NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|134073772|emb|CAM72510|]
View 

RNA editing comple protein MP63 [Leishmania infantum JPCM5]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 10621451)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

CATH:  3.30.160.60
Gene Ontology:  GO:0003677|GO:0008270|GO:0003700
PubMed:  11179890|12665246|11361095|10940247
SCOP:  4003583

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 142-625 2.13e-156

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


:

Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 456.25  E-value: 2.13e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 142 APKPLHQAEREVPSLVMEKMLSVWDDTGVKRMGDQFVHSSMVMRVFAARPSDGAEPLYGVMNPEGENPFEGGPYPPDAGG 221
Cdd:cd23959    1 APKPLHQPDREVPALVMEEMLGVWDKIGVKRLGGQFVHSSMVMKVFAARPSDQEEPLYGAVSPEGENPFDGPGLVTASTV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 222 PLTKN-EVNFYSIGIGDAFALACGESFGPLRPARCPNPFLRKLAKDAAKTA---PRVGLAEQQTAPVTPFGQLPMFGQTP 297
Cdd:cd23959   81 SDCYVgNANFYEVDMSDAFAMAPDESLGPFRAARVPNPFSASSSTQRETHKtaqVAPPKAEPQTAPVTPFGQLPMFGQHP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 298 SPATTPAPSAAEEPSTTIS-VVSSPFAAGandspfagttdfpfaGQGLSPFgslkkpadqaaaepgiaarSAASFEAPas 376
Cdd:cd23959  161 PPAKPLPAAAAAQQSSASPgEVASPFASG---------------TVSASPF-------------------ATATDTAP-- 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 377 pfvDAASALTPSPFAAAPSPFtesssaaapyaardaaavaggaeahdAVFFSSFSASSASRPAEVGPTATHVCTVCKKSF 456
Cdd:cd23959  205 ---SSGAPDGFPAEASAPSPF--------------------------AAPASAASFPAAPVANGEAATPTHACTICGKAF 255

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 457 STYDGLRMHSKAKHGEELPKELRNGRRNeKREVPDLPAFIPSPVDLTMTSPFGSSAQRSA-WTEVELKPYAQSVSNITVA 535
Cdd:cd23959  256 STHEGLRMHSKAKHGVELEKAKTAKRKK-RRSVPDLPAYIPSPVDLSMTSPFGSSSATNAsWIETELTPHAQAVSNITVA 334

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 536 GRVLDSEVSSDGALLLSLFVPDSSESESEVIPVRCSSAAFRTLGRTLVYGDLVFACGSLRVLPFTDKKTQKTYSSAVVHV 615
Cdd:cd23959  335 GRVLDVEQSDEGSLLVTVFVSGEASGEAETITVRCSGEASKIVADTVKRDDVVFACGTLRLLPVHDDSTNKYYVSPVVHV 414

                        490
                 ....*....|
gi 134073772 616 GLPTGMIAKL 625
Cdd:cd23959  415 SSPTGVIAKI 424
KREPA super family cl49620
Kinetoplastid RNA Editing Protein A (KREPA); The KREPA 1-6 (TbMP81, 63, 42, 24, 19, and 18, ...
 49-197 2.30e-09

Kinetoplastid RNA Editing Protein A (KREPA); The KREPA 1-6 (TbMP81, 63, 42, 24, 19, and 18, respectively) proteins are components of the RNA editing complex of parasitic protozoans such as Trypanosoma and Leishmania species. These parasites have a uniquely organized mitochondrial genome, the kinetoplast. Most kinetoplast-transcribed mRNAs are cryptic and encode multiple subunits for the electron transport chain following maturation through a uridine insertion/deletion process called RNA editing. KREPAs participate in the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. The editosome, a high molecular mass enzyme complex, carries out the reaction with the help of critical enzymes and structural proteins. Five related editosome proteins KREPA1 (TbMP81), KREPA2 (TbMP63), KREPA3 (TbMP42), KREPA4 (TbMP24), KREPA5 (TbMP19), and KREPA6 (TbMP18) play critical roles in the structure and auxiliary functions of the editing process without any predicted catalytic function. The KREPA1, KREPA2, and KREPA3 proteins contain C2H2 zinc finger motifs and KREPA4 and KREPA6, contain RNA-binding domains but all have a conserved C-terminal sequences that resemble an oligonucleotide-binding (OB)-fold domain. Thus, this group of five proteins is likely to be involved in protein-protein and/or protein-RNA interactions. RNA editing is crucial for the parasite's survival in both its bloodstream and procyclic form life cycle stages which allows the parasite to adapt to its environment and maintain its viability.


