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Conserved domains on  [gi|2049961942|gb|QWK51329|]
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RNA polymerase [Tenuivirus zeae]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Bunya_RdRp super family cl20265
Bunyavirus RNA dependent RNA polymerase; The bunyaviruses are enveloped viruses with a genome ...
1066-1802 0e+00

Bunyavirus RNA dependent RNA polymerase; The bunyaviruses are enveloped viruses with a genome consisting of 3 ssRNA segments (called L, M and S). The nucleocapsid protein is encode on the small (S) genomic RNA. The L segment codes for an RNA polymerase. This family contains the RNA dependent RNA polymerase on the L segment.


The actual alignment was detected with superfamily member pfam04196:

Pssm-ID: 282102  Cd Length: 739  Bit Score: 710.40  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1066 VNWVRCEAMMLAQRGFWRELFSVAPHIEEQEGMnePDTVCQMMS-WTLLILLNDKHQLEEMITMSRFVHMEGFVTYPAWP 1144
Cdd:pfam04196    1 LNKVRCLRLVKAPELFWKATYEVMYAVNPIFYC--TLTVKQILNfSSLLALLVTKPSLLEIFDPSRYVIMLGLSIYSNIP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1145 RPY-KMFEKLSITPRSRLECLVIKRLIMLMKHYSENPIK--FMIENEKKKWFGFKNMFLLdCNGALMDLSDQDQMLNLFY 1221
Cdd:pfam04196   79 SYIaKKFEPLSKTLRSVYMVRLIKRLLFTLFDQNGEPFKrsIYLGDLNDDQKGITNERLL-DSITFPILSTLKELINNVY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1222 LG-YLKNKDEEVEDNGMGQVVTKILGFETAMPKNR-DFLGMkdPEYGQIKKHEFSVSYVKDLCDNFL--NRLKRTHGIKD 1297
Cdd:pfam04196  158 LGfYLKNKGLHENHNVMIDLLKKILEWELKFREVRsKKLGK--PVNGAILVHLVSISYLADLCRHNLlrNRLENRHNFKA 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1298 PVTFLGDKIAKFLSTQfIETLASLKAS-SNFSSEYYLYTPNKrLKNQEQSHspnLVDAAGNTIPRVKGkLYHRSKVIEKL 1376
Cdd:pfam04196  236 PITTISTLTSSKLCLQ-IGTFAVIKALqSNFSKNWLEKTSRK-LRNINPTF---VEDKGTNLEVGEDN-YEHLSKAIEYI 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1377 TKIIKEEDPSKELKIVTDLLPRAMEALNKNQ---CLHICIFKKNQHGGLREIYVLNIYERIMQKTVEDFARAILECCPSE 1453
Cdd:pfam04196  310 ETKVKDKLYEKNKSVVLKLKPEIEEPMDMMKkefCMHQCLNKGQQTEGDREIFVLNLEERMCQYAVERISRAILKLNPSE 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1454 TMTSPKNK--FKIPEMHNSEAKKTLKNEYLTIATSDDA-SKWNQGHYVSKFLCMLLRLTPKIYHGFLVQSLQLWHHKKIF 1530
Cdd:pfam04196  390 MISEPKDKkiLAISEKHEMEARWTVEDTFKTLSTSDDAiSKKNQLMHVSADMSKWSASDLTYKYFFLIALLPILYPKEKF 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1531 LGDQLLQLFNQNSTLNTMDNTLLTVFKAYKGEITVP-WMKTGQS--FIETETGMMQGILHYTSSLFHALFLDQLAEECTk 1607
Cdd:pfam04196  470 LGLYLLCNYMSKTDLLPSDILLNLVDQKYYGRYDIIfWMTNGLNknFVEVKRNWLQGNLNYTSSLVHSCAMEVYKEFLK- 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1608 dinRCIKSIKKDeklkCIVNNMESSDDSSFIISIPNFKDNEAAQLYLLCVVNSWFKKKEKLGVYLGIYKSPKSTTQTLFV 1687
Cdd:pfam04196  549 ---RAIKLLDGS----CLVNSIVHSDDSQTSISIPCHVDDKQADFKSVLVANSAFRSKELIFKYLCIYASPKKTYVTLTV 621
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1688 MEFNSEFFFSGDVHRPTFRWVNAAILIGEQETLSGIQEELSNTLKDVIEGGGTYALTFFVQVAQAMIHYRLLGSSvSSVW 1767
Cdd:pfam04196  622 KEFNSEFFFSGEVSSSLLRWLLASVSDCAAEGLSDDLASLSSSLTNLLKLGCSPSLAWLAQAAVHSITYRLYGML-PGQS 700
                          730       740       750
                   ....*....|....*....|....*....|....*....
gi 2049961942 1768 PAFETLLKNSYD---PALGYFLMDNPKCAG-LLGFNYNV 1802
Cdd:pfam04196  701 NDPIFYLNRPNDkeiPILLGGLLDAPITALsLLGFKSND 739
DUF3770 super family cl13978
Protein of unknown function (DUF3770); This domain family is found in viruses, and is ...
648-889 1.05e-56

