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Conserved domains on  [gi|340629670|gb|AEK64757|]
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polyprotein, partial [Pennisetum mosaic virus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ps-ssRNAv_Potyviridae_RdRp cd23175
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Potyviridae of ...
1-204 3.37e-159

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Potyviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Potyviridae, order: Patatavirales. Potyviridae, is the largest family of RNA plant viruses, members of which have (+)ssRNA genomes and flexuous filamentous particles. The family is divided into eight genera: Brambyvirus, Bymovirus, Ipomovirus, Macluravirus, Poacevirus, Potyvirus, Rymovirus, and Tritimovirus. Most genomes are monopartite but those of members of the genus Bymovirus are bipartite. Some members cause serious disease epidemics in cultivated plants. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


:

Pssm-ID: 438025  Cd Length: 236  Bit Score: 455.76  E-value: 3.37e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670   1 PLETLLGGKVCVDDFNNQFYAHHLIGPWTVGITKFYGGWNQLLEKLPNGWVYCDADGSQFDSSLTPYLINAVLDIRLSFM 80
Cdd:cd23175   32 PIDTLLGGKVCVDDFNNQFYSLHLKAPWTVGITKFYGGWDKLLRKLPDGWVYCDADGSQFDSSLTPYLINAVLRIRLHFM 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  81 EEWDIGERMLMNLYTEIVFTPIATPDGSVIKKFKGNNSGQPSTVVDNTLMVILAFNYTMLSCGIDSDMIDSVCRMFANGD 160
Cdd:cd23175  112 EDWDIGEQMLRNLYTEIVYTPILTPDGTIVKKFKGNNSGQPSTVVDNTLMVMIAMYYALLKLGIDFEEIDERCVFFCNGD 191
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 340629670 161 DLLLAVNPDYEYILDLFSNHFSDLGLNFDFSSRTKDKSELWFMS 204
Cdd:cd23175  192 DLLIAVSPEHEHILDTFSSSFSELGLNYDFSSRTRDKEELWFMS 235
Poty_coat super family cl02961
Potyvirus coat protein;
395-627 1.43e-102

Potyvirus coat protein;


The actual alignment was detected with superfamily member pfam00767:

Pssm-ID: 279151  Cd Length: 243  Bit Score: 311.46  E-value: 1.43e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  395 DVNVGTSGTIAVPKLKAMSSKMRLPMAKGKNIL-HVEFLLGYKPAQQDISNTRATRAEFDRWYDAVKNEYEV-DDNQMTV 472
Cdd:pfam00767   1 DVAAATSITFEVPRRKGFGALWRPPKQKGAATPnRIEKLKKYLPDQNDISNTRATQAQLNDWYEAVRDDYGQtEEEFMDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  473 IMSGLMVWCIENGCSPNIN--GVW-----TMMDGEEQRTFPLKPVIENASPTFRQIMHHFSDAAEA-YIEFRNATERYMP 544
Cdd:pfam00767  81 ILPGWIVWCIENGTSPENRkaGSWravimAMMEDEEQVLYPIEPIIINAQPTLRQIMRHFSDLARAqYAESRNQGKPYMP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  545 RYGLQRNLTDYSLARYAFDFYEITSRTTARAKEAHMQMKAAAVRGSNTRMFGLDGNVGESQENTERHTAGDVSRNMHSLL 624
Cdd:pfam00767 161 KGGLKAGLADASLAAYAFDFYEDTSHDTARAREVHHQMKAAAVSGIKIRLFALAGPGSGQEEDTERHTVEDVAEGIHSLG 240

                  ...
gi 340629670  625 GVQ 627
Cdd:pfam00767 241 GAQ 243
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
339-394 8.06e-10

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


:

Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 61.01  E-value: 8.06e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  339 QTEEQKKAAEEQRQKAAADAEAKRKAAAD----EEARKAREAEAERKRQADAAAKGKQDK 394
Cdd:TIGR02794 113 QAEEKQKQAEEAKAKQAAEAKAKAEAEAErkakEEAAKQAEEEAKAKAAAEAKKKAEEAK 172
 
Name Accession Description Interval E-value
ps-ssRNAv_Potyviridae_RdRp cd23175
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Potyviridae of ...
1-204 3.37e-159

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Potyviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Potyviridae, order: Patatavirales. Potyviridae, is the largest family of RNA plant viruses, members of which have (+)ssRNA genomes and flexuous filamentous particles. The family is divided into eight genera: Brambyvirus, Bymovirus, Ipomovirus, Macluravirus, Poacevirus, Potyvirus, Rymovirus, and Tritimovirus. Most genomes are monopartite but those of members of the genus Bymovirus are bipartite. Some members cause serious disease epidemics in cultivated plants. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438025  Cd Length: 236  Bit Score: 455.76  E-value: 3.37e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670   1 PLETLLGGKVCVDDFNNQFYAHHLIGPWTVGITKFYGGWNQLLEKLPNGWVYCDADGSQFDSSLTPYLINAVLDIRLSFM 80
Cdd:cd23175   32 PIDTLLGGKVCVDDFNNQFYSLHLKAPWTVGITKFYGGWDKLLRKLPDGWVYCDADGSQFDSSLTPYLINAVLRIRLHFM 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  81 EEWDIGERMLMNLYTEIVFTPIATPDGSVIKKFKGNNSGQPSTVVDNTLMVILAFNYTMLSCGIDSDMIDSVCRMFANGD 160
Cdd:cd23175  112 EDWDIGEQMLRNLYTEIVYTPILTPDGTIVKKFKGNNSGQPSTVVDNTLMVMIAMYYALLKLGIDFEEIDERCVFFCNGD 191
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 340629670 161 DLLLAVNPDYEYILDLFSNHFSDLGLNFDFSSRTKDKSELWFMS 204
Cdd:cd23175  192 DLLIAVSPEHEHILDTFSSSFSELGLNYDFSSRTRDKEELWFMS 235
Poty_coat pfam00767
Potyvirus coat protein;
395-627 1.43e-102

Potyvirus coat protein;


Pssm-ID: 279151  Cd Length: 243  Bit Score: 311.46  E-value: 1.43e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  395 DVNVGTSGTIAVPKLKAMSSKMRLPMAKGKNIL-HVEFLLGYKPAQQDISNTRATRAEFDRWYDAVKNEYEV-DDNQMTV 472
Cdd:pfam00767   1 DVAAATSITFEVPRRKGFGALWRPPKQKGAATPnRIEKLKKYLPDQNDISNTRATQAQLNDWYEAVRDDYGQtEEEFMDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  473 IMSGLMVWCIENGCSPNIN--GVW-----TMMDGEEQRTFPLKPVIENASPTFRQIMHHFSDAAEA-YIEFRNATERYMP 544
Cdd:pfam00767  81 ILPGWIVWCIENGTSPENRkaGSWravimAMMEDEEQVLYPIEPIIINAQPTLRQIMRHFSDLARAqYAESRNQGKPYMP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  545 RYGLQRNLTDYSLARYAFDFYEITSRTTARAKEAHMQMKAAAVRGSNTRMFGLDGNVGESQENTERHTAGDVSRNMHSLL 624
Cdd:pfam00767 161 KGGLKAGLADASLAAYAFDFYEDTSHDTARAREVHHQMKAAAVSGIKIRLFALAGPGSGQEEDTERHTVEDVAEGIHSLG 240

                  ...
gi 340629670  625 GVQ 627
Cdd:pfam00767 241 GAQ 243
RdRP_1 pfam00680
Viral RNA-dependent RNA polymerase; This family represents the RNA-directed RNA polymerase ...
1-267 8.02e-65

Viral RNA-dependent RNA polymerase; This family represents the RNA-directed RNA polymerase found in many positive strand RNA eukaryotic viruses. Structural studies indicate that these proteins form the "right hand" structure found in all oligonucleotide polymerases, containing thumb, finger and palm domains, and also the additional bridging finger and thumb domains unique to RNA-directed RNA polymerases.