The actual alignment was detected with superfamily member cd23512:

Pssm-ID: 483960  Cd Length: 449  Bit Score: 59.80  E-value: 2.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772  49 LGAVRNQSAVPDRRFHCSVCKKSFRLEMAAKLHLQQVHSGEGTVEAGAGPGQGEdqALQTPVGVFRNAPPQAPTVVTAIV 128
Cdd:cd23512   85 LTVARRLPVDPTMRFHCSACGKAFRLRFSAEHHVKLRHPSDAKAAVVEGPGPGE--IIGSAPRVSAVKVPYNKTATLSLP 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 129 PDtheraarrekpapkplhqaerevpSLVMEKMLSVWDDTGVKR-------MGDQFVHSSMV----------MRVFAARP 191
Cdd:cd23512  163 SD------------------------ELIDELLKDVWDDVALARddipksnDGNFFIPFVLVvegtadnrkeLEEAAARP 218

                        170
                 ....*....|.
gi 134073772 192 S-----DGAEP 197
Cdd:cd23512  219 TaratpEGAAP 229
 
Name Accession Description Interval E-value
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 142-625 2.13e-156

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 456.25  E-value: 2.13e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 142 APKPLHQAEREVPSLVMEKMLSVWDDTGVKRMGDQFVHSSMVMRVFAARPSDGAEPLYGVMNPEGENPFEGGPYPPDAGG 221
Cdd:cd23959    1 APKPLHQPDREVPALVMEEMLGVWDKIGVKRLGGQFVHSSMVMKVFAARPSDQEEPLYGAVSPEGENPFDGPGLVTASTV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 222 PLTKN-EVNFYSIGIGDAFALACGESFGPLRPARCPNPFLRKLAKDAAKTA---PRVGLAEQQTAPVTPFGQLPMFGQTP 297
Cdd:cd23959   81 SDCYVgNANFYEVDMSDAFAMAPDESLGPFRAARVPNPFSASSSTQRETHKtaqVAPPKAEPQTAPVTPFGQLPMFGQHP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 298 SPATTPAPSAAEEPSTTIS-VVSSPFAAGandspfagttdfpfaGQGLSPFgslkkpadqaaaepgiaarSAASFEAPas 376
Cdd:cd23959  161 PPAKPLPAAAAAQQSSASPgEVASPFASG---------------TVSASPF-------------------ATATDTAP-- 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 377 pfvDAASALTPSPFAAAPSPFtesssaaapyaardaaavaggaeahdAVFFSSFSASSASRPAEVGPTATHVCTVCKKSF 456
Cdd:cd23959  205 ---SSGAPDGFPAEASAPSPF--------------------------AAPASAASFPAAPVANGEAATPTHACTICGKAF 255

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 457 STYDGLRMHSKAKHGEELPKELRNGRRNeKREVPDLPAFIPSPVDLTMTSPFGSSAQRSA-WTEVELKPYAQSVSNITVA 535
Cdd:cd23959  256 STHEGLRMHSKAKHGVELEKAKTAKRKK-RRSVPDLPAYIPSPVDLSMTSPFGSSSATNAsWIETELTPHAQAVSNITVA 334

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 536 GRVLDSEVSSDGALLLSLFVPDSSESESEVIPVRCSSAAFRTLGRTLVYGDLVFACGSLRVLPFTDKKTQKTYSSAVVHV 615
Cdd:cd23959  335 GRVLDVEQSDEGSLLVTVFVSGEASGEAETITVRCSGEASKIVADTVKRDDVVFACGTLRLLPVHDDSTNKYYVSPVVHV 414

                        490
                 ....*....|
gi 134073772 616 GLPTGMIAKL 625
Cdd:cd23959  415 SSPTGVIAKI 424
KREPA1 cd23512
Kinetoplastid RNA Editing Protein A1 (KREPA1); The KREPA1 (TbMP81) protein is a crucial ...
 49-197 2.30e-09

Kinetoplastid RNA Editing Protein A1 (KREPA1); The KREPA1 (TbMP81) protein is a crucial component of the parasitic protozoan's KREPA RNA editing complex. Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. However, the C-terminal zinc-finger domain in KREPA1 has additional amino acids. KREPA1 is involved in the insertion sub-complex of editing activities and interacts with KREPA6 of the 20S editosome core complex. When KREPA1 is down-regulated, insertion editing is preferentially inhibited.


