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Conserved domains on  [gi|19921138|ref|NP_609495|]
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uncharacterized protein Dmel_CG4751 [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPN_2A_DUB cd08067
Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase; This family includes histone H2A ...
 278-463 3.95e-93

Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase; This family includes histone H2A deubiquitinase (Histone H2A DUB;MYSM1; myb-like, SWIRM and MPN domains 1; 2ADUB; 2A-DUB; KIAA19152ADUB, or KIAA1915/MYSM1), a member of JAMM/MPN+ deubiquitinases (DUBs), with possible Zn2+-dependent ubiquitin isopeptidase activity. It contains the SWIRM (Swi3p, Rsc8p and Moira), and SANT (SWI-SNF, ADA N-CoR, TFIIIB)/Myb domains; the SANT, but not the SWIRM, domain can bind directly to DNA. 2A-DUB is specific for monoubiquitinated H2A (uH2A), regulating transcription by coordinating histone acetylation and deubiquitination, and destabilizing the association of linker histone H1 with nucleosomes. 2A-DUB interacts with p/CAF (p300/CBP-associated factor) in a co-regulatory protein complex, where the status of acetylation of nucleosomal histones modulates its deubiquitinase activity. 2A-DUB is a positive regulator of androgen receptor (AR) transactivation activity on a reporter gene; it participates in transcriptional regulation events in androgen receptor-dependent gene activation. In prostate tumors, the levels of uH2A are dramatically decreased, thus 2A-DUB serving as a cancer-related marker.


:

Pssm-ID: 163698 [Multi-domain]  Cd Length: 187  Bit Score: 298.03  E-value: 3.95e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138  278 KLQPFLITVNSSALLLADFHCHLTVREVCGYLGGTWDMNTHTLSITKTYPCRS--TRFDRQRAGEVERDIQKMMIQDQLL 355
Cdd:cd08067    1 KIQPFKVTVSSNALLLMDFHCHLTTSEVIGYLGGTWDPNTQNLTILQAFPCRSrlTGLDCEMDPVSETEIRESLESRGLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138  356 LVGWYHSHPKFQAEPTLRDCDAQLDYQIKMRGaSDLTYTPCVSLIISPYYDENPTLESVVKCIWIVPPNENRqSMEYGRP 435
Cdd:cd08067   81 VVGWYHSHPTFPPNPSLRDIDTQLDYQIMFKG-SDSGYEPCVGLICSPYDRRNSTPESQITCFWVMPPPENR-PNEYGVP 158

                        170       180
                 ....*....|....*....|....*...
gi 19921138  436 MLMQYSVLPDKEIPEEVRSEIQLCVDYY 463
Cdd:cd08067  159 MLMSYTVSQDEFLTQDVLKELRWLVEFY 186
RAMA pfam18755
Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with ...
 124-220 6.99e-37

Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with restriction enzymes across prokaryotes and fused to JAB deubiquitinases, and chromatin proteins in a wide range of eukaryotes. The domain is predicted to function as a modified-DNA reader domain.


:

Pssm-ID: 465856  Cd Length: 108  Bit Score: 134.74  E-value: 6.99e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138    124 TGRTVTLQTLMAANVLQPGLGLMTIEYLGQKFVGDLLADGKIKShETETIFLTPSAWAMHCKRiinpDKKSGCGWASVKY 203
Cdd:pfam18755   15 TGRRVTLQDLLEAGLLQPGEGLLSIEYKGQKHRADLLADGKIRL-EDGQIFASPSAWAKHVKR----GKKSGNGWASWKY 89

                           90
                   ....*....|....*...
gi 19921138    204 -KGKKLDAYKNTYLRKCA 220
Cdd:pfam18755   90 sKGKKLDDLRAELLKKVA 107
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 616-741 2.20e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.10  E-value: 2.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138   616 PLATPNPTSLPPVLPNLGAPVLPATPSQLLPPQVPAVTAPPAITPAVTTSaLTSALNASPRDSPITIQSNSASPAKFEVP 695
Cdd:PHA03247 2741 PPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS-LSESRESLPSPWDPADPPAAVLAPAAALP 2819

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 19921138   696 VRASPSPAKSDTSSHASTsrtrnSPAPSPGKFSVS-----------DIARNSPSITP 741
Cdd:PHA03247 2820 PAASPAGPLPPPTSAQPT-----APPPPPGPPPPSlplggsvapggDVRRRPPSRSP 2871
 
Name Accession Description Interval E-value
MPN_2A_DUB cd08067
Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase; This family includes histone H2A ...
 278-463 3.95e-93

Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase; This family includes histone H2A deubiquitinase (Histone H2A DUB;MYSM1; myb-like, SWIRM and MPN domains 1; 2ADUB; 2A-DUB; KIAA19152ADUB, or KIAA1915/MYSM1), a member of JAMM/MPN+ deubiquitinases (DUBs), with possible Zn2+-dependent ubiquitin isopeptidase activity. It contains the SWIRM (Swi3p, Rsc8p and Moira), and SANT (SWI-SNF, ADA N-CoR, TFIIIB)/Myb domains; the SANT, but not the SWIRM, domain can bind directly to DNA. 2A-DUB is specific for monoubiquitinated H2A (uH2A), regulating transcription by coordinating histone acetylation and deubiquitination, and destabilizing the association of linker histone H1 with nucleosomes. 2A-DUB interacts with p/CAF (p300/CBP-associated factor) in a co-regulatory protein complex, where the status of acetylation of nucleosomal histones modulates its deubiquitinase activity. 2A-DUB is a positive regulator of androgen receptor (AR) transactivation activity on a reporter gene; it participates in transcriptional regulation events in androgen receptor-dependent gene activation. In prostate tumors, the levels of uH2A are dramatically decreased, thus 2A-DUB serving as a cancer-related marker.


Pssm-ID: 163698 [Multi-domain]  Cd Length: 187  Bit Score: 298.03  E-value: 3.95e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138  278 KLQPFLITVNSSALLLADFHCHLTVREVCGYLGGTWDMNTHTLSITKTYPCRS--TRFDRQRAGEVERDIQKMMIQDQLL 355
Cdd:cd08067    1 KIQPFKVTVSSNALLLMDFHCHLTTSEVIGYLGGTWDPNTQNLTILQAFPCRSrlTGLDCEMDPVSETEIRESLESRGLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138  356 LVGWYHSHPKFQAEPTLRDCDAQLDYQIKMRGaSDLTYTPCVSLIISPYYDENPTLESVVKCIWIVPPNENRqSMEYGRP 435
Cdd:cd08067   81 VVGWYHSHPTFPPNPSLRDIDTQLDYQIMFKG-SDSGYEPCVGLICSPYDRRNSTPESQITCFWVMPPPENR-PNEYGVP 158

                        170       180
                 ....*....|....*....|....*...
gi 19921138  436 MLMQYSVLPDKEIPEEVRSEIQLCVDYY 463
Cdd:cd08067  159 MLMSYTVSQDEFLTQDVLKELRWLVEFY 186
RAMA pfam18755
Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with ...
 124-220 6.99e-37

Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with restriction enzymes across prokaryotes and fused to JAB deubiquitinases, and chromatin proteins in a wide range of eukaryotes. The domain is predicted to function as a modified-DNA reader domain.