Pssm-ID: 425815  Cd Length: 450  Bit Score: 219.97  E-value: 8.02e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670    1 PLETLLGGKVCVDDFNNQFYAHHLIGPWTVGITKFYGGWNQLLEKL--PNGWVYCDaDGSQFDSSLTPYLINAVLDIRLS 78
Cdd:pfam00680 176 PVEYLLLERAFFDPFNQAFMLNNGFHPIQVGINPFDRGWPRLLRRLarFGDYVYEL-DYSGFDSSVPPWLIRFAFEILRE 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670   79 FME-EWDIGErmLMNLYTEIVFTPIATPDGSVIKKFKGNNSGQPSTVVDNTLMVILAFNYTMLS----CGIDSDMIDSVC 153
Cdd:pfam00680 255 LLGfPSNVKE--WRAILELLIYTPIALPNGTVFKKTGGLPSGSPFTSIINSIVNYLLILYALLKslenDGPRVCNLDKYF 332
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  154 RMFANGDDLLLAVNPDYEYILDLFSNHFSDLGLNFDFSSRT----KDKSELWFMSTRGIKYNEMYIPKLEKERIVAILEW 229
Cdd:pfam00680 333 DFFTYGDDSLVAVSPDFDPVLDRLSPHLKELGLTITPAKKTfpvsRELEEVSFLKRTFRKTPGGYRPPLDRKRILAQLEY 412
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 340629670  230 DRSK-QPQHRLEAICAsMIEAWGYPDLLHEIRKFYAWLL 267
Cdd:pfam00680 413 IRSKpVPSGQLENIRA-YASHHGYEFYRDLLYRFVEWLA 450
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
339-394 8.06e-10

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 61.01  E-value: 8.06e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  339 QTEEQKKAAEEQRQKAAADAEAKRKAAAD----EEARKAREAEAERKRQADAAAKGKQDK 394
Cdd:TIGR02794 113 QAEEKQKQAEEAKAKQAAEAKAKAEAEAErkakEEAAKQAEEEAKAKAAAEAKKKAEEAK 172
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
339-395 2.79e-09

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 59.43  E-value: 2.79e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 340629670 339 QTEEQKKAAEEQRQKAAADAEAKRKAAADEEARKAREAEAERKRQADAAAKGKQDKD 395
Cdd:PRK09510 126 QAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE 182
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
339-395 9.21e-07

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 51.96  E-value: 9.21e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 340629670 339 QTEEQKKAAEEQRQKAAADAEAKRKAA------ADEEARKAReAEAERKRQADAAAKGKQDKD 395
Cdd:COG3064   20 QAEAEKRAAAEAEQKAKEEAEEERLAEleakrqAEEEAREAK-AEAEQRAAELAAEAAKKLAE 81
growth_prot_Scy NF041483
polarized growth protein Scy;
336-394 2.05e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 44.82  E-value: 2.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  336 TPPQTEEQKKAAEEQRQKAAADAEAKRKAAADEEARKAREAEAERKR-QADAAAKGKQDK 394
Cdd:NF041483  362 TAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRlRGEAADQAEQLK 421
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
341-383 3.39e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 41.56  E-value: 3.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 340629670  341 EEQKKAAEEQRQKAAADAEAKRKAAADEEAR----------KAREaEAERKRQ 383
Cdd:pfam05672  68 EERRREEEERQRKAEEEAEEREQREQEEQERlqkqkeeaeaKARE-EAERQRQ 119
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
338-450 8.28e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 42.33  E-value: 8.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670 338 PQTEEQKKAAEEQ--RQKAAADAEAKRKAAADEEARKAREAEAERKRQAdAAAKGKQDKDVNVGTSGTIAVPKLKAMSSK 415
Cdd:COG3064   95 AEKAKAAKEAEAAaaAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKA-AEAEAAAKAEAEAARAAAAAAAAAAAAAAR 173
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 340629670 416 MRLPMAKGKNILHVEFLLGYKPAQQDISNTRATRA 450
Cdd:COG3064  174 AAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAA 208
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
338-474 3.65e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 40.41  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670 338 PQTEEQKKAAEEQRQKAAADAEAKRKAAADEEARKAREAEAERKRQADAAAKGKQDKDVNVGTSGTIAVPKLKAMSSKMR 417
Cdd:COG3064  113 AAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEA 192
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 340629670 418 LPMAKGKNILHVEFLLGYKPAQQDISNTRATRAEFDRWYDAVKNEYEVDDNQMTVIM 474
Cdd:COG3064  193 ADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAE 249
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
341-389 5.00e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 35.71  E-value: 5.00e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 340629670 341 EEQKKAAEEQRQKAAADAEAKRKAA----ADEEARKAREAEAERKRQADAAAK 389
Cdd:cd22249   12 EAQLKKLEEERRKEREEEEKASEELirklQEEEERQRKREREEQLKQDEELAK 64
 
Name Accession Description Interval E-value
ps-ssRNAv_Potyviridae_RdRp cd23175
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Potyviridae of ...
1-204 3.37e-159

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Potyviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Potyviridae, order: Patatavirales. Potyviridae, is the largest family of RNA plant viruses, members of which have (+)ssRNA genomes and flexuous filamentous particles. The family is divided into eight genera: Brambyvirus, Bymovirus, Ipomovirus, Macluravirus, Poacevirus, Potyvirus, Rymovirus, and Tritimovirus. Most genomes are monopartite but those of members of the genus Bymovirus are bipartite. Some members cause serious disease epidemics in cultivated plants. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438025  Cd Length: 236  Bit Score: 455.76  E-value: 3.37e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670   1 PLETLLGGKVCVDDFNNQFYAHHLIGPWTVGITKFYGGWNQLLEKLPNGWVYCDADGSQFDSSLTPYLINAVLDIRLSFM 80
Cdd:cd23175   32 PIDTLLGGKVCVDDFNNQFYSLHLKAPWTVGITKFYGGWDKLLRKLPDGWVYCDADGSQFDSSLTPYLINAVLRIRLHFM 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  81 EEWDIGERMLMNLYTEIVFTPIATPDGSVIKKFKGNNSGQPSTVVDNTLMVILAFNYTMLSCGIDSDMIDSVCRMFANGD 160
Cdd:cd23175  112 EDWDIGEQMLRNLYTEIVYTPILTPDGTIVKKFKGNNSGQPSTVVDNTLMVMIAMYYALLKLGIDFEEIDERCVFFCNGD 191
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 340629670 161 DLLLAVNPDYEYILDLFSNHFSDLGLNFDFSSRTKDKSELWFMS 204
Cdd:cd23175  192 DLLIAVSPEHEHILDTFSSSFSELGLNYDFSSRTRDKEELWFMS 235
Poty_coat pfam00767
Potyvirus coat protein;
395-627 1.43e-102

Potyvirus coat protein;


Pssm-ID: 279151  Cd Length: 243  Bit Score: 311.46  E-value: 1.43e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  395 DVNVGTSGTIAVPKLKAMSSKMRLPMAKGKNIL-HVEFLLGYKPAQQDISNTRATRAEFDRWYDAVKNEYEV-DDNQMTV 472
Cdd:pfam00767   1 DVAAATSITFEVPRRKGFGALWRPPKQKGAATPnRIEKLKKYLPDQNDISNTRATQAQLNDWYEAVRDDYGQtEEEFMDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  473 IMSGLMVWCIENGCSPNIN--GVW-----TMMDGEEQRTFPLKPVIENASPTFRQIMHHFSDAAEA-YIEFRNATERYMP 544
Cdd:pfam00767  81 ILPGWIVWCIENGTSPENRkaGSWravimAMMEDEEQVLYPIEPIIINAQPTLRQIMRHFSDLARAqYAESRNQGKPYMP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  545 RYGLQRNLTDYSLARYAFDFYEITSRTTARAKEAHMQMKAAAVRGSNTRMFGLDGNVGESQENTERHTAGDVSRNMHSLL 624
Cdd:pfam00767 161 KGGLKAGLADASLAAYAFDFYEDTSHDTARAREVHHQMKAAAVSGIKIRLFALAGPGSGQEEDTERHTVEDVAEGIHSLG 240

                  ...
gi 340629670  625 GVQ 627
Cdd:pfam00767 241 GAQ 243
RdRP_1 pfam00680
Viral RNA-dependent RNA polymerase; This family represents the RNA-directed RNA polymerase ...
1-267 8.02e-65

Viral RNA-dependent RNA polymerase; This family represents the RNA-directed RNA polymerase found in many positive strand RNA eukaryotic viruses. Structural studies indicate that these proteins form the "right hand" structure found in all oligonucleotide polymerases, containing thumb, finger and palm domains, and also the additional bridging finger and thumb domains unique to RNA-directed RNA polymerases.