Protein of unknown function (DUF3770); This domain family is found in viruses, and is approximately 250 amino acids in length. The family is found in association with pfam04196.


The actual alignment was detected with superfamily member pfam12603:

Pssm-ID: 289377  Cd Length: 235  Bit Score: 197.53  E-value: 1.05e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942  648 QELILRLRVANQMKIQLadndinldSEMLLAPDV---------YRIKEMFRESFPN----DKFLAPITKEMYDHFVNpmI 714
Cdd:pfam12603    1 RELIIRLRVANQVKIEL--------SATLLAPEIddededkrsREIKAMFRSSQPNwnvtEKFFHPFSREMFEHFVN--I 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942  715 RGEQEYVENLkqtIDREVRDEQRKnleeltiKDGKKYSERKAEEALLETNSAEDQ------YKSYFDNDNFRKT--MKAP 786
Cdd:pfam12603   71 SPDKEYVANI---IDKELRDEQRK-------LDGKKYTEEKAETALREMSNAEESlnmvkhYRSYFENDNFRSTwsHKST 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942  787 VQLPLIIPEVSGHSLQFSTSDlsdKLNLANiKHPIHNIWMQAVSKHNSSptlghldelEISMLDGQVAKKVE-----ESY 861
Cdd:pfam12603  141 VQLPLIIPDVSSDDNQLSRLR---KLPVGG-DHPIYNIWRQAVNSRNCS---------EIERLEGDVAKEVEaalcsESY 207
                          250       260
                   ....*....|....*....|....*...
gi 2049961942  862 KKDRSSYNRTTLLTTVQEDIYLAERGIN 889
Cdd:pfam12603  208 KKDRSQYHRTTLLTGMKEDIYLAERGVN 235
OTU super family cl45892
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
39-151 2.34e-09

OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation.


The actual alignment was detected with superfamily member cd22792:

Pssm-ID: 459237 [Multi-domain]  Cd Length: 108  Bit Score: 57.23  E-value: 2.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942   39 TDVKGDGYCLFHSIlvsfGLVLNQLPTSLfMKKLRANPAinnLDPKDQVDLMRQLdwnEPNFWGEDVTIGFISAILRVKI 118
Cdd:cd22792      3 VPVPGDGNCFWHSL----GHFLGLSALEL-KKLLRDSLF---DDPELDEELDEQL---EPGVYAEDEAIAAAAKLFGVNI 71
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2049961942  119 EVYSILNDKWHKTTfGGDFDLTIKLKNKGNlHF 151
Cdd:cd22792     72 CVHDPDEGVLYTFT-PNESSKSIHLLLENE-HF 102
L_protein_N super family cl20011
L protein N-terminus; This endonuclease domain is found at the N-terminus of many bunyavirus L ...
512-599 3.03e-07

L protein N-terminus; This endonuclease domain is found at the N-terminus of many bunyavirus L proteins.


