|
Name |
Accession |
Description |
Interval |
E-value |
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
408-1005 |
9.12e-26 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 113.64 E-value: 9.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 408 ASPATLAGATAVSEWTEYKTADGKTYYYNNRTLESTWEKPQEL--KEKEKLDEkikepikeaseeplpmeteeedpkeep 485
Cdd:COG5104 3 AALLGMASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELlkGSEEDLDV--------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 486 vkeikeepkeeemteeekaaqkakpvattpipgTPWCVVWTGDERVFFYNPTTRLSMWDRPDDligRADVDKIIQEpphK 565
Cdd:COG5104 56 ---------------------------------DPWKECRTADGKVYYYNSITRESRWKIPPE---RKKVEPIAEQ---K 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 566 KGLEDMKKLRHPAPTMLSIQKWQFSmsaiKEEQELMEEMNEDEPIKAKKRKrddnkdidsekeaameaeikaareraivP 645
Cdd:COG5104 97 HDERSMIGGNGNDMAITDHETSEPK----YLLGRLMSQYGITSTKDAVYRL----------------------------T 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 646 LEARMKQFKDMLLERGVSAFSTWEKELHKIVfDPRYLLL--NPKERKQVFDQYVKTRAEEERREKKNKIMQAKEDFKKMM 723
Cdd:COG5104 145 KEEAEKEFITMLKENQVDSTWPIFRAIEELR-DPRYWMVdtDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCKML 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 724 E-EAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEKEDSKTRGEKIKSDFFELLSNHHLDSQSRWS 802
Cdd:COG5104 224 AgNSHIKYYTDWFTFKSIFSKHPYYSSVVNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGSETFIIWL 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 803 KVKDKVESDPRYKAvdSSSM----REDLFKQYIeKIAKNLdsekekelerqarieaslrerEREVQKARSEQTKEIDReR 878
Cdd:COG5104 304 LNHYVFDSVVRYLK--NKEMkpldRKDILFSFI-RYVRRL---------------------EKELLSAIEERKAAAAQ-N 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 879 EQHKREeaiqNFKALLSDMVRSSDVS----WSDTRRTLRKDHRWESGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDE 954
Cdd:COG5104 359 ARHHRD----EFRTLLRKLYSEGKIYyrmkWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYERE 434
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720393380 955 TSaITLTSTW--KEVKKIIKEDPRciKFSSSDRKKQREFEE---YIRDKYITAKAD 1005
Cdd:COG5104 435 TR-TGQISPTdrRAVDEIFEAIAE--KKEEGEIKFDKVDKEdisLIVDGLIKQRNE 487
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
781-830 |
1.68e-13 |
|
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: 65.56 E-value: 1.68e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720393380 781 KIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQY 830
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
942-997 |
1.19e-09 |
|
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: 54.89 E-value: 1.19e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720393380 942 KKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCiKFSSSDRKKQREFEEYIRD 997
Cdd:smart00441 1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRY-KALLSESEREQLFEDHIEE 55
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
420-449 |
9.07e-09 |
|
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: 51.76 E-value: 9.07e-09
10 20 30
....*....|....*....|....*....|
gi 1720393380 420 SEWTEYKTADGKTYYYNNRTLESTWEKPQE 449
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
137-162 |
5.43e-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: 49.43 E-value: 5.43e-08
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
132-164 |
5.67e-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: 49.52 E-value: 5.67e-08
10 20 30
....*....|....*....|....*....|...
gi 1720393380 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 |
1.52e-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: 48.29 E-value: 1.52e-07
10 20
....*....|....*....|....*...
