|
Name |
Accession |
Description |
Interval |
E-value |
| RNB |
pfam00773 |
RNB domain; This domain is the catalytic domain of ribonuclease II. |
496-827 |
6.86e-122 |
|
RNB domain; This domain is the catalytic domain of ribonuclease II.
:
Pssm-ID: 459934 [Multi-domain] Cd Length: 314 Bit Score: 373.54 E-value: 6.86e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 496 RKDFRDKLICSIDPPGCQDIDDALHACVLPNGNYEVGVHIADVTHFVKPNTSMDSEAASRGTTVYLVDKRIDMLPMLLGT 575
Cdd:pfam00773 1 RKDLRDLPFITIDPADAKDLDDAISVEKLPNGGYRLGVHIADVSHYVPPGSPLDREARKRGTSVYLPDRVIPMLPEKLSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 576 DLCSLRPYVERFAFSCIWEMDENANIIKVHFTKSVIASKEAFSYADAQARIDDQKMQDP---LTQGMRVLLKLSKILKQK 652
Cdd:pfam00773 81 DLCSLNPGEDRLALSVEITIDADGEVTSYEIYPSVIRSKARLTYEEVDDLLEGKDAEKDkpdLAEDLRLLYELAKILRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 653 RMDEGALNLASPEVRIQTDNETsdPMDVEIKQLLETNSLVEEFMLLANISVAQKIYdAFPQTAVLRRHAAPPLTNFDSLQ 732
Cdd:pfam00773 161 RLQRGALDLDTPENKLILDEEG--VIDILIQERTDAHSLIEEFMLLANEAVARHLQ-ELGIPALYRVHPEPDLEKLNSLI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 733 DILRvckgmhlKCDTSKSLAKSLDECVDPkepyfNTLLRILTTRCMLSAEYFcsgtfaPPDFRHYGLASPIYTHFTSPIR 812
Cdd:pfam00773 238 KLLQ-------LLPDDKGLSKSLEKIKDD-----ERLLSILLLRTMPRAEYS------PEPLGHFGLGLDIYTHFTSPIR 299
|
330
....*....|....*
gi 19113445 813 RYADVLAHRQLAAAI 827
Cdd:pfam00773 300 RYPDLIVHRQLKALL 314
|
|
| PIN_Rrp44-like |
cd09862 |
VapC-like PIN domain of yeast exosome subunit Rrp44 endoribonuclease and other eukaryotic ... |
27-213 |
3.99e-80 |
|
VapC-like PIN domain of yeast exosome subunit Rrp44 endoribonuclease and other eukaryotic homologs; PIN (PilT N terminus) domain of the Saccharomyces cerevisiae exosome subunit Rrp44 (Ribosomal RNA-processing protein 44 or Protein Dis3 homolog) and other similar eukaryotic homologs are included in this family. The eukaryotic exosome is a conserved macromolecular complex responsible for many RNA-processing and RNA-degradation reactions. It is composed of nine core subunits that directly binds Rrp44. The Rrp44 nuclease is the catalytic subunit of the exosome and has endonuclease activity in the PIN domain and an exoribonuclease activity in its RNase II-like region. Rrp44 binding to the exosome is mediated mainly by the PIN domain and by subunits Rrp41-Rrp45, and binding predictions indicate that the PIN domain active site is positioned on the outer surface of the exosome. This subgroup belongs to the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. PIN domains within this subgroup contain four of these residues which cluster at the C-terminal end of the beta-sheet and form a negatively charged pocket near the center of the molecule. Recombinant Rrp44 was shown to possess manganese-dependent endonuclease activity in vitro that was abolished by point mutations in these putative metal binding residues of its PIN domain. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.
:
Pssm-ID: 350211 Cd Length: 178 Bit Score: 257.52 E-value: 3.99e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 27 RGKVQKVVREQYLRNDIPCQSRACPLCRSKLPKDSRGNVLEPilsekpmflekfGHHYLIPDSNIFYHCIDALEHPNnFF 106
Cdd:cd09862 5 RGKVVKVVREHYLRDDIPCGSELCPLCPQTNPKLLLLSLLSD------------AKHYLIPDTNVVLHQIDLLEDPE-IT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 107 DVIILQTVFSEISSKSIPLYNRMKRLCQEKTKRFTPFSNEFFVDTFVERLDDESANDRNDRAIRNAASWFASHLASLGIK 186
Cdd:cd09862 72 NVIILQTVLEEVRHRSLPLYNRLRALLKDPRKRFYVFSNEFHRETYVEREPGESPNDRNDRAIRKAAKWYQNHLAKLGIP 151
|
170 180
....*....|....*....|....*..
gi 19113445 187 IVLLTDDRENARLAAEQGIQVSTLKDY 213
Cdd:cd09862 152 VVLLTDDADNREKAEEEGILALTVREY 178
|
|
| Rrp44_S1 |
pfam17215 |
S1 domain; This domain corresponds to the S1 domain found at the C-terminus of ribonucleases ... |
877-966 |
5.22e-35 |
|
S1 domain; This domain corresponds to the S1 domain found at the C-terminus of ribonucleases such as yeast Rrp44.
:
Pssm-ID: 435792 Cd Length: 87 Bit Score: 128.03 E-value: 5.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 877 AEEDAYVIKVFKNGFVVFIARFGLEGIVYTKSLSSVlEPNVEYVEDEYKLNIEIRDQPKPQTVqiQMFQQVRVRVTTVRD 956
Cdd:pfam17215 1 SEEEGYVIKVFNNGIVVFVPKFGIEGLIRLEDLTGD-EPEAEFDADEYSLTFPDKGSGKKRTV--GVFDKVRVRVKSVKD 77
|
90
....*....|
gi 19113445 957 EHSGKQKVQI 966
Cdd:pfam17215 78 ENTGKRKVKL 87
|
|
| OB_Dis3 |
pfam17849 |
Dis3-like cold-shock domain 2 (CSD2); This domain has an OB fold and is found in the Dis3l2 ... |
394-461 |
2.06e-23 |
|
Dis3-like cold-shock domain 2 (CSD2); This domain has an OB fold and is found in the Dis3l2 protein. This domain along with CSD1 binds to RNA.
:
Pssm-ID: 436091 [Multi-domain] Cd Length: 77 Bit Score: 94.60 E-value: 2.06e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113445 394 VLLTPMDRRVPKIRFRTRQAP--------RLVGRRIVVAIDLWDASSRYPEGHFVRDLGEMETKEAETEALLLEYD 461
Cdd:pfam17849 2 VLFVPRDKRIPRIRIPTKSAPeeflenpeDLEGKLFVVKIDDWPENSRYPLGHIVKVLGEIGDIETETEAILLENG 77
|
|
| Rrp44_CSD1 super family |
cl28867 |
Rrp44-like cold shock domain; |
251-370 |
1.03e-21 |
|
Rrp44-like cold shock domain;
The actual alignment was detected with superfamily member pfam17216:
Pssm-ID: 375054 Cd Length: 148 Bit Score: 92.53 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 251 HWSMSRLLACIKNGEVHKGLINISTYNYLEGSVVVPGYNKPVLVSGRENLNRAVQGDIVCIQILPQDQWKTEAEEIAD-- 328
Cdd:pfam17216 7 YYSTARVMGGLKNGVLYQGNIQISEYNFLEGSVSLPRFSKPVLIVGQKNLNRAFNGDQVIVELLPQSEWKAPSSIVLDse 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113445 329 -------------DDEDvvvSTAAEPDSARINDLE--------LITKRNA--HPTAKVVGILKRN 370
Cdd:pfam17216 87 hfdvndnpdieagDDDD---NNESSSNTTVISDKQrrllakdaMIAQRSKkiQPTAKVVYIQRRS 148
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RNB |
pfam00773 |
RNB domain; This domain is the catalytic domain of ribonuclease II. |
496-827 |
6.86e-122 |
|
RNB domain; This domain is the catalytic domain of ribonuclease II.