The actual alignment was detected with superfamily member pfam15518:

Pssm-ID: 373916  Cd Length: 93  Bit Score: 50.76  E-value: 3.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942  512 HSSSSIPEDYIYRKKLSEAKNIIHDFVFDILSHETDKSMKE---AELSLGTVSDNWTPDVIITREkddqyGDIVVFEFTT 588
Cdd:pfam15518    6 SRIGSARDPEIAKDIDSDLLNFRHDFTFRHLCDSTDIEFRNdfpAIDILLDGIDNLTPDNIITLN-----GTLYIIEFTT 80
                           90
                   ....*....|..
gi 2049961942  589 -RSTESKESLLR 599
Cdd:pfam15518   81 sVGNESGAITAA 92
MUN super family cl05671
MUN domain; This entry corresponds to the MUN domain found in Munc13 proteins. These ...
2326-2391 9.74e-04

MUN domain; This entry corresponds to the MUN domain found in Munc13 proteins. These constitute a family of three highly homologous molecules (Munc13-1, Munc13-2 and Munc13-3) with homology to Caenorhabditis elegans unc-13p. Munc13 proteins contain a phorbol ester-binding C1 domain and two C2 domains, which are Ca2+/phospholipid binding domains. Sequence analyses have uncovered two regions called Munc13 homology domains 1 (MHD1) and 2 (MHD2) that are arranged between two flanking C2 domains. MHD1 and MHD2 domains are present in a wide variety of proteins from Arabidopsis thaliana, C. elegans, Drosophila melanogaster, mouse, rat and human, some of which may function in a Munc13-like manner to regulate membrane trafficking. Structural studies have defined MHD1 and MHD2 to be part of the larger MUN domain which forms an elongated structure composed of any pairs of alpha helices.


The actual alignment was detected with superfamily member pfam06292:

Pssm-ID: 461870  Cd Length: 473  Bit Score: 44.70  E-value: 9.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 2326 NRLSILQEIISDdptLHWPDQETSlKQLEEKFREMAH---REYPKLTQEEFEK-------------NI-------EKVKE 2382
Cdd:pfam06292  202 WKLNQLQDFIKK---LEWPDPEFA-AHLEKRFKLMASdmlLAYAKRTRKAFDSklkkprtactmmnNIqqarvqlEKMFL 277

                   ....*....
gi 2049961942 2383 LMHEDSLRG 2391
Cdd:pfam06292  278 CMGGDELDG 286
 
Name Accession Description Interval E-value
Bunya_RdRp pfam04196
Bunyavirus RNA dependent RNA polymerase; The bunyaviruses are enveloped viruses with a genome ...
1066-1802 0e+00

Bunyavirus RNA dependent RNA polymerase; The bunyaviruses are enveloped viruses with a genome consisting of 3 ssRNA segments (called L, M and S). The nucleocapsid protein is encode on the small (S) genomic RNA. The L segment codes for an RNA polymerase. This family contains the RNA dependent RNA polymerase on the L segment.