Pssm-ID: 467777  Cd Length: 449  Bit Score: 59.80  E-value: 2.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772  49 LGAVRNQSAVPDRRFHCSVCKKSFRLEMAAKLHLQQVHSGEGTVEAGAGPGQGEdqALQTPVGVFRNAPPQAPTVVTAIV 128
Cdd:cd23512   85 LTVARRLPVDPTMRFHCSACGKAFRLRFSAEHHVKLRHPSDAKAAVVEGPGPGE--IIGSAPRVSAVKVPYNKTATLSLP 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 129 PDtheraarrekpapkplhqaerevpSLVMEKMLSVWDDTGVKR-------MGDQFVHSSMV----------MRVFAARP 191
Cdd:cd23512  163 SD------------------------ELIDELLKDVWDDVALARddipksnDGNFFIPFVLVvegtadnrkeLEEAAARP 218

                        170
                 ....*....|.
gi 134073772 192 S-----DGAEP 197
Cdd:cd23512  219 TaratpEGAAP 229
zf-C2H2_6 pfam13912
C2H2-type zinc finger;
447-472 1.18e-06

C2H2-type zinc finger;


Pssm-ID: 433576  Cd Length: 27  Bit Score: 44.93  E-value: 1.18e-06
                          10        20
                  ....*....|....*....|....*.
gi 134073772  447 HVCTVCKKSFSTYDGLRMHSKAKHGE 472
Cdd:pfam13912   2 HECSECGKSFPSYQALGGHKKSHRKE 27
PHA03247 PHA03247
large tegument protein UL36; Provisional
 252-396 2.84e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772  252 PARCPNPFLRKLAKDAAKTAPRVGLAEQQTAPVTPFGQLPmfgqtPSPATTPAPSAAEEPSTTISVVSSPFAAGANDSPF 331
Cdd:PHA03247 2702 PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAP-----PAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPA 2776

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134073772  332 AGttdfpfagqglsPFGSLKKPADQAAAEPGIAARSAASFEAPASPFVDAASALTPSPFAAAPSP 396
Cdd:PHA03247 2777 AG------------PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP 2829
 
Name Accession Description Interval E-value
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 142-625 2.13e-156

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 456.25  E-value: 2.13e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 142 APKPLHQAEREVPSLVMEKMLSVWDDTGVKRMGDQFVHSSMVMRVFAARPSDGAEPLYGVMNPEGENPFEGGPYPPDAGG 221
Cdd:cd23959    1 APKPLHQPDREVPALVMEEMLGVWDKIGVKRLGGQFVHSSMVMKVFAARPSDQEEPLYGAVSPEGENPFDGPGLVTASTV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 222 PLTKN-EVNFYSIGIGDAFALACGESFGPLRPARCPNPFLRKLAKDAAKTA---PRVGLAEQQTAPVTPFGQLPMFGQTP 297
Cdd:cd23959   81 SDCYVgNANFYEVDMSDAFAMAPDESLGPFRAARVPNPFSASSSTQRETHKtaqVAPPKAEPQTAPVTPFGQLPMFGQHP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 298 SPATTPAPSAAEEPSTTIS-VVSSPFAAGandspfagttdfpfaGQGLSPFgslkkpadqaaaepgiaarSAASFEAPas 376
Cdd:cd23959  161 PPAKPLPAAAAAQQSSASPgEVASPFASG---------------TVSASPF-------------------ATATDTAP-- 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 377 pfvDAASALTPSPFAAAPSPFtesssaaapyaardaaavaggaeahdAVFFSSFSASSASRPAEVGPTATHVCTVCKKSF 456
Cdd:cd23959  205 ---SSGAPDGFPAEASAPSPF--------------------------AAPASAASFPAAPVANGEAATPTHACTICGKAF 255

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 457 STYDGLRMHSKAKHGEELPKELRNGRRNeKREVPDLPAFIPSPVDLTMTSPFGSSAQRSA-WTEVELKPYAQSVSNITVA 535
Cdd:cd23959  256 STHEGLRMHSKAKHGVELEKAKTAKRKK-RRSVPDLPAYIPSPVDLSMTSPFGSSSATNAsWIETELTPHAQAVSNITVA 334

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 536 GRVLDSEVSSDGALLLSLFVPDSSESESEVIPVRCSSAAFRTLGRTLVYGDLVFACGSLRVLPFTDKKTQKTYSSAVVHV 615
Cdd:cd23959  335 GRVLDVEQSDEGSLLVTVFVSGEASGEAETITVRCSGEASKIVADTVKRDDVVFACGTLRLLPVHDDSTNKYYVSPVVHV 414

                        490
                 ....*....|
gi 134073772 616 GLPTGMIAKL 625
Cdd:cd23959  415 SSPTGVIAKI 424
KREPA1 cd23512
Kinetoplastid RNA Editing Protein A1 (KREPA1); The KREPA1 (TbMP81) protein is a crucial ...
 49-197 2.30e-09

Kinetoplastid RNA Editing Protein A1 (KREPA1); The KREPA1 (TbMP81) protein is a crucial component of the parasitic protozoan's KREPA RNA editing complex. Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. However, the C-terminal zinc-finger domain in KREPA1 has additional amino acids. KREPA1 is involved in the insertion sub-complex of editing activities and interacts with KREPA6 of the 20S editosome core complex. When KREPA1 is down-regulated, insertion editing is preferentially inhibited.