Pssm-ID: 459934 [Multi-domain] Cd Length: 314 Bit Score: 373.54 E-value: 6.86e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 496 RKDFRDKLICSIDPPGCQDIDDALHACVLPNGNYEVGVHIADVTHFVKPNTSMDSEAASRGTTVYLVDKRIDMLPMLLGT 575
Cdd:pfam00773 1 RKDLRDLPFITIDPADAKDLDDAISVEKLPNGGYRLGVHIADVSHYVPPGSPLDREARKRGTSVYLPDRVIPMLPEKLSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 576 DLCSLRPYVERFAFSCIWEMDENANIIKVHFTKSVIASKEAFSYADAQARIDDQKMQDP---LTQGMRVLLKLSKILKQK 652
Cdd:pfam00773 81 DLCSLNPGEDRLALSVEITIDADGEVTSYEIYPSVIRSKARLTYEEVDDLLEGKDAEKDkpdLAEDLRLLYELAKILRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 653 RMDEGALNLASPEVRIQTDNETsdPMDVEIKQLLETNSLVEEFMLLANISVAQKIYdAFPQTAVLRRHAAPPLTNFDSLQ 732
Cdd:pfam00773 161 RLQRGALDLDTPENKLILDEEG--VIDILIQERTDAHSLIEEFMLLANEAVARHLQ-ELGIPALYRVHPEPDLEKLNSLI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 733 DILRvckgmhlKCDTSKSLAKSLDECVDPkepyfNTLLRILTTRCMLSAEYFcsgtfaPPDFRHYGLASPIYTHFTSPIR 812
Cdd:pfam00773 238 KLLQ-------LLPDDKGLSKSLEKIKDD-----ERLLSILLLRTMPRAEYS------PEPLGHFGLGLDIYTHFTSPIR 299
|
330
....*....|....*
gi 19113445 813 RYADVLAHRQLAAAI 827
Cdd:pfam00773 300 RYPDLIVHRQLKALL 314
|
|
| VacB |
COG0557 |
Exoribonuclease R [Transcription]; |
353-909 |
2.74e-111 |
|
Exoribonuclease R [Transcription];
Pssm-ID: 440323 [Multi-domain] Cd Length: 711 Bit Score: 359.42 E-value: 2.74e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 353 TKRNAHPTAKVVGILKRNWRPYVGhvdnaTIAQSKGGsqqtVLLTPMDRRVPK-IRFRTRQAPRL-VGRRIVVAIDLWDA 430
Cdd:COG0557 116 EDRRGRPEGRVVEILERANTRVVG-----RFEKEKGF----GFVVPDDKRLLQdIFIPPDDLNGAkDGDLVVVEITRYPE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 431 SSRYPEGHFVRDLGEMETKEAETEALLLEYDVQHRpFPKAVL---DCLPEEghnwKVPADKthplwKNRKDFRDKLICSI 507
Cdd:COG0557 187 RRGPPEGRVVEVLGSPGDPGAEILIAIRKHGLPHE-FPEEVLaeaEALPDE----VPEADL-----KGRRDLRDLPLVTI 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 508 DPPGCQDIDDALHACVLPNGNYEVGVHIADVTHFVKPNTSMDSEAASRGTTVYLVDKRIDMLPMLLGTDLCSLRPYVERF 587
Cdd:COG0557 257 DGEDAKDFDDAVSAEKLDNGGWRLGVHIADVSHYVRPGSALDREARKRGTSVYLPDRVIPMLPERLSNGLCSLNPGEDRL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 588 AFSCIWEMDENANIIKVHFTKSVIASKEAFSYADAQARIDDQ-----KMQDPLTQGMRVLLKLSKILKQKRMDEGALNLA 662
Cdd:COG0557 337 AMSCEMEIDAKGEVVSYEFYRSVIRSDARLTYEEVQAILDGKdeelrEEYADLVPMLEELYELAKILRKAREKRGAIDFD 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 663 SPEVRIQTDnETSDPMDVEIKQLLETNSLVEEFMLLANISVAQKIYDAfPQTAVLRRHAAPPLTNFDSLQDILRVCkGMH 742
Cdd:COG0557 417 LPETKIILD-EEGKPEDIVPRERNDAHKLIEEFMLLANEAVAEFLEKL-KLPFLYRVHEEPDPEKLEALREFLANL-GLK 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 743 LKCD---TSKSLAKSLDECVD-PKEPYFNTLLRilttRCMLSAEYfcsgtfAPPDFRHYGLASPIYTHFTSPIRRYADVL 818
Cdd:COG0557 494 LKGGdepTPKDLQKLLEQVKGrPEEELLNTLLL----RSMKQAVY------SPENIGHFGLALEAYTHFTSPIRRYPDLL 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 819 AHRQLAAAIDyETINPSLS--DKSRLIEICNGINYRHRMAQMAGRASIEYYVGQALKGGVAEE-DAYVIKVFKNGFVVFI 895
Cdd:COG0557 564 VHRALKAYLE-GKRSPGLQeyLEEELEEIAEHCSETERRADEAERDVVDLKKAEYMKDRVGEEfEGVISGVTSFGLFVEL 642
|
570
....*....|....