Pssm-ID: 282102  Cd Length: 739  Bit Score: 710.40  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1066 VNWVRCEAMMLAQRGFWRELFSVAPHIEEQEGMnePDTVCQMMS-WTLLILLNDKHQLEEMITMSRFVHMEGFVTYPAWP 1144
Cdd:pfam04196    1 LNKVRCLRLVKAPELFWKATYEVMYAVNPIFYC--TLTVKQILNfSSLLALLVTKPSLLEIFDPSRYVIMLGLSIYSNIP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1145 RPY-KMFEKLSITPRSRLECLVIKRLIMLMKHYSENPIK--FMIENEKKKWFGFKNMFLLdCNGALMDLSDQDQMLNLFY 1221
Cdd:pfam04196   79 SYIaKKFEPLSKTLRSVYMVRLIKRLLFTLFDQNGEPFKrsIYLGDLNDDQKGITNERLL-DSITFPILSTLKELINNVY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1222 LG-YLKNKDEEVEDNGMGQVVTKILGFETAMPKNR-DFLGMkdPEYGQIKKHEFSVSYVKDLCDNFL--NRLKRTHGIKD 1297
Cdd:pfam04196  158 LGfYLKNKGLHENHNVMIDLLKKILEWELKFREVRsKKLGK--PVNGAILVHLVSISYLADLCRHNLlrNRLENRHNFKA 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1298 PVTFLGDKIAKFLSTQfIETLASLKAS-SNFSSEYYLYTPNKrLKNQEQSHspnLVDAAGNTIPRVKGkLYHRSKVIEKL 1376
Cdd:pfam04196  236 PITTISTLTSSKLCLQ-IGTFAVIKALqSNFSKNWLEKTSRK-LRNINPTF---VEDKGTNLEVGEDN-YEHLSKAIEYI 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1377 TKIIKEEDPSKELKIVTDLLPRAMEALNKNQ---CLHICIFKKNQHGGLREIYVLNIYERIMQKTVEDFARAILECCPSE 1453
Cdd:pfam04196  310 ETKVKDKLYEKNKSVVLKLKPEIEEPMDMMKkefCMHQCLNKGQQTEGDREIFVLNLEERMCQYAVERISRAILKLNPSE 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1454 TMTSPKNK--FKIPEMHNSEAKKTLKNEYLTIATSDDA-SKWNQGHYVSKFLCMLLRLTPKIYHGFLVQSLQLWHHKKIF 1530
Cdd:pfam04196  390 MISEPKDKkiLAISEKHEMEARWTVEDTFKTLSTSDDAiSKKNQLMHVSADMSKWSASDLTYKYFFLIALLPILYPKEKF 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1531 LGDQLLQLFNQNSTLNTMDNTLLTVFKAYKGEITVP-WMKTGQS--FIETETGMMQGILHYTSSLFHALFLDQLAEECTk 1607
Cdd:pfam04196  470 LGLYLLCNYMSKTDLLPSDILLNLVDQKYYGRYDIIfWMTNGLNknFVEVKRNWLQGNLNYTSSLVHSCAMEVYKEFLK- 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1608 dinRCIKSIKKDeklkCIVNNMESSDDSSFIISIPNFKDNEAAQLYLLCVVNSWFKKKEKLGVYLGIYKSPKSTTQTLFV 1687
Cdd:pfam04196  549 ---RAIKLLDGS----CLVNSIVHSDDSQTSISIPCHVDDKQADFKSVLVANSAFRSKELIFKYLCIYASPKKTYVTLTV 621
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1688 MEFNSEFFFSGDVHRPTFRWVNAAILIGEQETLSGIQEELSNTLKDVIEGGGTYALTFFVQVAQAMIHYRLLGSSvSSVW 1767
Cdd:pfam04196  622 KEFNSEFFFSGEVSSSLLRWLLASVSDCAAEGLSDDLASLSSSLTNLLKLGCSPSLAWLAQAAVHSITYRLYGML-PGQS 700
                          730       740       750
                   ....*....|....*....|....*....|....*....
gi 2049961942 1768 PAFETLLKNSYD---PALGYFLMDNPKCAG-LLGFNYNV 1802
Cdd:pfam04196  701 NDPIFYLNRPNDkeiPILLGGLLDAPITALsLLGFKSND 739
DUF3770 pfam12603
Protein of unknown function (DUF3770); This domain family is found in viruses, and is ...
648-889 1.05e-56

Protein of unknown function (DUF3770); This domain family is found in viruses, and is approximately 250 amino acids in length. The family is found in association with pfam04196.


Pssm-ID: 289377  Cd Length: 235  Bit Score: 197.53  E-value: 1.05e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942  648 QELILRLRVANQMKIQLadndinldSEMLLAPDV---------YRIKEMFRESFPN----DKFLAPITKEMYDHFVNpmI 714
Cdd:pfam12603    1 RELIIRLRVANQVKIEL--------SATLLAPEIddededkrsREIKAMFRSSQPNwnvtEKFFHPFSREMFEHFVN--I 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942  715 RGEQEYVENLkqtIDREVRDEQRKnleeltiKDGKKYSERKAEEALLETNSAEDQ------YKSYFDNDNFRKT--MKAP 786
Cdd:pfam12603   71 SPDKEYVANI---IDKELRDEQRK-------LDGKKYTEEKAETALREMSNAEESlnmvkhYRSYFENDNFRSTwsHKST 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942  787 VQLPLIIPEVSGHSLQFSTSDlsdKLNLANiKHPIHNIWMQAVSKHNSSptlghldelEISMLDGQVAKKVE-----ESY 861
Cdd:pfam12603  141 VQLPLIIPDVSSDDNQLSRLR---KLPVGG-DHPIYNIWRQAVNSRNCS---------EIERLEGDVAKEVEaalcsESY 207
                          250       260
                   ....*....|....*....|....*...
gi 2049961942  862 KKDRSSYNRTTLLTTVQEDIYLAERGIN 889
Cdd:pfam12603  208 KKDRSQYHRTTLLTGMKEDIYLAERGVN 235
OTU_RDRP-like cd22792
OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; ...
39-151 2.34e-09

OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; RNA replication polyprotein (RDRP) is a viral homolog of ovarian tumor protease (vOTU), which displays RNA helicase (EC 3.6.4.13), RNA-directed RNA polymerase (EC 2.7.7.48), viral methyltransferase, Fe(2+) 2-oxoglutarate dioxygenase and protease activities. The central part of this protein possibly functions as an ATP-binding helicase. It is an RNA-directed RNA polymerase involved in viral RNA replication. It also acts as a thiol protease that cleaves the polyprotein. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438613 [Multi-domain]  Cd Length: 108  Bit Score: 57.23  E-value: 2.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942   39 TDVKGDGYCLFHSIlvsfGLVLNQLPTSLfMKKLRANPAinnLDPKDQVDLMRQLdwnEPNFWGEDVTIGFISAILRVKI 118
Cdd:cd22792      3 VPVPGDGNCFWHSL----GHFLGLSALEL-KKLLRDSLF---DDPELDEELDEQL---EPGVYAEDEAIAAAAKLFGVNI 71
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2049961942  119 EVYSILNDKWHKTTfGGDFDLTIKLKNKGNlHF 151
Cdd:cd22792     72 CVHDPDEGVLYTFT-PNESSKSIHLLLENE-HF 102
L_protein_N pfam15518
L protein N-terminus; This endonuclease domain is found at the N-terminus of many bunyavirus L ...
512-599 3.03e-07

L protein N-terminus; This endonuclease domain is found at the N-terminus of many bunyavirus L proteins.


Pssm-ID: 373916  Cd Length: 93  Bit Score: 50.76  E-value: 3.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942  512 HSSSSIPEDYIYRKKLSEAKNIIHDFVFDILSHETDKSMKE---AELSLGTVSDNWTPDVIITREkddqyGDIVVFEFTT 588
Cdd:pfam15518    6 SRIGSARDPEIAKDIDSDLLNFRHDFTFRHLCDSTDIEFRNdfpAIDILLDGIDNLTPDNIITLN-----GTLYIIEFTT 80
                           90
                   ....*....|..
gi 2049961942  589 -RSTESKESLLR 599
Cdd:pfam15518   81 sVGNESGAITAA 92
MUN pfam06292
MUN domain; This entry corresponds to the MUN domain found in Munc13 proteins. These ...
2326-2391 9.74e-04

MUN domain; This entry corresponds to the MUN domain found in Munc13 proteins. These constitute a family of three highly homologous molecules (Munc13-1, Munc13-2 and Munc13-3) with homology to Caenorhabditis elegans unc-13p. Munc13 proteins contain a phorbol ester-binding C1 domain and two C2 domains, which are Ca2+/phospholipid binding domains. Sequence analyses have uncovered two regions called Munc13 homology domains 1 (MHD1) and 2 (MHD2) that are arranged between two flanking C2 domains. MHD1 and MHD2 domains are present in a wide variety of proteins from Arabidopsis thaliana, C. elegans, Drosophila melanogaster, mouse, rat and human, some of which may function in a Munc13-like manner to regulate membrane trafficking. Structural studies have defined MHD1 and MHD2 to be part of the larger MUN domain which forms an elongated structure composed of any pairs of alpha helices.


Pssm-ID: 461870  Cd Length: 473  Bit Score: 44.70  E-value: 9.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 2326 NRLSILQEIISDdptLHWPDQETSlKQLEEKFREMAH---REYPKLTQEEFEK-------------NI-------EKVKE 2382
Cdd:pfam06292  202 WKLNQLQDFIKK---LEWPDPEFA-AHLEKRFKLMASdmlLAYAKRTRKAFDSklkkprtactmmnNIqqarvqlEKMFL 277

                   ....*....
gi 2049961942 2383 LMHEDSLRG 2391
Cdd:pfam06292  278 CMGGDELDG 286
 
Name Accession Description Interval E-value
Bunya_RdRp pfam04196
Bunyavirus RNA dependent RNA polymerase; The bunyaviruses are enveloped viruses with a genome ...
1066-1802 0e+00

Bunyavirus RNA dependent RNA polymerase; The bunyaviruses are enveloped viruses with a genome consisting of 3 ssRNA segments (called L, M and S). The nucleocapsid protein is encode on the small (S) genomic RNA. The L segment codes for an RNA polymerase. This family contains the RNA dependent RNA polymerase on the L segment.