Pssm-ID: 465856  Cd Length: 108  Bit Score: 134.74  E-value: 6.99e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138    124 TGRTVTLQTLMAANVLQPGLGLMTIEYLGQKFVGDLLADGKIKShETETIFLTPSAWAMHCKRiinpDKKSGCGWASVKY 203
Cdd:pfam18755   15 TGRRVTLQDLLEAGLLQPGEGLLSIEYKGQKHRADLLADGKIRL-EDGQIFASPSAWAKHVKR----GKKSGNGWASWKY 89

                           90
                   ....*....|....*...
gi 19921138    204 -KGKKLDAYKNTYLRKCA 220
Cdd:pfam18755   90 sKGKKLDDLRAELLKKVA 107
Rri1 COG1310
Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif ...
 303-402 1.41e-07

Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440921  Cd Length: 127  Bit Score: 51.84  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138  303 REVCGYLGGTWDMNTHtlsITKTYPCRSTRFDRQR----AGEVERDIQKMMIQDQLLLVGWYHSHPKFQAEPTLRDcdaq 378
Cdd:COG1310   22 EECCGLLLGKGGGDKR---VTRVYPARNVAESPETrfeiDPEDLLAAEREARERGLEIVGIYHSHPDGPAYPSETD---- 94

                         90       100
                 ....*....|....*....|....
gi 19921138  379 ldyqikMRGAsdlTYTPCVSLIIS 402
Cdd:COG1310   95 ------RAQA---AWPGLPYLIVS 109
PHA03247 PHA03247
large tegument protein UL36; Provisional
 616-741 2.20e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.10  E-value: 2.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138   616 PLATPNPTSLPPVLPNLGAPVLPATPSQLLPPQVPAVTAPPAITPAVTTSaLTSALNASPRDSPITIQSNSASPAKFEVP 695
Cdd:PHA03247 2741 PPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS-LSESRESLPSPWDPADPPAAVLAPAAALP 2819

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 19921138   696 VRASPSPAKSDTSSHASTsrtrnSPAPSPGKFSVS-----------DIARNSPSITP 741
Cdd:PHA03247 2820 PAASPAGPLPPPTSAQPT-----APPPPPGPPPPSlplggsvapggDVRRRPPSRSP 2871
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
 304-395 1.79e-06

JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal subunits. Domain at Mpr1p and Pad1p N-termini. Domain of unknown function.


Pssm-ID: 214573  Cd Length: 135  Bit Score: 48.91  E-value: 1.79e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138     304 EVCGYLGGTWdmNTHTLSITKtypCRSTRFDRQ--RAGEVERDIQKMMIQDQ------LLLVGWYHSHPKFQAEPTLRDC 375
Cdd:smart00232   23 EVCGVLLGKS--NKDRPEVKE---VFAVPNEPQddSVQEYDEDYSHLMDEELkkvnkdLEIVGWYHSHPDESPFPSEVDV 97

                            90       100
                    ....*....|....*....|
gi 19921138     376 DAQLDYQIKMRGASDLTYTP 395
Cdd:smart00232   98 ATHESYQAPWPISVVLIVDP 117
Metaviral_G pfam09595
Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. ...
 651-743 5.28e-04

Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. It is high in serine and threonine suggesting it is highly glycosylated.


Pssm-ID: 462833 [Multi-domain]  Cd Length: 183  Bit Score: 42.63  E-value: 5.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138    651 AVTAPPAITPAVTTSALTSALNASPRDSPITIQSNSASP---AKFEVPVRASPSPAKSDTSSHASTSRTRNSPAPSPGKF 727
Cdd:pfam09595   31 ASLILIGESNKEAALIITDIIDININKQHPEQEHHENPPlneAAKEAPSESEDAPDIDPNNQHPSQDRSEAPPLEPAAKT 110

                           90
                   ....*....|....*.
gi 19921138    728 SVSDIARNSPSITPNK 743
Cdd:pfam09595  111 KPSEHEPANPPDASNR 126
JAB pfam01398
JAB1/Mov34/MPN/PAD-1 ubiquitin protease; Members of this family are found in proteasome ...
 285-382 8.41e-04

JAB1/Mov34/MPN/PAD-1 ubiquitin protease; Members of this family are found in proteasome regulatory subunits, eukaryotic initiation factor 3 (eIF3) subunits and regulators of transcription factors. This family is also known as the MPN domain and PAD-1-like domain, JABP1 domain or JAMM domain. These are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signalling and protein turnover pathways in eukaryotes. Versions of the domain in prokaryotic cognates of the ubiquitin-modification pathway are shown to have a similar role, and the archael protein from Haloferax volcanii is found to cleave ubiquitin-like small archaeal modifier proteins (SAMP1/2) from protein conjugates.


