|
Name |
Accession |
Description |
Interval |
E-value |
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
333-950 |
2.60e-23 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 105.55 E-value: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 333 ASPMSLAGAIPLPEWSEFKTADGRIYYYNNRTLESTWEKPFEL-KERDKDSDKardihnninldlklidmeakadfgksk 411
Cdd:COG5104 3 AALLGMASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELlKGSEEDLDV--------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 412 elpreedmteeekatqkgkpvatnpipgTPWCVVWTGDERVFYYNPTTRLSMWDRPEElvgradvdRYIQEPPHKRGLDD 491
Cdd:COG5104 56 ----------------------------DPWKECRTADGKVYYYNSITRESRWKIPPE--------RKKVEPIAEQKHDE 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 492 IKKIGFNkeEIDTAMEDMLDDEPSKAKKRKKDdvkepeaakDVAVEAELKAARDRAlvpLEARMNQFRDMLLERGVSAFS 571
Cdd:COG5104 100 RSMIGGN--GNDMAITDHETSEPKYLLGRLMS---------QYGITSTKDAVYRLT---KEEAEKEFITMLKENQVDSTW 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 572 TWDKELHKIVfDPRYLLL--NPKERKQVFDQYVKTRAEEERKEKKNKLMQSKDDFRRMME-DAKLHTRTTFSEFAAKHSK 648
Cdd:COG5104 166 PIFRAIEELR-DPRYWMVdtDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCKMLAgNSHIKYYTDWFTFKSIFSK 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 649 DPRFKAIEKMKDREVMFTEFMTAFRKKDKEDSKNKVDKVKQDFFDLLSDHHVDITQRWSKVKDKLETDQRYKAvessaar 728
Cdd:COG5104 245 HPYYSSVVNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGSETFIIWLLNHYVFDSVVRYLK------- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 729 eefykqyvEKQAKNVdaDKEKELERQARIeasLREREREVQRARSEQTKEIDReREQHKREEAIQHFRALMSDMVRSTDT 808
Cdd:COG5104 318 --------NKEMKPL--DRKDILFSFIRY---VRRLEKELLSAIEERKAAAAQ-NARHHRDEFRTLLRKLYSEGKIYYRM 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 809 SWSETRRNLRKDHRW------ETSSLLErhekekLFEDHVEALTKRKKEHFRQLLDETpmitlttawkevkkiikedpRC 882
Cdd:COG5104 384 KWKNAYPLIKDDPRFlnllgrTGSSPLD------LFFDFIVDLENMYGFARRSYERET--------------------RT 437
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688606731 883 MKFSSSDRKKQREFEDYIKDKYIIAKADFRTLLKETkfITYRSRKLIQESDQhlkDIEKVLQNDKRYL 950
Cdd:COG5104 438 GQISPTDRRAVDEIFEAIAEKKEEGEIKFDKVDKED--ISLIVDGLIKQRNE---KIQQKLQNERRIL 500
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
847-902 |
1.33e-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: 54.50 E-value: 1.33e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 688606731 847 KRKKEHFRQLLDETPMITLTTAWKEVKKIIKEDPRCmKFSSSDRKKQREFEDYIKD 902
Cdd:smart00441 1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRY-KALLSESEREQLFEDHIEE 55
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
686-735 |
1.47e-09 |
|
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.
Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 54.39 E-value: 1.47e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 688606731 686 KVKQDFFDLLSDHHVDITQRWSKVKDKLETDQRYKAVESSAAREEFYKQY 735
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
345-372 |
1.09e-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: 51.37 E-value: 1.09e-08
10 20
....*....|....*....|....*...
gi 688606731 345 PEWSEFKTADGRIYYYNNRTLESTWEKP 372
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDP 29
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
125-156 |
1.81e-07 |
|
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: 47.88 E-value: 1.81e-07
10 20 30
....*....|....*....|....*....|..
gi 688606731 125 LPSEeiWVENNTPEGKVYYYNARTRESAWTKP 156
Cdd:pfam00397 1 LPPG--WEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
126-158 |
2.66e-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: 47.60 E-value: 2.66e-07
10 20 30
....*....|....*....|....*....|...
