|
Name |
Accession |
Description |
Interval |
E-value |
| PAP1 |
COG5186 |
Poly(A) polymerase Pap1 [RNA processing and modification]; |
1-912 |
0e+00 |
|
Poly(A) polymerase Pap1 [RNA processing and modification];
Pssm-ID: 444067 [Multi-domain] Cd Length: 983 Bit Score: 579.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 1 MRTSEEIYHRVRWDARFDPARFVFGVLERGAAPKRVPLPAFVPGGEIPWHRVLFVEADGELVWDRATGVDRIDATDAGRV 80
Cdd:COG5186 19 MRTFEESYERMRWGARDAPARISLTVAEIPVHCKEYPRDKFVPGVRLPSLRELTVEDDADPIEPRPARPDFLDELPAGLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 81 RESRLLRAPFFTARTPHAWDGEQWAPVRAPRGADGAAGG--DNVRVLTWNTLWDRYDADLIDSAGRRPLLLRALRDAEVD 158
Cdd:COG5186 99 GRPRYLRASRFAENTPTFADPALSTLARRLPAEFTVASKpvLPDLLLTNLSLNDRYDLHRASTARRNALLPVALQELTAV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 159 VIALQEVEAALLAMLLSEPWVRAEWTLGSDPRGRDVAECGLLLLSRLPVREAAFHALGPHKAVASVVVEAGQRPLVVAAT 238
Cdd:COG5186 179 DADQIALEEYLLELLFAALGVGWVYVVSTSSFGDVADDAGVLSLSLLSRAEVLVLGEGSLKAGTAAVADLALPPAVAAAT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 239 HLSSDHSADGAGRRTAELARIAEGFAALDAGLVLLGDFNDGGDTPQVTLGMRDAWSEtHGPDDATPTFDPVANPLAAVSS 318
Cdd:COG5186 259 VLTSADLEDAELRDRTELAALEIGLAGVRAVVVLLVDLFDAEGGGFARAGKNDAWPL-ALPRRRPETFDPAFNPTAASLS 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 319 LTGRASRLDRVLVRGPgLAVRSAELYGDTPSPDGLFVSDHYGVRAEVGSGTADSAPAALDVGPTARTALAWLPPEELWPP 398
Cdd:COG5186 338 RRGSRALLDRRLLRRR-RQEVALRAPTPDSGPPGPAPPALLDRRGFGGSTVGVRCGGVVGEPATAATTVPPRPPTVAIPP 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 399 LQDIRRAHDPQIHRWPPHVNVLFGFVPEHAFEEAASVL--AGAVTAPFDVRLEGVHWFGHRD-DATVWLDPAAAGEWPWA 475
Cdd:COG5186 417 IQQVILAIDPPVDPPIPAQNGRLGFVPEFEFEEAAPLLlaAAAPEAEFLEALELIALRKRSThWTTVSLFPADALTPWKA 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 476 ELHSTLVRHFPRCRGRQEGFTPHLSLGRTTDPNALAAACAARLAPRSAR---VGELALLSRRGDEPMRVRATVSLGTGEV 552
Cdd:COG5186 497 LWARLRRRFPRRLRRSEAAAEPYTLGGQFDEPELAFAKLPVWHLRRGSRaaiALILRRLRRWFEVRRIIDAEVSLSDRRP 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 553 RWAEEAVPHAP------------------EGDREAGTADRVRRLVADALP-----GGVVHVAGSRRMGCALPGADLDLVA 609
Cdd:COG5186 577 KEAVEPAEVGTpklpkgaridvlreilsaGAWASQEQRDAVVARVKQALEeclgfGGVLHVTGSRRLGCALPGSDLDLVA 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 610 ALPGTVELGSLRREL-----GGASEVREVVGARVPGLRLRFDGLDVDLAVVATGAMDPGEAVDRRAELGEAAALAL-SAV 683
Cdd:COG5186 657 VLPGYLSLEDFETRVraalpEECSSLRRVLDARVPLLRLSLGGLDVDLLYVDVGVCPPEEAVARRGERLDEAAARAlSGV 736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 684 SDAEAVLASVGGRG---PAFAGLARQVKAWARARGLDSAPFGGLPGLAWSVLAARTAGEAGDLPPSCLLRHFFATWAAWD 760
Cdd:COG5186 737 WDADALLEAVGQEGarrERFRTLLRAVKAWAKARGLYSAPFGGLGGLSWAVLAARTCRDASDKSDGDLLANFFGTWAAWD 816
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 761 WREPVGGLEGAPA-------GPLTVATPSAPVRSCTDQVTADMRDLITQELFRAWELLEEG----ASWTEVLAPPPLHRR 829
Cdd:COG5186 817 WRQPIALTPSGPQygvpgprDPVPIITPIAPCRNTARNVTRSTLEILRDELYRAWEAVERAraerDAWAALFAPPPLHRR 896
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 830 HAAWAVVTAGAGTDGVVDE--GRVRGRMRALITDLAGLApgcHAWPRPFATAP--VRYAIGLGPTPPAAEALAAVADRRL 905
Cdd:COG5186 897 HAAWAVVTVEAPDPEGREKalGWVRGRIIALLIALEGDR---RAFPRPFPTAPrlARHAIGLGLRPPAAAALKELARPWA 973
|
....*..
gi 502766437 906 RGLAGVT 912
Cdd:COG5186 974 AGLHEVH 980
|
|
| TDP2 |
cd09080 |
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ... |
123-364 |
7.37e-48 |
|
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related domains; Human TDP2, also known as TTRAP (TRAF/TNFR-associated factors, and tumor necrosis factor receptor/TNFR-associated protein), is a 5'-tyrosyl DNA phosphodiesterase. It is required for the efficient repair of topoisomerase II-induced DNA double strand breaks. The topoisomerase is covalently linked by a phosphotyrosyl bond to the 5'-terminus of the break. TDP2 cleaves the DNA 5'-phosphodiester bond and restores 5'-phosphate termini, needed for subsequent DNA ligation, and hence repair of the break. TDP2 and 3'-tyrosyl DNA phosphodiesterase (TDP1) are complementary activities; together, they allow cells to remove trapped topoisomerase from both 3'- and 5'-DNA termini. TTRAP has been reported as being involved in apoptosis, embryonic development, and transcriptional regulation, and it may inhibit the activation of nuclear factor-kB. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.