gi 1720393380 137 WVENKTPDGKVYYYNARTRESAWTKPDG 164
Cdd:cd00201 4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
596-1037 |
1.74e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 596 EEQELMEEMNEDEPIKAKKRKRDDNKDIDSEKEAAMEAEIKAARERAIVPLEARMKQFKDMLLErgvsafstwekelhki 675
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE---------------- 1409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 676 vfdpryllLNPKERKQVFDQYVKTRAEEERR--EKKNKIMQAK--EDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIE 751
Cdd:PTZ00121 1410 --------LKKAAAAKKKADEAKKKAEEKKKadEAKKKAEEAKkaDEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 752 KMKDREAlfNEFVAAARKKEKEDSKTRGEKIKSDffELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYI 831
Cdd:PTZ00121 1482 AKKADEA--KKKAEEAKKKADEAKKAAEAKKKAD--EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 832 EKIAKNLDSEKEKELERQARIEASLREREREVQKARSEQTKEIDREREQHKREEAiqnfKALLSDMVRSSDVSWSDTRRt 911
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEELKKAEEEK- 1632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 912 lRKDHRWESGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDETSAitltstwKEVKKIIKEDPRCIKFSSSDRKKQREF 991
Cdd:PTZ00121 1633 -KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA-------EEAKKAEEDEKKAAEALKKEAEEAKKA 1704
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1720393380 992 EEyIRDKYITAKADFRTLLKETKFITYRSKKLIQESDQHLKDVEKI 1037
Cdd:PTZ00121 1705 EE-LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
124-173 |
1.41e-05 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 48.92 E-value: 1.41e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720393380 124 APGAPALPPTEEIWVENKTPDGKVYYYNARTRESAWTKPDgvKVIQQSEL 173
Cdd:COG5104 4 ALLGMASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPK--ELLKGSEE 51
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
1000-1064 |
2.48e-04 |
|
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: 39.86 E-value: 2.48e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720393380 1000 ITAKADFRTLLKETKFITYrskkliqesDQHLKDVEKILQNDKRYLVLDcVPEERRKLIVAYVDD 1064
Cdd:smart00441 1 EEAKEAFKELLKEHEVITP---------DTTWSEARKKLKNDPRYKALL-SESEREQLFEDHIEE 55
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
1002-1061 |
2.56e-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: 39.75 E-value: 2.56e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 1002 AKADFRTLLKETKfITYRSkkliqesdqHLKDVEKILQNDKRYLVLDcVPEERRKLIVAY 1061
Cdd:pfam01846 2 AREAFKELLKEHK-ITPYS---------TWSEIKKKIENDPRYKALL-DGSEREELFEDY 50
|
|
| half-pint |
TIGR01645 |
poly-U binding splicing factor, half-pint family; The proteins represented by this model ... |
304-469 |
6.45e-04 |
|
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: 43.91 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 304 SLAPTTQDQ-TPSSAV--SVATPTVsVSAPAPTATPVQTVPQPHPQTLPPAVPHSVPQpaaaipafppvmVPPFRVPLPG 380
Cdd:TIGR01645 323 VLGPRAQSPaTPSSSLptDIGNKAV-VSSAKKEAEEVPPLPQAAPAVVKPGPMEIPTP------------VPPPGLAIPS 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 381 MPIPLPGVLPGMAPPIV------PMIHPQVAIAASP--ATLAGATAVSEwtEYKTADGKTYYYNNRTLESTWEKPQElKE 452
Cdd:TIGR01645 390 LVAPPGLVAPTEINPSFlasprkKMKREKLPVTFGAldDTLAWKEPSKE--DQTSEDGKMLAIMGEAAAALALEPKK-KK 466
|
170
....*....|....*..
gi 1720393380 453 KEKLDEKIKEPIKEASE 469
Cdd:TIGR01645 467 KEKEGEELQPKLVMNSE 483
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
307-429 |
8.44e-04 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 42.54 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 307 PTTQDQTPSSAVSVATPTVSVSAPAPTATPVQTVPQPHPQTLP-PAVPHSVPQpaaaipafppvmvPPFRVPLPGMPIPL 385
Cdd:PHA02682 89 AAPAPACPACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPaPARPAPACP-------------PSTRQCPPAPPLPT 155
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1720393380 386 PGVLPGMAPPIV-PMIHPQVAIAASPATLAGATAVSEWTEYKTAD 429
Cdd:PHA02682 156 PKPAPAAKPIFLhNQLPPPDYPAASCPTIETAPAASPVLEPRIPD 200
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
258-352 |
2.08e-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: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 258 VGAPTPTTSSPAPAVSTSTPTstpssttattttatsvaqtvsmfsfSLAPTTQDQTPSSAVSVAT-----PTVSVSAPAP 332
Cdd:pfam05109 513 VTTPTPNATSPTPAVTTPTPN-------------------------ATSPTLGKTSPTSAVTTPTpnatsPTPAVTTPTP 567
|
90 100
....*....|....*....|....*...
gi 1720393380 333 TAT--------PVQTVPQPHPQTLPPAV 352
Cdd:pfam05109 568 NATiptlgktsPTSAVTTPTPNATSPTV 595
|
|
| KLF3_N |
cd21577 |
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ... |
300-397 |
4.62e-03 |
|
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: 39.64 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 300 MFSFSLAPTTQDQ-----------TPSSAVSVATPTVSVSAPAPTATPvqtvPQPH--------PQTLPPAVPHSvpqpa 360
Cdd:cd21577 8 ETSFYSPSHSQLEpvdlslskrssPPSSSSSSSSSSSSSSSPSSRASP----PSPYskssppspPQQRPLSPPLS----- 78
|
90 100 110
....*....|....*....|....*....|....*..