gi 688606731 126 PSEEIWVENNTPEGKVYYYNARTRESAWTKPEG 158
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
131-158 |
1.35e-06 |
|
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: 45.60 E-value: 1.35e-06
10 20
....*....|....*....|....*...
gi 688606731 131 WVENNTPEGKVYYYNARTRESAWTKPEG 158
Cdd:cd00201 4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
121-167 |
2.05e-05 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 48.54 E-value: 2.05e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 688606731 121 GAASLPSEEIWVENNTPEGKVYYYNARTRESAWTKPEgvKIIQQSEL 167
Cdd:COG5104 7 GMASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPK--ELLKGSEE 51
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
208-348 |
4.50e-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: 47.26 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 208 SPSHTLSTSPDPSTSPAptaSQPSITSVVSEMPPVVSTP---------------PVSVSVTPVAVVSVPTVTATVTAVQT 272
Cdd:pfam17823 286 MPSDTMARNPAAPMGAQ---AQGPIIQVSTDQPVHNTAGeptpspsnttlepntPKSVASTNLAVVTTTKAQAKEPSASP 362
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688606731 273 MPLLHQSLPPGLPVAPPAgaipfppvmvpPFRVPLPgmhiPLPGMGPPLVPMMHPQLTIAASPMSlAGAIPLPEWS 348
Cdd:pfam17823 363 VPVLHTSMIPEVEATSPT-----------TQPSPLL----PTQGAAGPGILLAPEQVATEATAGT-ASAGPTPRSS 422
|
|
| KLF8_12_N |
cd21093 |
N-terminal domain of Kruppel-like factor (KLF) 8, KLF12, and similar proteins; Kruppel-like ... |
206-281 |
5.92e-04 |
|
N-terminal domain of Kruppel-like factor (KLF) 8, KLF12, and similar proteins; Kruppel-like transcription factors (also known as Krueppel-like transcription factors, KLFs) belong to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Although these factors bind to similar elements in vitro, they have distinct activities in vivo depending on their expression profile and the sequence of the N-terminal activation/repression domain, which differ between members. This model represents the related N-terminal activation/repression domains of KLF8 and KLF12.
Pssm-ID: 410606 [Multi-domain] Cd Length: 172 Bit Score: 41.69 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 206 SMSPSHTLSTSPDPSTSPAPTASQPSITSVV--SEMPPVVSTPPVSVS------------VTPVAVVSVPTvtaTVTAVQ 271
Cdd:cd21093 56 SSPVSMSSSISSSSSSSPRPASSPTVITSVSsaSAIPTVLSPGSILASaqgvggqqilhvIHTVPSVSLPN---KMSHLH 132
|
90
....*....|
gi 688606731 272 TMPLLHQSLP 281
Cdd:cd21093 133 TIPVVVQSLP 142
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
486-902 |
1.64e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 486 KRGLDDIKKIGFNKEEIDTAMEDMLDDepskakKRKKDDVKEPEAAKDVAVEAELKAARDRALVPLEARMNQFRDMLLER 565
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAEED------KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK 1450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 566 GVSAFSTWDKELHKIVFDPRYL--LLNPKERKQVFDQyVKTRAEEERKE----KKNKLMQSKDDFRRMMEDAKLHTRTTF 639
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEAKKAdeAKKKAEEAKKADE-AKKKAEEAKKKadeaKKAAEAKKKADEAKKAEEAKKADEAKK 1529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 640 SEFAAKhsKDPRFKAIEKMKDREVMFTEFMTAFRKKDKEDSKNKVDKVKQDFFDLLSDHHVDITQRWSKVKDKLETDQRY 719
Cdd:PTZ00121 1530 AEEAKK--ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 720 KAVESSAAREEFYK----QYVEKQAKNVDADKEKELERQARIEASLREREREVQRARSEQTKEIDRER--EQHKREE--- 790
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKaeelKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKkaEEAKKAEede 1687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 791 ---AIQHFR----ALMSDMVRSTDTSWSETRRNLRKDH-----RWETSSLLERHEKEKLFEDHVEALTKRKKEHFRQLLD 858
Cdd:PTZ00121 1688 kkaAEALKKeaeeAKKAEELKKKEAEEKKKAEELKKAEeenkiKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 688606731 859 ETPmitlTTAWKEVKKIIKEDprcmkFSSSDRKKQREFEDYIKD 902
Cdd:PTZ00121 1768 KKA----EEIRKEKEAVIEEE-----LDEEDEKRRMEVDKKIKD 1802
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
221-386 |
2.85e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.40 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 221 TSPAPTASQPSITSVVSEMPP-VVSTPPVSVSVTPVAVVSVPTVTATVTAVQTMPLLHQSLPPGLPVAPPAGAIPFPPVM 299
Cdd:PRK12323 372 AGPATAAAAPVAQPAPAAAAPaAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 300 VPPFRVPLPGMHIPLPGMGPPLVPMMHPQLTIAASPMSLAGAIPLPEWSEFKTADGRIYYYNNRTLESTWEKPFELKERD 379
Cdd:PRK12323 452 PAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPAT 531
|
....*..
