLDcVPEERRKLIVAYVDD 1094
Cdd:smart00441 1 EEAKEAFKELLKEHEVITP---------DTTWSEARKKLKNDPRYKALL-SESEREQLFEDHIEE 55
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
1032-1091 |
7.63e-05 |
|
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: 41.29 E-value: 7.63e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 1032 AKADFRTLLKETKfITYRSkkliqesdqHLKDVEKILQNDKRYLVLDcVPEERRKLIVAY 1091
Cdd:pfam01846 2 AREAFKELLKEHK-ITPYS---------TWSEIKKKIENDPRYKALL-DGSEREELFEDY 50
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
306-424 |
7.97e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 46.63 E-value: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 306 PSSAVSVATPTVSVSTPAPTATPVqtVPQPHPQTLPPAVPHSVPQPTTAIPAFPPVMVPPFRVPLPGM--PIPLPGVAMM 383
Cdd:PRK14951 366 PAAAAEAAAPAEKKTPARPEAAAP--AAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAaaPAAAPAAAPA 443
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1841659210 384 QIVSCPYVKTVATTKTGVLPGMAPPIVPMIHPQVAIAASPA 424
Cdd:PRK14951 444 AVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPA 484
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
295-381 |
1.12e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 46.25 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 295 TVSTPTTQDQTPSSAVSVATPTVSVSTPAPTATPVQTVP---QPHPQTLPPAVPHSVPQPtTAIPAFPPVMVPPFRVPLP 371
Cdd:PRK14951 385 EAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPapvAAPAAAAPAAAPAAAPAA-VALAPAPPAQAAPETVAIP 463
|
90
....*....|
gi 1841659210 372 GMPIPLPGVA 381
Cdd:PRK14951 464 VRVAPEPAVA 473
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
715-1107 |
1.14e-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: 46.50 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 715 NPKERKQVFDQYVKTRAEEERREKKNKIMQAKEDfkkmmeeakfnpratfsefaakhakdsrfKAIEKMKDREALFNEFV 794
Cdd:pfam02463 151 KPERRLEIEEEAAGSRLKRKKKEALKKLIEETEN-----------------------------LAELIIDLEELKLQELK 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 795 AAARKKEKEDSKTRGEKIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKavDSSSMREDLFKQYIEKIAKNLDSEKEK 874
Cdd:pfam02463 202 LKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEE--IESSKQEIEKEEEKLAQVLKENKEEEK 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 875 ELERQARIEASLREREREVQKAR--SEQTKEIDREREQHKREEAIQNFKALLSDMVRSSDvswsdtRRTLRKDHRWESGS 952
Cdd:pfam02463 280 EKKLQEEELKLLAKEEEELKSELlkLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEE------LEKELKELEIKREA 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 953 LLEREE----KEKLFNEHIEALTKKKREHFRQLLDETSAITLTSTWKEVKKIIkedprcikfsSSDRKKQREFEEYIRDK 1028
Cdd:pfam02463 354 EEEEEEelekLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE----------AQLLLELARQLEDLLKE 423
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1841659210 1029 YITAKADFrtLLKETKFITYRSKKLIQESDqHLKDVEKILQNDKRYLVLDCVPEERRKLIVAYVDDLDRRGPPPPPTAS 1107
Cdd:pfam02463 424 EKKEELEI--LEEEEESIELKQGKLTEEKE-ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERS 499
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
714-1086 |
1.22e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 714 LNPKERKQVFDQYVKTRAEEERREKKNKIMQAKEDFKKMMEEAKfnpratFSEFAAKHAKDSRfKAIEKMKDREALFNEf 793
Cdd:PTZ00121 1072 LKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEAR------KAEEAKKKAEDAR-KAEEARKAEDARKAE- 1143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 794 vaAARKKEkEDSKTRGEKIKSDFFELLSNHHLDSQSRWSKVKDKVE---SDPRYKAVDSSSMREDLFKQYIEKIAKNLDS 870
Cdd:PTZ00121 1144 --EARKAE-DAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEvrkAEELRKAEDARKAEAARKAEEERKAEEARKA 1220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 871 EKEKELERQARIEaSLREREREVQKARSEQTKEIDREREQHKREEAIQNFKALLSDMVRSSDvswsdtrrTLRK-DHRWE 949
Cdd:PTZ00121 1221 EDAKKAEAVKKAE-EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAD--------ELKKaEEKKK 1291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 950 SGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDET--SAITLTSTWKEVKKIIKEDPRCIKFSSSDRKKQREFEEYIRD 1027
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841659210 1028 KYITAKADFRTLLK--ETKFITYRSKKLIQESDQHLKDVEKILQNDKRYLVLDCVPEERRK 1086
Cdd:PTZ00121 1372 KKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK 1432
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
532-559 |
2.48e-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: 39.41 E-value: 2.48e-04
10 20
....*....|....*....|....*...
gi 1841659210 532 TPWCVVWTGDERVFFYNPTTRLSMWDRP 559
Cdd:pfam00397 3 PGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
299-417 |
3.40e-04 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 44.08 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 299 PTTQDQ-TPSSAVsvATPTVSVSTPAPTA-TPVQTVPQPHPQTLPPAVPHSVPQPTTAIPAFPPVMVPPFRV---PLPGM 373
Cdd:PHA02682 76 PSGQSPlAPSPAC--AAPAPACPACAPAApAPAVTCPAPAPACPPATAPTCPPPAVCPAPARPAPACPPSTRqcpPAPPL 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1841659210 374 PIPLPGVAMMQIV-------------SCPYVKTvattktgvlpgmAPPIVPMIHPQV 417
Cdd:PHA02682 154 PTPKPAPAAKPIFlhnqlpppdypaaSCPTIET------------APAASPVLEPRI 198
|
|
| motB |
PRK12799 |
flagellar motor protein MotB; Reviewed |
258-365 |
3.85e-04 |
|
flagellar motor protein MotB; Reviewed
Pssm-ID: 183756 [Multi-domain] Cd Length: 421 Bit Score: 44.32 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 258 ASTPTTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQdqTPSSAVSVATPTVSVSTPAPTATPVQTVPQPH- 336
Cdd:PRK12799 303 AVTPSSAVTQSSAITPSSAAIPSPAVIPSSVTTQSATTTQASAVA--LSSAGVLPSDVTLPGTVALPAAEPVNMQPQPMs 380
|
90 100 110
....*....|....*....|....*....|...
gi 1841659210 337 -PQTLPPAVPHSVP---QPTTAIPAFPPVMVPP 365
Cdd:PRK12799 381 tTETQQSSTGNITStanGPTTSLPAAPASNIPV 413
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
258-383 |
3.86e-04 |
|
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: 44.76 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 258 ASTPTTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQDQTPSSAVSVATPTVSVST---PAPtATPVQTVPQ 334
Cdd:pfam03154 176 AQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPqrlPSP-HPPLQPMTQ 254
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1841659210 335 PHPqtlPPAV-PHSVPQPT--TAIPAFP-PVMVPPFRVPLPGMPIPLPGVAMM 383
Cdd:pfam03154 255 PPP---PSQVsPQPLPQPSlhGQMPPMPhSLQTGPSHMQHPVPPQPFPLTPQS 304
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
730-1012 |
5.06e-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: 44.18 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 730 RAEEERREKKNKIMQAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSrfKAIEKMKDREALFNEFVAAARKKEKEDSKTRG 809
Cdd:COG5185 257 KLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYT--KSIDIKKATESLEEQLAAAEAEQELEESKRET 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 810 EKIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEKIAKNLDSekekelerqarIEASLRER 889
Cdd:COG5185 335 ETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDE-----------IPQNQRGY 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 890 EREVQKARSEQTKEIDREREQHKR---------EEAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWESGSLLEREEKE 960
Cdd:COG5185 404 AQEILATLEDTLKAADRQIEELQRqieqatssnEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDL 483
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1841659210 961 --------------KLFNEHIEALTKKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCIKFSS 1012
Cdd:COG5185 484 neeltqiesrvstlKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASE 549
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