Pssm-ID: 282102  Cd Length: 739  Bit Score: 710.40  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1066 VNWVRCEAMMLAQRGFWRELFSVAPHIEEQEGMnePDTVCQMMS-WTLLILLNDKHQLEEMITMSRFVHMEGFVTYPAWP 1144
Cdd:pfam04196    1 LNKVRCLRLVKAPELFWKATYEVMYAVNPIFYC--TLTVKQILNfSSLLALLVTKPSLLEIFDPSRYVIMLGLSIYSNIP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1145 RPY-KMFEKLSITPRSRLECLVIKRLIMLMKHYSENPIK--FMIENEKKKWFGFKNMFLLdCNGALMDLSDQDQMLNLFY 1221
Cdd:pfam04196   79 SYIaKKFEPLSKTLRSVYMVRLIKRLLFTLFDQNGEPFKrsIYLGDLNDDQKGITNERLL-DSITFPILSTLKELINNVY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1222 LG-YLKNKDEEVEDNGMGQVVTKILGFETAMPKNR-DFLGMkdPEYGQIKKHEFSVSYVKDLCDNFL--NRLKRTHGIKD 1297
Cdd:pfam04196  158 LGfYLKNKGLHENHNVMIDLLKKILEWELKFREVRsKKLGK--PVNGAILVHLVSISYLADLCRHNLlrNRLENRHNFKA 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1298 PVTFLGDKIAKFLSTQfIETLASLKAS-SNFSSEYYLYTPNKrLKNQEQSHspnLVDAAGNTIPRVKGkLYHRSKVIEKL 1376
Cdd:pfam04196  236 PITTISTLTSSKLCLQ-IGTFAVIKALqSNFSKNWLEKTSRK-LRNINPTF---VEDKGTNLEVGEDN-YEHLSKAIEYI 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1377 TKIIKEEDPSKELKIVTDLLPRAMEALNKNQ---CLHICIFKKNQHGGLREIYVLNIYERIMQKTVEDFARAILECCPSE 1453
Cdd:pfam04196  310 ETKVKDKLYEKNKSVVLKLKPEIEEPMDMMKkefCMHQCLNKGQQTEGDREIFVLNLEERMCQYAVERISRAILKLNPSE 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1454 TMTSPKNK--FKIPEMHNSEAKKTLKNEYLTIATSDDA-SKWNQGHYVSKFLCMLLRLTPKIYHGFLVQSLQLWHHKKIF 1530
Cdd:pfam04196  390 MISEPKDKkiLAISEKHEMEARWTVEDTFKTLSTSDDAiSKKNQLMHVSADMSKWSASDLTYKYFFLIALLPILYPKEKF 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1531 LGDQLLQLFNQNSTLNTMDNTLLTVFKAYKGEITVP-WMKTGQS--FIETETGMMQGILHYTSSLFHALFLDQLAEECTk 1607
Cdd:pfam04196  470 LGLYLLCNYMSKTDLLPSDILLNLVDQKYYGRYDIIfWMTNGLNknFVEVKRNWLQGNLNYTSSLVHSCAMEVYKEFLK- 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1608 dinRCIKSIKKDeklkCIVNNMESSDDSSFIISIPNFKDNEAAQLYLLCVVNSWFKKKEKLGVYLGIYKSPKSTTQTLFV 1687
Cdd:pfam04196  549 ---RAIKLLDGS----CLVNSIVHSDDSQTSISIPCHVDDKQADFKSVLVANSAFRSKELIFKYLCIYASPKKTYVTLTV 621
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 1688 MEFNSEFFFSGDVHRPTFRWVNAAILIGEQETLSGIQEELSNTLKDVIEGGGTYALTFFVQVAQAMIHYRLLGSSvSSVW 1767
Cdd:pfam04196  622 KEFNSEFFFSGEVSSSLLRWLLASVSDCAAEGLSDDLASLSSSLTNLLKLGCSPSLAWLAQAAVHSITYRLYGML-PGQS 700
                          730       740       750
                   ....*....|....*....|....*....|....*....
gi 2049961942 1768 PAFETLLKNSYD---PALGYFLMDNPKCAG-LLGFNYNV 1802
Cdd:pfam04196  701 NDPIFYLNRPNDkeiPILLGGLLDAPITALsLLGFKSND 739
DUF3770 pfam12603
Protein of unknown function (DUF3770); This domain family is found in viruses, and is ...
648-889 1.05e-56