gi 688606731 380 KDSDKAR 386
Cdd:PRK12323 532 ADPDDAF 538
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
333-950 |
2.60e-23 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 105.55 E-value: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 333 ASPMSLAGAIPLPEWSEFKTADGRIYYYNNRTLESTWEKPFEL-KERDKDSDKardihnninldlklidmeakadfgksk 411
Cdd:COG5104 3 AALLGMASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPKELlKGSEEDLDV--------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 412 elpreedmteeekatqkgkpvatnpipgTPWCVVWTGDERVFYYNPTTRLSMWDRPEElvgradvdRYIQEPPHKRGLDD 491
Cdd:COG5104 56 ----------------------------DPWKECRTADGKVYYYNSITRESRWKIPPE--------RKKVEPIAEQKHDE 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 492 IKKIGFNkeEIDTAMEDMLDDEPSKAKKRKKDdvkepeaakDVAVEAELKAARDRAlvpLEARMNQFRDMLLERGVSAFS 571
Cdd:COG5104 100 RSMIGGN--GNDMAITDHETSEPKYLLGRLMS---------QYGITSTKDAVYRLT---KEEAEKEFITMLKENQVDSTW 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 572 TWDKELHKIVfDPRYLLL--NPKERKQVFDQYVKTRAEEERKEKKNKLMQSKDDFRRMME-DAKLHTRTTFSEFAAKHSK 648
Cdd:COG5104 166 PIFRAIEELR-DPRYWMVdtDPLWRKDLFKKYFENQEKDQREEEENKQRKYINEFCKMLAgNSHIKYYTDWFTFKSIFSK 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 649 DPRFKAIEKMKDREVMFTEFMTAFRKKDKEDSKNKVDKVKQDFFDLLSDHHVDITQRWSKVKDKLETDQRYKAvessaar 728
Cdd:COG5104 245 HPYYSSVVNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGSETFIIWLLNHYVFDSVVRYLK------- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 729 eefykqyvEKQAKNVdaDKEKELERQARIeasLREREREVQRARSEQTKEIDReREQHKREEAIQHFRALMSDMVRSTDT 808
Cdd:COG5104 318 --------NKEMKPL--DRKDILFSFIRY---VRRLEKELLSAIEERKAAAAQ-NARHHRDEFRTLLRKLYSEGKIYYRM 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 809 SWSETRRNLRKDHRW------ETSSLLErhekekLFEDHVEALTKRKKEHFRQLLDETpmitlttawkevkkiikedpRC 882
Cdd:COG5104 384 KWKNAYPLIKDDPRFlnllgrTGSSPLD------LFFDFIVDLENMYGFARRSYERET--------------------RT 437
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688606731 883 MKFSSSDRKKQREFEDYIKDKYIIAKADFRTLLKETkfITYRSRKLIQESDQhlkDIEKVLQNDKRYL 950
Cdd:COG5104 438 GQISPTDRRAVDEIFEAIAEKKEEGEIKFDKVDKED--ISLIVDGLIKQRNE---KIQQKLQNERRIL 500
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
847-902 |
1.33e-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: 54.50 E-value: 1.33e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 688606731 847 KRKKEHFRQLLDETPMITLTTAWKEVKKIIKEDPRCmKFSSSDRKKQREFEDYIKD 902
Cdd:smart00441 1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRY-KALLSESEREQLFEDHIEE 55
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
686-735 |
1.47e-09 |
|
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.
Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 54.39 E-value: 1.47e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 688606731 686 KVKQDFFDLLSDHHVDITQRWSKVKDKLETDQRYKAVESSAAREEFYKQY 735
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
557-601 |
3.04e-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: 53.61 E-value: 3.04e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 688606731 557 QFRDMLLERGVSAFSTWDKELHKIVFDPRYL-LLNPKERKQVFDQY 601
Cdd:pfam01846 5 AFKELLKEHKITPYSTWSEIKKKIENDPRYKaLLDGSEREELFEDY 50
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
621-668 |
3.99e-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: 3.99e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 688606731 621 KDDFRRMMEDAKLHTRTTFSEFAAKHSKDPRFKAIEKMKDREVMFTEF 668
Cdd:pfam01846 3 REAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
345-372 |
1.09e-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: 51.37 E-value: 1.09e-08
10 20
....*....|....*....|....*...
gi 688606731 345 PEWSEFKTADGRIYYYNNRTLESTWEKP 372
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDP 29
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
345-372 |
1.31e-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: 51.35 E-value: 1.31e-08
10 20
....*....|....*....|....*...
gi 688606731 345 PEWSEFKTADGRIYYYNNRTLESTWEKP 372
Cdd:pfam00397 3 PGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
343-372 |
3.17e-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: 50.29 E-value: 3.17e-08
10 20 30
....*....|....*....|....*....|.
gi 688606731 343 PLPE-WSEFKTADGRIYYYNNRTLESTWEKP 372
Cdd:smart00456 1 PLPPgWEERKDPDGRPYYYNHETKETQWEKP 31
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
790-841 |
4.19e-08 |
|
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: 50.15 E-value: 4.19e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 688606731 790 EAIQHFRALMSDMVRSTDTSWSETRRNLRKDHRWetSSLLERHEKEKLFEDH 841
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRY--KALLDGSEREELFEDY 50
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
125-156 |
1.81e-07 |
|
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: 47.88 E-value: 1.81e-07
10 20 30
....*....|....*....|....*....|..
gi 688606731 125 LPSEeiWVENNTPEGKVYYYNARTRESAWTKP 156
Cdd:pfam00397 1 LPPG--WEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
126-158 |
2.66e-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: 47.60 E-value: 2.66e-07
10 20 30
....*....|....*....|....*....|...
gi 688606731 126 PSEEIWVENNTPEGKVYYYNARTRESAWTKPEG 158
Cdd:smart00456 1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
347-899 |
6.28e-07 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 53.16 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 347 WSEFKTADGRIYYYNNRTLESTWEKPFELKERDKDSDKARDIHNNInldlKLIDMEAKADFGKSKELPREEDMTEEEkat 426
Cdd:COG5104 58 WKECRTADGKVYYYNSITRESRWKIPPERKKVEPIAEQKHDERSMI----GGNGNDMAITDHETSEPKYLLGRLMSQ--- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 427 qkgkpvatnpipgtpwcvvwtgdervfYYNPTTRLSMWDRPEELVGRADVDRYiqeppHKRGLDDIKKIGFNKEEIDTAM 506
Cdd:COG5104 131 ---------------------------YGITSTKDAVYRLTKEEAEKEFITML-----KENQVDSTWPIFRAIEELRDPR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 507 EDMLDDEPSKAKKRKKDDVKEPEAAKDVAVEAELKAARdralvplearmNQFRDMLL-ERGVSAFSTWDKELHKIVFDPR 585
Cdd:COG5104 179 YWMVDTDPLWRKDLFKKYFENQEKDQREEEENKQRKYI-----------NEFCKMLAgNSHIKYYTDWFTFKSIFSKHPY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 586 Y-LLLNPKERKQVFDQYVKTRAEEERKEKKNKLMQSKDDFRRMMEDAKLHTRTTFSEFAAKHSKDPRFKAIEKMK--DRE 662
Cdd:COG5104 248 YsSVVNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLRSLGSETFIIWLLNHYVFDSVVRYLKNKEMKplDRK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 663 VMFTEFMTAFRKKDKE---------DSKNKVDKVKQDFF-----DLLSDHHVDITQRWSKVKDKLETDQRYKAV---ESS 725
Cdd:COG5104 328 DILFSFIRYVRRLEKEllsaieerkAAAAQNARHHRDEFrtllrKLYSEGKIYYRMKWKNAYPLIKDDPRFLNLlgrTGS 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 726 AAREEFYKQYVekqaknvdadkekELERQARIEASLREREREVQRARSEQTKEIDR--EREQHKREEAIQHFRALMSDMV 803
Cdd:COG5104 408 SPLDLFFDFIV-------------DLENMYGFARRSYERETRTGQISPTDRRAVDEifEAIAEKKEEGEIKFDKVDKEDI 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 804 rstdtswsetrrNLRKDhrwetSSLLERHEKEKLFEDHVEALTKRKKEHFRQLLDETPMIT---LTTAWKEVKKIIKEDP 880
Cdd:COG5104 475 ------------SLIVD-----GLIKQRNEKIQQKLQNERRILEQKKHYFWLLLQRTYTKTgkpKPSTWDLASKELGESL 537
|
570
....*....|....*....
