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Conserved domains on  [gi|332010300|gb|AED97683|]
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Ubiquitin carboxyl-terminal hydrolase family protein [Arabidopsis thaliana]

Protein Classification

PORR domain-containing protein( domain architecture ID 10571663)

PORR (plant organelle RNA recognition) domain-containing protein similar to Arabidopsis thaliana protein ROOT PRIMORDIUM DEFECTIVE 1 that is involved in pre-arranging the maintenance of the active cell proliferation during root primordium development

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PORR pfam11955
Plant organelle RNA recognition domain; This family, which was previously known as DUF860, has ...
60-393 1.61e-121

Plant organelle RNA recognition domain; This family, which was previously known as DUF860, has been shown to be a component of group II intron ribonucleoprotein particles in maize chloroplasts. The domain is required for the splicing of the introns with which it associates, and promotes splicing in the context of a heterodimer with the RNase III-domain protein RNC1. All of the members are predicted to localize to mitochondria or chloroplasts. It seems likely that most PORR proteins function in organellar RNA metabolism.


:

Pssm-ID: 432218  Cd Length: 328  Bit Score: 358.73  E-value: 1.61e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332010300   60 VRSPSLDRHVVKQNRVRFVQKLNTLLLSKPKHYIPIEILYKCRSYLCIenPLAILSMIRRYPTIFELFTTPTPHLPmnat 139
Cdd:pfam11955   1 VRDPGLDKAVEREKKLRAVLRLKDLILSEPSHVLPLRDLSKLRRQLGL--KRKVLRFLRKYPSIFEEFRHPDGPLP---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332010300  140 kplsqlCVRLTSAASSLAMQELNLKSEISDKLATKLQKLLMLSSHRRLLLSKLVHIAPDFGFPPNFRSRLCNDYPDKFKT 219
Cdd:pfam11955  75 ------WVRLTPEALDLLEEEERVLEEHEPDLVERLRKLLMMSKDRRLPLSKIDHLKWDLGLPDDFRDSLVPKYPDYFRL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332010300  220 VDTS-YGRALELVSSDPELANQMP----SPEVDRGLIVDRPLKFKrLNLRRGLNLKRRHQGFLIKFRESPDVCPYKMSSD 294
Cdd:pfam11955 149 VDTPdGGRGLELVSWDPELAVSALekrrEYREKGEDKGDGPLAFP-LKFPKGFRLKKKYREWLEEWQKLPYVSPYEDASH 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332010300  295 yLASESIEAEKRACAVVREVLGLTVEKRTLIDHLTHFRKEFSLPNKLRDLIVRHPELFYVSIKGMRDSVFLVEAYnDNGD 374
Cdd:pfam11955 228 -LDPRSDEAEKRAVGVLHELLSLTVEKRTEVDHLSHFRKEFGLPQKFRKLLLRHPGIFYLSLKGKTHTVFLREAY-DRGE 305
                         330
                  ....*....|....*....
gi 332010300  375 LLDKDERLVIRERLIDLIQ 393
Cdd:pfam11955 306 LIEKHPLLVIREKYLELML 324
 
Name Accession Description Interval E-value
PORR pfam11955
Plant organelle RNA recognition domain; This family, which was previously known as DUF860, has ...
60-393 1.61e-121

Plant organelle RNA recognition domain; This family, which was previously known as DUF860, has been shown to be a component of group II intron ribonucleoprotein particles in maize chloroplasts. The domain is required for the splicing of the introns with which it associates, and promotes splicing in the context of a heterodimer with the RNase III-domain protein RNC1. All of the members are predicted to localize to mitochondria or chloroplasts. It seems likely that most PORR proteins function in organellar RNA metabolism.