Pssm-ID: 425815  Cd Length: 450  Bit Score: 219.97  E-value: 8.02e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670    1 PLETLLGGKVCVDDFNNQFYAHHLIGPWTVGITKFYGGWNQLLEKL--PNGWVYCDaDGSQFDSSLTPYLINAVLDIRLS 78
Cdd:pfam00680 176 PVEYLLLERAFFDPFNQAFMLNNGFHPIQVGINPFDRGWPRLLRRLarFGDYVYEL-DYSGFDSSVPPWLIRFAFEILRE 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670   79 FME-EWDIGErmLMNLYTEIVFTPIATPDGSVIKKFKGNNSGQPSTVVDNTLMVILAFNYTMLS----CGIDSDMIDSVC 153
Cdd:pfam00680 255 LLGfPSNVKE--WRAILELLIYTPIALPNGTVFKKTGGLPSGSPFTSIINSIVNYLLILYALLKslenDGPRVCNLDKYF 332
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  154 RMFANGDDLLLAVNPDYEYILDLFSNHFSDLGLNFDFSSRT----KDKSELWFMSTRGIKYNEMYIPKLEKERIVAILEW 229
Cdd:pfam00680 333 DFFTYGDDSLVAVSPDFDPVLDRLSPHLKELGLTITPAKKTfpvsRELEEVSFLKRTFRKTPGGYRPPLDRKRILAQLEY 412
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 340629670  230 DRSK-QPQHRLEAICAsMIEAWGYPDLLHEIRKFYAWLL 267
Cdd:pfam00680 413 IRSKpVPSGQLENIRA-YASHHGYEFYRDLLYRFVEWLA 450
RNA_dep_RNAP cd01699
RNA_dep_RNAP: RNA-dependent RNA polymerase (RdRp) is an essential protein encoded in the ...
1-229 5.74e-39

RNA_dep_RNAP: RNA-dependent RNA polymerase (RdRp) is an essential protein encoded in the genomes of all RNA containing viruses with no DNA stage. RdRp catalyzes synthesis of the RNA strand complementary to a given RNA template. RdRps of many viruses are products of processing of polyproteins. Some RdRps consist of one polypeptide chain, and others are complexes of several subunits. The domain organization and the 3D structure of the catalytic center of a wide range of RdRps, including those with a low overall sequence homology, are conserved. The catalytic center is formed by several motifs containing a number of conserved amino acid residues. This subfamily represents the RNA-dependent RNA polymerases from all positive-strand RNA eukaryotic viruses with no DNA stage.


Pssm-ID: 238843 [Multi-domain]  Cd Length: 278  Bit Score: 144.73  E-value: 5.74e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670   1 PLETLLGGKVCVDDFNNQFYAHHLIGPWTVGITKFYGGWNQLLEKL-PNGWVYCDADGSQFDSSLTPYLINAVLDIRLSF 79
Cdd:cd01699   46 PLDYNIALRMYLGPFEAKLMKNRGGLPIAVGINPYSRDWTILANKLrSFSPVAIALDYSRFDSSLSPQLLEAEHSIYNAL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  80 MEewDIGERMLMNLYTEIVFTPIATPDGSVIKKFKGNNSGQPSTVVDNTLMVILAFNYTMLSCGIDSDMIDsvCRMFANG 159
Cdd:cd01699  126 YD--DDDELERRNLLRSLTNNSLHIGFNEVYKVRGGRPSGDPLTSIGNSIINCILVRYAFRKLGGKSFFKN--VRLLNYG 201
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 340629670 160 DDLLLAVNPD-YEYILDLFSNHFSDLGLNFDFSSRTKDK----SELWFMStRGIKYNE--MYIPKLEKERIVAILEW 229
Cdd:cd01699  202 DDCLLSVEKAdDKFNLETLAEWLKEYGLTMTDEDKVESPfrplEEVEFLK-RRFVLDEggGWRAPLDPSSILSKLSW 277
ps-ssRNAv-Picornavirales cd23169
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Picornavirales of ...
1-268 5.44e-24

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Picornavirales of positive-sense single-stranded RNA [(+)ssRNA] viruses; This family contains the catalytic core domain of RdRp of Picornavirales, an order of (+)ssRNA viruses. The order Picornavirales comprises viruses that historically are referred to as picorna-like viruses and which are classified into eight virus families: Caliciviridae, Dicistroviridae, Iflaviridae, Marnaviridae, Picornaviridae, Polycipiviridae, Secoviridae, and Solinviviridae. All known genomes of Picornavirales members encode proteins with helicase, 3C-like protease, and RdRp domains, as well as capsid proteins with related structures, although the genome organizations can differ among viruses. The picornavirus genome is replicated via a negative-sense (-) RNA intermediate by the viral RdRp, named 3Dpol, which uses VPg (the product of 3B) as a primer to initiate the replication process. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438019  Cd Length: 309  Bit Score: 102.67  E-value: 5.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670   1 PLETLLGGKVCVDDFNNQFYAHHLIGPWTVGITKFYGGWNQLLEKLP-NGWVYCDADGSQFDSSLTPYLINAVLDIRLSF 79
Cdd:cd23169   29 PLDYTIAFRKYFGDFIAAFQKNRIKLEHAVGINPDSVEWTRLYRRLLkKGPNIFAGDYSNFDGSLPPDVMEAAFDIINDW 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  80 MEEW--DIGERMLMNLYTEIVfTPIATPDGSVIKKFKGNNSGQPSTVVDNTLMVILAFNYTMLSCGIDSDMID--SVCRM 155
Cdd:cd23169  109 YDEYvdDEDERVRKVLFEELI-NTIHLVGNLVYQVHGGNPSGNPLTTIINSIVNLLYIRYAWLRITGLTSLSDfkKNVRL 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670 156 FANGDDLLLAVNPDYEYILD--LFSNHFSDLGLNFdfssRTKDKS----------ELWFMStRGIKYNE---MYIPKLEK 220
Cdd:cd23169  188 VTYGDDVIISVSDEVKDEFNfvTISEFLKELGITY----TDADKSgdivpyrpleEVTFLK-RGFRPHPtpgLVLAPLDL 262
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 340629670 221 ERIVAILEWDRSKqpQHRLEAICASMIEA------WGypdllheiRKFYAWLLE 268
Cdd:cd23169  263 ESIEEQLNWTRKE--DDLLEATIENARAAlllafgHG--------PEYYNKFRQ 306
ps-ssRNAv_Astroviridae_RdRp cd23172
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Astroviridae of ...
14-181 7.28e-14

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Astroviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Astroviridae, order, Stellavirales. Astrovirus has a non-segmented, (+)ssRNA genome within a non-enveloped icosahedral capsid. The family Astroviridae comprises two genera, Mamastrovirus, which infect mammals, and Avastrovirus, which infect birds. Astroviruses have been isolated from stools from a wide variety of mammals and birds. Human astroviruses have been shown to be an important cause of gastroenteritis in young children. Duck astrovirus causes an often-fatal hepatitis in ducklings. Astroviruses infecting turkeys, guinea fowl and chickens affect multiple organs, including the kidney and thymus. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438022  Cd Length: 243  Bit Score: 71.73  E-value: 7.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  14 DFNNQFYAHHLIGPWTVGITKFYGGWNQLLEKL-PNGWVYCDADGSQFDSSLTPYLINAVLDIRLSFM-EEWDIGERMLM 91
Cdd:cd23172   43 DQNNLMKERTLTNEGQVGWSPFYGGFDARVRRLgSKGNYFVEFDWTRFDGTIPAELFRHIRKLRWSFLdPEKTEENRKVY 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  92 NLYTE-IVFTPIATPDGSVIKKFKGNNSGQPSTVVDNTlMV---ILAFNYTML--SCGIDSDMIDSVCRMFANGDDLLLA 165
Cdd:cd23172  123 DWYVHnLLNRYVLLPTGEVTRVTKGNPSGQISTTMDNC-MVntfLTAFEFAYVygPKTGTLKELWDNYDTIVYGDDRLSG 201
                        170       180
                 ....*....|....*....|
gi 340629670 166 VN--PDY--EYILDLFSNHF 181
Cdd:cd23172  202 YPslPDPyvERVVDMYKDVF 221
Caliciviridae_RdRp cd23192
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Caliciviridae of ...
17-187 2.83e-13

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Caliciviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Caliciviridae, order Picornavirales. Member viruses have a viral (+)ssRNA genome, which is not segmented. The family Caliciviridae, includes eleven genera: seven genera of which infect mammals (Lagovirus, Norovirus, Nebovirus, Recovirus, Sapovirus, Valovirus, and Vesivirus), two genera of which infect birds (Bavovirus, Nacovirus), and two genera of which infect fish (Minovirus and Salovirus). Each genus includes 1-2 species. Human noroviruses are a leading cause of acute gastroenteritis in humans. Furthermore, unclassified caliciviruses have been detected in geese, yellowfin seabream, greater green snake, arctic lamprey, frogs and various Australian birds, highlighting the wide host range of viruses in the family Caliciviridae. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438042  Cd Length: 310  Bit Score: 71.14  E-value: 2.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  17 NQFYAHHLIGPWTVGITKFYGGWNQLLEKLPNGWVYCDADGSQFDSSLTPYLINAVLDIRLSFMEEWDIGERMLMNLYTe 96
Cdd:cd23192   45 DALKAVCPTGPIAVGINMDSEDVEVIFERLSGFRYHYCLDYSKWDSTQSPAVTAAAIDILADLSEETPLRDSVVETLSS- 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  97 ivfTPIATPDGSVIKKFKGNNSGQPSTVVDNTLMVILAFNYTMLSC----GIDSDMIDSVCRMFANGDDLLLAVNPDYEY 172
Cdd:cd23192  124 ---PPMGIFDDVIFVTKRGLPSGMPFTSVINSLNHWLLFSAAVLKAyelvGIYTGNVFDEADFFTYGDDGVYAMPPATAS 200
                        170
                 ....*....|....*
gi 340629670 173 ILDLFSNHFSDLGLN 187
Cdd:cd23192  201 VMDEIIENLKSYGLK 215
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
339-394 8.06e-10