Pssm-ID: 197314 [Multi-domain] Cd Length: 248 Bit Score: 170.60 E-value: 7.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 123 RVLTWNTLWDRYdadlIDSAGRRPLLLRALRDAEVDVIALQEVEAALLAMLLSEPWVRAEWTLGSDPRGRDVAECGLLLL 202
Cdd:cd09080 2 KVLTWNVDFLDD----VNLAERMRAILKLLEELDPDVIFLQEVTPPFLAYLLSQPWVRKNYYFSEGPPSPAVDPYGVLIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 203 SRLPVREAAFH---ALGPHKAVASVVVEAGQRPLVVAATHLSSDHSadGAGRRTAELARIAEGFAALD--AGLVLLGDFN 277
Cdd:cd09080 78 SKKSLVVRRVPftsTRMGRNLLAAEINLGSGEPLRLATTHLESLKS--HSSERTAQLEEIAKKLKKPPgaANVILGGDFN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 278 DGGDTPQVTL---GMRDAWSETHGPDDATPTFDPVANPLAAvSSLTGRASRLDRVLVRGPGLAVRSAELYGDTPSP---D 351
Cdd:cd09080 156 LRDKEDDTGGlpnGFVDAWEELGPPGEPGYTWDTQKNPMLR-KGEAGPRKRFDRVLLRGSDLKPKSIELIGTEPIPgdeE 234
|
250
....*....|...
gi 502766437 352 GLFVSDHYGVRAE 364
Cdd:cd09080 235 GLFPSDHFGLLAE 247
|
|
| 2_5_RNA_ligase2 |
pfam13563 |
2'-5' RNA ligase superfamily; This family contains proteins related to pfam02834. These ... |
391-537 |
6.71e-24 |
|
2'-5' RNA ligase superfamily; This family contains proteins related to pfam02834. These proteins are likely to be enzymes, but they may not share the RNA ligase activity.
Pssm-ID: 433312 [Multi-domain] Cd Length: 152 Bit Score: 98.65 E-value: 6.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 391 PPEELWPPLQDIRRAH-DPQIHRWPPHVNVLFGFVPEHAFEEAASVLAGAV--TAPFDVRLEGVHWFGHRDDaTVWLDPA 467
Cdd:pfam13563 1 PPDSLAARIEELRRSLgDKLYPRWPPHITLLYPFVPDELLPELLEALAEVAaeTEPFELTLGGFGTFGHRGG-VVYLSVE 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502766437 468 AAGewPWAELHSTLVRHFPRCRGRQ--EGFTPHLSLGRTTDPNALA---AACAARLAPRSARVGELALLSRRGDE 537
Cdd:pfam13563 80 GSE--PLRALHAALREALPPCLLKQdsGPFTPHLTIAYKVDDAPAAellEKLQRALPPLEFTVDELALLRRDGGG 152
|
|
| PTZ00418 |
PTZ00418 |
Poly(A) polymerase; Provisional |
585-862 |
1.29e-17 |
|
Poly(A) polymerase; Provisional
Pssm-ID: 240410 [Multi-domain] Cd Length: 593 Bit Score: 87.55 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 585 GGVVHVAGSRRMGCALPGADLDLVAALPGTV-------ELGSLRRELGGASEVREVVGARVPGLRLRFDGLDVDL--AVV 655
Cdd:PTZ00418 126 SGKLFTFGSYRLGVVAPGSDIDTLCLAPRHItresffsDFYAKLQQDPNITKLQPVPDAYTPVIKFVYDGIDIDLlfANL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 656 ATGAMDP------GEAVDRRAELGEAAALALSAVSDAeaVLASVGGRgPAFAGLARQVKAWARARGLDSAPFGGLPGLAW 729
Cdd:PTZ00418 206 PLPTIPDclnsldDDYILRNVDEKTVRSLNGCRVADL--ILASVPNK-DYFRTTLRFIKLWAKRRGIYSNVLGYLGGVSW 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 730 SVLAARTAGEAGDLPPSCLLRHFFATWAAWDWREPV-----------GGLEGAP-----------AGPLTVATPSAPVRS 787
Cdd:PTZ00418 283 AILTARICQLYPNFAPSQLIHKFFRVYSIWNWKNPVllckikevpniPGLMNFKvwdprvnpqdrAHLMPIITPAFPSMN 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 788 CTDQVTADMRDLITQELFRAWELL-----EEGASWTEVLAPPPLHRRHAAWAVVTAGAGTDGVVD--EGRVRGRMRALIT 860
Cdd:PTZ00418 363 STHNVTYTTKRVITEEFKRAHEIIkyiekNSENTWTNVLEPLDFFTSYKHFLVIQVYATNEHVHNkwEGWIESKIRFLIK 442
|
..