gi 1720393380 361 aaipafppvmVPPFRVPLPGMPIPLPGVLPGMAPPIV 397
Cdd:cd21577 79 ----------LPPPVAPPPLSPGSVPGGLPVISPVMV 105
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
408-1005 |
9.12e-26 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 113.64 E-value: 9.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 408 ASPATLAGATAVSEWTEYKTADGKTYYYNNRTLESTWEKPQEL--KEKEKLDEkikepikeaseeplpmeteeedpkeep 485
Cdd:COG5104 3 AALLGMASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELlkGSEEDLDV--------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 486 vkeikeepkeeemteeekaaqkakpvattpipgTPWCVVWTGDERVFFYNPTTRLSMWDRPDDligRADVDKIIQEpphK 565
Cdd:COG5104 56 ---------------------------------DPWKECRTADGKVYYYNSITRESRWKIPPE---RKKVEPIAEQ---K 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 566 KGLEDMKKLRHPAPTMLSIQKWQFSmsaiKEEQELMEEMNEDEPIKAKKRKrddnkdidsekeaameaeikaareraivP 645
Cdd:COG5104 97 HDERSMIGGNGNDMAITDHETSEPK----YLLGRLMSQYGITSTKDAVYRL----------------------------T 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 646 LEARMKQFKDMLLERGVSAFSTWEKELHKIVfDPRYLLL--NPKERKQVFDQYVKTRAEEERREKKNKIMQAKEDFKKMM 723
Cdd:COG5104 145 KEEAEKEFITMLKENQVDSTWPIFRAIEELR-DPRYWMVdtDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCKML 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 724 E-EAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEKEDSKTRGEKIKSDFFELLSNHHLDSQSRWS 802
Cdd:COG5104 224 AgNSHIKYYTDWFTFKSIFSKHPYYSSVVNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGSETFIIWL 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 803 KVKDKVESDPRYKAvdSSSM----REDLFKQYIeKIAKNLdsekekelerqarieaslrerEREVQKARSEQTKEIDReR 878
Cdd:COG5104 304 LNHYVFDSVVRYLK--NKEMkpldRKDILFSFI-RYVRRL---------------------EKELLSAIEERKAAAAQ-N 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 879 EQHKREeaiqNFKALLSDMVRSSDVS----WSDTRRTLRKDHRWESGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDE 954
Cdd:COG5104 359 ARHHRD----EFRTLLRKLYSEGKIYyrmkWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYERE 434
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720393380 955 TSaITLTSTW--KEVKKIIKEDPRciKFSSSDRKKQREFEE---YIRDKYITAKAD 1005
Cdd:COG5104 435 TR-TGQISPTdrRAVDEIFEAIAE--KKEEGEIKFDKVDKEdisLIVDGLIKQRNE 487
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
781-830 |
1.68e-13 |
|
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: 65.56 E-value: 1.68e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720393380 781 KIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQY 830
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
714-763 |
1.69e-11 |
|
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: 60.16 E-value: 1.69e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720393380 714 QAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEF 763
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
649-696 |
1.17e-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: 1.17e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720393380 649 RMKQFKDMLLERGVSAFSTWEKELHKIVFDPRYL-LLNPKERKQVFDQY 696
Cdd:pfam01846 2 AREAFKELLKEHKITPYSTWSEIKKKIENDPRYKaLLDGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
942-997 |
1.19e-09 |
|
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: 54.89 E-value: 1.19e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720393380 942 KKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCiKFSSSDRKKQREFEEYIRD 997
Cdd:smart00441 1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRY-KALLSESEREQLFEDHIEE 55
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
780-833 |
2.52e-09 |
|
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: 54.12 E-value: 2.52e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1720393380 780 EKIKSDFFELLSNHHLD-SQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEK 833
Cdd:smart00441 1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
885-936 |
3.97e-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: 53.23 E-value: 3.97e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1720393380 885 EAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWEsgSLLEREEKEKLFNEH 936
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYK--ALLDGSEREELFEDY 50
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
420-449 |
9.07e-09 |
|
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: 51.76 E-value: 9.07e-09
10 20 30
....*....|....*....|....*....|
gi 1720393380 420 SEWTEYKTADGKTYYYNNRTLESTWEKPQE 449
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
420-447 |
3.11e-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: 50.20 E-value: 3.11e-08
10 20
....*....|....*....|....*...
gi 1720393380 420 SEWTEYKTADGKTYYYNNRTLESTWEKP 447
Cdd:pfam00397 3 PGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
137-162 |
5.43e-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: 49.43 E-value: 5.43e-08
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
132-164 |
5.67e-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: 49.52 E-value: 5.67e-08
10 20 30
....*....|....*....|....*....|...