Protein of unknown function (DUF3770); This domain family is found in viruses, and is approximately 250 amino acids in length. The family is found in association with pfam04196.


Pssm-ID: 289377  Cd Length: 235  Bit Score: 197.53  E-value: 1.05e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942  648 QELILRLRVANQMKIQLadndinldSEMLLAPDV---------YRIKEMFRESFPN----DKFLAPITKEMYDHFVNpmI 714
Cdd:pfam12603    1 RELIIRLRVANQVKIEL--------SATLLAPEIddededkrsREIKAMFRSSQPNwnvtEKFFHPFSREMFEHFVN--I 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942  715 RGEQEYVENLkqtIDREVRDEQRKnleeltiKDGKKYSERKAEEALLETNSAEDQ------YKSYFDNDNFRKT--MKAP 786
Cdd:pfam12603   71 SPDKEYVANI---IDKELRDEQRK-------LDGKKYTEEKAETALREMSNAEESlnmvkhYRSYFENDNFRSTwsHKST 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942  787 VQLPLIIPEVSGHSLQFSTSDlsdKLNLANiKHPIHNIWMQAVSKHNSSptlghldelEISMLDGQVAKKVE-----ESY 861
Cdd:pfam12603  141 VQLPLIIPDVSSDDNQLSRLR---KLPVGG-DHPIYNIWRQAVNSRNCS---------EIERLEGDVAKEVEaalcsESY 207
                          250       260
                   ....*....|....*....|....*...
gi 2049961942  862 KKDRSSYNRTTLLTTVQEDIYLAERGIN 889
Cdd:pfam12603  208 KKDRSQYHRTTLLTGMKEDIYLAERGVN 235
OTU_RDRP-like cd22792
OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; ...
39-151 2.34e-09

OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; RNA replication polyprotein (RDRP) is a viral homolog of ovarian tumor protease (vOTU), which displays RNA helicase (EC 3.6.4.13), RNA-directed RNA polymerase (EC 2.7.7.48), viral methyltransferase, Fe(2+) 2-oxoglutarate dioxygenase and protease activities. The central part of this protein possibly functions as an ATP-binding helicase. It is an RNA-directed RNA polymerase involved in viral RNA replication. It also acts as a thiol protease that cleaves the polyprotein. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438613 [Multi-domain]  Cd Length: 108  Bit Score: 57.23  E-value: 2.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942   39 TDVKGDGYCLFHSIlvsfGLVLNQLPTSLfMKKLRANPAinnLDPKDQVDLMRQLdwnEPNFWGEDVTIGFISAILRVKI 118
Cdd:cd22792      3 VPVPGDGNCFWHSL----GHFLGLSALEL-KKLLRDSLF---DDPELDEELDEQL---EPGVYAEDEAIAAAAKLFGVNI 71
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2049961942  119 EVYSILNDKWHKTTfGGDFDLTIKLKNKGNlHF 151
Cdd:cd22792     72 CVHDPDEGVLYTFT-PNESSKSIHLLLENE-HF 102
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
40-154 5.45e-08

OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation.