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 61.01  E-value: 8.06e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  339 QTEEQKKAAEEQRQKAAADAEAKRKAAAD----EEARKAREAEAERKRQADAAAKGKQDK 394
Cdd:TIGR02794 113 QAEEKQKQAEEAKAKQAAEAKAKAEAEAErkakEEAAKQAEEEAKAKAAAEAKKKAEEAK 172
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
339-394 9.56e-10

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 60.63  E-value: 9.56e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  339 QTEEQKKAAEEQRQKAA----ADAEAKRKAAAdeEARKAREAEAERKRQADAAAKGKQDK 394
Cdd:TIGR02794  99 AAEKAAKQAEQAAKQAEekqkQAEEAKAKQAA--EAKAKAEAEAERKAKEEAAKQAEEEA 156
Dicistroviridae_RdRp cd23194
RNA-dependent RNA polymerase (RdRp) in the family Dicistroviridae of positive-sense ...
30-249 2.05e-09

RNA-dependent RNA polymerase (RdRp) in the family Dicistroviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses, in the order Picornavirales; This group contains the RdRp of RNA viruses belonging to the family Dicistroviridae, order Picornavirales. Dicistroviridae is a family of small non-enveloped viruses with a (+)ssRNA genome of approximately 8-10 kilobases. The family contains 3 genera: Aparavirus, Cripavirus, and Triatovirus. All members infect arthropod hosts with some having devastating economic consequences, such as acute bee paralysis virus, Kashmir bee virus, and Israeli acute paralysis virus in domesticated honeybees, and taura syndrome virus and mud crab virus in the seafood industry. On the contrary, host specificity and other desirable traits make several members of this group amenable to development as biopesticides for insect control, such as Solenopsis invicta virus 1 against fire ants, and triatoma virus against triatomine bugs that vector Chagas disease. Members in the family Dicistroviridae have similarity to viruses in the Picornavirales members (Iflaviridae, Picornaviridae, Marnaviridae and Secoviridae). The genomes of viruses of these taxa encode proteins with helicase, 3C-like protease, and RdRp domains, as well as capsid proteins with related structures, although the genome organizations can differ among viruses. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438044 [Multi-domain]  Cd Length: 315  Bit Score: 59.44  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  30 VGITKFYGGWNQLLEKL-PNGWVYCDADGSQFDSSLTPYLINAVLDIrlsfMEEW---DIGERMLMN-LYTEIVFTPIAT 104
Cdd:cd23194   63 VGTNVYSLDWDKLARKLlSKGDKVIAGDFSNFDGSLNPQILWAILDI----INEWyddGEENALIRRvLWEDIVNSVHIC 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670 105 pDGSVIKKFKGNNSGQPSTVVDNTLMVILAFNYTMLSCGIDS-----DMIDSVCRMFANGDDLLLAVNPDyeyILDLF-- 177
Cdd:cd23194  139 -GGYVYQWTHSQPSGNPLTAIINSIYNSIIMRYVYLLLTKEAglmtmSDFNKHVSMVSYGDDNVINVSDE---VSEWFnq 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670 178 ---SNHFSDLGLnfDFSSRTKDKSELWFMS-------TRGIKYNE---MYIPKLEKERIVAILEWDRSKQPQhrlEAICA 244
Cdd:cd23194  215 ltiTEAMAEIGM--TYTDETKTGEIVPYRSleevsflKRGFRYDDdlgRWVAPLDLDTILEMPNWVRKGKDP---EEITK 289

                 ....*
gi 340629670 245 SMIEA 249
Cdd:cd23194  290 QNVEN 294
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
339-395 2.79e-09

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 59.43  E-value: 2.79e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 340629670 339 QTEEQKKAAEEQRQKAAADAEAKRKAAADEEARKAREAEAERKRQADAAAKGKQDKD 395
Cdd:PRK09510 126 QAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE 182
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
341-395 7.98e-09

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 57.89  E-value: 7.98e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 340629670 341 EEQKKAAEEQRQKAAADA----EAKRKAAADEEARKAREAEAERKRQADAAAKGKQDKD 395
Cdd:PRK09510 166 EAKKKAEAEAAKKAAAEAkkkaEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAK 224
ps-ssRNAv_RdRp-like cd23167
conserved catalytic core domain of RNA-dependent RNA polymerase (RdRp) from the positive-sense ...
51-167 8.80e-09

conserved catalytic core domain of RNA-dependent RNA polymerase (RdRp) from the positive-sense single-stranded RNA [(+)ssRNA] viruses and closely related viruses; This family contains the catalytic core domain of RdRp of RNA viruses which belong to Group IV of the Baltimore classification system, and are a group of related viruses that have positive-sense (+), single-stranded (ss) genomes made of ribonucleic acid (RNA). RdRp (also known as RNA replicase) catalyzes the replication of RNA from an RNA template; specifically, it catalyzes the synthesis of the RNA strand complementary to a given RNA template. The Baltimore Classification is divided into 7 classes, 3 of which include RNA viruses: Group IV (+) RNA viruses, Group III double-stranded (ds) RNA viruses, and Group V negative-sense (-) RNA viruses. Baltimore groups of viruses differ with respect to the nature of their genome (i.e., the nucleic acid form that is packaged into virions) and correspond to distinct strategies of genome replication and expression. (+) viral RNA is similar to mRNA and thus can be immediately translated by the host cell. (+)ssRNA viruses can also produce (+) copies of the genome from (-) strands of an intermediate dsRNA genome. This acts as both a transcription and a replication process since the replicated RNA is also mRNA. RdRps belong to the expansive class of polymerases containing so-called palm catalytic domains along with the accessory fingers and thumb domains. All RdRps also have six conserved structural motifs (A-F), located in its majority in the palm subdomain (A-E motifs) and the F motif is located on the finger subdomain. All these motifs have been shown to be implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides. In addition to Group IV viruses, this model also includes Picobirnaviruses (PBVs), members of the family Picobirnaviridae of dsRNA viruses (Baltimore classification Group III), which are bi-segmented dsRNA viruses. The phylogenetic tree of the RdRps of RNA viruses (realm Riboviria) showed that picobirnaviruses are embedded in the branch of diverse (+)RNA viruses; sometimes they are collectively referred to as the picornavirus supergroup. RdRps of members of the family Permutatetraviridae, a distinct group of RNA viruses that encompass a circular permutation within the RdRp palm domain, are not included in this model.


Pssm-ID: 438017 [Multi-domain]  Cd Length: 73  Bit Score: 52.34  E-value: 8.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  51 VYCDADGSQFDSSLTPYLINAvldirlsfmeewdigermlmnlyteivftpiatpdgsvikkfkGNNSGQPSTVVDNTLM 130
Cdd:cd23167    1 HVVESDYSGFDSSISPDLLKA-------------------------------------------GQPSGSPNTSADNSLI 37
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 340629670 131 VILAFNYTMLSCGIDSDMIDSVCrMFANGDDLLLAVN 167
Cdd:cd23167   38 NLLLARLALRKACGRAEFLNSVG-ILVYGDDSLVSVP 73
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
341-394 1.10e-08

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 57.16  E-value: 1.10e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 340629670  341 EEQKKAAEEQRQKAAAD----AEAKRKAAADEEARKAREAEAerKRQADAAAKGKQDK 394
Cdd:TIGR02794 162 AEAKKKAEEAKKKAEAEakakAEAEAKAKAEEAKAKAEAAKA--KAAAEAAAKAEAEA 217
ps-ssRNA_Picornaviridae cd23193
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Picornaviridae of ...
39-169 1.84e-08