gi 502766437 861 DL 862
Cdd:PTZ00418 443 KL 444
|
|
| 2_5_ligase |
TIGR02258 |
2'-5' RNA ligase; This protein family consists of bacterial and archaeal proteins with two ... |
384-508 |
3.43e-03 |
|
2'-5' RNA ligase; This protein family consists of bacterial and archaeal proteins with two tandem copies of Pfam domain pfam02834. Members for which activity has been measured perform a reversible, ATP-independent 2'-5'-ligation of what is presumably a non-phyiological substrate: half-tRNA splice intermediates from an intron-containing yeast tRNA. The physiological substrate(s) in prokaryotes may include small 2'-5'-link-containing oligonucleotides, perhaps with regulatory or biosynthetic roles. [Transcription, RNA processing]
Pssm-ID: 274058 [Multi-domain] Cd Length: 179 Bit Score: 39.57 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 384 RTALAWLPPEELWPPLQDIRRAHDPQIH--RWPP----HVNVLF-GFVPEHAFEEAASVLAGAVTAPFDVRLEGVHWFGH 456
Cdd:TIGR02258 2 RLFIAIDLPPEIREQLSRIQRKLKSPLDgiKWVPpenlHITLKFlGEVDEEQVEELEDALAKIAEPPFTLKLEGIGVFGN 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 502766437 457 RDDATV-WLDPAAAGEWP--WAELHSTLVRH-FPRcrgRQEGFTPHLSLGRTTDPN 508
Cdd:TIGR02258 82 PKRPRVlWAGVEQSEELTqlHADLERELAKLgFSK---EERPFTPHITLARKKSGK 134
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PAP1 |
COG5186 |
Poly(A) polymerase Pap1 [RNA processing and modification]; |
1-912 |
0e+00 |
|
Poly(A) polymerase Pap1 [RNA processing and modification];
Pssm-ID: 444067 [Multi-domain] Cd Length: 983 Bit Score: 579.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 1 MRTSEEIYHRVRWDARFDPARFVFGVLERGAAPKRVPLPAFVPGGEIPWHRVLFVEADGELVWDRATGVDRIDATDAGRV 80
Cdd:COG5186 19 MRTFEESYERMRWGARDAPARISLTVAEIPVHCKEYPRDKFVPGVRLPSLRELTVEDDADPIEPRPARPDFLDELPAGLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 81 RESRLLRAPFFTARTPHAWDGEQWAPVRAPRGADGAAGG--DNVRVLTWNTLWDRYDADLIDSAGRRPLLLRALRDAEVD 158
Cdd:COG5186 99 GRPRYLRASRFAENTPTFADPALSTLARRLPAEFTVASKpvLPDLLLTNLSLNDRYDLHRASTARRNALLPVALQELTAV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 159 VIALQEVEAALLAMLLSEPWVRAEWTLGSDPRGRDVAECGLLLLSRLPVREAAFHALGPHKAVASVVVEAGQRPLVVAAT 238
Cdd:COG5186 179 DADQIALEEYLLELLFAALGVGWVYVVSTSSFGDVADDAGVLSLSLLSRAEVLVLGEGSLKAGTAAVADLALPPAVAAAT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 239 HLSSDHSADGAGRRTAELARIAEGFAALDAGLVLLGDFNDGGDTPQVTLGMRDAWSEtHGPDDATPTFDPVANPLAAVSS 318
Cdd:COG5186 259 VLTSADLEDAELRDRTELAALEIGLAGVRAVVVLLVDLFDAEGGGFARAGKNDAWPL-ALPRRRPETFDPAFNPTAASLS 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 319 LTGRASRLDRVLVRGPgLAVRSAELYGDTPSPDGLFVSDHYGVRAEVGSGTADSAPAALDVGPTARTALAWLPPEELWPP 398
Cdd:COG5186 338 RRGSRALLDRRLLRRR-RQEVALRAPTPDSGPPGPAPPALLDRRGFGGSTVGVRCGGVVGEPATAATTVPPRPPTVAIPP 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 399 LQDIRRAHDPQIHRWPPHVNVLFGFVPEHAFEEAASVL--AGAVTAPFDVRLEGVHWFGHRD-DATVWLDPAAAGEWPWA 475
Cdd:COG5186 417 IQQVILAIDPPVDPPIPAQNGRLGFVPEFEFEEAAPLLlaAAAPEAEFLEALELIALRKRSThWTTVSLFPADALTPWKA 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 476 ELHSTLVRHFPRCRGRQEGFTPHLSLGRTTDPNALAAACAARLAPRSAR---VGELALLSRRGDEPMRVRATVSLGTGEV 552
Cdd:COG5186 497 LWARLRRRFPRRLRRSEAAAEPYTLGGQFDEPELAFAKLPVWHLRRGSRaaiALILRRLRRWFEVRRIIDAEVSLSDRRP 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 553 RWAEEAVPHAP------------------EGDREAGTADRVRRLVADALP-----GGVVHVAGSRRMGCALPGADLDLVA 609
Cdd:COG5186 577 KEAVEPAEVGTpklpkgaridvlreilsaGAWASQEQRDAVVARVKQALEeclgfGGVLHVTGSRRLGCALPGSDLDLVA 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 610 ALPGTVELGSLRREL-----GGASEVREVVGARVPGLRLRFDGLDVDLAVVATGAMDPGEAVDRRAELGEAAALAL-SAV 683
Cdd:COG5186 657 VLPGYLSLEDFETRVraalpEECSSLRRVLDARVPLLRLSLGGLDVDLLYVDVGVCPPEEAVARRGERLDEAAARAlSGV 736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 684 SDAEAVLASVGGRG---PAFAGLARQVKAWARARGLDSAPFGGLPGLAWSVLAARTAGEAGDLPPSCLLRHFFATWAAWD 760
Cdd:COG5186 737 WDADALLEAVGQEGarrERFRTLLRAVKAWAKARGLYSAPFGGLGGLSWAVLAARTCRDASDKSDGDLLANFFGTWAAWD 816
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 761 WREPVGGLEGAPA-------GPLTVATPSAPVRSCTDQVTADMRDLITQELFRAWELLEEG----ASWTEVLAPPPLHRR 829
Cdd:COG5186 817 WRQPIALTPSGPQygvpgprDPVPIITPIAPCRNTARNVTRSTLEILRDELYRAWEAVERAraerDAWAALFAPPPLHRR 896
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 830 HAAWAVVTAGAGTDGVVDE--GRVRGRMRALITDLAGLApgcHAWPRPFATAP--VRYAIGLGPTPPAAEALAAVADRRL 905
Cdd:COG5186 897 HAAWAVVTVEAPDPEGREKalGWVRGRIIALLIALEGDR---RAFPRPFPTAPrlARHAIGLGLRPPAAAALKELARPWA 973
|
....*..