gi 688606731 881 RCMKFSSSDRKKQREFEDY 899
Cdd:COG5104 538 EYKALGDEDNIRRQIFEDF 556
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
131-158 |
1.35e-06 |
|
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: 45.60 E-value: 1.35e-06
10 20
....*....|....*....|....*...
gi 688606731 131 WVENNTPEGKVYYYNARTRESAWTKPEG 158
Cdd:cd00201 4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
441-469 |
2.68e-06 |
|
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: 44.90 E-value: 2.68e-06
10 20
....*....|....*....|....*....
gi 688606731 441 PWCVVWTGDERVFYYNPTTRLSMWDRPEE 469
Cdd:smart00456 5 GWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
440-469 |
5.46e-06 |
|
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: 43.67 E-value: 5.46e-06
10 20 30
....*....|....*....|....*....|
gi 688606731 440 TPWCVVWTGDERVFYYNPTTRLSMWDRPEE 469
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
789-844 |
1.26e-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: 43.33 E-value: 1.26e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 688606731 789 EEAIQHFRALMSDMVRST-DTSWSETRRNLRKDHRWEtsSLLERHEKEKLFEDHVEA 844
Cdd:smart00441 1 EEAKEAFKELLKEHEVITpDTTWSEARKKLKNDPRYK--ALLSESEREQLFEDHIEE 55
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
848-899 |
1.33e-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: 43.21 E-value: 1.33e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 688606731 848 RKKEHFRQLLDETPmITLTTAWKEVKKIIKEDPR--CMKfSSSDRKkqREFEDY 899
Cdd:pfam01846 1 KAREAFKELLKEHK-ITPYSTWSEIKKKIENDPRykALL-DGSERE--ELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
552-603 |
1.50e-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: 43.33 E-value: 1.50e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 688606731 552 EARMNQFRDMLLERGVS-AFSTWDKELHKIVFDPRY-LLLNPKERKQVFDQYVK 603
Cdd:smart00441 1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYkALLSESEREQLFEDHIE 54
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
121-167 |
2.05e-05 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 48.54 E-value: 2.05e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 688606731 121 GAASLPSEEIWVENNTPEGKVYYYNARTRESAWTKPEgvKIIQQSEL 167
Cdd:COG5104 7 GMASGEARSEWEELKAPDGRIYYYNKRTGKSSWEKPK--ELLKGSEE 51
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
440-467 |
3.25e-05 |
|
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: 41.72 E-value: 3.25e-05
10 20
....*....|....*....|....*...
gi 688606731 440 TPWCVVWTGDERVFYYNPTTRLSMWDRP 467
Cdd:pfam00397 3 PGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
208-348 |
4.50e-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: 47.26 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 208 SPSHTLSTSPDPSTSPAptaSQPSITSVVSEMPPVVSTP---------------PVSVSVTPVAVVSVPTVTATVTAVQT 272
Cdd:pfam17823 286 MPSDTMARNPAAPMGAQ---AQGPIIQVSTDQPVHNTAGeptpspsnttlepntPKSVASTNLAVVTTTKAQAKEPSASP 362
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688606731 273 MPLLHQSLPPGLPVAPPAgaipfppvmvpPFRVPLPgmhiPLPGMGPPLVPMMHPQLTIAASPMSlAGAIPLPEWS 348
Cdd:pfam17823 363 VPVLHTSMIPEVEATSPT-----------TQPSPLL----PTQGAAGPGILLAPEQVATEATAGT-ASAGPTPRSS 422
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
907-966 |
8.41e-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: 40.90 E-value: 8.41e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 907 AKADFRTLLKETKfITYRSRkliqesdqhLKDIEKVLQNDKRYLVLDcVPEERRKLIMFY 966
Cdd:pfam01846 2 AREAFKELLKEHK-ITPYST---------WSEIKKKIENDPRYKALL-DGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
621-669 |
8.62e-05 |
|
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.
Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 41.02 E-value: 8.62e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 688606731 621 KDDFRRMMEDA-KLHTRTTFSEFAAKHSKDPRFKAIEKMKDREVMFTEFM 669
Cdd:smart00441 4 KEAFKELLKEHeVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHI 53
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
205-345 |
1.08e-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: 46.30 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 205 QSMSPSHTLSTSPDPSTSPAPTAS-QPSITSVVSEMPPVVSTPPVSvSVTPVAVVSVPTVTATVTAvQTMPLLHQSLPPg 283
Cdd:pfam03154 175 QAQSGAASPPSPPPPGTTQAATAGpTPSAPSVPPQGSPATSQPPNQ-TQSTAAPHTLIQQTPTLHP-QRLPSPHPPLQP- 251
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688606731 284 LPVAPPAGAIPFPPVMVPPFRVPLPGMHIPLPGmGPPLVPMMHPQLTIAASPMSLAGAIPLP 345
Cdd:pfam03154 252 MTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQT-GPSHMQHPVPPQPFPLTPQSSQSQVPPG 312
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
720-847 |
1.32e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 44.88 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 720 KAVESSAAREEFY--KQYVEK---QAKNVDADKEKELErQARIEASLREREREVQRARSEQTKEIDREREQHKREeaiqH 794
Cdd:cd16269 164 KGVKAEEVLQEFLqsKEAEAEailQADQALTEKEKEIE-AERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEE----H 238
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 688606731 795 FRALMSDMVrstdtswsETRRNLRKDHRWETSSLLERHEK--EKLFEDHVEALTK 847
Cdd:cd16269 239 LRQLKEKME--------EERENLLKEQERALESKLKEQEAllEEGFKEQAELLQE 285
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
625-843 |
4.22e-04 |
|
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: 44.34 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 625 RRMMEDAKLHTRTTFSEFAAKHSKDPRFkAIEKMKDREVMFTEFmtafRKKDKEDSKNKVDKVKQDFFDLLSDHHVDITQ 704
Cdd:pfam17380 315 RRKLEEAEKARQAEMDRQAAIYAEQERM-AMERERELERIRQEE----RKRELERIRQEEIAMEISRMRELERLQMERQQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 705 RWSKVKDKLETDQRYKAVEssaarEEFYKQYVEKQAKNVDADKEKELERQARIEASLREREREVQRARSEQtKEIDRERE 784
Cdd:pfam17380 390 KNERVRQELEAARKVKILE-----EERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEE-QERQQQVE 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 785 QHKREEAIQHFRALMSDMVRSTDTSWSETRRN-LRKDHRWETSSLLERHEKEKLFEDHVE 843
Cdd:pfam17380 464 RLRQQEEERKRKKLELEKEKRDRKRAEEQRRKiLEKELEERKQAMIEEERKRKLLEKEME 523
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
685-738 |
4.87e-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: 39.09 E-value: 4.87e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 688606731 685 DKVKQDFFDLLSDHHVDIT-QRWSKVKDKLETDQRYKAVESSAAREEFYKQYVEK 738
Cdd:smart00441 1 EEAKEAFKELLKEHEVITPdTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
|
|
| KLF8_12_N |
cd21093 |
N-terminal domain of Kruppel-like factor (KLF) 8, KLF12, and similar proteins; Kruppel-like ... |
206-281 |
5.92e-04 |
|
N-terminal domain of Kruppel-like factor (KLF) 8, KLF12, and similar proteins; Kruppel-like transcription factors (also known as Krueppel-like transcription factors, KLFs) belong to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Although these factors bind to similar elements in vitro, they have distinct activities in vivo depending on their expression profile and the sequence of the N-terminal activation/repression domain, which differ between members. This model represents the related N-terminal activation/repression domains of KLF8 and KLF12.