Pssm-ID: 432218  Cd Length: 328  Bit Score: 358.73  E-value: 1.61e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332010300   60 VRSPSLDRHVVKQNRVRFVQKLNTLLLSKPKHYIPIEILYKCRSYLCIenPLAILSMIRRYPTIFELFTTPTPHLPmnat 139
Cdd:pfam11955   1 VRDPGLDKAVEREKKLRAVLRLKDLILSEPSHVLPLRDLSKLRRQLGL--KRKVLRFLRKYPSIFEEFRHPDGPLP---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332010300  140 kplsqlCVRLTSAASSLAMQELNLKSEISDKLATKLQKLLMLSSHRRLLLSKLVHIAPDFGFPPNFRSRLCNDYPDKFKT 219
Cdd:pfam11955  75 ------WVRLTPEALDLLEEEERVLEEHEPDLVERLRKLLMMSKDRRLPLSKIDHLKWDLGLPDDFRDSLVPKYPDYFRL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332010300  220 VDTS-YGRALELVSSDPELANQMP----SPEVDRGLIVDRPLKFKrLNLRRGLNLKRRHQGFLIKFRESPDVCPYKMSSD 294
Cdd:pfam11955 149 VDTPdGGRGLELVSWDPELAVSALekrrEYREKGEDKGDGPLAFP-LKFPKGFRLKKKYREWLEEWQKLPYVSPYEDASH 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332010300  295 yLASESIEAEKRACAVVREVLGLTVEKRTLIDHLTHFRKEFSLPNKLRDLIVRHPELFYVSIKGMRDSVFLVEAYnDNGD 374
Cdd:pfam11955 228 -LDPRSDEAEKRAVGVLHELLSLTVEKRTEVDHLSHFRKEFGLPQKFRKLLLRHPGIFYLSLKGKTHTVFLREAY-DRGE 305
                         330
                  ....*....|....*....
gi 332010300  375 LLDKDERLVIRERLIDLIQ 393
Cdd:pfam11955 306 LIEKHPLLVIREKYLELML 324
 
Name Accession Description Interval E-value
PORR pfam11955
Plant organelle RNA recognition domain; This family, which was previously known as DUF860, has ...
60-393 1.61e-121

Plant organelle RNA recognition domain; This family, which was previously known as DUF860, has been shown to be a component of group II intron ribonucleoprotein particles in maize chloroplasts. The domain is required for the splicing of the introns with which it associates, and promotes splicing in the context of a heterodimer with the RNase III-domain protein RNC1. All of the members are predicted to localize to mitochondria or chloroplasts. It seems likely that most PORR proteins function in organellar RNA metabolism.


Pssm-ID: 432218  Cd Length: 328  Bit Score: 358.73  E-value: 1.61e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332010300   60 VRSPSLDRHVVKQNRVRFVQKLNTLLLSKPKHYIPIEILYKCRSYLCIenPLAILSMIRRYPTIFELFTTPTPHLPmnat 139
Cdd:pfam11955   1 VRDPGLDKAVEREKKLRAVLRLKDLILSEPSHVLPLRDLSKLRRQLGL--KRKVLRFLRKYPSIFEEFRHPDGPLP---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332010300  140 kplsqlCVRLTSAASSLAMQELNLKSEISDKLATKLQKLLMLSSHRRLLLSKLVHIAPDFGFPPNFRSRLCNDYPDKFKT 219
Cdd:pfam11955  75 ------WVRLTPEALDLLEEEERVLEEHEPDLVERLRKLLMMSKDRRLPLSKIDHLKWDLGLPDDFRDSLVPKYPDYFRL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332010300  220 VDTS-YGRALELVSSDPELANQMP----SPEVDRGLIVDRPLKFKrLNLRRGLNLKRRHQGFLIKFRESPDVCPYKMSSD 294
Cdd:pfam11955 149 VDTPdGGRGLELVSWDPELAVSALekrrEYREKGEDKGDGPLAFP-LKFPKGFRLKKKYREWLEEWQKLPYVSPYEDASH 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332010300  295 yLASESIEAEKRACAVVREVLGLTVEKRTLIDHLTHFRKEFSLPNKLRDLIVRHPELFYVSIKGMRDSVFLVEAYnDNGD 374
Cdd:pfam11955 228 -LDPRSDEAEKRAVGVLHELLSLTVEKRTEVDHLSHFRKEFGLPQKFRKLLLRHPGIFYLSLKGKTHTVFLREAY-DRGE 305
                         330
                  ....*....|....*....
gi 332010300  375 LLDKDERLVIRERLIDLIQ 393
Cdd:pfam11955 306 LIEKHPLLVIREKYLELML 324
 
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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