gi 19113445 896 ARFGLEGIVYTKSL 909
Cdd:COG0557 643 DELGVEGLVHVSSL 656
|
|
| RNB |
smart00955 |
This domain is the catalytic domain of ribonuclease II; |
496-828 |
1.37e-101 |
|
This domain is the catalytic domain of ribonuclease II;
Pssm-ID: 214935 [Multi-domain] Cd Length: 286 Bit Score: 319.21 E-value: 1.37e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 496 RKDFRDKLICSIDPPGCQDIDDALHACVLPNGNYEVGVHIADVTHFVKPNTSMDSEAASRGTTVYLVDKRIDMLPMLLGT 575
Cdd:smart00955 1 RVDLRDLPLFTIDPEDAKDIDDAVSVEKLDNGGYRLGVHIADVSHYVKPGSALDREARKRGTSVYLPDRVIPMLPEELSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 576 DLCSLRPYVERFAFSCIWEMDENA-NIIKVHFTKSVIASKEAFSYADAQARIDdqkmqdpltqgmrvllklskilkqkrm 654
Cdd:smart00955 81 GLCSLNPGEDRLALSVEMTLDADGgEILDYEFYRSVIRSKARLTYEEVDAILE--------------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 655 degalnlaspevRIQTDNETSdPMDVEIKQLLETNSLVEEFMLLANISVAQKIYDAFPQtAVLRRHAAPPLTN-FDSLQD 733
Cdd:smart00955 134 ------------KIVLDEEGK-IEDIVPRERNDAHSLVEEFMILANEAVARFLAKNGIP-GLYRVHEGPDPEKlAELLKE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 734 ILRVCKGMHLKCDTSKSLAKSLDECVDPKEpyfNTLLRILTTRCMLSAEYFCSGTfappdfRHYGLASPIYTHFTSPIRR 813
Cdd:smart00955 200 FLALLGLLLLGGDGPKALAKLLEKIRDSPE---ERLLELLLLRSMPHAEYSVDNS------GHFGLALDAYTHFTSPIRR 270
|
330
....*....|....*
gi 19113445 814 YADVLAHRQLAAAID 828
Cdd:smart00955 271 YPDLIVHRQLKAALR 285
|
|
| RNase_R |
TIGR02063 |
ribonuclease R; This family consists of an exoribonuclease, ribonuclease R, also called VacB. ... |
325-954 |
5.09e-99 |
|
ribonuclease R; This family consists of an exoribonuclease, ribonuclease R, also called VacB. It is one of the eight exoribonucleases reported in E. coli and is broadly distributed throughout the bacteria. In E. coli, double mutants of this protein and polynucleotide phosphorylase are not viable. Scoring between trusted and noise cutoffs to the model are shorter, divergent forms from the Chlamydiae, and divergent forms from the Campylobacterales (including Helicobacter pylori) and Leptospira interrogans. [Transcription, Degradation of RNA]
Pssm-ID: 273947 [Multi-domain] Cd Length: 709 Bit Score: 326.54 E-value: 5.09e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 325 EIADDDEDVVVSTAAEPDSARINDLELIT-----KRNAHPTAKVVGILKRNWRPYVGhvdnaTIAQSKGGsqqtVLLTPM 399
Cdd:TIGR02063 84 RPEDDDEDDIFIPPRQMNGAMHGDRVLVRitgkpDGGDRFEARVIKILERANDQIVG-----TFYIENGI----GFVIPD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 400 DRRVP-KIRFRTRQAPRLV-GRRIVVAIDLWDASSRYPEGHFVRDLGEMETKEAETEALLLEYDVQHRpFPKAVLDCLPe 477
Cdd:TIGR02063 155 DKRIYlDIFIPPEQILGAEeGDKVLVEITKYPDRNRPAIGKVVEILGHADDPGIDILIIIRKHGIPYE-FPEEVLDEAA- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 478 eghnwKVPADKTHPLWKNRKDFRDKLICSIDPPGCQDIDDALHACVLPNGNYEVGVHIADVTHFVKPNTSMDSEAASRGT 557
Cdd:TIGR02063 233 -----KIPEEVPEEEIKGRKDLRDLPFVTIDGEDAKDFDDAVYVEKLKDGNYKLGVAIADVSHYVREGSALDKEALKRGT 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 558 TVYLVDKRIDMLPMLLGTDLCSLRPYVERFAFSCIWEMDENANIIKVHFTKSVIASKEAFSYADAQARIDDQ----KMQD 633
Cdd:TIGR02063 308 SVYLPDRVIPMLPERLSNGICSLNPNEDRLTLSCEMEIDKKGRVKKYEFYEAVINSHARLTYNQVNDIIEGKdaldKKEP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 634 PLTQGMRVLLKLSKILKQKRMDEGALNLASPEVRIQTDnETSDPMDVEIKQLLETNSLVEEFMLLANISVAQKIyDAFPQ 713
Cdd:TIGR02063 388 PLKEMLKNLFELYKILRKKRKKRGAIDFDSKEAKIILD-ENGKPIDIVPRERGDAHKLIEEFMIAANETVAEHL-EKAKL 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 714 TAVLRRHAAPPLTNFDSLQDILR----VCKGMHLKCDTSKSLAKSLDECVD-PKEPYFNTLLriltTRCMLSAEYfcsgt 788
Cdd:TIGR02063 466 PFIYRVHERPSEEKLQNLREFLKtlgiTLKGGTSDKPQPKDFQKLLEKVKGrPEEELINTVL----LRSMQQAKY----- 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 789 fAPPDFRHYGLASPIYTHFTSPIRRYADVLAHRQLAAAIDYETINPSLSDKSR----LIEICNGINYRHRMAQMAGRASI 864
Cdd:TIGR02063 537 -SPENIGHFGLALEYYTHFTSPIRRYPDLIVHRLIKKALFGGENTTTEKEREYleakLEEIAEHSSKTERRADEAERDVN 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 865 EYYVGQALKGGVAEEdayvikvFkNGFVVFIARFGL---------EGIVYTKSLssvlePNVEYVEDEykLNIEIRDQPK 935
Cdd:TIGR02063 616 DWKKAEYMSEKIGEE-------F-EGVISGVTSFGLfvelenntiEGLVHISTL-----KDDYYVFDE--KGLALVGERT 680
|
650
....*....|....*....
gi 19113445 936 PQTvqIQMFQQVRVRVTTV 954
Cdd:TIGR02063 681 GKV--FRLGDRVKVRVVKA 697
|
|
| PIN_Rrp44-like |
cd09862 |
VapC-like PIN domain of yeast exosome subunit Rrp44 endoribonuclease and other eukaryotic ... |
27-213 |
3.99e-80 |
|
VapC-like PIN domain of yeast exosome subunit Rrp44 endoribonuclease and other eukaryotic homologs; PIN (PilT N terminus) domain of the Saccharomyces cerevisiae exosome subunit Rrp44 (Ribosomal RNA-processing protein 44 or Protein Dis3 homolog) and other similar eukaryotic homologs are included in this family. The eukaryotic exosome is a conserved macromolecular complex responsible for many RNA-processing and RNA-degradation reactions. It is composed of nine core subunits that directly binds Rrp44. The Rrp44 nuclease is the catalytic subunit of the exosome and has endonuclease activity in the PIN domain and an exoribonuclease activity in its RNase II-like region. Rrp44 binding to the exosome is mediated mainly by the PIN domain and by subunits Rrp41-Rrp45, and binding predictions indicate that the PIN domain active site is positioned on the outer surface of the exosome. This subgroup belongs to the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. PIN domains within this subgroup contain four of these residues which cluster at the C-terminal end of the beta-sheet and form a negatively charged pocket near the center of the molecule. Recombinant Rrp44 was shown to possess manganese-dependent endonuclease activity in vitro that was abolished by point mutations in these putative metal binding residues of its PIN domain. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.
Pssm-ID: 350211 Cd Length: 178 Bit Score: 257.52 E-value: 3.99e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 27 RGKVQKVVREQYLRNDIPCQSRACPLCRSKLPKDSRGNVLEPilsekpmflekfGHHYLIPDSNIFYHCIDALEHPNnFF 106
Cdd:cd09862 5 RGKVVKVVREHYLRDDIPCGSELCPLCPQTNPKLLLLSLLSD------------AKHYLIPDTNVVLHQIDLLEDPE-IT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 107 DVIILQTVFSEISSKSIPLYNRMKRLCQEKTKRFTPFSNEFFVDTFVERLDDESANDRNDRAIRNAASWFASHLASLGIK 186
Cdd:cd09862 72 NVIILQTVLEEVRHRSLPLYNRLRALLKDPRKRFYVFSNEFHRETYVEREPGESPNDRNDRAIRKAAKWYQNHLAKLGIP 151
|
170 180
....*....|....*....|....*..
gi 19113445 187 IVLLTDDRENARLAAEQGIQVSTLKDY 213
Cdd:cd09862 152 VVLLTDDADNREKAEEEGILALTVREY 178
|
|
| Rrp44_S1 |
pfam17215 |
S1 domain; This domain corresponds to the S1 domain found at the C-terminus of ribonucleases ... |
877-966 |
5.22e-35 |
|
S1 domain; This domain corresponds to the S1 domain found at the C-terminus of ribonucleases such as yeast Rrp44.