Pssm-ID: 410606 [Multi-domain] Cd Length: 172 Bit Score: 41.69 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 206 SMSPSHTLSTSPDPSTSPAPTASQPSITSVV--SEMPPVVSTPPVSVS------------VTPVAVVSVPTvtaTVTAVQ 271
Cdd:cd21093 56 SSPVSMSSSISSSSSSSPRPASSPTVITSVSsaSAIPTVLSPGSILASaqgvggqqilhvIHTVPSVSLPN---KMSHLH 132
|
90
....*....|
gi 688606731 272 TMPLLHQSLP 281
Cdd:cd21093 133 TIPVVVQSLP 142
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
127-166 |
1.36e-03 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 42.37 E-value: 1.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 688606731 127 SEEIWVENNTPEGKVYYYNARTRESAWTKPEGVKIIQQSE 166
Cdd:COG5104 54 DVDPWKECRTADGKVYYYNSITRESRWKIPPERKKVEPIA 93
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
486-902 |
1.64e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 486 KRGLDDIKKIGFNKEEIDTAMEDMLDDepskakKRKKDDVKEPEAAKDVAVEAELKAARDRALVPLEARMNQFRDMLLER 565
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAEED------KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK 1450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 566 GVSAFSTWDKELHKIVFDPRYL--LLNPKERKQVFDQyVKTRAEEERKE----KKNKLMQSKDDFRRMMEDAKLHTRTTF 639
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEAKKAdeAKKKAEEAKKADE-AKKKAEEAKKKadeaKKAAEAKKKADEAKKAEEAKKADEAKK 1529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 640 SEFAAKhsKDPRFKAIEKMKDREVMFTEFMTAFRKKDKEDSKNKVDKVKQDFFDLLSDHHVDITQRWSKVKDKLETDQRY 719
Cdd:PTZ00121 1530 AEEAKK--ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 720 KAVESSAAREEFYK----QYVEKQAKNVDADKEKELERQARIEASLREREREVQRARSEQTKEIDRER--EQHKREE--- 790
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKaeelKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKkaEEAKKAEede 1687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 791 ---AIQHFR----ALMSDMVRSTDTSWSETRRNLRKDH-----RWETSSLLERHEKEKLFEDHVEALTKRKKEHFRQLLD 858
Cdd:PTZ00121 1688 kkaAEALKKeaeeAKKAEELKKKEAEEKKKAEELKKAEeenkiKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 688606731 859 ETPmitlTTAWKEVKKIIKEDprcmkFSSSDRKKQREFEDYIKD 902
Cdd:PTZ00121 1768 KKA----EEIRKEKEAVIEEE-----LDEEDEKRRMEVDKKIKD 1802
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
698-973 |
1.86e-03 |
|
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: 42.03 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 698 HHVDITQRWSKVKDKLETDQRYKAVESSAAREefykqyVEKQAKNVDADKEK--ELERQARIEASLR----EREREVQRA 771
Cdd:pfam17380 280 HQKAVSERQQQEKFEKMEQERLRQEKEEKARE------VERRRKLEEAEKARqaEMDRQAAIYAEQErmamERERELERI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 772 RSEQTKeidREREQHKREEAIQHfralMSDMVRSTDTSWSETRRNLRKDHRWETS---SLLERHEKEKLFEDHVEALTKR 848
Cdd:pfam17380 354 RQEERK---RELERIRQEEIAME----ISRMRELERLQMERQQKNERVRQELEAArkvKILEEERQRKIQQQKVEMEQIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 849 K-KEHFRQlldetpmitlttawKEVKKIIKEDPRCMkfsssDRKKQREFEDYIKDKYIIAKADFRTLLKETKFITYRSRK 927
Cdd:pfam17380 427 AeQEEARQ--------------REVRRLEEERAREM-----ERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRK 487
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 688606731 928 LIQEsdQHLKDIEKVLQNDKRYLVldcvpEERRKLIMFYIEDLDRR 973
Cdd:pfam17380 488 RAEE--QRRKILEKELEERKQAMI-----EEERKRKLLEKEMEERQ 526
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
221-386 |
2.85e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.40 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 221 TSPAPTASQPSITSVVSEMPP-VVSTPPVSVSVTPVAVVSVPTVTATVTAVQTMPLLHQSLPPGLPVAPPAGAIPFPPVM 299
Cdd:PRK12323 372 AGPATAAAAPVAQPAPAAAAPaAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 300 VPPFRVPLPGMHIPLPGMGPPLVPMMHPQLTIAASPMSLAGAIPLPEWSEFKTADGRIYYYNNRTLESTWEKPFELKERD 379
Cdd:PRK12323 452 PAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPAT 531
|
....*..