Pssm-ID: 396120  Cd Length: 117  Bit Score: 40.41  E-value: 8.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138    285 TVNSSALLLADFHCHLT-----VREVCGYLGGTWDMNThTLSITKTYPcrsTRF--DRQRAGEVERDIQKMMIQDQLLL- 356
Cdd:pfam01398    5 TVIIHPLVLLKILDHANrggkiGEEVMGVLLGKLEGDG-TIEITNSFA---LPQeeTEDDVNAVALDQEYMENMHEMLKk 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 19921138    357 -------VGWYHSHPKFqAEPTLRDCDAQLDYQ 382
Cdd:pfam01398   81 vnrkeevVGWYHTHPGL-CWLSSVDVHTHALYQ 112
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 609-727 8.22e-03

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: 40.24  E-value: 8.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138  609 NPVRMLSPLATPNPTSLPPVLPNLGAPVLPATPSQLLPpqVPAVTAPPAITPAVTTSALTSALNASPRDSPITIQSNSAS 688
Cdd:cd23959  117 NPFSASSSTQRETHKTAQVAPPKAEPQTAPVTPFGQLP--MFGQHPPPAKPLPAAAAAQQSSASPGEVASPFASGTVSAS 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 19921138  689 PakFEVPVRASPSPAKSDTS----SHASTSRTRNSPAPSPGKF 727
Cdd:cd23959  195 P--FATATDTAPSSGAPDGFpaeaSAPSPFAAPASAASFPAAP 235
 
Name Accession Description Interval E-value
MPN_2A_DUB cd08067
Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase; This family includes histone H2A ...
 278-463 3.95e-93

Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase; This family includes histone H2A deubiquitinase (Histone H2A DUB;MYSM1; myb-like, SWIRM and MPN domains 1; 2ADUB; 2A-DUB; KIAA19152ADUB, or KIAA1915/MYSM1), a member of JAMM/MPN+ deubiquitinases (DUBs), with possible Zn2+-dependent ubiquitin isopeptidase activity. It contains the SWIRM (Swi3p, Rsc8p and Moira), and SANT (SWI-SNF, ADA N-CoR, TFIIIB)/Myb domains; the SANT, but not the SWIRM, domain can bind directly to DNA. 2A-DUB is specific for monoubiquitinated H2A (uH2A), regulating transcription by coordinating histone acetylation and deubiquitination, and destabilizing the association of linker histone H1 with nucleosomes. 2A-DUB interacts with p/CAF (p300/CBP-associated factor) in a co-regulatory protein complex, where the status of acetylation of nucleosomal histones modulates its deubiquitinase activity. 2A-DUB is a positive regulator of androgen receptor (AR) transactivation activity on a reporter gene; it participates in transcriptional regulation events in androgen receptor-dependent gene activation. In prostate tumors, the levels of uH2A are dramatically decreased, thus 2A-DUB serving as a cancer-related marker.


Pssm-ID: 163698 [Multi-domain]  Cd Length: 187  Bit Score: 298.03  E-value: 3.95e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138  278 KLQPFLITVNSSALLLADFHCHLTVREVCGYLGGTWDMNTHTLSITKTYPCRS--TRFDRQRAGEVERDIQKMMIQDQLL 355
Cdd:cd08067    1 KIQPFKVTVSSNALLLMDFHCHLTTSEVIGYLGGTWDPNTQNLTILQAFPCRSrlTGLDCEMDPVSETEIRESLESRGLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138  356 LVGWYHSHPKFQAEPTLRDCDAQLDYQIKMRGaSDLTYTPCVSLIISPYYDENPTLESVVKCIWIVPPNENRqSMEYGRP 435
Cdd:cd08067   81 VVGWYHSHPTFPPNPSLRDIDTQLDYQIMFKG-SDSGYEPCVGLICSPYDRRNSTPESQITCFWVMPPPENR-PNEYGVP 158