Pssm-ID: 438581 [Multi-domain]  Cd Length: 128  Bit Score: 53.98  E-value: 5.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942   40 DVKGDGYCLFHSIlvSFGLVLNQLPTS----LFMKKLRANPAInnLDPKDQVDLMRQLDWNE-------PNFWGEDVTIG 108
Cdd:cd22744      4 DVPGDGNCLFRAL--AHALYGDQESHRelrqEVVDYLRENPDL--YEPAELADEDDGEDFDEylqrmrkPGTWGGELELQ 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2049961942  109 FISAILRVKIEVYSILNDKWHKTTFGGDFDL---TIKLKNKGNLHFVSL 154
Cdd:cd22744     80 ALANALNVPIVVYSEDGGFLPVSVFGPGPGPsgrPIHLLYTGGNHYDAL 128
L_protein_N pfam15518
L protein N-terminus; This endonuclease domain is found at the N-terminus of many bunyavirus L ...
512-599 3.03e-07

L protein N-terminus; This endonuclease domain is found at the N-terminus of many bunyavirus L proteins.


Pssm-ID: 373916  Cd Length: 93  Bit Score: 50.76  E-value: 3.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942  512 HSSSSIPEDYIYRKKLSEAKNIIHDFVFDILSHETDKSMKE---AELSLGTVSDNWTPDVIITREkddqyGDIVVFEFTT 588
Cdd:pfam15518    6 SRIGSARDPEIAKDIDSDLLNFRHDFTFRHLCDSTDIEFRNdfpAIDILLDGIDNLTPDNIITLN-----GTLYIIEFTT 80
                           90
                   ....*....|..
gi 2049961942  589 -RSTESKESLLR 599
Cdd:pfam15518   81 sVGNESGAITAA 92
OTU_232R-like cd22758
OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase ...
40-154 6.36e-06

OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase 232R and similar proteins; This subfamily contains putative ubiquitin thioesterases 232R from Invertebrate iridescent virus and L96 from Tipula iridescent virus (TIV), Dictyostelium discoideum OTU domain-containing protein DDB_G0284757, and similar proteins. L96 may be involved in TIV genomic DNA packaging in a manner related to the Gag polyproteins of the mammalian viruses. Proteins in this subfamily contain an OTU domain. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438595 [Multi-domain]  Cd Length: 135  Bit Score: 48.03  E-value: 6.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942   40 DVKGDGYCLFHSILVSF-GLVLNQLPTSL---FMKKLRANPaiNNLDPKDQVDLMRQLDWNE-------PNFWGEDVTIG 108
Cdd:cd22758     10 DVPGDGNCFFHAVSDQLyGNGIEHSHKELrqqAVNYLRENP--ELYDGFFLSEFDEEESWEEylnrmskDGTWGDHIILQ 87
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2049961942  109 FISAILRVKIEVYSILNDKWHkTTF---GGDFDLTIKLKNKGNLHFVSL 154
Cdd:cd22758     88 AAANLFNVRIVIISSDGSDET-TIIepgNSKNGRTIYLGHIGENHYVSL 135
MUN pfam06292
MUN domain; This entry corresponds to the MUN domain found in Munc13 proteins. These ...
2326-2391 9.74e-04

MUN domain; This entry corresponds to the MUN domain found in Munc13 proteins. These constitute a family of three highly homologous molecules (Munc13-1, Munc13-2 and Munc13-3) with homology to Caenorhabditis elegans unc-13p. Munc13 proteins contain a phorbol ester-binding C1 domain and two C2 domains, which are Ca2+/phospholipid binding domains. Sequence analyses have uncovered two regions called Munc13 homology domains 1 (MHD1) and 2 (MHD2) that are arranged between two flanking C2 domains. MHD1 and MHD2 domains are present in a wide variety of proteins from Arabidopsis thaliana, C. elegans, Drosophila melanogaster, mouse, rat and human, some of which may function in a Munc13-like manner to regulate membrane trafficking. Structural studies have defined MHD1 and MHD2 to be part of the larger MUN domain which forms an elongated structure composed of any pairs of alpha helices.


Pssm-ID: 461870  Cd Length: 473  Bit Score: 44.70  E-value: 9.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049961942 2326 NRLSILQEIISDdptLHWPDQETSlKQLEEKFREMAH---REYPKLTQEEFEK-------------NI-------EKVKE 2382
Cdd:pfam06292  202 WKLNQLQDFIKK---LEWPDPEFA-AHLEKRFKLMASdmlLAYAKRTRKAFDSklkkprtactmmnNIqqarvqlEKMFL 277

                   ....*....
gi 2049961942 2383 LMHEDSLRG 2391
Cdd:pfam06292  278 CMGGDELDG 286
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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