gi 502766437 906 RGLAGVT 912
Cdd:COG5186 974 AGLHEVH 980
|
|
| TDP2 |
cd09080 |
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ... |
123-364 |
7.37e-48 |
|
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related domains; Human TDP2, also known as TTRAP (TRAF/TNFR-associated factors, and tumor necrosis factor receptor/TNFR-associated protein), is a 5'-tyrosyl DNA phosphodiesterase. It is required for the efficient repair of topoisomerase II-induced DNA double strand breaks. The topoisomerase is covalently linked by a phosphotyrosyl bond to the 5'-terminus of the break. TDP2 cleaves the DNA 5'-phosphodiester bond and restores 5'-phosphate termini, needed for subsequent DNA ligation, and hence repair of the break. TDP2 and 3'-tyrosyl DNA phosphodiesterase (TDP1) are complementary activities; together, they allow cells to remove trapped topoisomerase from both 3'- and 5'-DNA termini. TTRAP has been reported as being involved in apoptosis, embryonic development, and transcriptional regulation, and it may inhibit the activation of nuclear factor-kB. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.
Pssm-ID: 197314 [Multi-domain] Cd Length: 248 Bit Score: 170.60 E-value: 7.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 123 RVLTWNTLWDRYdadlIDSAGRRPLLLRALRDAEVDVIALQEVEAALLAMLLSEPWVRAEWTLGSDPRGRDVAECGLLLL 202
Cdd:cd09080 2 KVLTWNVDFLDD----VNLAERMRAILKLLEELDPDVIFLQEVTPPFLAYLLSQPWVRKNYYFSEGPPSPAVDPYGVLIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 203 SRLPVREAAFH---ALGPHKAVASVVVEAGQRPLVVAATHLSSDHSadGAGRRTAELARIAEGFAALD--AGLVLLGDFN 277
Cdd:cd09080 78 SKKSLVVRRVPftsTRMGRNLLAAEINLGSGEPLRLATTHLESLKS--HSSERTAQLEEIAKKLKKPPgaANVILGGDFN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 278 DGGDTPQVTL---GMRDAWSETHGPDDATPTFDPVANPLAAvSSLTGRASRLDRVLVRGPGLAVRSAELYGDTPSP---D 351
Cdd:cd09080 156 LRDKEDDTGGlpnGFVDAWEELGPPGEPGYTWDTQKNPMLR-KGEAGPRKRFDRVLLRGSDLKPKSIELIGTEPIPgdeE 234
|
250
....*....|...
gi 502766437 352 GLFVSDHYGVRAE 364
Cdd:cd09080 235 GLFPSDHFGLLAE 247
|
|
| 2_5_RNA_ligase2 |
pfam13563 |
2'-5' RNA ligase superfamily; This family contains proteins related to pfam02834. These ... |
391-537 |
6.71e-24 |
|
2'-5' RNA ligase superfamily; This family contains proteins related to pfam02834. These proteins are likely to be enzymes, but they may not share the RNA ligase activity.
Pssm-ID: 433312 [Multi-domain] Cd Length: 152 Bit Score: 98.65 E-value: 6.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 391 PPEELWPPLQDIRRAH-DPQIHRWPPHVNVLFGFVPEHAFEEAASVLAGAV--TAPFDVRLEGVHWFGHRDDaTVWLDPA 467
Cdd:pfam13563 1 PPDSLAARIEELRRSLgDKLYPRWPPHITLLYPFVPDELLPELLEALAEVAaeTEPFELTLGGFGTFGHRGG-VVYLSVE 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502766437 468 AAGewPWAELHSTLVRHFPRCRGRQ--EGFTPHLSLGRTTDPNALA---AACAARLAPRSARVGELALLSRRGDE 537
Cdd:pfam13563 80 GSE--PLRALHAALREALPPCLLKQdsGPFTPHLTIAYKVDDAPAAellEKLQRALPPLEFTVDELALLRRDGGG 152
|
|
| MJ1316 |
pfam04457 |
MJ1316 RNA cyclic group end recognition domain; RNA repair domain predicted to be involved ... |
1-65 |
9.81e-24 |
|
MJ1316 RNA cyclic group end recognition domain; RNA repair domain predicted to be involved specifically in the recognition of RNA 3' ends with 2'-3' cyclic phosphate groups.
Pssm-ID: 461317 Cd Length: 75 Bit Score: 95.41 E-value: 9.81e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502766437 1 MRTSEEIYHRVRWDARFDPARFVFGVLERGAAPKRVPLPAFVPGGE----------IPWHRVLFVEADGELVWDR 65
Cdd:pfam04457 1 MRTIQDVLNRIRWDPRLDKSKFVVGYLDRFDGIKEVPFSEFTWIEDliedddgelaIPQHRIRYFKRDGEVVWDR 75
|
|
| PTZ00418 |
PTZ00418 |
Poly(A) polymerase; Provisional |
585-862 |
1.29e-17 |
|
Poly(A) polymerase; Provisional
Pssm-ID: 240410 [Multi-domain] Cd Length: 593 Bit Score: 87.55 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 585 GGVVHVAGSRRMGCALPGADLDLVAALPGTV-------ELGSLRRELGGASEVREVVGARVPGLRLRFDGLDVDL--AVV 655
Cdd:PTZ00418 126 SGKLFTFGSYRLGVVAPGSDIDTLCLAPRHItresffsDFYAKLQQDPNITKLQPVPDAYTPVIKFVYDGIDIDLlfANL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 656 ATGAMDP------GEAVDRRAELGEAAALALSAVSDAeaVLASVGGRgPAFAGLARQVKAWARARGLDSAPFGGLPGLAW 729
Cdd:PTZ00418 206 PLPTIPDclnsldDDYILRNVDEKTVRSLNGCRVADL--ILASVPNK-DYFRTTLRFIKLWAKRRGIYSNVLGYLGGVSW 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 730 SVLAARTAGEAGDLPPSCLLRHFFATWAAWDWREPV-----------GGLEGAP-----------AGPLTVATPSAPVRS 787
Cdd:PTZ00418 283 AILTARICQLYPNFAPSQLIHKFFRVYSIWNWKNPVllckikevpniPGLMNFKvwdprvnpqdrAHLMPIITPAFPSMN 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 788 CTDQVTADMRDLITQELFRAWELL-----EEGASWTEVLAPPPLHRRHAAWAVVTAGAGTDGVVD--EGRVRGRMRALIT 860
Cdd:PTZ00418 363 STHNVTYTTKRVITEEFKRAHEIIkyiekNSENTWTNVLEPLDFFTSYKHFLVIQVYATNEHVHNkwEGWIESKIRFLIK 442
|
..