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Picornaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Picornaviridae, order Picornavirales. The Picornaviridae family consists of small, icosahedral viruses with (+)ssRNA genomes. Characteristic features of all members of the family Picornaviridae are three capsid proteins with beta-barrel folding, polyprotein processing by virus-encoded cysteine proteinase(s), and replication by an RdRp with a YGDD sequence motif. The family Picornaviridae comprises 68 genera containing 158 species, but many viruses are presently awaiting classification. The established genera of the family include: Aphthovirus, Avisivirus, Crohivirus, Enterovirus, Teschovirus, Cardiovirus, Erbovirus, Kobuvirus, Hepatovirus, Parechovirus, Aquamavirus, Avihepatovirus, Avisivirus, Cosavirus, Dicipivirus, Fipivirus, Gallivirus, Hunnivirus, Kunsagivirus, Limnipivirus, Megrivirus, Mischivirus, Mosavirus, Oscivirus, Pasivirus, Passerivirus, Rabovirus, Rosavirus, Sakobuvirus, Salivirus, Sapelovirus, Senecavirus, Sicinivirus, and Tremovirus. The Picornaviridae contains many important human and animal pathogens including enteroviruses (such as poliovirus, enterovirus, coxsackievirus, and rhinovirus), cardioviruses (such as encephalomyocarditis virus and Theiler's virus), hepatitis A virus and foot-and-mouth disease virus. Infection with various picornaviruses may cause encephalitis, febrile rash illnesses (hand-foot-and-mouth disease), aseptic meningitis, hepatitis, conjunctivitis, herpangina, myositis and myocarditis, and the common cold. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438043  Cd Length: 345  Bit Score: 56.79  E-value: 1.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  39 WNQLLEKLPNGWVYCdADGSQFDSSLTPYLINAVLDIRLSFMEEWDIGERMLMNLY--TEIVFTPIATPDGsvikkfkGN 116
Cdd:cd23193  124 WTRLFASLKQDNVYD-LDYSGFDASLSSQLFEAAVEVLAECHGDPELVLRYLEPIInsKHVVGDERYTVEG-------GM 195
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 340629670 117 NSGQPSTVVDNTLMVILAFNYTMLSCGIDSdmiDSVCRMFANGDDLLLAVNPD 169
Cdd:cd23193  196 PSGCPCTSILNSICNNLVVRYALLETGKFD---PDEYYILAYGDDVLVSTDEP 245
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
339-393 2.53e-08

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 56.39  E-value: 2.53e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 340629670  339 QTEEQK-KAAEEQRQKAAADAEAKRKAAAD---EEARKAREAEAERKRQADAAAKGKQD 393
Cdd:TIGR02794 120 QAEEAKaKQAAEAKAKAEAEAERKAKEEAAkqaEEEAKAKAAAEAKKKAEEAKKKAEAE 178
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
333-391 2.69e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 56.35  E-value: 2.69e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 340629670 333 DAGTPPQTEEQKKAAEEQRQKAAADAEAKRKAAADEEA-----RKAREAEAERKRQADAAAKGK 391
Cdd:PRK09510 182 EAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAaaeakAAAAKAAAEAKAAAEKAAAAK 245
ps-ssRNAv_Nidovirales_RdRp cd23168
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Nidovirales of ...
1-223 2.78e-08

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Nidovirales of positive-sense single-stranded RNA [(+)ssRNA] viruses; This family contains the catalytic core domain of RdRP of Nidovirales, an order of enveloped, (+)ssRNA viruses which infect vertebrates and invertebrates. Host organisms include mammals, birds, reptiles, amphibians, fish, arthropods, mollusks, and helminths. The order Nidovirales currently comprises 88 formally recognized virus species of (+)ssRNA viruses which are classified into nine virus families: Abyssoviridae, Arteriviridae, Coronaviridae, Euroniviridae, Medioniviridae, Mesoniviridae, Mononiviridae, Roniviridae, and Tobaniviridae. Based on the genome size, the members of the order Nidovirales can be divided into two groups, large and small nidoviruses. The genomes of the large nidoviruses are well over 25 kb in length with size differences in the 5 kb range. Planarian secretory cell nidovirus (PSCNV), only member of the Mononiviridae family, has the largest known non-segmented RNA genome of 41.1 kb; its host is the planarian flatworm. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438018 [Multi-domain]  Cd Length: 310  Bit Score: 55.83  E-value: 2.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670   1 PLETLLGGKVCVDDFNNQFY---------AHHLIGPwtVGITKFYGGWNQLLEKLPNGwVYCD-----ADGSQFD---SS 63
Cdd:cd23168   16 RARTILGVSIISTDVGRQLHqavlaaivnTRSANIV--IIGTKFYGGWHKMLRYLYPG-VIEDpvlmgWDYPKCDrsvPN 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  64 LTPYLINAVL----DIRLSFMEEWdigeRMLMNLYTEIVFTPIATpDGSVIKKFKGNNSGQPSTVVDNTLMVILAFNYTM 139
Cdd:cd23168   93 MLRYLANLLLaslyDNCCNLSEIV----HLLINECAQVLYDYVVY-GGNLYRKPGGVSSGDSTTAISNSIYNYFQTFIAN 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670 140 LSCGIDSdmidsvcrmfangDDLLLAVNPD-YEYILDLFSNHF--SDLGLNFDF-SSRTKDKSELWFMSTRGIKYNEMYI 215
Cdd:cd23168  168 VRLAILS-------------DDGVACINPDlIDLGDVASVSFFlaSYYYTNNKKkYSSTCWVEPHEFCSPHEFKSDDKYQ 234

                 ....*...
gi 340629670 216 PKLEKERI 223
Cdd:cd23168  235 DRVERVYL 242
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
339-396 4.78e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 55.58  E-value: 4.78e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 340629670 339 QTEEQKKAAEEQRQKAAADAEAKRKAAADEEARKAREAEAERKRQADAAAKGKQDKDV 396
Cdd:PRK09510 112 AAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKK 169
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
341-394 4.36e-07

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 52.16  E-value: 4.36e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 340629670  341 EEQKKAAEEQRQKAAADAEAKRKAA---ADEEARKAreAEAERKRQA-DAAAKGKQDK 394
Cdd:TIGR02794 147 EAAKQAEEEAKAKAAAEAKKKAEEAkkkAEAEAKAK--AEAEAKAKAeEAKAKAEAAK 202
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
339-395 9.21e-07

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 51.96  E-value: 9.21e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 340629670 339 QTEEQKKAAEEQRQKAAADAEAKRKAA------ADEEARKAReAEAERKRQADAAAKGKQDKD 395
Cdd:COG3064   20 QAEAEKRAAAEAEQKAKEEAEEERLAEleakrqAEEEAREAK-AEAEQRAAELAAEAAKKLAE 81
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
341-393 1.48e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 50.96  E-value: 1.48e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 340629670 341 EEQKKAAEEQRQKAAADA------EAKRKAAAD------EEARKAREAEAERKRQADAAAKGKQD 393
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAkkkaeaEAAKKAAAEakkkaeAEAAAKAAAEAKKKAEAEAKKKAAAE 214
Polycipiviridae_RdRp cd23198
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Polycipiviridae of ...
39-234 2.27e-06

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Polycipiviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses, in the order Picornavirales; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Polycipiviridae (polycistronic picorna-like viruses), order Picornavirales. Polycipiviridae is a family of picorna-like viruses with non-segmented, linear, (+)ssRNA genomes of approximately 10-12 kb. Their genomes are polycistronic, with four (or more) consecutive 5'-proximal open reading frames (ORFs) encoding structural (and possibly other) proteins and a long 3' ORF encoding the replication polyprotein. Members of species within the family are typically found in ants, with Apple picorna-like virus 1 and the unnamed Polycipiviridae virus in fruit bat stool as exceptions. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438048  Cd Length: 317  Bit Score: 50.10  E-value: 2.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  39 WNQL---LEKLPNGwvyCDADGSQFDSSLTPYLINAVLDIrLSFMEEWDIGER---MLMNLYTEIVFTPIATPDgSVIKK 112
Cdd:cd23198   73 WNRLyhyLNRHPNA---VDFDVSNWDGHLPAELFYAVLDI-IKTVLGLKPNSPnakVIYSILTEVMNCHIQFED-IIYQK 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670 113 FKGNNSGQPSTVVDNTLMVILAFNYTMLSCGIDSDMIDSVCRMFAN------GDDLLLAVNpdyEYILDLFSNH-----F 181
Cdd:cd23198  148 LRGLISGFPGTAEVNTLAHWLLIYYIYLYLAQNTIYDMTITAFLRNvsaifyGDDIIITIS---DEILHWFNGKtiqrmY 224
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 340629670 182 SDLGlnFDFSSRTKDK--------SELWFMSTrgiKYNEM----YIPKLEKERIVAILEWDRSKQ 234
Cdd:cd23198  225 EEHG--YPVTSAAKDTeipeskplSDCQFLKS---SWNPIlpgyYIRKMDIEVVYDLVYWVRAKE 284
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
339-393 2.69e-06