gi 1720393380 132 PTEEIWVENKTPDGKVYYYNARTRESAWTKPDG 164
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
422-449 |
6.13e-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: 49.52 E-value: 6.13e-08
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
137-164 |
1.52e-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: 48.29 E-value: 1.52e-07
10 20
....*....|....*....|....*...
gi 1720393380 137 WVENKTPDGKVYYYNARTRESAWTKPDG 164
Cdd:cd00201 4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
596-1037 |
1.74e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 596 EEQELMEEMNEDEPIKAKKRKRDDNKDIDSEKEAAMEAEIKAARERAIVPLEARMKQFKDMLLErgvsafstwekelhki 675
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE---------------- 1409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 676 vfdpryllLNPKERKQVFDQYVKTRAEEERR--EKKNKIMQAK--EDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIE 751
Cdd:PTZ00121 1410 --------LKKAAAAKKKADEAKKKAEEKKKadEAKKKAEEAKkaDEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 752 KMKDREAlfNEFVAAARKKEKEDSKTRGEKIKSDffELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYI 831
Cdd:PTZ00121 1482 AKKADEA--KKKAEEAKKKADEAKKAAEAKKKAD--EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 832 EKIAKNLDSEKEKELERQARIEASLREREREVQKARSEQTKEIDREREQHKREEAiqnfKALLSDMVRSSDVSWSDTRRt 911
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEELKKAEEEK- 1632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 912 lRKDHRWESGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDETSAitltstwKEVKKIIKEDPRCIKFSSSDRKKQREF 991
Cdd:PTZ00121 1633 -KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA-------EEAKKAEEDEKKAAEALKKEAEEAKKA 1704
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1720393380 992 EEyIRDKYITAKADFRTLLKETKFITYRSKKLIQESDQHLKDVEKI 1037
Cdd:PTZ00121 1705 EE-LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
713-766 |
1.95e-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: 48.72 E-value: 1.95e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1720393380 713 MQAKEDFKKMMEEAKFN-PRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAA 766
Cdd:smart00441 1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
943-994 |
4.01e-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: 47.45 E-value: 4.01e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1720393380 943 KKREHFRQLLDETSaITLTSTWKEVKKIIKEDPRCIKFSSSDRKKQrEFEEY 994
Cdd:pfam01846 1 KAREAFKELLKEHK-ITPYSTWSEIKKKIENDPRYKALLDGSEREE-LFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
884-939 |
3.81e-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: 3.81e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720393380 884 EEAIQNFKALLSDMVRS-SDVSWSDTRRTLRKDHRWESgsLLEREEKEKLFNEHIEA 939
Cdd:smart00441 1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKA--LLSESEREQLFEDHIEE 55
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
647-698 |
9.77e-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: 43.72 E-value: 9.77e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1720393380 647 EARMKQFKDMLLERGVS-AFSTWEKELHKIVFDPRY-LLLNPKERKQVFDQYVK 698
Cdd:smart00441 1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYkALLSESEREQLFEDHIE 54
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
520-548 |
1.00e-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: 43.36 E-value: 1.00e-05
10 20
....*....|....*....|....*....
gi 1720393380 520 PWCVVWTGDERVFFYNPTTRLSMWDRPDD 548
Cdd:smart00456 5 GWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
124-173 |
1.41e-05 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 48.92 E-value: 1.41e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720393380 124 APGAPALPPTEEIWVENKTPDGKVYYYNARTRESAWTKPDgvKVIQQSEL 173
Cdd:COG5104 4 ALLGMASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPK--ELLKGSEE 51
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
519-548 |
1.78e-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: 42.52 E-value: 1.78e-05
10 20 30
....*....|....*....|....*....|
gi 1720393380 519 TPWCVVWTGDERVFFYNPTTRLSMWDRPDD 548
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
688-938 |
1.95e-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: 48.58 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 688 ERKQVfDQYVKTRAEEERREKKNKIMQAKEdfKKMMEEAKFNPRATFSEFAAKHAKDSRFkAIEKMKDREALFNEfvaaa 767
Cdd:pfam17380 286 ERQQQ-EKFEKMEQERLRQEKEEKAREVER--RRKLEEAEKARQAEMDRQAAIYAEQERM-AMERERELERIRQE----- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 768 rKKEKEDSKTRGEKIKSDFFEL--LSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMRE-DLFKQYIEKIaknldsEKEK 844
Cdd:pfam17380 357 -ERKRELERIRQEEIAMEISRMreLERLQMERQQKNERVRQELEAARKVKILEEERQRKiQQQKVEMEQI------RAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 845 ELERQARIEASLREREREVQKARSEQ---TKEIDREREQhkrEEAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWESG 921
Cdd:pfam17380 430 EEARQREVRRLEEERAREMERVRLEEqerQQQVERLRQQ---EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQ 506
|
250
....*....|....*..