Pssm-ID: 467777  Cd Length: 449  Bit Score: 59.80  E-value: 2.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772  49 LGAVRNQSAVPDRRFHCSVCKKSFRLEMAAKLHLQQVHSGEGTVEAGAGPGQGEdqALQTPVGVFRNAPPQAPTVVTAIV 128
Cdd:cd23512   85 LTVARRLPVDPTMRFHCSACGKAFRLRFSAEHHVKLRHPSDAKAAVVEGPGPGE--IIGSAPRVSAVKVPYNKTATLSLP 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 129 PDtheraarrekpapkplhqaerevpSLVMEKMLSVWDDTGVKR-------MGDQFVHSSMV----------MRVFAARP 191
Cdd:cd23512  163 SD------------------------ELIDELLKDVWDDVALARddipksnDGNFFIPFVLVvegtadnrkeLEEAAARP 218

                        170
                 ....*....|.
gi 134073772 192 S-----DGAEP 197
Cdd:cd23512  219 TaratpEGAAP 229
zf-C2H2_6 pfam13912
C2H2-type zinc finger;
447-472 1.18e-06

C2H2-type zinc finger;


Pssm-ID: 433576  Cd Length: 27  Bit Score: 44.93  E-value: 1.18e-06
                          10        20
                  ....*....|....*....|....*.
gi 134073772  447 HVCTVCKKSFSTYDGLRMHSKAKHGE 472
Cdd:pfam13912   2 HECSECGKSFPSYQALGGHKKSHRKE 27
KREPA cd23514
Kinetoplastid RNA Editing Protein A (KREPA); The KREPA 1-6 (TbMP81, 63, 42, 24, 19, and 18, ...
 530-624 1.87e-05

Kinetoplastid RNA Editing Protein A (KREPA); The KREPA 1-6 (TbMP81, 63, 42, 24, 19, and 18, respectively) proteins are components of the RNA editing complex of parasitic protozoans such as Trypanosoma and Leishmania species. These parasites have a uniquely organized mitochondrial genome, the kinetoplast. Most kinetoplast-transcribed mRNAs are cryptic and encode multiple subunits for the electron transport chain following maturation through a uridine insertion/deletion process called RNA editing. KREPAs participate in the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. The editosome, a high molecular mass enzyme complex, carries out the reaction with the help of critical enzymes and structural proteins. Five related editosome proteins KREPA1 (TbMP81), KREPA2 (TbMP63), KREPA3 (TbMP42), KREPA4 (TbMP24), KREPA5 (TbMP19), and KREPA6 (TbMP18) play critical roles in the structure and auxiliary functions of the editing process without any predicted catalytic function. The KREPA1, KREPA2, and KREPA3 proteins contain C2H2 zinc finger motifs and KREPA4 and KREPA6, contain RNA-binding domains but all have a conserved C-terminal sequences that resemble an oligonucleotide-binding (OB)-fold domain. Thus, this group of five proteins is likely to be involved in protein-protein and/or protein-RNA interactions. RNA editing is crucial for the parasite's survival in both its bloodstream and procyclic form life cycle stages which allows the parasite to adapt to its environment and maintain its viability.


Pssm-ID: 467779  Cd Length: 109  Bit Score: 43.94  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772 530 SNITVAGRVLDSE---VSSDGALLLSLFV----PDSSESESEV----IPVRC--SSAAFRTLGRTLVYGDLVFACGSLRV 596
Cdd:cd23514    1 NNVTLVGVVHDIQmgfLGEDAVTQFTLTVtsedPTKETVEDQLekehHTVRCfgDEDYSAAVKETVKEGCIVLVTGRLRL 80

                         90       100
                 ....*....|....*....|....*...
gi 134073772 597 LPFTDKKTQKTYSSAVVHVGLPTGMIAK 624
Cdd:cd23514   81 EPQYEPSTNKLYKFPCIQVEPPTGSVAV 108
PHA03247 PHA03247
large tegument protein UL36; Provisional
 252-396 2.84e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134073772  252 PARCPNPFLRKLAKDAAKTAPRVGLAEQQTAPVTPFGQLPmfgqtPSPATTPAPSAAEEPSTTISVVSSPFAAGANDSPF 331
Cdd:PHA03247 2702 PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAP-----PAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPA 2776

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 134073772  332 AGttdfpfagqglsPFGSLKKPADQAAAEPGIAARSAASFEAPASPFVDAASALTPSPFAAAPSP 396
Cdd:PHA03247 2777 AG------------PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP 2829
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH