|
Name |
Accession |
Description |
Interval |
E-value |
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
226-811 |
7.42e-18 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 88.21 E-value: 7.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 226 WNEFNAPDGRKYYFNSITQENTWEKPKALIDQENgggaspepvqsaaiaeaqakaqaalaafmaqqktssnggggmplsk 305
Cdd:COG5104 17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSE---------------------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 306 aqasgaaaaaavnaeaakkkdstrpissTPVSGTPWCVVWTGDDKVFFYNPSTKCSVWERPPDtygredvDKLVQNPPSP 385
Cdd:COG5104 51 ----------------------------EDLDVDPWKECRTADGKVYYYNSITRESRWKIPPE-------RKKVEPIAEQ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 386 KAEEENnqskkesesesesdedgppkakKSRAEKKKEALIAAQKKEKER--PRQMLQKPVDPAIEAEMQAAKErekvple 463
Cdd:COG5104 96 KHDERS----------------------MIGGNGNDMAITDHETSEPKYllGRLMSQYGITSTKDAVYRLTKE------- 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 464 ERLKQFKEMLEEKNVSTSSTFEKELSKIVFDKRYLSLGATERRAC-FDAFCREKIESEKAERRKRVKEAKEEFQKLLA-E 541
Cdd:COG5104 147 EAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDlFKKYFENQEKDQREEEENKQRKYINEFCKMLAgN 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 542 CELNGRSSYSSFTSKFGKDPRYKAVERNRDREDAFNDFVGELHKKEKDEKRAKKEKLKAAFVKLLEeQTGLTRKSKWSTT 621
Cdd:COG5104 227 SHIKYYTDWFTFKSIFSKHPYYSSVVNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLR-SLGSETFIIWLLN 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 622 KKTLEDEERYIALdssstreslfrefvanlgdetasdieEEQEREKRLAAQTAIANRQKEVEAELGNQLRERTKESEkQK 701
Cdd:COG5104 306 HYVFDSVVRYLKN--------------------------KEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAA-QN 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 702 MGEHEDTYRNLLIDL----IKSTENSWHEARRILRKDERYANCDMLDKTRKESLFDDHIKSLERKRREAFFQVLDNHE-- 775
Cdd:COG5104 359 ARHHRDEFRTLLRKLysegKIYYRMKWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYERETRtg 438
|
570 580 590
....*....|....*....|....*....|....*.
gi 1831508436 776 KITPMMRwRDAKKIiqdeeetfvkIASNSERKVERD 811
Cdd:COG5104 439 QISPTDR-RAVDEI----------FEAIAEKKEEGE 463
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
530-579 |
1.17e-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: 1.17e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1831508436 530 EAKEEFQKLLAECELNGRSSYSSFTSKFGKDPRYKAVERNRDREDAFNDF 579
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
596-650 |
7.42e-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: 52.58 E-value: 7.42e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1831508436 596 EKLKAAFVKLLEEQTGLTRKSKWSTTKKTLEDEERYIALDSSSTRESLFREFVAN 650
Cdd:smart00441 1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
386-863 |
1.43e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 386 KAEEENNQSKKESESESESDEDGPPKAKKSRAEKKKEALIAAQKKEKERPRQMLQKpvdPAIEAEMQAAKEREKVPLEER 465
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK---KAEEDKKKADELKKAAAAKKK 1419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 466 LKQFKEMLEEKNVStsstfeKELSKIVFDKRY---LSLGATERRACFDAFCREKIESEKAERRKRVKEAK--EEFQKLLA 540
Cdd:PTZ00121 1420 ADEAKKKAEEKKKA------DEAKKKAEEAKKadeAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkaDEAKKKAE 1493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 541 ECELNGRSSYSSFTSKFGKDPRYKAVERNRDREDAFNDfvgelHKKEKDEKRAKKEKLKAAFVKLLEEQTGLTRKSKWST 620
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE-----EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 621 TKKtlEDEERYIALDSSstreslfrEFVANLGDETASDIEEEQEREKRLAAQTAIANRQKEVEAELGNQLRERTKESEKQ 700
Cdd:PTZ00121 1569 AKK--AEEDKNMALRKA--------EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 701 KMGEHEDTYRNLliDLIKSTENSWHEARRILRKDERyancdmlDKTRKESLFDDhiKSLERKRREAFFQVLDNHEKITPM 780
Cdd:PTZ00121 1639 KKKEAEEKKKAE--ELKKAEEENKIKAAEEAKKAEE-------DKKKAEEAKKA--EEDEKKAAEALKKEAEEAKKAEEL 1707
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 781 MRW-----RDAKKIIQDEEETFVKiASNSERKVERDFRDWQERRHDH-----LTDEFKEMLSETKIITHKSKKLMEEGEQ 850
Cdd:PTZ00121 1708 KKKeaeekKKAEELKKAEEENKIK-AEEAKKEAEEDKKKAEEAKKDEeekkkIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
490
....*....|...
gi 1831508436 851 HMDILSVLENDKR 863
Cdd:PTZ00121 1787 EEDEKRRMEVDKK 1799
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
226-251 |
3.80e-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: 44.06 E-value: 3.80e-06
10 20
....*....|....*....|....*.
gi 1831508436 226 WNEFNAPDGRKYYFNSITQENTWEKP 251
Cdd:cd00201 4 WEERWDPDGRVYYYNHNTKETQWEDP 29
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
159-186 |
1.78e-05 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 42.20 E-value: 1.78e-05
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
159-184 |
3.70e-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: 41.36 E-value: 3.70e-05
10 20
....*....|....*....|....*.
gi 1831508436 159 WVETETAEGKKYFYHPVNRNTIWERP 184
Cdd:cd00201 4 WEERWDPDGRVYYYNHNTKETQWEDP 29
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
159-184 |
6.92e-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: 40.57 E-value: 6.92e-05
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
825-882 |
1.84e-03 |
|
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: 37.05 E-value: 1.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1831508436 825 DEFKEMLSETKiITHKSKklmeegeqHMDILSVLENDKRWVRMtaMSASERDRMLEDH 882
Cdd:pfam01846 4 EAFKELLKEHK-ITPYST--------WSEIKKKIENDPRYKAL--LDGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
821-885 |
3.77e-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: 36.40 E-value: 3.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831508436 821 DHLTDEFKEMLSETKIITHKSKklMEEgeqhmdILSVLENDKRWVRMtaMSASERDRMLEDHIEN 885
Cdd:smart00441 1 EEAKEAFKELLKEHEVITPDTT--WSE------ARKKLKNDPRYKAL--LSESEREQLFEDHIEE 55
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
226-811 |
7.42e-18 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 88.21 E-value: 7.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 226 WNEFNAPDGRKYYFNSITQENTWEKPKALIDQENgggaspepvqsaaiaeaqakaqaalaafmaqqktssnggggmplsk 305
Cdd:COG5104 17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSE---------------------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 306 aqasgaaaaaavnaeaakkkdstrpissTPVSGTPWCVVWTGDDKVFFYNPSTKCSVWERPPDtygredvDKLVQNPPSP 385
Cdd:COG5104 51 ----------------------------EDLDVDPWKECRTADGKVYYYNSITRESRWKIPPE-------RKKVEPIAEQ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 386 KAEEENnqskkesesesesdedgppkakKSRAEKKKEALIAAQKKEKER--PRQMLQKPVDPAIEAEMQAAKErekvple 463
Cdd:COG5104 96 KHDERS----------------------MIGGNGNDMAITDHETSEPKYllGRLMSQYGITSTKDAVYRLTKE------- 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 464 ERLKQFKEMLEEKNVSTSSTFEKELSKIVFDKRYLSLGATERRAC-FDAFCREKIESEKAERRKRVKEAKEEFQKLLA-E 541
Cdd:COG5104 147 EAEKEFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDPLWRKDlFKKYFENQEKDQREEEENKQRKYINEFCKMLAgN 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 542 CELNGRSSYSSFTSKFGKDPRYKAVERNRDREDAFNDFVGELHKKEKDEKRAKKEKLKAAFVKLLEeQTGLTRKSKWSTT 621
Cdd:COG5104 227 SHIKYYTDWFTFKSIFSKHPYYSSVVNEKTKRQTFQKYKDKLGCYEKYVGKHMGGTALGRLEEVLR-SLGSETFIIWLLN 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 622 KKTLEDEERYIALdssstreslfrefvanlgdetasdieEEQEREKRLAAQTAIANRQKEVEAELGNQLRERTKESEkQK 701
Cdd:COG5104 306 HYVFDSVVRYLKN--------------------------KEMKPLDRKDILFSFIRYVRRLEKELLSAIEERKAAAA-QN 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 702 MGEHEDTYRNLLIDL----IKSTENSWHEARRILRKDERYANCDMLDKTRKESLFDDHIKSLERKRREAFFQVLDNHE-- 775
Cdd:COG5104 359 ARHHRDEFRTLLRKLysegKIYYRMKWKNAYPLIKDDPRFLNLLGRTGSSPLDLFFDFIVDLENMYGFARRSYERETRtg 438
|
570 580 590
....*....|....*....|....*....|....*.
gi 1831508436 776 KITPMMRwRDAKKIiqdeeetfvkIASNSERKVERD 811
Cdd:COG5104 439 QISPTDR-RAVDEI----------FEAIAEKKEEGE 463
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
530-579 |
1.17e-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: 1.17e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1831508436 530 EAKEEFQKLLAECELNGRSSYSSFTSKFGKDPRYKAVERNRDREDAFNDF 579
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
597-647 |
2.31e-10 |
|
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.
Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 56.70 E-value: 2.31e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1831508436 597 KLKAAFVKLLEEqTGLTRKSKWSTTKKTLEDEERYIALDSSSTRESLFREF 647
Cdd:pfam01846 1 KAREAFKELLKE-HKITPYSTWSEIKKKIENDPRYKALLDGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
596-650 |
7.42e-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: 52.58 E-value: 7.42e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1831508436 596 EKLKAAFVKLLEEQTGLTRKSKWSTTKKTLEDEERYIALDSSSTRESLFREFVAN 650
Cdd:smart00441 1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
529-582 |
5.06e-08 |
|
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.
Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 50.26 E-value: 5.06e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1831508436 529 KEAKEEFQKLLAECELN-GRSSYSSFTSKFGKDPRYKAVERNRDREDAFNDFVGE 582
Cdd:smart00441 1 EEAKEAFKELLKEHEVItPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIEE 55
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
761-818 |
1.01e-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: 49.11 E-value: 1.01e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1831508436 761 RKRREAFFQVLDNHEKITPMMRWRDAKKIIQDEEETfvkIASNSERKVERDFRDWQER 818
Cdd:smart00441 1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRY---KALLSESEREQLFEDHIEE 55
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
464-512 |
1.32e-07 |
|
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.
Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 48.61 E-value: 1.32e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1831508436 464 ERLKQFKEMLEEKNVSTSSTFEKELSKIVFDKRYLSLG-ATERRACFDAF 512
Cdd:pfam01846 1 KAREAFKELLKEHKITPYSTWSEIKKKIENDPRYKALLdGSEREELFEDY 50
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
159-563 |
1.49e-07 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 55.09 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 159 WVETETAEGKKYFYHPVNRNTIWERPQnakivtqpelaQLIHRatEEEKNREermphgqipqnpdDAWNEFNAPDGRKYY 238
Cdd:COG5104 17 WEELKAPDGRIYYYNKRTGKSSWEKPK-----------ELLKG--SEEDLDV-------------DPWKECRTADGKVYY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 239 FNSITQENTWEKP---KALIDQENGGGASPEPVQSAAIAEAQAKAQAALAAFMAQQKTSSNGGGGMPLS-KAQASGAAAA 314
Cdd:COG5104 71 YNSITRESRWKIPperKKVEPIAEQKHDERSMIGGNGNDMAITDHETSEPKYLLGRLMSQYGITSTKDAvYRLTKEEAEK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 315 AAVNAEAAKKKDSTRPISSTPVSGTPWCVVWTGDD--------KVFFYNPSTKCSVWERPPDTYGREDVDKLVQNPPSPK 386
Cdd:COG5104 151 EFITMLKENQVDSTWPIFRAIEELRDPRYWMVDTDplwrkdlfKKYFENQEKDQREEEENKQRKYINEFCKMLAGNSHIK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 387 AEEENnqskkesesesesdedgpPKAKKsraEKKKEALIAAQKKEKERpRQMLQKPVDPAIEAEMQAAKEREKvpleERL 466
Cdd:COG5104 231 YYTDW------------------FTFKS---IFSKHPYYSSVVNEKTK-RQTFQKYKDKLGCYEKYVGKHMGG----TAL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 467 KQFKEMLEEKNVSTSSTFEKELSKIVFDKRYLSLGATE---RRACFDAFCR----------EKIESEKAERRKRVKEAKE 533
Cdd:COG5104 285 GRLEEVLRSLGSETFIIWLLNHYVFDSVVRYLKNKEMKpldRKDILFSFIRyvrrlekellSAIEERKAAAAQNARHHRD 364
|
410 420 430
....*....|....*....|....*....|....
gi 1831508436 534 EFQKLLAECELNG----RSSYSSFTSKFGKDPRY 563
Cdd:COG5104 365 EFRTLLRKLYSEGkiyyRMKWKNAYPLIKDDPRF 398
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
386-863 |
1.43e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 386 KAEEENNQSKKESESESESDEDGPPKAKKSRAEKKKEALIAAQKKEKERPRQMLQKpvdPAIEAEMQAAKEREKVPLEER 465
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK---KAEEDKKKADELKKAAAAKKK 1419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 466 LKQFKEMLEEKNVStsstfeKELSKIVFDKRY---LSLGATERRACFDAFCREKIESEKAERRKRVKEAK--EEFQKLLA 540
Cdd:PTZ00121 1420 ADEAKKKAEEKKKA------DEAKKKAEEAKKadeAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkaDEAKKKAE 1493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 541 ECELNGRSSYSSFTSKFGKDPRYKAVERNRDREDAFNDfvgelHKKEKDEKRAKKEKLKAAFVKLLEEQTGLTRKSKWST 620
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE-----EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 621 TKKtlEDEERYIALDSSstreslfrEFVANLGDETASDIEEEQEREKRLAAQTAIANRQKEVEAELGNQLRERTKESEKQ 700
Cdd:PTZ00121 1569 AKK--AEEDKNMALRKA--------EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 701 KMGEHEDTYRNLliDLIKSTENSWHEARRILRKDERyancdmlDKTRKESLFDDhiKSLERKRREAFFQVLDNHEKITPM 780
Cdd:PTZ00121 1639 KKKEAEEKKKAE--ELKKAEEENKIKAAEEAKKAEE-------DKKKAEEAKKA--EEDEKKAAEALKKEAEEAKKAEEL 1707
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 781 MRW-----RDAKKIIQDEEETFVKiASNSERKVERDFRDWQERRHDH-----LTDEFKEMLSETKIITHKSKKLMEEGEQ 850
Cdd:PTZ00121 1708 KKKeaeekKKAEELKKAEEENKIK-AEEAKKEAEEDKKKAEEAKKDEeekkkIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
490
....*....|...
gi 1831508436 851 HMDILSVLENDKR 863
Cdd:PTZ00121 1787 EEDEKRRMEVDKK 1799
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
226-251 |
1.75e-06 |
|
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: 45.19 E-value: 1.75e-06
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
226-251 |
3.80e-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: 44.06 E-value: 3.80e-06
10 20
....*....|....*....|....*.
gi 1831508436 226 WNEFNAPDGRKYYFNSITQENTWEKP 251
Cdd:cd00201 4 WEERWDPDGRVYYYNHNTKETQWEDP 29
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
704-757 |
3.86e-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: 3.86e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1831508436 704 EHEDTYRNLLIDLIKSTENS-WHEARRILRKDERYAncDMLDKTRKESLFDDHIK 757
Cdd:smart00441 2 EAKEAFKELLKEHEVITPDTtWSEARKKLKNDPRYK--ALLSESEREQLFEDHIE 54
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
226-251 |
4.17e-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: 44.13 E-value: 4.17e-06
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
463-515 |
1.25e-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: 1.25e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1831508436 463 EERLKQFKEMLEEKNVSTS-STFEKELSKIVFDKRY-LSLGATERRACFDAFCRE 515
Cdd:smart00441 1 EEAKEAFKELLKEHEVITPdTTWSEARKKLKNDPRYkALLSESEREQLFEDHIEE 55
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
762-815 |
1.26e-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: 1.26e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1831508436 762 KRREAFFQVLDNHeKITPMMRWRDAKKIIQDEEEtFVKIASNSERkvERDFRDW 815
Cdd:pfam01846 1 KAREAFKELLKEH-KITPYSTWSEIKKKIENDPR-YKALLDGSER--EELFEDY 50
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
386-886 |
1.43e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 386 KAEEENNQSKKESESESESDEDGPPKAK----KSRAEKKKEALIAAQKKEKERPRQMLQKPVDPAIEAEMQAAKEREKVP 461
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKadeaKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 462 LEERLKQFKEMLEEKNVSTSSTFEKELSKIVFDKRYLSLGATERRACFDAfcREKIESEKAERRKRVKEAKEEFQKLLAE 541
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA--KKADEAKKAEEAKKADEAKKAEEKKKAD 1549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 542 cELNGRSSYSSFTSKFGKDPRYKAVERN----------RDREDAFNDFVGELHKKEKDEK-----RAKKEKLKAAFVKLL 606
Cdd:PTZ00121 1550 -ELKKAEELKKAEEKKKAEEAKKAEEDKnmalrkaeeaKKAEEARIEEVMKLYEEEKKMKaeeakKAEEAKIKAEELKKA 1628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 607 EEQtgltRKSKWSTTKKTLEDEERYIALDSSSTRESLFREFVANLGDETASDIEE--EQEREKRLAAQtaiANRQKEVEA 684
Cdd:PTZ00121 1629 EEE----KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEakKAEEDEKKAAE---ALKKEAEEA 1701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 685 ELGNQLRERTKEsEKQKMGE--HEDTYRNLLIDLIKSTENSWHEARRILRKDERyancdmlDKTRKESLFDDHIKSLERK 762
Cdd:PTZ00121 1702 KKAEELKKKEAE-EKKKAEElkKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE-------EKKKIAHLKKEEEKKAEEI 1773
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 763 RREAfFQVLDNHEKITPMMRWRDAKKIIQDeeetfvkIASNSERKVERDfrdwqeRRHDHLTDEFKEM-LSETKIITHKS 841
Cdd:PTZ00121 1774 RKEK-EAVIEEELDEEDEKRRMEVDKKIKD-------IFDNFANIIEGG------KEGNLVINDSKEMeDSAIKEVADSK 1839
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1831508436 842 KKLMEEG---EQHMDILSVLENDKRwvRMTAMSASERDrMLEDHIENL 886
Cdd:PTZ00121 1840 NMQLEEAdafEKHKFNKNNENGEDG--NKEADFNKEKD-LKEDDEEEI 1884
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
159-186 |
1.78e-05 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 42.20 E-value: 1.78e-05
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
159-184 |
3.70e-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: 41.36 E-value: 3.70e-05
10 20
....*....|....*....|....*.
gi 1831508436 159 WVETETAEGKKYFYHPVNRNTIWERP 184
Cdd:cd00201 4 WEERWDPDGRVYYYNHNTKETQWEDP 29
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
414-881 |
3.75e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 414 KSRAEKKKEALIAAQKKEKERPR-QMLQKPVDPAIEAEMQAAKEREKVPLEERLKQFKEMLEEKNVSTSSTFEKELSKiv 492
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK-- 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 493 fdkrylslGATERRACFDAFCREKIESEKAERRKRVKEAKEEFQKLLAECELNGRSSyssfTSKFGKDPRYKAVERNRDR 572
Cdd:PTZ00121 1386 --------KAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD----EAKKKAEEAKKADEAKKKA 1453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 573 EDAFNdfVGELHKKEKDEKRAKKEKLKAAFVKLLEEQtgltrKSKWSTTKKTLEDEERyiALDSSSTRESLFREFVANLG 652
Cdd:PTZ00121 1454 EEAKK--AEEAKKKAEEAKKADEAKKKAEEAKKADEA-----KKKAEEAKKKADEAKK--AAEAKKKADEAKKAEEAKKA 1524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 653 DETASDIEEEQEREKRLAAQTAIANRQKEVEaELgnQLRERTKESEKQKMGEHEDTYRNLLIDLIKSTENSWHEARRILR 732
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKKAE-EL--KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 733 KDERYANCDMLDKTRKESLFDDHIKSLERKRREAFFQVLDNHEKItpmmrwRDAKKIIQDEEETFVKiASNSERKVERDF 812
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK------KKAEELKKAEEENKIK-AAEEAKKAEEDK 1674
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831508436 813 RDWQERRHDH-----LTDEFKEMLSETKIITHKSKKLMEEGEQHMDILSVLENDKRWVRMTAMSASERDRMLED 881
Cdd:PTZ00121 1675 KKAEEAKKAEedekkAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
159-184 |
6.92e-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: 40.57 E-value: 6.92e-05
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
706-755 |
7.83e-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: 7.83e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1831508436 706 EDTYRNLLIDLIKSTENSWHEARRILRKDERYANcdMLDKTRKESLFDDH 755
Cdd:pfam01846 3 REAFKELLKEHKITPYSTWSEIKKKIENDPRYKA--LLDGSEREELFEDY 50
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
339-366 |
1.23e-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: 39.80 E-value: 1.23e-04
10 20
....*....|....*....|....*...
gi 1831508436 339 TPWCVVWTGDDKVFFYNPSTKCSVWERP 366
Cdd:pfam00397 3 PGWEERWDPDGRVYYYNHETGETQWEKP 30
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
411-702 |
3.39e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.58 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 411 KAKKSRAEKKKEALIAAQKKEKERPRQMLQkpvdpaiEAEMQAAKEREKVPLEERLKQFKEMLEEKNVSTSSTFEKELSK 490
Cdd:pfam02463 733 KINEELKLLKQKIDEEEEEEEKSRLKKEEK-------EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRA 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 491 IVFDKRYlslgaterracfdAFCREKIESEKAERRKRVKEAKEEFQKLLAEcelngrssyssftsKFGKDPRYKAVERNR 570
Cdd:pfam02463 806 LEEELKE-------------EAELLEEEQLLIEQEEKIKEEELEELALELK--------------EEQKLEKLAEEELER 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 571 DREDAFNDfVGELHKKEKDEKRAKKEKLKAAFVKLLEEQTGLTRKSKWSTTKKTLEDEERYIALDSSSTRESL------- 643
Cdd:pfam02463 859 LEEEITKE-ELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILlkyeeep 937
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831508436 644 --FREFVANLGDETASDIEEEQEREKRLAAQTAIANRQKE--VEAELGNQLRERTKESEKQKM 702
Cdd:pfam02463 938 eeLLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLmaIEEFEEKEERYNKDELEKERL 1000
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
339-368 |
4.94e-04 |
|
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: 38.28 E-value: 4.94e-04
10 20 30
....*....|....*....|....*....|
gi 1831508436 339 TPWCVVWTGDDKVFFYNPSTKCSVWERPPD 368
Cdd:cd00201 2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
340-368 |
5.59e-04 |
|
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: 37.97 E-value: 5.59e-04
10 20
....*....|....*....|....*....
gi 1831508436 340 PWCVVWTGDDKVFFYNPSTKCSVWERPPD 368
Cdd:smart00456 5 GWEERKDPDGRPYYYNHETKETQWEKPRE 33
|
|
| FF |
pfam01846 |
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
825-882 |
1.84e-03 |
|
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: 37.05 E-value: 1.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1831508436 825 DEFKEMLSETKiITHKSKklmeegeqHMDILSVLENDKRWVRMtaMSASERDRMLEDH 882
Cdd:pfam01846 4 EAFKELLKEHK-ITPYST--------WSEIKKKIENDPRYKAL--LDGSEREELFEDY 50
|
|
| FF |
smart00441 |
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
821-885 |
3.77e-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: 36.40 E-value: 3.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831508436 821 DHLTDEFKEMLSETKIITHKSKklMEEgeqhmdILSVLENDKRWVRMtaMSASERDRMLEDHIEN 885
Cdd:smart00441 1 EEAKEAFKELLKEHEVITPDTT--WSE------ARKKLKNDPRYKAL--LSESEREQLFEDHIEE 55
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
411-739 |
5.67e-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: 40.73 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 411 KAKKSRAEKKKEALIAAQKKEKERPRQMLQKPVDpaieaEMQAAKEREKVPLEERL--KQFKEMLEEKNVSTSSTFEKEL 488
Cdd:pfam02463 197 LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD-----YLKLNEERIDLLQELLRdeQEEIESSKQEIEKEEEKLAQVL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 489 SKIVFDKRYLSLGATERRACFDAFCREKIESEKAERRK---RVKEAKEEFQKLLAECELNGRSSYSSFTSKFgkdprYKA 565
Cdd:pfam02463 272 KENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKvddEEKLKESEKEKKKAEKELKKEKEEIEELEKE-----LKE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 566 VERNRdredafndfvgELHKKEKDEKRAKKEKLKAAFVKLLEEQTGLTRKSKWSTTKKTLEDEERYIALDSSSTRESLFR 645
Cdd:pfam02463 347 LEIKR-----------EAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELAR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 646 EFVANLGDETASDIEEEQEREKRLAAQTAIANRQKEveaelgnqlrERTKESEKQKMGEHEDTYRNLLIDLIKSTENSWH 725
Cdd:pfam02463 416 QLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKE----------ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
330
....*....|....
gi 1831508436 726 EARRILRKDERYAN 739
Cdd:pfam02463 486 LELLLSRQKLEERS 499
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
436-765 |
6.27e-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: 40.34 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 436 RQMLQKPVDPAIEAEMQAAKEREKVPLEERLKQFKEMLEEKNvstsstfEKELSKIVFDKRYLSLGATERRACFDAFCRE 515
Cdd:pfam02463 145 EIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLA-------ELIIDLEELKLQELKLKEQAKKALEYYQLKE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 516 KIESEKAERR-----KRVKEAKEEFQKLLAECELNGRSSYSSFTSKFGKDPRYKAVERNRDREDAFNDFVGELHKKEKDE 590
Cdd:pfam02463 218 KLELEEEYLLyldylKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 591 KRAKKEKLKAAFVKLLEEQTGL---TRKSKWSTTKKTLEDEERYIALDSSSTRESLFREFVANLGDETAsdiEEEQEREK 667
Cdd:pfam02463 298 LKSELLKLERRKVDDEEKLKESekeKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQE---KLEQLEEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 668 RLAAQTAIANRQKEVEAELGNQLRER-TKESEKQKMGEHEDTYRNLLIDLIKSTENSWHEARRILRKDERYA-----NCD 741
Cdd:pfam02463 375 LLAKKKLESERLSSAAKLKEEELELKsEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLteekeELE 454
|
330 340
....*....|....*....|....
gi 1831508436 742 MLDKTRKESLFDDHIKSLERKRRE 765
Cdd:pfam02463 455 KQELKLLKDELELKKSEDLLKETQ 478
|
|
| PRP40 |
COG5104 |
Splicing factor [RNA processing and modification]; |
612-814 |
9.65e-03 |
|
Splicing factor [RNA processing and modification];
Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 39.68 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 612 LTRKSKWSTTKKTLEDEERYIALD---------------SSSTRESLFREfvanLGDETASDIEEEQEREKRLAAQT--- 673
Cdd:COG5104 33 RTGKSSWEKPKELLKGSEEDLDVDpwkecrtadgkvyyyNSITRESRWKI----PPERKKVEPIAEQKHDERSMIGGngn 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 674 --AIANRQKEVEAELGNQLRE-----RTKESEKQKMGEH-EDTYRNLLIDLIKSTENSWHEARRILRkDERYANCDMLDK 745
Cdd:COG5104 109 dmAITDHETSEPKYLLGRLMSqygitSTKDAVYRLTKEEaEKEFITMLKENQVDSTWPIFRAIEELR-DPRYWMVDTDPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831508436 746 TRKEsLFDDHIKSLE-----------RKRREAFFQVLDNHEKITPMMRWRDAKKIIQDEEETFVKIASNSERKVERDFRD 814
Cdd:COG5104 188 WRKD-LFKKYFENQEkdqreeeenkqRKYINEFCKMLAGNSHIKYYTDWFTFKSIFSKHPYYSSVVNEKTKRQTFQKYKD 266
|
|
| |