gi 1720393380 922 SLLEREEKEKLFNEHIE 938
Cdd:pfam17380 507 AMIEEERKRKLLEKEME 523
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
424-1016 |
5.46e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 424 EYKTADGKTYYYNNRTLESTWEKPQELKEKEKLDEKIKEPIKEASEepLPMETEEEDPKEEPVKEIKEEPKEEEMTEEEK 503
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE--LKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 504 AAQKAKPVATtpipgtpwcvvwTGDERVFFYNPTTRLSMWDRPDDLIGRADVDKIIQEPphKKGLEDMKKLRHPAptmls 583
Cdd:PTZ00121 1442 EAKKADEAKK------------KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA--KKKAEEAKKKADEA----- 1502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 584 iQKWQFSMSAIKEEQELMEEMNEDEPIKAKKRKRDDNKDIDSEKEAAMEA----EIKAARERAIVPLEARMKQFKDMLLE 659
Cdd:PTZ00121 1503 -KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkkaeELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 660 RGVSAFSTWEKELhkivfdprylllnpKERKQVFDQYVKTRAEEERREKKNKImqAKEDFKKMMEEAKfnpratFSEFAA 739
Cdd:PTZ00121 1582 KAEEAKKAEEARI--------------EEVMKLYEEEKKMKAEEAKKAEEAKI--KAEELKKAEEEKK------KVEQLK 1639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 740 KHAKDSRFKAIEKMKDREAlfNEFVAAARKKEKEDSKTRGEKIKSDffellsnhhlDSQSRWSKVKDKVESDPRYKAvds 819
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEE--NKIKAAEEAKKAEEDKKKAEEAKKA----------EEDEKKAAEALKKEAEEAKKA--- 1704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 820 ssmrEDLFKQYIEKIAKNLDSEKEKElERQARIEASLREREREVQKARSEQTKEIDREREQH-------KREEAIQNFKA 892
Cdd:PTZ00121 1705 ----EELKKKEAEEKKKAEELKKAEE-ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHlkkeeekKAEEIRKEKEA 1779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 893 LLSDMVRSSDVSWSDTRRTLRKDHRWESGSLLEREEKEKLFnehiealTKKKREHFRQLLDETsAITLTSTWKEVKKIIK 972
Cdd:PTZ00121 1780 VIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLV-------INDSKEMEDSAIKEV-ADSKNMQLEEADAFEK 1851
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1720393380 973 EDPRCIKFSSSDRKKQREFEeyiRDKYItaKADFRTLLKETKFI 1016
Cdd:PTZ00121 1852 HKFNKNNENGEDGNKEADFN---KEKDL--KEDDEEEIEEADEI 1890
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
596-969 |
8.33e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 596 EEQELMEEM---NEDEPIKAKKRKRDDNKDidseKEAAMEAEIKAARERAIVPLEARMKQFKdmlleRGVSAFSTWEKEl 672
Cdd:PTZ00121 1209 EEERKAEEArkaEDAKKAEAVKKAEEAKKD----AEEAKKAEEERNNEEIRKFEEARMAHFA-----RRQAAIKAEEAR- 1278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 673 hkivfdpRYLLLNPKERKQVFDQYVKTRAEEERREKKNKIMQAK--EDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAI 750
Cdd:PTZ00121 1279 -------KADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKkaDEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE 1351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 751 EKMKDREALFNEFVAAARKKEKEDSKTRGEKIKSDFFELLSNHHLDSQSRwskvKDKVESDPRYKAVDSSSMREDLfKQY 830
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE----EDKKKADELKKAAAAKKKADEA-KKK 1426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 831 IEKIAKNLDSEKEKELERQARieaSLREREREVQKARSEQTKEIDREREQHKREEAIQNFKAllSDMVRSSDVSWSDTRR 910
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEAKKAD---EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA--DEAKKKAEEAKKKADE 1501
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720393380 911 TLRKDHRWESGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDETSAITLTSTwKEVKK 969
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKA-EELKK 1559
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
137-172 |
9.72e-05 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 46.23 E-value: 9.72e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1720393380 137 WVENKTPDGKVYYYNARTRESAWTKPDGVKVIQQSE 172
Cdd:COG5104 58 WKECRTADGKVYYYNSITRESRWKIPPERKKVEPIA 93
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
519-546 |
1.89e-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: 1.89e-04
10 20
....*....|....*....|....*...