293-416 |
7.17e-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: 43.87 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 293 AQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPtATPVQTVPQPHPQTLPPAVPHSVPQPTTAIPAFPPVMVPPF------ 366
Cdd:pfam09770 228 QQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQ-GHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTqilqnp 306
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1841659210 367 -RVPLPGMPIPLPGVAMMQivscPYVKTVATTKTGVLPGMAPPIVpmiHPQ 416
Cdd:pfam09770 307 nRLSAARVGYPQNPQPGVQ----PAPAHQAHRQQGSFGRQAPIIT---HPQ 350
|
|
| PRK10856 |
PRK10856 |
cytoskeleton protein RodZ; |
293-371 |
7.35e-04 |
|
cytoskeleton protein RodZ;
Pssm-ID: 236776 [Multi-domain] Cd Length: 331 Bit Score: 43.09 E-value: 7.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1841659210 293 AQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPTATPVQTvPQPHPQTLPPAVPHSVPQPTTAIPAFPPVMVPPFRVPLP 371
Cdd:PRK10856 161 SVPLDTSTTTDPATTPAPAAPVDTTPTNSQTPAVATAPA-PAVDPQQNAVVAPSQANVDTAATPAPAAPATPDGAAPLP 238
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
296-382 |
1.05e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 43.23 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 296 VSTPTTQDQTPSSAVSVATPTVSVSTPAPTATPVQTVPQPHPQT--LPPAVPHSVPQPTTAIPAFPPvmvPPFRVPLPGM 373
Cdd:PRK14971 383 FTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTvsVDPPAAVPVNPPSTAPQAVRP---AQFKEEKKIP 459
|
....*....
gi 1841659210 374 PIPLPGVAM 382
Cdd:PRK14971 460 VSKVSSLGP 468
|
|
| DUF3729 |
pfam12526 |
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ... |
306-379 |
1.48e-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: 39.68 E-value: 1.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841659210 306 PSSAVSVATPTVSVSTPAPTATPVQTVPQPHPqtlpPAVPHSVPQPTTAIPAFPPVMVPPfRVPLPGMPIPLPG 379
Cdd:pfam12526 37 PDPPPPVGDPRPPVVDTPPPVSAVWVLPPPSE----PAAPEPDLVPPVTGPAGPPSPLAP-PAPAQKPPLPPPR 105
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
733-1067 |
1.50e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 733 EERREKKNKIMQAKEDFKKMMEE-AKFNPRA-TFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEK--EDSKTR 808
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRlEELEERHeLYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEieEEISKI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 809 GEKIKSdfFELLSNHHLDSQSRWSKVKDKVesdPRYKAVDSSSMREDLFKQYIEKIAKnldseKEKELERQARIEASLRE 888
Cdd:PRK03918 411 TARIGE--LKKEIKELKKAIEELKKAKGKC---PVCGRELTEEHRKELLEEYTAELKR-----IEKELKEIEEKERKLRK 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 889 REREVQKARS------------EQTKEIDREREQHKREEAIQNFKALLSDMVRSsdvswsdtrRTLRKDHRwesgSLLER 956
Cdd:PRK03918 481 ELRELEKVLKkeseliklkelaEQLKELEEKLKKYNLEELEKKAEEYEKLKEKL---------IKLKGEIK----SLKKE 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 957 EEKEKLFNEHIEALTKKKREHFRQLldetsaitltstwKEVKKIIKEdprcIKFSSSD--RKKQREFEEYIRdKYIT--- 1031
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELEEEL-------------AELLKELEE----LGFESVEelEERLKELEPFYN-EYLElkd 609
|
330 340 350
....*....|....*....|....*....|....*.
gi 1841659210 1032 AKADFRTLLKETKFITYRSKKLIQESDQHLKDVEKI 1067
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
553-929 |
2.31e-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: 42.27 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 553 LSMWDR----PDDLIGRADVDKiiqepphkKGMEELKKLRHPTPTMLSIQ-------------KWQFSmSAIKEEQELME 615
Cdd:pfam02463 148 AMMKPErrleIEEEAAGSRLKR--------KKKEALKKLIEETENLAELIidleelklqelklKEQAK-KALEYYQLKEK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 616 EINEDEpvkAKKRKRMSKKSFMWIARASLFRRDDNKDIDSEKEAAMEAEIKAARERAIVPLEARMKQFKDMLLERGVSAF 695
Cdd:pfam02463 219 LELEEE---YLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 696 STWEKELHKIVfdpryLLLNPKERKQVFDQYVKTRAEEErrekKNKIMQAKEDFKKMMEE--AKFNPRATFSEFAAKHAK 773
Cdd:pfam02463 296 EELKSELLKLE-----RRKVDDEEKLKESEKEKKKAEKE----LKKEKEEIEELEKELKEleIKREAEEEEEEELEKLQE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 774 DSRFKAIEKMKDREALFNEFVAAARKKEKEDS-KTRGEKIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSssm 852
Cdd:pfam02463 367 KLEQLEEELLAKKKLESERLSSAAKLKEEELElKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ--- 443
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1841659210 853 REDLFKQYIEKIAKNLDSEKEKELERQARIEAslREREREVQKARSEQTKEIDREREQHKREEAIQNFKALLSDMVR 929
Cdd:pfam02463 444 GKLTEEKEELEKQELKLLKDELELKKSEDLLK--ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKD 518
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
861-1070 |
2.49e-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: 41.98 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 861 IEKIAKNLDSEKEKELERQARIEASLREREREVQKARSEQT---KEIDREREQ-HKREEAIQNFKALLSD-MVRSSDVSW 935
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleARIEELEEDlHKLEEALNDLEARLSHsRIPEIQAEL 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 936 SDtrrtLRKDHRWESGSL--LEREEKEKLFNEHIEaltKKKREHFRQLLDEtsaitLTSTWKEVKKIIKEDPRCIKFSSS 1013
Cdd:TIGR02169 801 SK----LEEEVSRIEARLreIEQKLNRLTLEKEYL---EKEIQELQEQRID-----LKEQIKSIEKEIENLNGKKEELEE 868
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 1014 DRKKQREFEEYIRDKYITAKADFRTLLKETKFITYRSKKL---IQESDQHLKDVEKILQN 1070
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELeaqIEKKRKRLSELKAKLEA 928
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
262-431 |
2.51e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 41.90 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 262 TTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQDQTpSSAVSVATPtVSVSTPAPTATPVQTVPQPHP---Q 338
Cdd:PRK12727 65 TAAAPAPAPQAPTKPAAPVHAPLKLSANANMSQRQRVASAAEDM-IAAMALRQP-VSVPRQAPAAAPVRAASIPSPaaqA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 339 TLPPAVPHSVPQPTTAIPAFPPVMvppFRVPLPGMPIPLPGVAMMQIVSCPYVKTVATT--------------------- 397
Cdd:PRK12727 143 LAHAAAVRTAPRQEHALSAVPEQL---FADFLTTAPVPRAPVQAPVVAAPAPVPAIAAAlaahaayaqdddeqldddgfd 219
|
170 180 190
....*....|....*....|....*....|....*
gi 1841659210 398 -KTGVLPGMAPPIVPmihPQVAIAASPATLAGATA 431
Cdd:PRK12727 220 lDDALPQILPPAALP---PIVVAPAAPAALAAVAA 251
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
305-376 |
2.56e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 2.56e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841659210 305 TPSSAVSVATPTVSVSTPAPTATPVQTVPQ-PHPQTLPPAVPHSVPQP-TTAIPAFPPVMVPPFRVPLPGMPIP 376
Cdd:PHA03247 393 TPFARGPGGDDQTRPAAPVPASVPTPAPTPvPASAPPPPATPLPSAEPgSDDGPAPPPERQPPAPATEPAPDDP 466
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
853-984 |
3.13e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 853 REDLFKQYIEKIAKNLDSEKEKELERQARIEAsLREREREVQKARSEQ--------TKEIDR-EREQHKREEAIQNFKAL 923
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDA-LREELDELEAQIRGNggdrleqlEREIERlERELEERERRRARLEAL 367
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1841659210 924 LSDMvrssDVSWSDTRRTLRKDHRwESGSLLER--EEKEKLFNEHIEALTKKK--REHFRQLLDE 984
Cdd:COG4913 368 LAAL----GLPLPASAEEFAALRA-EAAALLEAleEELEALEEALAEAEAALRdlRRELRELEAE 427
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
293-387 |
3.15e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 41.68 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 293 AQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPTATPVQTVPQPHPQTLPPAVPHSVPQPTtaiPAFPPVMVPPfRVPLPG 372
Cdd:PRK14971 376 KQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAV---PVNPPSTAPQ-AVRPAQ 451
|
90
....*....|....*
gi 1841659210 373 MPIPLPgVAMMQIVS 387
Cdd:PRK14971 452 FKEEKK-IPVSKVSS 465
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
266-433 |
3.45e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 41.61 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 266 PAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQdQTPSSAVSVATPTVSVSTPAPTATPVQTVPQPHPQTLPPAVP 345
Cdd:PRK10263 403 PQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPE-QPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQP 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 346 HSVPQPTTAIPAFPPVMVPPFRVPLPGM-------------------PIPLPGVAmmqivSCPYVKTVATTKTGVLPGMA 406
Cdd:PRK10263 482 QPVEQQPVVEPEPVVEETKPARPPLYYFeeveekrarereqlaawyqPIPEPVKE-----PEPIKSSLKAPSVAAVPPVE 556
|
170 180
....*....|....*....|....*..
gi 1841659210 407 PpiVPMIHPqVAIAASPATLAGATAVS 433
Cdd:PRK10263 557 A--AAAVSP-LASGVKKATLATGAAAT 580
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
258-487 |
3.53e-03 |
|
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: 41.48 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 258 ASTPTTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVStPTTQDQTPSSAVSVAT-----------PTVSVSTPAPTA 326
Cdd:pfam17823 128 QSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASA-PHAASPAPRTAASSTTaassttaassaPTTAASSAPATL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 327 TPVQTvpqphpqTLPPAVPHSVPQPTTAIPAFPPVMVPPFRVPLPGMPIPLPGVAMMqivsCPYVKTVATTKTGVlpGMA 406
Cdd:pfam17823 207 TPARG-------ISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATL----AAAAGTVASAAGTI--NMG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 407 PPIV----PMIH-PQVAIAASPATLAGATAVSEWTE-------YKTADGKTYYYNNRTLESTWEKPQELKEKEKLEEKIK 474
Cdd:pfam17823 274 DPHArrlsPAKHmPSDTMARNPAAPMGAQAQGPIIQvstdqpvHNTAGEPTPSPSNTTLEPNTPKSVASTNLAVVTTTKA 353
|
250
....*....|...