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 49.84  E-value: 2.69e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 340629670  339 QTEEQKKAAEEQRQKAAADaEAKRKA-AADEEARK--AREAEAERKRQADAAAKGKQD 393
Cdd:TIGR02794 174 KAEAEAKAKAEAEAKAKAE-EAKAKAeAAKAKAAAeaAAKAEAEAAAAAAAEAERKAD 230
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
339-402 2.96e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 49.80  E-value: 2.96e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 340629670 339 QTEEQKKAAEEQRQKAAADAEAKRKAAADEEARKAREAEAERKRQADAAAKGKQDKD--VNVGTSG 402
Cdd:PRK09510 204 EAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDdlFGGLDSG 269
Fipivirus_RdRp cd23229
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Fipivirus of ...
39-180 4.79e-06

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Fipivirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the catalytic core domain of the RdRp of RNA viruses belonging to the Fipivirus genus within the family Picornaviridae, order Picornavirales. The Fipivirus contains viruses with (+)ssRNA genomes that produce nonenveloped virions. This genus contains five species: Fipivirus A (Wuhan sharpbelly picornavirus 2), Fipivirus B (Wuhan sharpbelly picornavirus 3), Fipivirus C (Wenling crossorhombus picornavirus), Fipivirus D (Wenling jack mackerels picornavirus) and Fipivirus E (Wenling banjofish picornavirus 1). All contain viruses from fish. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438079  Cd Length: 394  Bit Score: 49.42  E-value: 4.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  39 WNQLLEKLPnGWVYCDADGSQFDSSLTPYLINAVLDIRLSFMEEWDIGERMLMNLYTE---IVFTPIATPDGSVikkfkg 115
Cdd:cd23229  136 WTDIALARP-GWPVIALDYSNFDGSLQSFVITGAVRILGYIAGLPDGQSYRLAEFVYDvkqIVGKYLYTTVGPL------ 208
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 340629670 116 nNSGQPSTVVDNTLMVILAFNYTMlsCGIDSDMIDSV---CRMFANGDDLLLAVNPDYEYILDLFSNH 180
Cdd:cd23229  209 -PSGCPSTSIIGSLCNVLMLLYTL--SHATGQRYSAFrdwMHVVTYGDDVLVFVHPEVVVVLDTLAHE 273
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
341-389 1.62e-05

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 47.73  E-value: 1.62e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 340629670 341 EEQKKAAEEQRQKAAADAEAKRKAAADEEARKAREAEAER------KRQADAAAK 389
Cdd:COG3064    4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERlaeleaKRQAEEEAR 58
Nora-virus_RdRp cd23200
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in a novel picorna-like ...
1-251 1.74e-05

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in a novel picorna-like Drosophila virus, Nora virus; This group contains the catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the unclassified Nora virus, a new picorna-like virus family. Nora virus has a (+)ssRNA genome followed by a poly(A) tail. Unlike other picorna-like viruses, the genome has four open reading frames (ORFs). One ORF encodes a picornavirus-like cassette of proteins for virus replication, including an iflavirus-like RdRp and a helicase that is related to those of mammalian picornaviruses. The three other ORFs are not closely related to any previously described viruses. Nora virus is present as a persistent infection in several tested laboratory stocks and wild-caught flies. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438050  Cd Length: 306  Bit Score: 47.22  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670   1 PLETLLGGKVCVDDFNNQFYAHHLIGPWTVGITKFYGGWNQLLEKLPNGWVYCDADGSQFDSSLTPYLINAVLDIRLSFM 80
Cdd:cd23200   29 PVDLILFSGALYGPYKEAYTKAGLKCYHAVGIDPKSVGWQQLATYMTKHPNYFDADYKNYDKYLHRQVFKAVRKIQRSVI 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  81 E-----EWDIGERMLmnlyTEIVFTPIATPDGSVIKKFKGNNSGQPSTVVDNTLMVIL--AFNYTMLSCGIDSDMIDSVC 153
Cdd:cd23200  109 QqvcpdKWDKARAVE----ELDAIDTYVVDYQTVYKTNRGNKSGSYTTTIDNCLANDIygLYAWVKTTGLRSLWDYRQNV 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670 154 RMFANGDDLLLAVNPDY--EYILDLFSNHFSDLGLNFDFSSRTKDK------SELWFMSTRGIKYNEMYIPKLEKERIVA 225
Cdd:cd23200  185 SSVAFGDDIIKSVSDEYkdKYNYCTYRDVLNATGHIMTPGSKDGEEkpftsfENLQFLKRGFKLENGMVLAPLLQRSIEG 264
                        250       260       270
                 ....*....|....*....|....*....|
gi 340629670 226 ILEWD--RSKQPQHRLEAICASMIEA--WG 251
Cdd:cd23200  265 PFVWTdiREDQITVWVNLVQEQLIEAalWG 294
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
342-391 1.89e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 47.15  E-value: 1.89e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 340629670  342 EQKKAAEEQRQKAA-----ADAEAKRKAAADeearKAREAEAERKRQADAAAKGK 391
Cdd:TIGR02794 186 EAKAKAEEAKAKAEaakakAAAEAAAKAEAE----AAAAAAAEAERKADEAELGD 236
PTZ00121 PTZ00121
MAEBL; Provisional
339-394 1.96e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 1.96e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 340629670  339 QTEEQKKAAEEQRQKAAA--DAEAKRKAaadEEARKAREA-EAERKRQADAAAKGKQDK 394
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAkkKADEAKKA---EEAKKADEAkKAEEAKKADEAKKAEEKK 1546
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
339-395 2.14e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 47.11  E-value: 2.14e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 340629670 339 QTEEQKKAAEEQrQKAAADAEAKRKAAAD--EEARKAREAEAERKRQADAAAKGKQDKD 395
Cdd:PRK09510 141 AAAAAKAKAEAE-AKRAAAAAKKAAAEAKkkAEAEAAKKAAAEAKKKAEAEAAAKAAAE 198
PTZ00121 PTZ00121
MAEBL; Provisional
339-394 2.55e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 2.55e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 340629670  339 QTEEQKKAAEEQRQKAAADA---EAKRKAaadEEARKAREA--EAERKRQADAAAKGKQDK 394
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKkadEAKKKA---EEKKKADEAkkKAEEAKKADEAKKKAEEA 1456
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
331-391 3.32e-05

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 46.51  E-value: 3.32e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 340629670 331 RVDAGTPPQTEEQKKAAEEQRQKAAADAEAKRKAAADEEARKAREAEAERKRQADAAAKGK 391
Cdd:PRK07735 146 KREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAK 206
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
334-394 4.21e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 45.99  E-value: 4.21e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 340629670  334 AGTPPQTEEQKKAAEEQRQKAAA-DAEAKRKAAADEEAR----KAREAEAERKRQADAAAKGKQDK 394
Cdd:TIGR02794  52 ANRIQQQKKPAAKKEQERQKKLEqQAEEAEKQRAAEQARqkelEQRAAAEKAAKQAEQAAKQAEEK 117
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
338-394 6.87e-05

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 45.80  E-value: 6.87e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 340629670 338 PQTEEQKKAAEEQrQKAAADAEAKRKAA-ADEEARKAREAEAERKRQADAAAKGKQDK 394
Cdd:COG3064   85 AAAEAEKKAAAEK-AKAAKEAEAAAAAEkAAAAAEKEKAEEAKRKAEEEAKRKAEEER 141
Aalivirus_RdRp cd23216
RNA-dependent RNA polymerase (RdRp) in the genus Aalivirus of positive-sense single-stranded ...
36-167 1.07e-04

RNA-dependent RNA polymerase (RdRp) in the genus Aalivirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the RdRp of RNA viruses belonging to the Aalivirus genus within the family Picornaviridae, order Picornavirales. Member viruses have a (+)ssRNA genome. Aalivirus is a new picornavirus found in ducks in China. It is most closely related to duck hepatitis A virus (genus Avihepatovirus) and to avisivirus A1 (genus Avisivirus). The name "aalivirus" is derived from Avihepatovirus/Avisivirus-like virus. RdRps are multi-domain proteins that play a pivotal role in enterovirus replication. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438066  Cd Length: 337  Bit Score: 44.66  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  36 YGGWNQLLEKLPngWVYCDADGSQFDSSLTPYLINAVLDIRLSFMEEwdigERMLMNLYTEIVFTPIATPDGSVIKKfKG 115
Cdd:cd23216  112 YTHFDSLMDQVK--WNVLALDFKKFDGSLSPQVMEEAVDILASFHDM----PQMVVDIHKHTIYSTNVVSDETWFVE-GG 184
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 340629670 116 NNSGQPSTVVDNTLMVILAFNYTMLSCGIDSDMIdsvcRMFANGDDLLLAVN 167
Cdd:cd23216  185 MCSGSPCTTVLNTICNLLVNTTILLSEGIQPDNF----YIAAYGDDTIISVD 232
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
331-411 1.08e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 45.03  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670 331 RVDAGTPPQTEEQKKAAEEQRQKAAADAEAKR-------KAAADEEARkaREAEAERKRQADAAAKGKQDKDVNVGTSGT 403
Cdd:COG3064   79 LAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAekaaaaaEKEKAEEAK--RKAEEEAKRKAEEERKAAEAEAAAKAEAEA 156