gi 1720393380 519 TPWCVVWTGDERVFFYNPTTRLSMWDRP 546
Cdd:pfam00397 3 PGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
1000-1064 |
2.48e-04 |
|
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: 39.86 E-value: 2.48e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720393380 1000 ITAKADFRTLLKETKFITYrskkliqesDQHLKDVEKILQNDKRYLVLDcVPEERRKLIVAYVDD 1064
Cdd:smart00441 1 EEAKEAFKELLKEHEVITP---------DTTWSEARKKLKNDPRYKALL-SESEREQLFEDHIEE 55
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
1002-1061 |
2.56e-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: 39.75 E-value: 2.56e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 1002 AKADFRTLLKETKfITYRSkkliqesdqHLKDVEKILQNDKRYLVLDcVPEERRKLIVAY 1061
Cdd:pfam01846 2 AREAFKELLKEHK-ITPYS---------TWSEIKKKIENDPRYKALL-DGSEREELFEDY 50
|
|
| half-pint |
TIGR01645 |
poly-U binding splicing factor, half-pint family; The proteins represented by this model ... |
304-469 |
6.45e-04 |
|
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: 43.91 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 304 SLAPTTQDQ-TPSSAV--SVATPTVsVSAPAPTATPVQTVPQPHPQTLPPAVPHSVPQpaaaipafppvmVPPFRVPLPG 380
Cdd:TIGR01645 323 VLGPRAQSPaTPSSSLptDIGNKAV-VSSAKKEAEEVPPLPQAAPAVVKPGPMEIPTP------------VPPPGLAIPS 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 381 MPIPLPGVLPGMAPPIV------PMIHPQVAIAASP--ATLAGATAVSEwtEYKTADGKTYYYNNRTLESTWEKPQElKE 452
Cdd:TIGR01645 390 LVAPPGLVAPTEINPSFlasprkKMKREKLPVTFGAldDTLAWKEPSKE--DQTSEDGKMLAIMGEAAAALALEPKK-KK 466
|
170
....*....|....*..
gi 1720393380 453 KEKLDEKIKEPIKEASE 469
Cdd:TIGR01645 467 KEKEGEELQPKLVMNSE 483
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
684-1056 |
6.99e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 684 LNPKERKQVFDQYVKTRAEEERREKKNKIMQAKEDFKKMMEEAKfnpratFSEFAAKHAKDSRfKAIEKMKDREALFNEf 763
Cdd:PTZ00121 1072 LKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEAR------KAEEAKKKAEDAR-KAEEARKAEDARKAE- 1143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 764 vaAARKKEkEDSKTRGEKIKSDFFELLSNHHLDSQSRWSKVKDKVE---SDPRYKAVDSSSMREDLFKQYIEKIAKNLDS 840
Cdd:PTZ00121 1144 --EARKAE-DAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEvrkAEELRKAEDARKAEAARKAEEERKAEEARKA 1220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 841 EKEKELERQARIEaSLREREREVQKARSEQTKEIDREREQHKREEAIQNFKALLSDMVRSSDvswsdtrrTLRK-DHRWE 919
Cdd:PTZ00121 1221 EDAKKAEAVKKAE-EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAD--------ELKKaEEKKK 1291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 920 SGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDET--SAITLTSTWKEVKKIIKEDPRCIKFSSSDRKKQREFEEYIRD 997
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720393380 998 KYITAKADFRTLLK--ETKFITYRSKKLIQESDQHLKDVEKILQNDKRYLVLDCVPEERRK 1056
Cdd:PTZ00121 1372 KKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK 1432
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
307-429 |
8.44e-04 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 42.54 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 307 PTTQDQTPSSAVSVATPTVSVSAPAPTATPVQTVPQPHPQTLP-PAVPHSVPQpaaaipafppvmvPPFRVPLPGMPIPL 385
Cdd:PHA02682 89 AAPAPACPACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPaPARPAPACP-------------PSTRQCPPAPPLPT 155
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1720393380 386 PGVLPGMAPPIV-PMIHPQVAIAASPATLAGATAVSEWTEYKTAD 429
Cdd:PHA02682 156 PKPAPAAKPIFLhNQLPPPDYPAASCPTIETAPAASPVLEPRIPD 200
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
703-1057 |
1.34e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 703 EERREKKNKIMQAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSRF-----KAIEKMKDREALFNEFVAAARKKEKEDSKT 777
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELreeleKLEKEVKELEELKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 778 RGEKIKsdffelLSNhhldSQSRWSKVKDKVEsDPRYKAVDSSSMREDLfKQYIEkiaknLDSEKEKELERQARIE---A 854
Cdd:PRK03918 255 RKLEEK------IRE----LEERIEELKKEIE-ELEEKVKELKELKEKA-EEYIK-----LSEFYEEYLDELREIEkrlS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 855 SLREREREVQKARSEQTKEIDREREQHKREEAIQNFKALLSDMVRSSDvswsDTRRTLRKDHRWESGslLEREEKEKLFN 934
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE----EAKAKKEELERLKKR--LTGLTPEKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 935 EhIEALTKKKREHFRQLLdetsaiTLTSTWKEVKKIIKEDPRCIKFSSSDRKK----QREFEEYIRDKYITA-KADFRTL 1009
Cdd:PRK03918 392 E-LEELEKAKEEIEEEIS------KITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELLEEyTAELKRI 464
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1720393380 1010 LKETKFITYRSKKLIQEsdqhLKDVEKILQNDKRYLVLDCVPEERRKL 1057
Cdd:PRK03918 465 EKELKEIEEKERKLRKE----LRELEKVLKKESELIKLKELAEQLKEL 508
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
258-352 |
2.08e-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: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 258 VGAPTPTTSSPAPAVSTSTPTstpssttattttatsvaqtvsmfsfSLAPTTQDQTPSSAVSVAT-----PTVSVSAPAP 332
Cdd:pfam05109 513 VTTPTPNATSPTPAVTTPTPN-------------------------ATSPTLGKTSPTSAVTTPTpnatsPTPAVTTPTP 567
|
90 100
....*....|....*....|....*...