gi 502766437 861 DL 862
Cdd:PTZ00418 443 KL 444
|
|
| ElsH |
COG3568 |
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ... |
116-365 |
2.93e-17 |
|
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function prediction only];
Pssm-ID: 442789 [Multi-domain] Cd Length: 167 Bit Score: 79.95 E-value: 2.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 116 AAGGDNVRVLTWNTLWD-----RYDADLIdsagrrpllLRALRDAEVDVIALQEVeaallamllsepwvraewtlgsdpr 190
Cdd:COG3568 2 AAAAATLRVMTYNIRYGlgtdgRADLERI---------ARVIRALDPDVVALQEN------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 191 grdvaecglLLLSRLPVREAAFHALGPH----KAVASVVVEAGQRPLVVAATHLSSDhsadGAGRRTAELARIAEGFAAL 266
Cdd:COG3568 48 ---------AILSRYPIVSSGTFDLPDPggepRGALWADVDVPGKPLRVVNTHLDLR----SAAARRRQARALAELLAEL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 267 DAG--LVLLGDFNDggdtpqvtlgmrdawsethgpddatptfdpvanplaavssltgrasrLDRVLVRgPGLAVRSAELY 344
Cdd:COG3568 115 PAGapVILAGDFND-----------------------------------------------IDYILVS-PGLRVLSAEVL 146
|
250 260
....*....|....*....|.
gi 502766437 345 gdtPSPDGLFVSDHYGVRAEV 365
Cdd:COG3568 147 ---DSPLGRAASDHLPVVADL 164
|
|
| ThpR |
COG1514 |
RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and ... |
384-548 |
2.77e-16 |
|
RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441123 [Multi-domain] Cd Length: 181 Bit Score: 77.76 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 384 RTALAWLPPEELWPPLQDIRRAHDPQIH-RWPP----HVNVLF-GFVPEHAFEEAASVLAGAV--TAPFDVRLEGVHWFG 455
Cdd:COG1514 2 RLFIALPPPEELREALAALRARLKAAPGgRWVRpenlHLTLAFlGEVDEERLEALAEALARAAagAPPFELRLDGLGAFP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 456 HRDDATVWLDPAAAGEwpWAELHSTLVRHFPRCRGRQEG--FTPHLSLGRTTDPNALAA---ACAARLAPRSARVGELAL 530
Cdd:COG1514 82 RPRPRVLWLGVEPSPE--LLALHRRLRAALARAGLPPERrpFVPHVTLARGKRPAPPLApalAELRDFEFPEFTVDEFVL 159
|
170 180
....*....|....*....|.
gi 502766437 531 LS---RRGDEPMRVRATVSLG 548
Cdd:COG1514 160 YEselTPDGPRYEVLAEFPLG 180
|
|
| YafD |
COG3021 |
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ... |
105-365 |
1.93e-15 |
|
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily [General function prediction only];
Pssm-ID: 442257 [Multi-domain] Cd Length: 310 Bit Score: 78.11 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 105 APVRAPRGADGAAGGDNVRVLTWNTLWDRYDADLIDSAgrrplllraLRDAEVDVIALQEVeaallamllSEPWVRAEWT 184
Cdd:COG3021 78 LPYTLPAPKSAPAGGPDLRVLTANVLFGNADAEALAAL---------VREEDPDVLVLQET---------TPAWEEALAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 185 LGSD-----PRGRDVAeCGLLLLSRLPVREAAFHALGP-HKAVASVVVEAGQRPLVVAATHLSSdhSADGAGRRTAELAR 258
Cdd:COG3021 140 LEADypyrvLCPLDNA-YGMALLSRLPLTEAEVVYLVGdDIPSIRATVELPGGPVRLVAVHPAP--PVGGSAERDAELAA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 259 IAEGFAALDAGLVLLGDFNDGGDTPQVTL-----GMRDAWSETHgpddATPTFdPVANPLAAVssltgrasRLDRVLVRg 333
Cdd:COG3021 217 LAKAVAALDGPVIVAGDFNATPWSPTLRRllrasGLRDARAGRG----LGPTW-PANLPFLRL--------PIDHVLVS- 282
|
250 260 270
....*....|....*....|....*....|..