gi 1841659210 475 EPiKEPSEEPLPM 487
Cdd:pfam17823 354 QA-KEPSASPVPV 365
|
|
| half-pint |
TIGR01645 |
poly-U binding splicing factor, half-pint family; The proteins represented by this model ... |
297-434 |
5.21e-03 |
|
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: 40.82 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 297 STPTTQDQTPSSAVSvATPTvSVSTPaPTATPVQTVPQPHPqTLPPAVPHSVPqpttaipafPPVMVPPFRVPLPGMPIP 376
Cdd:TIGR01645 322 AVLGPRAQSPATPSS-SLPT-DIGNK-AVVSSAKKEAEEVP-PLPQAAPAVVK---------PGPMEIPTPVPPPGLAIP 388
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841659210 377 LpGVAMMQIVScpyvktvattKTGVLPG-MAPPIVPMIHPQVAIAASP--ATLAGATAVSE 434
Cdd:TIGR01645 389 S-LVAPPGLVA----------PTEINPSfLASPRKKMKREKLPVTFGAldDTLAWKEPSKE 438
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
292-435 |
5.50e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 40.79 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 292 VAQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPTATPVQTVPQPHPQTLPPAVPHSVPQPTTAIPAFPPVMVPPFRVPLP 371
Cdd:PRK10811 887 VVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETA 966
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841659210 372 GMPIPLPGVAMMQIVSCPYVKTVATTKTGVL-PGMAPPIVPMIHPQVAIAASPATLAGATA-------VSEW 435
Cdd:PRK10811 967 EVVVAEPEVVAQPAAPVVAEVAAEVETVTAVePEVAPAQVPEATVEHNHATAPMTRAPAPEyvpeaprHSDW 1038
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
292-378 |
6.81e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 40.56 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 292 VAQTVSTPTTQDQTPSSAVsvATPTVSVSTPAPTATPVQTVPQPHPQTlpPAVPHSVPQPTTAIP--AFPPVMVPPFRVP 369
Cdd:PRK14950 355 VIEALLVPVPAPQPAKPTA--AAPSPVRPTPAPSTRPKAAAAANIPPK--EPVRETATPPPVPPRpvAPPVPHTPESAPK 430
|
....*....
gi 1841659210 370 LPGMPIPLP 378
Cdd:PRK14950 431 LTRAAIPVD 439
|
|
| PRK14959 |
PRK14959 |
DNA polymerase III subunits gamma and tau; Provisional |
293-374 |
7.39e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 40.43 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 293 AQTVSTPTTQ-DQTPSSAVSVATPTVSVSTPAPTATPVQTVPQphpQTLPPAVPHSvpqpttAIPAFPPVMVPPfRVPLP 371
Cdd:PRK14959 394 AATIPTPGTQgPQGTAPAAGMTPSSAAPATPAPSAAPSPRVPW---DDAPPAPPRS------GIPPRPAPRMPE-ASPVP 463
|
...
gi 1841659210 372 GMP 374
Cdd:PRK14959 464 GAP 466
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
259-424 |
7.43e-03 |
|
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: 40.33 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 259 STPTTS-----SPAPAVSTSTSSSTPSSTTSTTTTATSVAQT--VSTPTTqdQTPSSAVSVATPTVSVSTPAPTATPVQT 331
Cdd:pfam17823 98 SEPATRegaadGAASRALAAAASSSPSSAAQSLPAAIAALPSeaFSAPRA--AACRANASAAPRAAIAAASAPHAASPAP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 332 VPQPHPQTLPPAVPHSVPQPTTAIPAFPPVMVP--PFRVPLPGMPIPLPGVAMMQIvscPYVKTVATTKTGVLPGMAPPI 409
Cdd:pfam17823 176 RTAASSTTAASSTTAASSAPTTAASSAPATLTParGISTAATATGHPAAGTALAAV---GNSSPAAGTVTAAVGTVTPAA 252
|
170
....*....|....*
gi 1841659210 410 VPMIHPQVAIAASPA 424
Cdd:pfam17823 253 LATLAAAAGTVASAA 267
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
850-935 |
7.89e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 40.24 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 850 SSMREDLFKQYiekiaknLDSEKEKELERQARIEASlREREREVQKARSEQTKEIDREREQHKREEAIQNFKA--LLSDM 927
Cdd:PLN02316 239 GGMDEHSFEDF-------LLEEKRRELEKLAKEEAE-RERQAEEQRRREEEKAAMEADRAQAKAEVEKRREKLqnLLKKA 310
|
....*...
gi 1841659210 928 VRSSDVSW 935
Cdd:PLN02316 311 SRSADNVW 318
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
293-375 |
8.40e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 40.14 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841659210 293 AQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPTATPVQ-TVPQPHPQTLPPavPHSVPQPTTAIPAFPPVMVPPFRVPLP 371
Cdd:PRK14971 389 APQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTvSVDPPAAVPVNP--PSTAPQAVRPAQFKEEKKIPVSKVSSL 466
|
....
gi 1841659210 372 GMPI 375
Cdd:PRK14971 467 GPST 470
|
|
| |