Pssm-ID: 435792 Cd Length: 87 Bit Score: 128.03 E-value: 5.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 877 AEEDAYVIKVFKNGFVVFIARFGLEGIVYTKSLSSVlEPNVEYVEDEYKLNIEIRDQPKPQTVqiQMFQQVRVRVTTVRD 956
Cdd:pfam17215 1 SEEEGYVIKVFNNGIVVFVPKFGIEGLIRLEDLTGD-EPEAEFDADEYSLTFPDKGSGKKRTV--GVFDKVRVRVKSVKD 77
|
90
....*....|
gi 19113445 957 EHSGKQKVQI 966
Cdd:pfam17215 78 ENTGKRKVKL 87
|
|
| PRK11642 |
PRK11642 |
ribonuclease R; |
494-829 |
4.30e-34 |
|
ribonuclease R;
Pssm-ID: 236944 [Multi-domain] Cd Length: 813 Bit Score: 141.03 E-value: 4.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 494 KNRKDFRDKLICSIDPPGCQDIDDALHACVLPNGNYEVGVHIADVTHFVKPNTSMDSEAASRGTTVYLVDKRIDMLPMLL 573
Cdd:PRK11642 258 AGRVDLRDLPLVTIDGEDARDFDDAVYCEKKRGGGWRLWVAIADVSYYVRPPTPLDREARNRGTSVYFPSQVVPMLPEVL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 574 GTDLCSLRPYVERFAFSCIWEMDENANIIKVHFTKSVIASKEAFSYADAQARID-DQKMQD---PLTQGMRVLLKLSKIL 649
Cdd:PRK11642 338 SNGLCSLNPQVDRLCMVCEMTISSKGRLTGYKFYEAVMSSHARLTYTKVWHILQgDQDLREqyaPLVKHLEELHNLYKVL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 650 KQKRMDEGALNLASPEVRIQTDNEtsdpMDVE-IKQLLETNS--LVEEFMLLANISVAqKIYDAFPQTAVLRRHAAPPLT 726
Cdd:PRK11642 418 DKAREERGGISFESEEAKFIFNAE----RRIErIEQTQRNDAhkLIEECMILANISAA-RFVEKAKEPALFRIHDKPSTE 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 727 NFDSLQDILRVCkGMHLKCDTS---KSLAKSLDECVD-PKEPYFNTLLriltTRCMLSAEYfcsgtfAPPDFRHYGLASP 802
Cdd:PRK11642 493 AITSFRSVLAEL-GLELPGGNKpepRDYAELLESVADrPDAEMLQTML----LRSMKQAIY------DPENRGHFGLALQ 561
|
330 340
....*....|....*....|....*..
gi 19113445 803 IYTHFTSPIRRYADVLAHRqlaaAIDY 829
Cdd:PRK11642 562 SYAHFTSPIRRYPDLSLHR----AIKY 584
|
|
| OB_Dis3 |
pfam17849 |
Dis3-like cold-shock domain 2 (CSD2); This domain has an OB fold and is found in the Dis3l2 ... |
394-461 |
2.06e-23 |
|
Dis3-like cold-shock domain 2 (CSD2); This domain has an OB fold and is found in the Dis3l2 protein. This domain along with CSD1 binds to RNA.
Pssm-ID: 436091 [Multi-domain] Cd Length: 77 Bit Score: 94.60 E-value: 2.06e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113445 394 VLLTPMDRRVPKIRFRTRQAP--------RLVGRRIVVAIDLWDASSRYPEGHFVRDLGEMETKEAETEALLLEYD 461
Cdd:pfam17849 2 VLFVPRDKRIPRIRIPTKSAPeeflenpeDLEGKLFVVKIDDWPENSRYPLGHIVKVLGEIGDIETETEAILLENG 77
|
|
| Rrp44_CSD1 |
pfam17216 |
Rrp44-like cold shock domain; |
251-370 |
1.03e-21 |
|
Rrp44-like cold shock domain;
Pssm-ID: 375054 Cd Length: 148 Bit Score: 92.53 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 251 HWSMSRLLACIKNGEVHKGLINISTYNYLEGSVVVPGYNKPVLVSGRENLNRAVQGDIVCIQILPQDQWKTEAEEIAD-- 328
Cdd:pfam17216 7 YYSTARVMGGLKNGVLYQGNIQISEYNFLEGSVSLPRFSKPVLIVGQKNLNRAFNGDQVIVELLPQSEWKAPSSIVLDse 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113445 329 -------------DDEDvvvSTAAEPDSARINDLE--------LITKRNA--HPTAKVVGILKRN 370
Cdd:pfam17216 87 hfdvndnpdieagDDDD---NNESSSNTTVISDKQrrllakdaMIAQRSKkiQPTAKVVYIQRRS 148
|
|
| PINc |
smart00670 |
Large family of predicted nucleotide-binding domains; From similarities to 5'-exonucleases, ... |
83-198 |
1.80e-17 |
|
Large family of predicted nucleotide-binding domains; From similarities to 5'-exonucleases, these domains are predicted to be RNases. PINc domains in nematode SMG-5 and yeast NMD4p are predicted to be involved in RNAi.
Pssm-ID: 214771 [Multi-domain] Cd Length: 111 Bit Score: 79.00 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 83 HYLIPDSNIFYHCI--DALEHPNNF-FDVIILQTVFSEISSKSIPLYNRMKRLCQEKTKRFTPFSNEFFVDTFVERLDDE 159
Cdd:smart00670 1 MKVVLDTNVLIDGLirDALEKLLEKkGEVYIPQTVLEELEYLALRSLKKLEELALEGKIILKVLKEERIEEEILERLSLK 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 19113445 160 SANDRNDRAIRNAASWFAshlaslgiKIVLLTDDRENAR 198
Cdd:smart00670 81 LELLPNDALILATAKELG--------NVVLVTNDRDLRR 111
|
|
| PIN_4 |
pfam13638 |
PIN domain; Members of this family of bacterial domains are predicted to be RNases (from ... |
85-211 |
1.03e-15 |
|
PIN domain; Members of this family of bacterial domains are predicted to be RNases (from similarities to 5'-exonucleases).
Pssm-ID: 433369 Cd Length: 131 Bit Score: 74.58 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 85 LIPDSNIFYHCIDALEHPNNFFDVIILQTVFSEISSKSIPLYNRmKRLCQEKTKRFTPFSNEFFVDT----FVERLDDE- 159
Cdd:pfam13638 1 YVLDTNVLLHDPDALFNFGEENDVVIPITVLEELDGLKKGSDES-GRELARLARQANRWLDELLENNggrlRGQTLDERl 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 19113445 160 --SANDRNDRAIRNAASWFASHLAslGIKIVLLTDDRENARLAAEQGIQVSTLK 211
Cdd:pfam13638 80 ppDPFDKNDNRILAVALYLKEELP--DRPVILVSKDINLRIKADALGIPAEDYE 131
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RNB |
pfam00773 |
RNB domain; This domain is the catalytic domain of ribonuclease II. |
496-827 |
6.86e-122 |
|
RNB domain; This domain is the catalytic domain of ribonuclease II.