                 ....*...
gi 340629670 404 IAVPKLKA 411
Cdd:COG3064  157 ARAAAAAA 164
PTZ00121 PTZ00121
MAEBL; Provisional
296-398 1.13e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  296 NGVNESEIEKYFQQfkTDLQGYVEDYNEDVYHQsgRVDAGTPPQTEEQKKAAEEQRQKAAADAEAKRKAAA----DEEAR 371
Cdd:PTZ00121 1053 DGNHEGKAEAKAHV--GQDEGLKPSYKDFDFDA--KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEakkkAEDAR 1128
                          90       100
                  ....*....|....*....|....*...
gi 340629670  372 KAREA-EAERKRQADAAAKGKQDKDVNV 398
Cdd:PTZ00121 1129 KAEEArKAEDARKAEEARKAEDAKRVEI 1156
PTZ00121 PTZ00121
MAEBL; Provisional
339-394 1.28e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 1.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 340629670  339 QTEEQKKAAEEQRQkaaADaEAKRKAaadEEARKAREA--EAERKRQADAAAKGKQDK 394
Cdd:PTZ00121 1432 KADEAKKKAEEAKK---AD-EAKKKA---EEAKKAEEAkkKAEEAKKADEAKKKAEEA 1482
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
339-396 1.46e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 44.65  E-value: 1.46e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 340629670 339 QTEEQKKAAEEQRQKAAADAEAKR------KAAADEEARKAREAEAERKRQ-ADAAAKGKQDKDV 396
Cdd:COG3064   61 KAEAEQRAAELAAEAAKKLAEAEKaaaeaeKKAAAEKAKAAKEAEAAAAAEkAAAAAEKEKAEEA 125
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
339-395 1.46e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 44.65  E-value: 1.46e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 340629670 339 QTEEQKKAAEEQRQKAAADAEAKRKAAADEEARKAREAEAE----RKRQADAAAKGKQDKD 395
Cdd:COG3064   45 AELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAaaeaEKKAAAEKAKAAKEAE 105
growth_prot_Scy NF041483
polarized growth protein Scy;
336-394 2.05e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 44.82  E-value: 2.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  336 TPPQTEEQKKAAEEQRQKAAADAEAKRKAAADEEARKAREAEAERKR-QADAAAKGKQDK 394
Cdd:NF041483  362 TAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRlRGEAADQAEQLK 421
PTZ00121 PTZ00121
MAEBL; Provisional
339-396 2.75e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 2.75e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 340629670  339 QTEEQKKAAEEQRQKAAADAEAKRKAaadEEARKAREA-EAERKRQADAAAKGKQDKDV 396
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKA---DELKKAEELkKAEEKKKAEEAKKAEEDKNM 1578
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
339-389 3.06e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.30  E-value: 3.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 340629670  339 QTEEQKKAAEEQRQKAAADAEAKrkaaADEEARKAREAEAERKRQADAAAK 389
Cdd:TIGR02794 190 KAEEAKAKAEAAKAKAAAEAAAK----AEAEAAAAAAAEAERKADEAELGD 236
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
341-383 3.39e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 41.56  E-value: 3.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 340629670  341 EEQKKAAEEQRQKAAADAEAKRKAAADEEAR----------KAREaEAERKRQ 383
Cdd:pfam05672  68 EERRREEEERQRKAEEEAEEREQREQEEQERlqkqkeeaeaKARE-EAERQRQ 119
PRK12472 PRK12472
hypothetical protein; Provisional
339-387 3.55e-04

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 43.71  E-value: 3.55e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 340629670 339 QTEEQKKAAEEQRQKAA--------------ADAEAKRKA--AADEEARKAREAEAERKRQADAA 387
Cdd:PRK12472 252 KTDEAKARAEERQQKAAqqaaeaatqldtakADAEAKRAAaaATKEAAKAAAAKKAETAKAATDA 316
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
339-396 3.68e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 43.49  E-value: 3.68e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 340629670 339 QTEEQKKAAEEQRQKAAADAEAKRKAAADEEA----RKAREAEAERKRQADAAAKGKQDKDV 396
Cdd:COG3064   55 EEAREAKAEAEQRAAELAAEAAKKLAEAEKAAaeaeKKAAAEKAKAAKEAEAAAAAEKAAAA 116
PTZ00121 PTZ00121
MAEBL; Provisional
339-394 5.04e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 5.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 340629670  339 QTEEQKKAAEEQR--QKAAADAEAKRKA----AADEEARKAREAEA---ERKRQADAAAKGKQDK 394
Cdd:PTZ00121 1445 KADEAKKKAEEAKkaEEAKKKAEEAKKAdeakKKAEEAKKADEAKKkaeEAKKKADEAKKAAEAK 1509
PTZ00121 PTZ00121
MAEBL; Provisional
341-394 5.30e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 5.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 340629670  341 EEQKKAAEEQRQKAAADAEAKRKAaadEEARKAREA-EAERKRQADAAAKGKQDK 394
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKA---EEAKKADEAkKAEEKKKADELKKAEELK 1558
ps-ssRNAv_Flaviviridae_RdRp cd23178
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Flaviviridae of ...
35-164 6.39e-04

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Flaviviridae of positive-sense single-stranded RNA (+ssRNA) viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Flaviviridae, order Amarillovirales. Flaviviridae, is a family of small, enveloped viruses with RNA genomes of 9-13 kb. Most infect mammals and birds. Many flaviviruses are host-specific and pathogenic, such as hepatitis C virus in the genus Hepacivirus. The majority of known members in the genus Flavivirus are arthropod borne, and many are important human and veterinary pathogens (e.g., yellow fever virus, dengue virus). Virions are typically spherical in shape with a lipid envelope. Virions have a single, small, basic capsid (C) protein and two (genera Flavivirus, Hepacivirus and Pegivirus) or three (genus Pestivirus) envelope proteins. They contain a single, long ORF flanked by 5'- and 3'-terminal non-coding regions, which form specific secondary structures required for genome replication and translation. Translational initiation of genomic RNA is cap dependent in the case of members of the genus Flavivirus. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438028  Cd Length: 284  Bit Score: 42.12  E-value: 6.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  35 FYGGWNQLLEKLPNGW-------VYCDaDGSQFDSSLTPYlinavlDIRL-------SFMEEWDIGERMLMNLYTeiVFT 100
Cdd:cd23178   60 FQYSPNQRVEILRKAWkskkgpmAYSY-DTRCFDSTVTED------DIQVeeeiyqaCSLKEARQAIVSITERLY--VEG 130
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 340629670 101 PIATPDGSVIKKFKGNNSGQPSTVVDNTLMVILAFNYTMLSCGIdsdmidSVCRMFANGDDLLL 164
Cdd:cd23178  131 PMVNSDGQICGRRRCRASGVLTTSAGNT*TCYLK*LAACREAGI------RLPTMLVCGDDCVV 188
PTZ00121 PTZ00121
MAEBL; Provisional
339-424 6.44e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 6.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  339 QTEEQKKAAEEQRQKAaadAEAKRKAaadEEARKAREA-EAERKRQADAAAKGKQDKDVNvgtsgtiavpKLKAMSSKMR 417
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKA---DAAKKKA---EEAKKAAEAaKAEAEAAADEAEAAEEKAEAA----------EKKKEEAKKK 1379

                  ....*..
gi 340629670  418 LPMAKGK 424
Cdd:PTZ00121 1380 ADAAKKK 1386
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
341-394 6.46e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 40.79  E-value: 6.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 340629670  341 EEQKKAAEE--QRQKAAADAEAKRKAAADEEARKAREaEAERKRQADAAAKGKQDK 394
Cdd:pfam05672  47 ELRRRAEEEraRREEEARRLEEERRREEEERQRKAEE-EAEEREQREQEEQERLQK 101
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
331-424 6.47e-04