gi 1720393380 333 TAT--------PVQTVPQPHPQTLPPAV 352
Cdd:pfam05109 568 NATiptlgktsPTSAVTTPTPNATSPTV 595
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
685-1077 |
2.63e-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: 41.88 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 685 NPKERKQVFDQYVKTRAEEERREKKNKIMQAKEDfkkmmeeakfnpratfsefaakhakdsrfKAIEKMKDREALFNEFV 764
Cdd:pfam02463 151 KPERRLEIEEEAAGSRLKRKKKEALKKLIEETEN-----------------------------LAELIIDLEELKLQELK 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 765 AAARKKEKEDSKTRGEKIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKavDSSSMREDLFKQYIEKIAKNLDSEKEK 844
Cdd:pfam02463 202 LKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEE--IESSKQEIEKEEEKLAQVLKENKEEEK 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 845 ELERQARIEASLREREREVQKAR--SEQTKEIDREREQHKREEAIQNFKALLSDMVRSSDvswsdtRRTLRKDHRWESGS 922
Cdd:pfam02463 280 EKKLQEEELKLLAKEEEELKSELlkLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEE------LEKELKELEIKREA 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 923 LLEREE----KEKLFNEHIEALTKKKREHFRQLLDETSAITLTSTWKEVKKIIkedprcikfsSSDRKKQREFEEYIRDK 998
Cdd:pfam02463 354 EEEEEEelekLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE----------AQLLLELARQLEDLLKE 423
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720393380 999 YITAKADFrtLLKETKFITYRSKKLIQESDqHLKDVEKILQNDKRYLVLDCVPEERRKLIVAYVDDLDRRGPPPPPTAS 1077
Cdd:pfam02463 424 EKKEELEI--LEEEEESIELKQGKLTEEKE-ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERS 499
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
700-982 |
2.90e-03 |
|
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: 41.48 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 700 RAEEERREKKNKIMQAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSrfKAIEKMKDREALFNEFVAAARKKEKEDSKTRG 779
Cdd:COG5185 257 KLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYT--KSIDIKKATESLEEQLAAAEAEQELEESKRET 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 780 EKIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEKIAKNLDSekekelerqarIEASLRER 859
Cdd:COG5185 335 ETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDE-----------IPQNQRGY 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 860 EREVQKARSEQTKEIDREREQHKR---------EEAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWESGSLLEREEKE 930
Cdd:COG5185 404 AQEILATLEDTLKAADRQIEELQRqieqatssnEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDL 483
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720393380 931 --------------KLFNEHIEALTKKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCIKFSS 982
Cdd:COG5185 484 neeltqiesrvstlKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASE 549
|
|
| KLF3_N |
cd21577 |
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ... |
300-397 |
4.62e-03 |
|
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: 39.64 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 300 MFSFSLAPTTQDQ-----------TPSSAVSVATPTVSVSAPAPTATPvqtvPQPH--------PQTLPPAVPHSvpqpa 360
Cdd:cd21577 8 ETSFYSPSHSQLEpvdlslskrssPPSSSSSSSSSSSSSSSPSSRASP----PSPYskssppspPQQRPLSPPLS----- 78
|
90 100 110
....*....|....*....|....*....|....*..