Pssm-ID: 459934 [Multi-domain] Cd Length: 314 Bit Score: 373.54 E-value: 6.86e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 496 RKDFRDKLICSIDPPGCQDIDDALHACVLPNGNYEVGVHIADVTHFVKPNTSMDSEAASRGTTVYLVDKRIDMLPMLLGT 575
Cdd:pfam00773 1 RKDLRDLPFITIDPADAKDLDDAISVEKLPNGGYRLGVHIADVSHYVPPGSPLDREARKRGTSVYLPDRVIPMLPEKLSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 576 DLCSLRPYVERFAFSCIWEMDENANIIKVHFTKSVIASKEAFSYADAQARIDDQKMQDP---LTQGMRVLLKLSKILKQK 652
Cdd:pfam00773 81 DLCSLNPGEDRLALSVEITIDADGEVTSYEIYPSVIRSKARLTYEEVDDLLEGKDAEKDkpdLAEDLRLLYELAKILRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 653 RMDEGALNLASPEVRIQTDNETsdPMDVEIKQLLETNSLVEEFMLLANISVAQKIYdAFPQTAVLRRHAAPPLTNFDSLQ 732
Cdd:pfam00773 161 RLQRGALDLDTPENKLILDEEG--VIDILIQERTDAHSLIEEFMLLANEAVARHLQ-ELGIPALYRVHPEPDLEKLNSLI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 733 DILRvckgmhlKCDTSKSLAKSLDECVDPkepyfNTLLRILTTRCMLSAEYFcsgtfaPPDFRHYGLASPIYTHFTSPIR 812
Cdd:pfam00773 238 KLLQ-------LLPDDKGLSKSLEKIKDD-----ERLLSILLLRTMPRAEYS------PEPLGHFGLGLDIYTHFTSPIR 299
|
330
....*....|....*
gi 19113445 813 RYADVLAHRQLAAAI 827
Cdd:pfam00773 300 RYPDLIVHRQLKALL 314
|
|
| VacB |
COG0557 |
Exoribonuclease R [Transcription]; |
353-909 |
2.74e-111 |
|
Exoribonuclease R [Transcription];
Pssm-ID: 440323 [Multi-domain] Cd Length: 711 Bit Score: 359.42 E-value: 2.74e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 353 TKRNAHPTAKVVGILKRNWRPYVGhvdnaTIAQSKGGsqqtVLLTPMDRRVPK-IRFRTRQAPRL-VGRRIVVAIDLWDA 430
Cdd:COG0557 116 EDRRGRPEGRVVEILERANTRVVG-----RFEKEKGF----GFVVPDDKRLLQdIFIPPDDLNGAkDGDLVVVEITRYPE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 431 SSRYPEGHFVRDLGEMETKEAETEALLLEYDVQHRpFPKAVL---DCLPEEghnwKVPADKthplwKNRKDFRDKLICSI 507
Cdd:COG0557 187 RRGPPEGRVVEVLGSPGDPGAEILIAIRKHGLPHE-FPEEVLaeaEALPDE----VPEADL-----KGRRDLRDLPLVTI 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 508 DPPGCQDIDDALHACVLPNGNYEVGVHIADVTHFVKPNTSMDSEAASRGTTVYLVDKRIDMLPMLLGTDLCSLRPYVERF 587
Cdd:COG0557 257 DGEDAKDFDDAVSAEKLDNGGWRLGVHIADVSHYVRPGSALDREARKRGTSVYLPDRVIPMLPERLSNGLCSLNPGEDRL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 588 AFSCIWEMDENANIIKVHFTKSVIASKEAFSYADAQARIDDQ-----KMQDPLTQGMRVLLKLSKILKQKRMDEGALNLA 662
Cdd:COG0557 337 AMSCEMEIDAKGEVVSYEFYRSVIRSDARLTYEEVQAILDGKdeelrEEYADLVPMLEELYELAKILRKAREKRGAIDFD 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 663 SPEVRIQTDnETSDPMDVEIKQLLETNSLVEEFMLLANISVAQKIYDAfPQTAVLRRHAAPPLTNFDSLQDILRVCkGMH 742
Cdd:COG0557 417 LPETKIILD-EEGKPEDIVPRERNDAHKLIEEFMLLANEAVAEFLEKL-KLPFLYRVHEEPDPEKLEALREFLANL-GLK 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 743 LKCD---TSKSLAKSLDECVD-PKEPYFNTLLRilttRCMLSAEYfcsgtfAPPDFRHYGLASPIYTHFTSPIRRYADVL 818
Cdd:COG0557 494 LKGGdepTPKDLQKLLEQVKGrPEEELLNTLLL----RSMKQAVY------SPENIGHFGLALEAYTHFTSPIRRYPDLL 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 819 AHRQLAAAIDyETINPSLS--DKSRLIEICNGINYRHRMAQMAGRASIEYYVGQALKGGVAEE-DAYVIKVFKNGFVVFI 895
Cdd:COG0557 564 VHRALKAYLE-GKRSPGLQeyLEEELEEIAEHCSETERRADEAERDVVDLKKAEYMKDRVGEEfEGVISGVTSFGLFVEL 642
|
570
....*....|....
gi 19113445 896 ARFGLEGIVYTKSL 909
Cdd:COG0557 643 DELGVEGLVHVSSL 656
|
|
| RNB |
smart00955 |
This domain is the catalytic domain of ribonuclease II; |
496-828 |
1.37e-101 |
|
This domain is the catalytic domain of ribonuclease II;
Pssm-ID: 214935 [Multi-domain] Cd Length: 286 Bit Score: 319.21 E-value: 1.37e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 496 RKDFRDKLICSIDPPGCQDIDDALHACVLPNGNYEVGVHIADVTHFVKPNTSMDSEAASRGTTVYLVDKRIDMLPMLLGT 575
Cdd:smart00955 1 RVDLRDLPLFTIDPEDAKDIDDAVSVEKLDNGGYRLGVHIADVSHYVKPGSALDREARKRGTSVYLPDRVIPMLPEELSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 576 DLCSLRPYVERFAFSCIWEMDENA-NIIKVHFTKSVIASKEAFSYADAQARIDdqkmqdpltqgmrvllklskilkqkrm 654
Cdd:smart00955 81 GLCSLNPGEDRLALSVEMTLDADGgEILDYEFYRSVIRSKARLTYEEVDAILE--------------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 655 degalnlaspevRIQTDNETSdPMDVEIKQLLETNSLVEEFMLLANISVAQKIYDAFPQtAVLRRHAAPPLTN-FDSLQD 733
Cdd:smart00955 134 ------------KIVLDEEGK-IEDIVPRERNDAHSLVEEFMILANEAVARFLAKNGIP-GLYRVHEGPDPEKlAELLKE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 734 ILRVCKGMHLKCDTSKSLAKSLDECVDPKEpyfNTLLRILTTRCMLSAEYFCSGTfappdfRHYGLASPIYTHFTSPIRR 813
Cdd:smart00955 200 FLALLGLLLLGGDGPKALAKLLEKIRDSPE---ERLLELLLLRSMPHAEYSVDNS------GHFGLALDAYTHFTSPIRR 270
|
330
....*....|....*
gi 19113445 814 YADVLAHRQLAAAID 828
Cdd:smart00955 271 YPDLIVHRQLKAALR 285
|
|
| RNase_R |
TIGR02063 |
ribonuclease R; This family consists of an exoribonuclease, ribonuclease R, also called VacB. ... |
325-954 |
5.09e-99 |
|