gi 502766437 334 PGLAVRSAELYGDtpspdglFVSDHYGVRAEV 365
Cdd:COG3021 283 RGLTVVDVRVLPV-------IGSDHRPLLAEL 307
|
|
| COG2374 |
COG2374 |
Predicted extracellular nuclease [General function prediction only]; |
116-363 |
3.68e-12 |
|
Predicted extracellular nuclease [General function prediction only];
Pssm-ID: 441941 [Multi-domain] Cd Length: 362 Bit Score: 68.89 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 116 AAGGDNVRVLTWNTLW--DRYDADLIDSAGRRPLLLR-----------ALRDAevDVIALQEVE--AALLAMLLSEP--- 177
Cdd:COG2374 63 APVGGDLRVATFNVENlfDTDDDDDDFGRGADTPEEYerklakiaaaiAALDA--DIVGLQEVEnnGSALQDLVAALnla 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 178 ---WVRAEWTLGSDPRGRDVAecgllLLSR---LPVREAAFHALGPHKA-----------VASVVVEAGQrPLVVAATHL 240
Cdd:COG2374 141 ggtYAFVHPPDGPDGDGIRVA-----LLYRpdrVTLVGSATIADLPDSPgnpdrfsrpplAVTFELANGE-PFTVIVNHF 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 241 SS---DHSADGAG----RRTAE---LARIAEGFAALDAG--LVLLGDFNDGGDTPQV-----TLGMRDAWSETHGPDDAT 303
Cdd:COG2374 215 KSkgsDDPGDGQGaseaKRTAQaeaLRAFVDSLLAADPDapVIVLGDFNDYPFEDPLrallgAGGLTNLAEKLPAAERYS 294
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502766437 304 PTFDpvanplaavssltGRASRLDRVLV--------RGPGLAVRSAELY-------GDTPSPDGLFVSDHYGVRA 363
Cdd:COG2374 295 YVYD-------------GNSGLLDHILVspalaarvTGADIWHINADIYnddfkpdFRTYADDPGRASDHDPVVV 356
|
|
| nSMase |
cd09078 |
Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological ... |
154-364 |
2.94e-10 |
|
Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological membranes to ceramide and phosphorylcholine; Sphingomyelinases (SMase) are phosphodiesterases that catalyze the hydrolysis of sphingomyelin to ceramide and phosphorylcholine. Eukaryotic SMases have been classified according to their pH optima and are known as acid SMase, alkaline SMase, and neutral SMase (nSMase). Eukaryotic proteins in this family are nSMases, and are activated by a variety of stress-inducing agents such as cytokines or UV radiation. Ceramides and other metabolic derivatives, including sphingosine, are lipid "second messenger" molecules that participate in the regulation of stress-induced cellular responses, including cell death, adhesion, differentiation, and proliferation. Bacterial neutral SMases, which also belong to this domain family, are secreted proteins that act as membrane-damaging virulence factors. They promote colonization of the host tissue. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.
Pssm-ID: 197312 [Multi-domain] Cd Length: 280 Bit Score: 61.97 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 154 DAEVDVIALQEV---EAA--LLAMLLSEPWVRAEwTLGSDPRGRDVAEC--GLLLLSRLPVREAAFHALGP--------H 218
Cdd:cd09078 34 LLQYDVVVLQEVfdaRARkrLLNGLKKEYPYQTD-VVGRSPSGWSSKLVdgGVVILSRYPIVEKDQYIFPNgcgadclaA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 219 KAVASVVVE-AGQRPLVVAATHL-SSDHSADGAGRRTA---ELARIAEGFAALDAGLVLL-GDFN-DGGDTPQVTLGM-- 289
Cdd:cd09078 113 KGVLYAKINkGGTKVYHVFGTHLqASDGSCLDRAVRQKqldELRAFIEEKNIPDNEPVIIaGDFNvDKRSSRDEYDDMle 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 290 ---RDAWSETHGPDDATPTFDPVANPLAAVSSLTGRASRLDRVLVRGPGLAVRSAE-----LYGDTPSPDGLFV----SD 357
Cdd:cd09078 193 qlhDYNAPEPITAGETPLTWDPGTNLLAKYNYPGGGGERLDYILYSNDHLQPSSWSnevevPKSPTWSVTNGYTfadlSD 272
|
....*..
gi 502766437 358 HYGVRAE 364
Cdd:cd09078 273 HYPVSAT 279
|
|
| EEP-1 |
cd09083 |
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ... |
228-365 |
3.60e-10 |
|
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, EEP, domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds. Their substrates range from nucleic acids to phospholipids and perhaps, proteins.
Pssm-ID: 197317 [Multi-domain] Cd Length: 252 Bit Score: 61.46 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 228 AGQRPLVVAATHLssDHSADGAGRRTAEL--ARIAEgfAALDAGLVLLGDFNDGGDTPQVTL----GMRDAWSE-THGPD 300
Cdd:cd09083 123 KTGKEFYVFNTHL--DHVGEEAREESAKLilERIKE--IAGDLPVILTGDFNAEPDSEPYKTltsgGLKDARDTaATTDG 198
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502766437 301 DATPTFdpvanplaavSSLTGRA--SRLDRVLVRgPGLAVRSAELygDTPSPDGLFVSDHYGVRAEV 365
Cdd:cd09083 199 GPEGTF----------HGFKGPPggSRIDYIFVS-PGVKVLSYEI--LTDRYDGRYPSDHFPVVADL 252
|
|
| NT_PAP_TUTase |
cd05402 |
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ... |
573-652 |
3.25e-09 |
|
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.
Pssm-ID: 143392 [Multi-domain] Cd Length: 114 Bit Score: 55.26 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 573 DRVRRLVADALPGGVVHVAGSRRMGCALPGADLDLVAALPGTVE-----LGSLRREL---GGASEVREVVGARVPGLRLR 644
Cdd:cd05402 7 DRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGPNHRVdredfLRKLAKLLkksGEVVEVEPIINARVPIIKFV 86
|
90
....*....|
gi 502766437 645 FD--GLDVDL 652
Cdd:cd05402 87 DKptGIEVDI 96
|
|
| COG1531 |
COG1531 |
Uncharacterized conserved protein, UPF0248 family [Function unknown]; |
3-65 |
1.83e-08 |
|
Uncharacterized conserved protein, UPF0248 family [Function unknown];
Pssm-ID: 441140 Cd Length: 78 Bit Score: 52.17 E-value: 1.83e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502766437 3 TSEEIYHRVRWDARFDPARFVFGVLERGAAP--KRVPLP--AFVP--------GGEIPWHRVLFVEADGELVWDR 65
Cdd:COG1531 1 MIKELLNRILWDPRYDREDYEIVYLDRGAPGglKEIPGSeiVRVDrgyivlddGTVIPYHRILEIRYKGEVIWRR 75
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
155-699 |
2.57e-08 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 57.96 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 155 AEVDVIALQEVEAALLAMLLSEPWVRaewTLGSDPRGRDVAECGLLLLSRLPVREAAFHALGPHkAVASVVVEAGQRPLV 234
Cdd:COG3321 845 VPVDWSALYPGRGRRRVPLPTYPFQR---EDAAAALLAAALAAALAAAAALGALLLAALAAALA-AALLALAAAAAAALA 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 235 VAATHLSSDHSADGAGRRTAELARIAEGFAALDAGLVLLGDFNDGGDTPQVTLGMRDAWSETHGPDDATPTFDPVANPLA 314
Cdd:COG3321 921 LAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAA 1000
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 315 AVSSLTGRASRLDRVLVRGPGLAVRSAELYGDTPSPDGLFVSDHYGVRAEVGSGTADSAPAALDVGPTARTALAWLPPEE 394
Cdd:COG3321 1001 ALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALA 1080
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 395 LWPPLQDIRRAHDPQIHRWPPHVNVLFGFVPEHAFEEAASVLAGAVTAPFDVRLEGVHWFGHRDDATVWLDPAAAGEWPW 474
Cdd:COG3321 1081 AAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALA 1160
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 475 AELHSTLVRHFPRCRGRQEGFTPHLSLGRTTDPNALAAACAARLAPRSARVGELALLSRRGDEPMRVRATVSLGTGEVRW 554
Cdd:COG3321 1161 AALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAA 1240
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 555 AEEAVP-HAPEGDREAGTADRVRRLVADALPGGVVHVAGSRRMGCALPGADLDLVAALPGTVELGSLRRELGGASEVREV 633
Cdd:COG3321 1241 AAAAVAaLAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAA 1320
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502766437 634 VGARVPGLRLRFDGLDVDLAVVATGAMDPGEAVDRRAELGEAAALALSAVSDAEAVLASVGGRGPA 699
Cdd:COG3321 1321 LAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
|
|
| Exo_endo_phos |
pfam03372 |
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ... |
125-278 |
4.21e-08 |
|
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.
Pssm-ID: 460902 [Multi-domain] Cd Length: 183 Bit Score: 54.15 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 125 LTWNTLWDRYDADliDSAGRRPLLLRALRDAEVDVIALQEVEAALLAMLLsEPWVRAEWTLGSDPRGRDVAECGLLLLSR 204
Cdd:pfam03372 1 LTWNVNGGNADAA--GDDRKLDALAALIRAYDPDVVALQETDDDDASRLL-LALLAYGGFLSYGGPGGGGGGGGVAILSR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502766437 205 LPVREAAFHALG----PHKAVASVVVEAGQRPLVVAATHLSSDHSADGAGRRTAELARIAEGFAALDAGLVLLGDFND 278
Cdd:pfam03372 78 YPLSSVILVDLGefgdPALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFNA 155
|
|
| PAP_central |
pfam04928 |
Poly(A) polymerase central domain; The central domain of Poly(A) polymerase shares structural ... |
585-823 |
1.60e-06 |
|
Poly(A) polymerase central domain; The central domain of Poly(A) polymerase shares structural similarity with the allosteric activity domain of ribonucleotide reductase R1, which comprises a four-helix bundle and a three-stranded mixed beta- sheet. Even though the two enzymes bind ATP, the ATP-recognition motifs are different.
Pssm-ID: 461486 [Multi-domain] Cd Length: 344 Bit Score: 51.36 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 585 GGVVHVAGSRRMGCALPGADLDLVAALPGTVE-------LGSLRRELGGASEVREVVGARVPGLRLRFDGLDVDLaVVAT 657
Cdd:pfam04928 74 GGKIFTFGSYRLGVHGPGSDIDTLCVVPKHVTredfftsFLEMLRERPEVTELTAVPDAFVPVIKFKFSGISIDL-LFAR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 658 GAMdpgeavdrraelgeaaalalSAVSD-------------AEAVLASVGG-----------------RgpafagLA-RQ 706
Cdd:pfam04928 153 LAL--------------------PSVPDdldlsddnllrnlDEKCVRSLNGcrvtdeilrlvpnvetfR------TAlRA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 707 VKAWARARGLDSAPFGGLPGLAWSVLAART------AgeagdlPPSCLLRHFFATWAAWDWREPV-------GGLEGAPA 773
Cdd:pfam04928 207 IKLWAKRRGIYSNVLGFPGGVAWAMLVARIcqlypnA------APSTLVSKFFRIFSQWKWPQPVllkpieeGPLQLRVW 280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502766437 774 GPLT----------VATPSAPVRSCTDQVTADMRDLITQELFRAWELLEE----GASWTEVLAP 823
Cdd:pfam04928 281 NPRInpsdrfhlmpIITPAYPSMNSTHNVSRSTLEVIKEEFKRGLEITDEimlgKAPWKDLFEK 344
|
|
| RgfB-like |
cd09079 |
Streptococcus agalactiae RgfB, part of a putative two component signal transduction system, ... |
156-365 |
2.50e-06 |
|
Streptococcus agalactiae RgfB, part of a putative two component signal transduction system, and related proteins; This family includes Streptococcus agalactiae RgfB (for regulator of fibrinogen binding) and related proteins. The function of RgfB is unknown. It is part of a putative two component signal transduction system designated rgfBDAC (the rgf locus was identified in a screen for mutants of Streptococcus agalactiae with altered binding to fibrinogen). RgfA,-C,and -D do not belong to this superfamily: rgfA encodes a putative response regulator, and rgfC, a putative histidine kinase. All four genes are co-transcribed, and may be involved in regulating expression of bacterial cell surface components. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.