gi 688606731 380 KDSDKAR 386
Cdd:PRK12323 532 ADPDDAF 538
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
746-810 |
3.20e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 41.39 E-value: 3.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688606731 746 DKEKELERQARIEASlREREREVQRARSEQTKEIDREREQHKREEAIQH--FRALMSDMVRSTDTSW 810
Cdd:PLN02316 253 EKRRELEKLAKEEAE-RERQAEEQRRREEEKAAMEADRAQAKAEVEKRRekLQNLLKKASRSADNVW 318
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
653-948 |
3.78e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 653 KAIEKMKDR-EVMFTEFMTAFRKKDK-----EDSKNKVDKVKQDFFDLLSDHHVDITQ---RWSKVKDKLETDQRyKAVE 723
Cdd:pfam01576 176 KSLSKLKNKhEAMISDLEERLKKEEKgrqelEKAKRKLEGESTDLQEQIAELQAQIAElraQLAKKEEELQAALA-RLEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 724 SSAAREEFYKQYVEKQAKNVDADKEKELERQARIEASLRERE--REVQRARSEQTKEIDREREQH----KREEAIQHFRA 797
Cdd:pfam01576 255 ETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDlgEELEALKTELEDTLDTTAAQQelrsKREQEVTELKK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 798 LMSDMVRSTDTSWSEtrrnLRKDHRWETSSLLERHEKEKLFEDHVEALTKRKKEHFRQLLDEtpMITLTTAWKEVK-KII 876
Cdd:pfam01576 335 ALEEETRSHEAQLQE----MRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAE--LRTLQQAKQDSEhKRK 408
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688606731 877 KEDPRC----MKFSSSDRKKQREFEDYIKDKYIIAKADfrTLLKETKFITYRSRKLIQESDQHLKDIEKVLQNDKR 948
Cdd:pfam01576 409 KLEGQLqelqARLSESERQRAELAEKLSKLQSELESVS--SLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETR 482
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
206-341 |
5.01e-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: 40.71 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 206 SMSPSHTLSTSPDPSTSPAPTASQPSITSVVSEMPPVVSTPPVSVSVTPVAVVSV-PTVTATVTAVQtmPLLHQSLPPGL 284
Cdd:pfam17823 155 SAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPArGISTAATATGH--PAAGTALAAVG 232
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688606731 285 PVAPPAGAIPFPPVMVPPFRVPLPGMHI-------PLPGMGPP----LVPMMH-PQLTIAASPMSLAGA 341
Cdd:pfam17823 233 NSSPAAGTVTAAVGTVTPAALATLAAAAgtvasaaGTINMGDPharrLSPAKHmPSDTMARNPAAPMGA 301
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
907-969 |
6.24e-03 |
|
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: 36.01 E-value: 6.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688606731 907 AKADFRTLLKETKFITYrsrkliqesDQHLKDIEKVLQNDKRYLVLDcvpEERRKLIMF--YIED 969
Cdd:smart00441 3 AKEAFKELLKEHEVITP---------DTTWSEARKKLKNDPRYKALL---SESEREQLFedHIEE 55
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
651-781 |
8.11e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688606731 651 RFKAIEKMKDREVMFTEFMTAFRKKDKEDSKNKVDKVKQDFFDLLSDHHVDITQRWSKVKDKLETDQRykavessaaREE 730
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQ---------KEE 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 688606731 731 FykqyVEKQAKNVDaDKEKELERQ----ARIEASLREREREVQRARSEQTKEIDR 781
Cdd:PRK12704 97 N----LDRKLELLE-KREEELEKKekelEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| |