ribonuclease R; This family consists of an exoribonuclease, ribonuclease R, also called VacB. It is one of the eight exoribonucleases reported in E. coli and is broadly distributed throughout the bacteria. In E. coli, double mutants of this protein and polynucleotide phosphorylase are not viable. Scoring between trusted and noise cutoffs to the model are shorter, divergent forms from the Chlamydiae, and divergent forms from the Campylobacterales (including Helicobacter pylori) and Leptospira interrogans. [Transcription, Degradation of RNA]
Pssm-ID: 273947 [Multi-domain] Cd Length: 709 Bit Score: 326.54 E-value: 5.09e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 325 EIADDDEDVVVSTAAEPDSARINDLELIT-----KRNAHPTAKVVGILKRNWRPYVGhvdnaTIAQSKGGsqqtVLLTPM 399
Cdd:TIGR02063 84 RPEDDDEDDIFIPPRQMNGAMHGDRVLVRitgkpDGGDRFEARVIKILERANDQIVG-----TFYIENGI----GFVIPD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 400 DRRVP-KIRFRTRQAPRLV-GRRIVVAIDLWDASSRYPEGHFVRDLGEMETKEAETEALLLEYDVQHRpFPKAVLDCLPe 477
Cdd:TIGR02063 155 DKRIYlDIFIPPEQILGAEeGDKVLVEITKYPDRNRPAIGKVVEILGHADDPGIDILIIIRKHGIPYE-FPEEVLDEAA- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 478 eghnwKVPADKTHPLWKNRKDFRDKLICSIDPPGCQDIDDALHACVLPNGNYEVGVHIADVTHFVKPNTSMDSEAASRGT 557
Cdd:TIGR02063 233 -----KIPEEVPEEEIKGRKDLRDLPFVTIDGEDAKDFDDAVYVEKLKDGNYKLGVAIADVSHYVREGSALDKEALKRGT 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 558 TVYLVDKRIDMLPMLLGTDLCSLRPYVERFAFSCIWEMDENANIIKVHFTKSVIASKEAFSYADAQARIDDQ----KMQD 633
Cdd:TIGR02063 308 SVYLPDRVIPMLPERLSNGICSLNPNEDRLTLSCEMEIDKKGRVKKYEFYEAVINSHARLTYNQVNDIIEGKdaldKKEP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 634 PLTQGMRVLLKLSKILKQKRMDEGALNLASPEVRIQTDnETSDPMDVEIKQLLETNSLVEEFMLLANISVAQKIyDAFPQ 713
Cdd:TIGR02063 388 PLKEMLKNLFELYKILRKKRKKRGAIDFDSKEAKIILD-ENGKPIDIVPRERGDAHKLIEEFMIAANETVAEHL-EKAKL 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 714 TAVLRRHAAPPLTNFDSLQDILR----VCKGMHLKCDTSKSLAKSLDECVD-PKEPYFNTLLriltTRCMLSAEYfcsgt 788
Cdd:TIGR02063 466 PFIYRVHERPSEEKLQNLREFLKtlgiTLKGGTSDKPQPKDFQKLLEKVKGrPEEELINTVL----LRSMQQAKY----- 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 789 fAPPDFRHYGLASPIYTHFTSPIRRYADVLAHRQLAAAIDYETINPSLSDKSR----LIEICNGINYRHRMAQMAGRASI 864
Cdd:TIGR02063 537 -SPENIGHFGLALEYYTHFTSPIRRYPDLIVHRLIKKALFGGENTTTEKEREYleakLEEIAEHSSKTERRADEAERDVN 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 865 EYYVGQALKGGVAEEdayvikvFkNGFVVFIARFGL---------EGIVYTKSLssvlePNVEYVEDEykLNIEIRDQPK 935
Cdd:TIGR02063 616 DWKKAEYMSEKIGEE-------F-EGVISGVTSFGLfvelenntiEGLVHISTL-----KDDYYVFDE--KGLALVGERT 680
|
650
....*....|....*....
gi 19113445 936 PQTvqIQMFQQVRVRVTTV 954
Cdd:TIGR02063 681 GKV--FRLGDRVKVRVVKA 697
|
|
| PIN_Rrp44-like |
cd09862 |
VapC-like PIN domain of yeast exosome subunit Rrp44 endoribonuclease and other eukaryotic ... |
27-213 |
3.99e-80 |
|
VapC-like PIN domain of yeast exosome subunit Rrp44 endoribonuclease and other eukaryotic homologs; PIN (PilT N terminus) domain of the Saccharomyces cerevisiae exosome subunit Rrp44 (Ribosomal RNA-processing protein 44 or Protein Dis3 homolog) and other similar eukaryotic homologs are included in this family. The eukaryotic exosome is a conserved macromolecular complex responsible for many RNA-processing and RNA-degradation reactions. It is composed of nine core subunits that directly binds Rrp44. The Rrp44 nuclease is the catalytic subunit of the exosome and has endonuclease activity in the PIN domain and an exoribonuclease activity in its RNase II-like region. Rrp44 binding to the exosome is mediated mainly by the PIN domain and by subunits Rrp41-Rrp45, and binding predictions indicate that the PIN domain active site is positioned on the outer surface of the exosome. This subgroup belongs to the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions, in some members, additional metal coordinating residues can be found. Some members of the superfamily lack several of these key catalytic residues. PIN domains within this subgroup contain four of these residues which cluster at the C-terminal end of the beta-sheet and form a negatively charged pocket near the center of the molecule. Recombinant Rrp44 was shown to possess manganese-dependent endonuclease activity in vitro that was abolished by point mutations in these putative metal binding residues of its PIN domain. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.
Pssm-ID: 350211 Cd Length: 178 Bit Score: 257.52 E-value: 3.99e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 27 RGKVQKVVREQYLRNDIPCQSRACPLCRSKLPKDSRGNVLEPilsekpmflekfGHHYLIPDSNIFYHCIDALEHPNnFF 106
Cdd:cd09862 5 RGKVVKVVREHYLRDDIPCGSELCPLCPQTNPKLLLLSLLSD------------AKHYLIPDTNVVLHQIDLLEDPE-IT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 107 DVIILQTVFSEISSKSIPLYNRMKRLCQEKTKRFTPFSNEFFVDTFVERLDDESANDRNDRAIRNAASWFASHLASLGIK 186
Cdd:cd09862 72 NVIILQTVLEEVRHRSLPLYNRLRALLKDPRKRFYVFSNEFHRETYVEREPGESPNDRNDRAIRKAAKWYQNHLAKLGIP 151
|
170 180
....*....|....*....|....*..
gi 19113445 187 IVLLTDDRENARLAAEQGIQVSTLKDY 213
Cdd:cd09862 152 VVLLTDDADNREKAEEEGILALTVREY 178
|
|
| 3_prime_RNase |
TIGR00358 |
VacB and RNase II family 3'-5' exoribonucleases; This model is defined to identify a pair of ... |
418-957 |
2.17e-66 |
|
VacB and RNase II family 3'-5' exoribonucleases; This model is defined to identify a pair of paralogous 3-prime exoribonucleases in E. coli, plus the set of proteins apparently orthologous to one or the other in other eubacteria. VacB was characterized originally as required for the expression of virulence genes, but is now recognized as the exoribonuclease RNase R (Rnr). Its paralog in E. coli and H. influenzae is designated exoribonuclease II (Rnb). Both are involved in the degradation of mRNA, and consequently have strong pleiotropic effects that may be difficult to disentangle. Both these proteins share domain-level similarity (RNB, S1) with a considerable number of other proteins, and full-length similarity scoring below the trusted cutoff to proteins associated with various phenotypes but uncertain biochemistry; it may be that these latter proteins are also 3-prime exoribonucleases. [Transcription, Degradation of RNA]
Pssm-ID: 273033 [Multi-domain] Cd Length: 654 Bit Score: 235.76 E-value: 2.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 418 GRRIVVAIDLWDASSRYPEGHFVRDLGEMETKEAETEALLLEYDVQHRpFPKAVldclpeEGHNWKVPADKTHPLWKNRK 497
Cdd:TIGR00358 123 GDKVVVELTEYPLRRNLFYGEITQILGNNDDPLIPWWVTLARHEIPFE-FPDGV------EQQAAKLQFDVDEQAKKYRE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 498 DFRDKLICSIDPPGCQDIDDALHACVLPNGNYEVGVHIADVTHFVKPNTSMDSEAASRGTTVYLVDKRIDMLPMLLGTDL 577
Cdd:TIGR00358 196 DLTDLAFVTIDGADAKDLDDAVYVKKLPDGGWKLYVAIADVSYYVAENSPLDKEAKHRGFSVYLPGFVIPMLPEELSNGL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 578 CSLRPYVERFAFSCIWEMDENANIIKVHFTKSVIASKEAFSYAD-AQARIDDQKMQD---PLTQGMRVLLKLSKILKQKR 653
Cdd:TIGR00358 276 CSLNPNEDRLVLVCEMTISAQGRITDNEFYPATIESKARLTYDKvNDWLENDDELQPeyeTLVEQLKALHQLSQALGEWR 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 654 MDEGALNLASPEVRIQTDnETSDPMDVEIKQLLETNSLVEEFMLLANISVAQKIYDAfPQTAVLRRHAAPPLTNFDSLQD 733
Cdd:TIGR00358 356 HKRGLIDFEHPETKFIVD-EEGRVIDIVAEVRRIAEKIIEEAMIVANICAARFLHNH-KVPGIYRVHPGPSKKKLQSLLE 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 734 ILR----VCKGMHLKCDTSKSLAKSLDECVD-PKEPYFNTLLRilttRCMLSAEYfcsgtfAPPDFRHYGLASPIYTHFT 808
Cdd:TIGR00358 434 FLAelglTLPGGNAENVTTLDGACWLREVKDrPEYEILVTRLL----RSLSQAEY------SPEPLGHFGLGLEHYAHFT 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 809 SPIRRYADVLAHRQLAAAIDYE-TINPSLSDKSRLIEICNGINYRHRMAQMAGRASIEYYVGQALKGGVAEE-DAYVIKV 886
Cdd:TIGR00358 504 SPIRRYPDLTNHRLIKAVLAKEqTDTERYQPQDELLQIAEHCSDTERRARDAERDVADWLKCRYLLDKVGTEfSGEISSV 583
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113445 887 FKNGFVVFIARFGLEGIVYTKSLssvlePNVEYVEDEYKLNIEIRDQPKpqtvQIQMFQQVRVRVTTVRDE 957
Cdd:TIGR00358 584 TRFGMFVRLDDNGIDGLIHISTL-----HNDYYVFDQEKMALIGKGTGK----VYRIGDRVTVKLTEVNME 645
|
|
| Rrp44_S1 |
pfam17215 |
S1 domain; This domain corresponds to the S1 domain found at the C-terminus of ribonucleases ... |
877-966 |
5.22e-35 |
|
S1 domain; This domain corresponds to the S1 domain found at the C-terminus of ribonucleases such as yeast Rrp44.
Pssm-ID: 435792 Cd Length: 87 Bit Score: 128.03 E-value: 5.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 877 AEEDAYVIKVFKNGFVVFIARFGLEGIVYTKSLSSVlEPNVEYVEDEYKLNIEIRDQPKPQTVqiQMFQQVRVRVTTVRD 956
Cdd:pfam17215 1 SEEEGYVIKVFNNGIVVFVPKFGIEGLIRLEDLTGD-EPEAEFDADEYSLTFPDKGSGKKRTV--GVFDKVRVRVKSVKD 77
|
90
....*....|
gi 19113445 957 EHSGKQKVQI 966
Cdd:pfam17215 78 ENTGKRKVKL 87
|
|
| PRK11642 |
PRK11642 |
ribonuclease R; |
494-829 |
4.30e-34 |
|
ribonuclease R;
Pssm-ID: 236944 [Multi-domain] Cd Length: 813 Bit Score: 141.03 E-value: 4.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 494 KNRKDFRDKLICSIDPPGCQDIDDALHACVLPNGNYEVGVHIADVTHFVKPNTSMDSEAASRGTTVYLVDKRIDMLPMLL 573
Cdd:PRK11642 258 AGRVDLRDLPLVTIDGEDARDFDDAVYCEKKRGGGWRLWVAIADVSYYVRPPTPLDREARNRGTSVYFPSQVVPMLPEVL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 574 GTDLCSLRPYVERFAFSCIWEMDENANIIKVHFTKSVIASKEAFSYADAQARID-DQKMQD---PLTQGMRVLLKLSKIL 649
Cdd:PRK11642 338 SNGLCSLNPQVDRLCMVCEMTISSKGRLTGYKFYEAVMSSHARLTYTKVWHILQgDQDLREqyaPLVKHLEELHNLYKVL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 650 KQKRMDEGALNLASPEVRIQTDNEtsdpMDVE-IKQLLETNS--LVEEFMLLANISVAqKIYDAFPQTAVLRRHAAPPLT 726
Cdd:PRK11642 418 DKAREERGGISFESEEAKFIFNAE----RRIErIEQTQRNDAhkLIEECMILANISAA-RFVEKAKEPALFRIHDKPSTE 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 727 NFDSLQDILRVCkGMHLKCDTS---KSLAKSLDECVD-PKEPYFNTLLriltTRCMLSAEYfcsgtfAPPDFRHYGLASP 802
Cdd:PRK11642 493 AITSFRSVLAEL-GLELPGGNKpepRDYAELLESVADrPDAEMLQTML----LRSMKQAIY------DPENRGHFGLALQ 561
|
330 340
....*....|....*....|....*..