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 42.66  E-value: 6.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670 331 RVDAGTPPQTEEQK-----KAAEEQRQKAAADAEAKRKAAADEEARKAREAEAERKRQADAAAKGK-----QDKDVNVGT 400
Cdd:PRK07735 111 QKREGTEEVTEEEKaaakaKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKaaalaKQKAAEAGE 190
                         90       100
                 ....*....|....*....|....
gi 340629670 401 SGTIAVPKLKAMSSKMRLPMAKGK 424
Cdd:PRK07735 191 GTEEVTEEEKAKAKAKAAAAAKAK 214
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
339-395 6.79e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 42.72  E-value: 6.79e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 340629670 339 QTEEQKKAAEEQR---QKAAADAEAKRKAAADEEARKAR-------EAEAERKRQADAAAKGKQDKD 395
Cdd:COG3064   74 EAAKKLAEAEKAAaeaEKKAAAEKAKAAKEAEAAAAAEKaaaaaekEKAEEAKRKAEEEAKRKAEEE 140
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
341-392 7.03e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 39.90  E-value: 7.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 340629670  341 EEQKKAAEEQRQKAAADAEAKRKAAADEEARKAREAEAERKRQADAAAKGKQ 392
Cdd:pfam20492  69 ESAEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
PTZ00121 PTZ00121
MAEBL; Provisional
339-394 7.08e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 7.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 340629670  339 QTEEQKKAAEEQRQ----KAAADaEAKRKA----AADEEARKAREA-EAERKRQADAAAKGKQDK 394
Cdd:PTZ00121 1471 KADEAKKKAEEAKKadeaKKKAE-EAKKKAdeakKAAEAKKKADEAkKAEEAKKADEAKKAEEAK 1534
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
338-450 8.28e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 42.33  E-value: 8.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670 338 PQTEEQKKAAEEQ--RQKAAADAEAKRKAAADEEARKAREAEAERKRQAdAAAKGKQDKDVNVGTSGTIAVPKLKAMSSK 415
Cdd:COG3064   95 AEKAKAAKEAEAAaaAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKA-AEAEAAAKAEAEAARAAAAAAAAAAAAAAR 173
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 340629670 416 MRLPMAKGKNILHVEFLLGYKPAQQDISNTRATRA 450
Cdd:COG3064  174 AAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAA 208
PTZ00121 PTZ00121
MAEBL; Provisional
339-394 1.00e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.00e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 340629670  339 QTEEQKKAAEEQRQkaaADaEAKRKAaadEEARKAREA---EAERKRQADAAAKGKQDK 394
Cdd:PTZ00121 1303 KADEAKKKAEEAKK---AD-EAKKKA---EEAKKKADAakkKAEEAKKAAEAAKAEAEA 1354
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
334-424 1.26e-03

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 41.50  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670 334 AGTPPQTEEQK-----KAAEEQRQKAAADAEAKRKA---AADEEARKAREAEAERKRQADAAAKGKQDKDVNVGTSGTIA 405
Cdd:PRK07735  80 EGTEEVTEEEKakakaKAAAAAKAKAAALAKQKREGteeVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEE 159
                         90
                 ....*....|....*....
gi 340629670 406 VPKLKAMSSKMRLPMAKGK 424
Cdd:PRK07735 160 TDKEKAKAKAAAAAKAKAA 178
PTZ00121 PTZ00121
MAEBL; Provisional
339-394 1.35e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 340629670  339 QTEEQKKAAEEQRQKAAADAEAKRKA----AADEEARKAREAEA---ERKRQADAAAKGKQDK 394
Cdd:PTZ00121 1279 KADELKKAEEKKKADEAKKAEEKKKAdeakKKAEEAKKADEAKKkaeEAKKKADAAKKKAEEA 1341
PTZ00121 PTZ00121
MAEBL; Provisional
339-394 1.64e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 340629670  339 QTEEQKKAAEEQRQKA--------AADAEAKRKA----AADEEARKAREAEAERKRQADAAAKGKQDK 394
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAeeakkaaeAAKAEAEAAAdeaeAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
Caldesmon pfam02029
Caldesmon;
341-389 1.68e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.39  E-value: 1.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 340629670  341 EEQKKAAEEQRQKAAaDAEAKRKAAADEEARKAREaEAERKRqADAAAK 389
Cdd:pfam02029 287 EERRKLLEEEEQRRK-QEEAERKLREEEEKRRMKE-EIERRR-AEAAEK 332
Marnaviridae_RdRp cd23195
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Marnaviridae of ...
56-210 1.68e-03

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Marnaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses, in the order Picornavirales; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Marnaviridae, order Picornavirales. Member viruses have a (+)ssRNA genome. They are mono- or dicistronic, have a polyadenylate tail and have conserved motifs for RNA helicase, RdRp, and structural protein domains. The first RNA virus isolated and characterized that infects a marine protist was Heterosigma akashiwo RNA virus (HaRNAV) in the genus Marnavirus, that infects the toxic bloom-forming Raphidophyte alga, Heterosigma akashiwo. Recently, it has undergone a major taxonomic revision and now includes 20 species within 7 genera, which include Bacillarnavirus, Kusarnavirus, Labyrnavirus, Locarnavirus, Marnavirus, Salisharnavirus, and Sogarnavirus. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438045  Cd Length: 310  Bit Score: 40.89  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670  56 DGSQFDSSLTPYLINAVLDIRLSFMEE---WDIGERMLM-NLYTEIVFtPIATPDGSVIKKFKGNNSGQPSTVV----DN 127
Cdd:cd23195   83 DYSKYDKRMSAQLILAAFKILIDIAAKsggYSEEDLKIMrGIATDIAY-PLVDFNGDLIQFFGSNPSGHPLTVIinsiVN 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670 128 TLMVILAFnYTMLSCGIDSDMiDSVCRMFANGDDLLLAVNPDYEYildlfsnhfsdlglnFDFSSRTKdkselwFMSTRG 207
Cdd:cd23195  162 SLYMRYAY-YSLYPEKEVPPF-RDVVALMTYGDDNIMSVSPGYPW---------------FNHTSIAE------FLAKIG 218

                 ...
gi 340629670 208 IKY 210
Cdd:cd23195  219 IKY 221
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
338-474 3.65e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 40.41  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670 338 PQTEEQKKAAEEQRQKAAADAEAKRKAAADEEARKAREAEAERKRQADAAAKGKQDKDVNVGTSGTIAVPKLKAMSSKMR 417
Cdd:COG3064  113 AAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEA 192
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 340629670 418 LPMAKGKNILHVEFLLGYKPAQQDISNTRATRAEFDRWYDAVKNEYEVDDNQMTVIM 474
Cdd:COG3064  193 ADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAE 249
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
339-392 4.19e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 39.86  E-value: 4.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 340629670 339 QTEEQKKAAEEQRQKAAAD----AEAKRKAA-ADEEArkarEAEAERKRqADAAAKGKQ 392
Cdd:COG2268  291 EIELQEKEAEREEAELEADvrkpAEAEKQAAeAEAEA----EAEAIRAK-GLAEAEGKR 344
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
339-424 4.59e-03

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 39.96  E-value: 4.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340629670 339 QTEEQKKAAEEQRQKAAAD--------AEAKRKAAADEEA-----RKAREAEAER---------KRQADAAAKGKQ---D 393
Cdd:PRK07735  30 HGAEISKLEEENREKEKALpknddmtiEEAKRRAAAAAKAkaaalAKQKREGTEEvteeekakaKAKAAAAAKAKAaalA 109
                         90       100       110
                 ....*....|....*....|....*....|.
gi 340629670 394 KDVNVGTSGTIAVPKLKAMSSKMRLPMAKGK 424
Cdd:PRK07735 110 KQKREGTEEVTEEEKAAAKAKAAAAAKAKAA 140
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
341-389 5.00e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 35.71  E-value: 5.00e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 340629670 341 EEQKKAAEEQRQKAAADAEAKRKAA----ADEEARKAREAEAERKRQADAAAK 389
Cdd:cd22249   12 EAQLKKLEEERRKEREEEEKASEELirklQEEEERQRKREREEQLKQDEELAK 64
PRK00247 PRK00247
putative inner membrane protein translocase component YidC; Validated
339-392 9.35e-03

putative inner membrane protein translocase component YidC; Validated


Pssm-ID: 178945 [Multi-domain]  Cd Length: 429  Bit Score: 38.68  E-value: 9.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 340629670 339 QTEEQKKAAEEQRQKAAADaeaKRKAA---ADEEARKAREAEAERKRQADAAAKGKQ 392
Cdd:PRK00247 334 KTRTAEKNEAKARKKEIAQ---KRRAAereINREARQERAAAMARARARRAAVKAKK 387
 
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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