gi 1720393380 361 aaipafppvmVPPFRVPLPGMPIPLPGVLPGMAPPIV 397
Cdd:cd21577 79 ----------LPPPVAPPPLSPGSVPGGLPVISPVMV 105
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
823-954 |
5.68e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 823 REDLFKQYIEKIAKNLDSEKEKELERQARIEAsLREREREVQKARSEQ--------TKEIDR-EREQHKREEAIQNFKAL 893
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDA-LREELDELEAQIRGNggdrleqlEREIERlERELEERERRRARLEAL 367
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720393380 894 LSDMvrssDVSWSDTRRTLRKDHRwESGSLLER--EEKEKLFNEHIEALTKKK--REHFRQLLDE 954
Cdd:COG4913 368 LAAL----GLPLPASAEEFAALRA-EAAALLEAleEELEALEEALAEAEAALRdlRRELRELEAE 427
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
595-1037 |
5.83e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 595 KEEQELMEEMNEDEPIKAKKRKRDDNKDIDSEKEAAMEAEIKAARERaIVPLEARMKQFKDmlLERGVSAFSTWEKELHK 674
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE-IEELEEKVKELKE--LKEKAEEYIKLSEFYEE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 675 IVFDPRYLllnpKERKQVFDQYVKTRAE--EERREKKNKIMQAKEDFKKMMEE-AKFNPRA-TFSEFAAKHAKDSRFKAI 750
Cdd:PRK03918 305 YLDELREI----EKRLSRLEEEINGIEEriKELEEKEERLEELKKKLKELEKRlEELEERHeLYEEAKAKKEELERLKKR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 751 EKMKDREALFNEFVAAARKKEK--EDSKTRGEKIKSdfFELLSNHHLDSQSRWSKVKDKVesdPRYKAVDSSSMREDLFK 828
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEieEEISKITARIGE--LKKEIKELKKAIEELKKAKGKC---PVCGRELTEEHRKELLE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 829 QYIEKIAKnldseKEKELERQARIEASLREREREVQKARS------------EQTKEIDREREQHKREEAIQNFKALLSD 896
Cdd:PRK03918 456 EYTAELKR-----IEKELKEIEEKERKLRKELRELEKVLKkeseliklkelaEQLKELEEKLKKYNLEELEKKAEEYEKL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 897 MVRSsdvswsdtrRTLRKDHRwesgSLLEREEKEKLFNEHIEALTKKKREHFRQLldetsaitltstwKEVKKIIKEdpr 976
Cdd:PRK03918 531 KEKL---------IKLKGEIK----SLKKELEKLEELKKKLAELEKKLDELEEEL-------------AELLKELEE--- 581
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720393380 977 cIKFSSSD--RKKQREFEEYIRdKYIT---AKADFRTLLKETKFITYRSKKLIQESDQHLKDVEKI 1037
Cdd:PRK03918 582 -LGFESVEelEERLKELEPFYN-EYLElkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
|
| PHA03369 |
PHA03369 |
capsid maturational protease; Provisional |
316-473 |
8.68e-03 |
|
capsid maturational protease; Provisional
Pssm-ID: 223061 [Multi-domain] Cd Length: 663 Bit Score: 39.98 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 316 SAVSVATPTVSVSAPAPTATPV----QTVPQPHP--QTLPPAVPHSVPQPAAAIPAFPPVMVPPFRVPLPGMPIPLPGVL 389
Cdd:PHA03369 355 APSRVLAAAAKVAVIAAPQTHTgpadRQRPQRPDgiPYSVPARSPMTAYPPVPQFCGDPGLVSPYNPQSPGTSYGPEPVG 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 390 PGMAPPIVPMIHPQvAIAASPATLAGATAVSEWTEYKTADGKTYYYNNRTLESTWEKPQELKEKEKLDEKIKEPIKEASE 469
Cdd:PHA03369 435 PVPPQPTNPYVMPI-SMANMVYPGHPQEHGHERKRKRGGELKEELIETLKLVKKLKEEQESLAKELEATAHKSEIKKIAE 513
|
....
gi 1720393380 470 EPLP 473
Cdd:PHA03369 514 SEFK 517
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
820-905 |
9.29e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 40.24 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720393380 820 SSMREDLFKQYiekiaknLDSEKEKELERQARIEASlREREREVQKARSEQTKEIDREREQHKREEAIQNFKA--LLSDM 897
Cdd:PLN02316 239 GGMDEHSFEDF-------LLEEKRRELEKLAKEEAE-RERQAEEQRRREEEKAAMEADRAQAKAEVEKRREKLqnLLKKA 310
|
....*...
gi 1720393380 898 VRSSDVSW 905
Cdd:PLN02316 311 SRSADNVW 318
|
|
| |