gi 19113445 803 IYTHFTSPIRRYADVLAHRqlaaAIDY 829
Cdd:PRK11642 562 SYAHFTSPIRRYPDLSLHR----AIKY 584
|
|
| PRK05054 |
PRK05054 |
exoribonuclease II; Provisional |
507-856 |
1.19e-30 |
|
exoribonuclease II; Provisional
Pssm-ID: 179920 [Multi-domain] Cd Length: 644 Bit Score: 129.23 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 507 IDPPGCQDIDDALHACVLPNGNYEVGVHIADVTHFVKPNTSMDSEAASRGTTVYLVDKRIDMLPMLLGTDLCSLRPYVER 586
Cdd:PRK05054 201 IDSASTEDMDDALYVEKLPDGGLQLTVAIADPTAYIAEGSKLDKAARQRAFTNYLPGFNIPMLPRELSDDLCSLRPNERR 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 587 FAFSCIWEMDENANII-KVHFTKSVIASKEAFSY---ADAQARIDDQKMQDP-LTQGMRVLLKLSKILKQKRMDEGALNL 661
Cdd:PRK05054 281 PALACRVTIDADGTIEdDIRFFAAWIESKAKLAYdnvSDWLENGGDWQPESEaIAEQIRLLHQFCLARSEWRKQHALVFK 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 662 ASPEVRIQTdNETSDPMDVEIKQLLETNSLVEEFMLLANISVAQKIYDAFpQTAVLRRHAAPPLTNFDSLQDILrvckgm 741
Cdd:PRK05054 361 DRPDYRFEL-GEKGEVLDIVAEPRRIANRIVEESMIAANICAARVLRDKL-GFGIYNVHSGFDPANAEQAVALL------ 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 742 hlkcdtskslaKSLDECVDPKE----PYFNTLLRILTTrcmLSAEYFCS-----GTFAppDFR-----HYGLASPIYTHF 807
Cdd:PRK05054 433 -----------KEHGLHFDAEElltlEGFCKLRRELDA---QPTGYLDSrirrfQSFA--EIStepgpHFGLGLEAYATW 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 19113445 808 TSPIRRYADVLAHRQLAAAIDYET-INPSLSDKSRLIEicngINYRHRMA 856
Cdd:PRK05054 497 TSPIRKYGDMINHRLLKAVIKGETaERPQDEITVQLAE----RRRLNRMA 542
|
|
| Rnb |
COG4776 |
Exoribonuclease II [Transcription]; |
495-861 |
1.66e-30 |
|
Exoribonuclease II [Transcription];
Pssm-ID: 443808 [Multi-domain] Cd Length: 644 Bit Score: 128.43 E-value: 1.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 495 NRKDFRDKLICSIDPPGCQDIDDALHACVLPNGNYEVGVHIADVTHFVKPNTSMDSEAASRGTTVYLVDKRIDMLPMLLG 574
Cdd:COG4776 189 EREDLTALPFVTIDSESTEDMDDALYIEKLENGGWKLTVAIADPTAYIPEGSELDKEARQRAFTNYLPGFNIPMLPRELS 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 575 TDLCSLRPYVERFAFSCIWEMDENANII-KVHFTKSVIASKEAFSYAD----AQARIDDQKMQDPLTQGMRVLLKLSKIL 649
Cdd:COG4776 269 DDLCSLKENEKRPALVCRVTIDADGSIGdDIEFFAAWIRSKAKLAYDNvsdwLEGKGEWQPENEEIAEQIRLLHQFALAR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 650 KQKRMDEGALNLASPEVRIQTDnETSDPMDVEIKQLLETNSLVEEFMLLANISVAQKIYDAfPQTAVLRRHAAPPLTNFD 729
Cdd:COG4776 349 SQWRQQHALVFKDRPDYRFELD-EKGNVLDIHAEPRRIANRIVEEAMIAANICAARVLREH-LGFGIFNVHSGFDPEKLE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 730 SLQDIL-----RVCKGMHLKCDTSKSLAKSLDEcvdPKEPYFNTLLRilttRCMLSAEYfcSGTFAPpdfrHYGLASPIY 804
Cdd:COG4776 427 QAVELLaehgiEFDPEQLLTLEGFCALRRELDA---QPTSYLDSRLR----RFQTFAEI--STEPGP----HFGLGLDAY 493
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 19113445 805 THFTSPIRRYADVLAHRQLAAAIDYETIN-PSLSDKSRLIEicnginyRHRMAQMAGR 861
Cdd:COG4776 494 ATWTSPIRKYGDMVNHRLIKAVILGQPAEkPDEELTERLAE-------RRRLNRMAER 544
|
|
| OB_Dis3 |
pfam17849 |
Dis3-like cold-shock domain 2 (CSD2); This domain has an OB fold and is found in the Dis3l2 ... |
394-461 |
2.06e-23 |
|
Dis3-like cold-shock domain 2 (CSD2); This domain has an OB fold and is found in the Dis3l2 protein. This domain along with CSD1 binds to RNA.
Pssm-ID: 436091 [Multi-domain] Cd Length: 77 Bit Score: 94.60 E-value: 2.06e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113445 394 VLLTPMDRRVPKIRFRTRQAP--------RLVGRRIVVAIDLWDASSRYPEGHFVRDLGEMETKEAETEALLLEYD 461
Cdd:pfam17849 2 VLFVPRDKRIPRIRIPTKSAPeeflenpeDLEGKLFVVKIDDWPENSRYPLGHIVKVLGEIGDIETETEAILLENG 77
|
|
| Rrp44_CSD1 |
pfam17216 |
Rrp44-like cold shock domain; |
251-370 |
1.03e-21 |
|
Rrp44-like cold shock domain;
Pssm-ID: 375054 Cd Length: 148 Bit Score: 92.53 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 251 HWSMSRLLACIKNGEVHKGLINISTYNYLEGSVVVPGYNKPVLVSGRENLNRAVQGDIVCIQILPQDQWKTEAEEIAD-- 328
Cdd:pfam17216 7 YYSTARVMGGLKNGVLYQGNIQISEYNFLEGSVSLPRFSKPVLIVGQKNLNRAFNGDQVIVELLPQSEWKAPSSIVLDse 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113445 329 -------------DDEDvvvSTAAEPDSARINDLE--------LITKRNA--HPTAKVVGILKRN 370
Cdd:pfam17216 87 hfdvndnpdieagDDDD---NNESSSNTTVISDKQrrllakdaMIAQRSKkiQPTAKVVYIQRRS 148
|
|
| PINc |
smart00670 |
Large family of predicted nucleotide-binding domains; From similarities to 5'-exonucleases, ... |
83-198 |
1.80e-17 |
|
Large family of predicted nucleotide-binding domains; From similarities to 5'-exonucleases, these domains are predicted to be RNases. PINc domains in nematode SMG-5 and yeast NMD4p are predicted to be involved in RNAi.
Pssm-ID: 214771 [Multi-domain] Cd Length: 111 Bit Score: 79.00 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 83 HYLIPDSNIFYHCI--DALEHPNNF-FDVIILQTVFSEISSKSIPLYNRMKRLCQEKTKRFTPFSNEFFVDTFVERLDDE 159
Cdd:smart00670 1 MKVVLDTNVLIDGLirDALEKLLEKkGEVYIPQTVLEELEYLALRSLKKLEELALEGKIILKVLKEERIEEEILERLSLK 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 19113445 160 SANDRNDRAIRNAASWFAshlaslgiKIVLLTDDRENAR 198
Cdd:smart00670 81 LELLPNDALILATAKELG--------NVVLVTNDRDLRR 111
|
|
| PIN_4 |
pfam13638 |
PIN domain; Members of this family of bacterial domains are predicted to be RNases (from ... |
85-211 |
1.03e-15 |
|
PIN domain; Members of this family of bacterial domains are predicted to be RNases (from similarities to 5'-exonucleases).
Pssm-ID: 433369 Cd Length: 131 Bit Score: 74.58 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113445 85 LIPDSNIFYHCIDALEHPNNFFDVIILQTVFSEISSKSIPLYNRmKRLCQEKTKRFTPFSNEFFVDT----FVERLDDE- 159
Cdd:pfam13638 1 YVLDTNVLLHDPDALFNFGEENDVVIPITVLEELDGLKKGSDES-GRELARLARQANRWLDELLENNggrlRGQTLDERl 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 19113445 160 --SANDRNDRAIRNAASWFASHLAslGIKIVLLTDDRENARLAAEQGIQVSTLK 211
Cdd:pfam13638 80 ppDPFDKNDNRILAVALYLKEELP--DRPVILVSKDINLRIKADALGIPAEDYE 131
|
|
| |