Pssm-ID: 197313 [Multi-domain] Cd Length: 259 Bit Score: 49.95 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 156 EVDVIALQEV-----------------EAALLAMLLSEPWVRAEWTLGSDPRGRDVAECGLLLLSRLPVREAAFHALGPH 218
Cdd:cd09079 29 DYDVIALQEVnqsidapvsqvpikednFALLLYEKLRELGATYYWTWILSHIGYDKYDEGLAILSKRPIAEVEDFYVSKS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 219 KAVA--------SVVVEAGQRPLVVAATHLS--SDHSADGAGrrtaELARIAEGFAALDAGLVLLGDFN-------DGGD 281
Cdd:cd09079 109 QDYTdyksrkilGATIEINGQPIDVYSCHLGwwYDEEEPFAY----EWSKLEKALAEAGRPVLLMGDFNnpagsrgEGYD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 282 TpQVTLGMRDAWsETHGPDDATPTfdpVANPLAAVSSLTGrASRLDRVLVrGPGLAVRSAELY---GDTPSpdglfVSDH 358
Cdd:cd09079 185 L-ISSLGLQDTY-DLAEEKDGGVT---VEKAIDGWRGNKE-AKRIDYIFV-NRKVKVKSSRVIfngKNPPI-----VSDH 252
|
....*..
gi 502766437 359 YGVRAEV 365
Cdd:cd09079 253 FGVEVEL 259
|
|
| EEP |
cd08372 |
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ... |
157-365 |
5.09e-06 |
|
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes the catalytic domain (exonuclease/endonuclease/phosphatase or EEP domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps proteins.
Pssm-ID: 197306 [Multi-domain] Cd Length: 241 Bit Score: 49.02 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 157 VDVIALQEVEA----ALLAMLLSEPWVRAEWTLGSDPRGRDvaecGLLLLSRLPVRE-AAFHALGPHKAVAS------VV 225
Cdd:cd08372 27 PDIVCLQEVKDsqysAVALNQLLPEGYHQYQSGPSRKEGYE----GVAILSKTPKFKiVEKHQYKFGEGDSGerravvVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 226 VEAGQRPLVVAATHLSSDHSAdgAGRRTAELARIAEGF----AALDAGLVLLGDFN-----------DGGDTPQVTLGMR 290
Cdd:cd08372 103 FDVHDKELCVVNAHLQAGGTR--ADVRDAQLKEVLEFLkrlrQPNSAPVVICGDFNvrpsevdsenpSSMLRLFVALNLV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502766437 291 DAWSETHGPddatPTFDpvanplaavSSLTGRASRLDRVLVRGPGL-AVRSAELYGDTPSPdgLFVSDHYGVRAEV 365
Cdd:cd08372 181 DSFETLPHA----YTFD---------TYMHNVKSRLDYIFVSKSLLpSVKSSKILSDAARA--RIPSDHYPIEVTL 241
|
|
| EEP-2 |
cd09084 |
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ... |
124-365 |
2.96e-04 |
|
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, EEP, domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps, proteins.
Pssm-ID: 197318 [Multi-domain] Cd Length: 246 Bit Score: 43.44 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 124 VLTWNT-LWDRYD--------ADLIDsagrrplllralrDAEVDVIALQEVEAALLAMLLSEPWVRAEWTLGSDPRGRDV 194
Cdd:cd09084 1 VMSYNVrSFNRYKwkddpdkiLDFIK-------------KQDPDILCLQEYYGSEGDKDDDLRLLLKGYPYYYVVYKSDS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 195 AECGLLLLSRLPVREAAFHaLGPHKA--VASVVVEAGQRPLVVAATHLSS--------DHSADGAGRRTAE---LARIAE 261
Cdd:cd09084 68 GGTGLAIFSKYPILNSGSI-DFPNTNnnAIFADIRVGGDTIRVYNVHLESfritpsdkELYKEEKKAKELSrnlLRKLAE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 262 GFAA-----------LDAG---LVLLGDFNdggDTP------QVTLGMRDAWSET-HGPddaTPTFDPVANPLaavsslt 320
Cdd:cd09084 147 AFKRraaqadllaadIAASpypVIVCGDFN---DTPasyvyrTLKKGLTDAFVEAgSGF---GYTFNGLFFPL------- 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 502766437 321 grasRLDRVLVrGPGLAVRSAELYGDTpspdglfVSDHYGVRAEV 365
Cdd:cd09084 214 ----RIDYILT-SKGFKVLRYRVDPGK-------YSDHYPIVATL 246
|
|
| PRK04257 |
PRK04257 |
hypothetical protein; Provisional |
6-65 |
5.07e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 179802 Cd Length: 78 Bit Score: 39.67 E-value: 5.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502766437 6 EIYHRVRWDARFDPARFVFGVLERGAA--PKRVPLPAFVPGG--------EIPWHRVLFV--EADGELVWDR 65
Cdd:PRK04257 4 EVLNKILWHPDYNEEDYYIVILHRGAYgnKKKIPLENIELGHsylvygetHIPYHRILEIvnKKTGEILYKK 75
|
|
| 2_5_ligase |
TIGR02258 |
2'-5' RNA ligase; This protein family consists of bacterial and archaeal proteins with two ... |
384-508 |
3.43e-03 |
|
2'-5' RNA ligase; This protein family consists of bacterial and archaeal proteins with two tandem copies of Pfam domain pfam02834. Members for which activity has been measured perform a reversible, ATP-independent 2'-5'-ligation of what is presumably a non-phyiological substrate: half-tRNA splice intermediates from an intron-containing yeast tRNA. The physiological substrate(s) in prokaryotes may include small 2'-5'-link-containing oligonucleotides, perhaps with regulatory or biosynthetic roles. [Transcription, RNA processing]
Pssm-ID: 274058 [Multi-domain] Cd Length: 179 Bit Score: 39.57 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502766437 384 RTALAWLPPEELWPPLQDIRRAHDPQIH--RWPP----HVNVLF-GFVPEHAFEEAASVLAGAVTAPFDVRLEGVHWFGH 456
Cdd:TIGR02258 2 RLFIAIDLPPEIREQLSRIQRKLKSPLDgiKWVPpenlHITLKFlGEVDEEQVEELEDALAKIAEPPFTLKLEGIGVFGN 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 502766437 457 RDDATV-WLDPAAAGEWP--WAELHSTLVRH-FPRcrgRQEGFTPHLSLGRTTDPN 508
Cdd:TIGR02258 82 PKRPRVlWAGVEQSEELTqlHADLERELAKLgFSK---EERPFTPHITLARKKSGK 134
|
|
| |