                        170       180
                 ....*....|....*....|....*...
gi 19921138  436 MLMQYSVLPDKEIPEEVRSEIQLCVDYY 463
Cdd:cd08067  159 MLMSYTVSQDEFLTQDVLKELRWLVEFY 186
RAMA pfam18755
Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with ...
 124-220 6.99e-37

Restriction Enzyme Adenine Methylase Associated; An alpha+beta fold domain associated with restriction enzymes across prokaryotes and fused to JAB deubiquitinases, and chromatin proteins in a wide range of eukaryotes. The domain is predicted to function as a modified-DNA reader domain.


Pssm-ID: 465856  Cd Length: 108  Bit Score: 134.74  E-value: 6.99e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138    124 TGRTVTLQTLMAANVLQPGLGLMTIEYLGQKFVGDLLADGKIKShETETIFLTPSAWAMHCKRiinpDKKSGCGWASVKY 203
Cdd:pfam18755   15 TGRRVTLQDLLEAGLLQPGEGLLSIEYKGQKHRADLLADGKIRL-EDGQIFASPSAWAKHVKR----GKKSGNGWASWKY 89

                           90
                   ....*....|....*...
gi 19921138    204 -KGKKLDAYKNTYLRKCA 220
Cdd:pfam18755   90 sKGKKLDDLRAELLKKVA 107
MPN_euk_mb cd08058
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 290-410 1.04e-12

Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); eukaryotic; This family contains eukaryotic MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+) domains found in proteins with a variety of functions, including AMSH (associated molecule with the Src homology 3 domain (SH3) of STAM), H2A-DUB (histone H2A deubiquitinase), BRCC36 (BRCA1/BRCA2-containing complex subunit 36), as well as Rpn11 (regulatory particle number 11) and CSN5 (COP9 signalosome complex subunit 5). These domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity. Rpn11 is responsible for substrate deubiquitination during proteasomal degradation. It is essential for maintaining a correct cell cycle and normal mitochondrial morphology and physiology. CSN5 is critical for nuclear export and the degradation of several tumor suppressor proteins, including p53, p27, and Smad4. Over-expression of CSN5 has been implicated in cancer initiation and progression. AMSH specifically cleaves Lys 63 and not Lys48-linked polyubiquitin (poly-Ub) chains, thus facilitating the recycling and subsequent trafficking of receptors to the cell surface. It is involved in the degradation of EGF receptor (EGFR) and possibly other ubiquitinated endocytosed proteins. BRCC36 is part of the BRCA1/BRCA2/BARD1-containing nuclear complex that displays an E3 ubiquitin ligase activity; it is targeted to DNA damage foci after irradiation. 2A-DUB is specific for monoubiquitinated H2A (uH2A), regulating transcription by coordinating histone acetylation and deubiquitination, and destabilizing the association of linker histone H1 with nucleosomes. It is a positive regulator of androgen receptor (AR) transactivation activity on a reporter gene and serves as a marker in prostate tumors.


Pssm-ID: 163689  Cd Length: 119  Bit Score: 66.06  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138  290 ALLLADFHCHLTVR-EVCGYLGGTWDMNTHT---LSITKTYPCrstrfdrQRAGEVERDIQKMMIQDQ--LLLVGWYHSH 363
Cdd:cd08058    2 ALLKMLQHAESNTGiEVMGLLCGELTHNEFTdkhVIVPKQSAG-------PDSCTGENVEELFNVQTGrpLLVVGWYHSH 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 19921138  364 PKFQAEPTLRDCDAQLDYQIKMRGAsdltytpcVSLIISPYYDENPT 410
Cdd:cd08058   75 PTFTAWLSSVDIHTQASYQLMLPEA--------IAIVVSPKHRNKDT 113
Rri1 COG1310
Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif ...
 303-402 1.41e-07

Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440921  Cd Length: 127  Bit Score: 51.84  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138  303 REVCGYLGGTWDMNTHtlsITKTYPCRSTRFDRQR----AGEVERDIQKMMIQDQLLLVGWYHSHPKFQAEPTLRDcdaq 378
Cdd:COG1310   22 EECCGLLLGKGGGDKR---VTRVYPARNVAESPETrfeiDPEDLLAAEREARERGLEIVGIYHSHPDGPAYPSETD---- 94

                         90       100
                 ....*....|....*....|....
gi 19921138  379 ldyqikMRGAsdlTYTPCVSLIIS 402
Cdd:COG1310   95 ------RAQA---AWPGLPYLIVS 109
PHA03247 PHA03247
large tegument protein UL36; Provisional
 616-741 2.20e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.10  E-value: 2.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138   616 PLATPNPTSLPPVLPNLGAPVLPATPSQLLPPQVPAVTAPPAITPAVTTSaLTSALNASPRDSPITIQSNSASPAKFEVP 695
Cdd:PHA03247 2741 PPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS-LSESRESLPSPWDPADPPAAVLAPAAALP 2819

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 19921138   696 VRASPSPAKSDTSSHASTsrtrnSPAPSPGKFSVS-----------DIARNSPSITP 741
Cdd:PHA03247 2820 PAASPAGPLPPPTSAQPT-----APPPPPGPPPPSlplggsvapggDVRRRPPSRSP 2871
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
 304-395 1.79e-06

JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal subunits. Domain at Mpr1p and Pad1p N-termini. Domain of unknown function.


Pssm-ID: 214573  Cd Length: 135  Bit Score: 48.91  E-value: 1.79e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138     304 EVCGYLGGTWdmNTHTLSITKtypCRSTRFDRQ--RAGEVERDIQKMMIQDQ------LLLVGWYHSHPKFQAEPTLRDC 375
Cdd:smart00232   23 EVCGVLLGKS--NKDRPEVKE---VFAVPNEPQddSVQEYDEDYSHLMDEELkkvnkdLEIVGWYHSHPDESPFPSEVDV 97

                            90       100
                    ....*....|....*....|
gi 19921138     376 DAQLDYQIKMRGASDLTYTP 395
Cdd:smart00232   98 ATHESYQAPWPISVVLIVDP 117
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 604-726 1.22e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 49.86  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138   604 SGLNMNPVRML---------SPLATPNPTSLPPVLPNLGAPVLPATPSQLLPPQVPAVTAPPAITPAVTTSALTSALNAS 674
Cdd:PRK07994  347 MGVEMTLLRMLafhpaaplpEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAAR 426

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 19921138   675 PrdsPITIQSNSASPAKFEVPVRASPSPAKSDTSSHASTSRTRNSPAPSPGK 726
Cdd:PRK07994  427 Q---QLQRAQGATKAKKSEPAAASRARPVNSALERLASVRPAPSALEKAPAK 475
PHA03247 PHA03247
large tegument protein UL36; Provisional
 610-722 3.34e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 3.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138   610 PVRMLS-PLATPNPTSL---PPVLPNLGAPVLPATPSQLLPPQVPAVTAPPAITPAVTTSALTSALNASPRDSPITIQSN 685
Cdd:PHA03247 2882 PVRRLArPAVSRSTESFalpPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQ 2961

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 19921138   686 ----SASPAKFEVPVRASPSPAKSDTSSHASTSRTRNSPAP 722
Cdd:PHA03247 2962 pwlgALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLS 3002
PHA03247 PHA03247
large tegument protein UL36; Provisional
 610-741 1.64e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138   610 PVRMLSPLATPNPTSLPPVLPNLGA----PVLPATPSQLLPPQVPAVTAPPA---------------ITPAVTTSALTSA 670
Cdd:PHA03247 2673 AAQASSPPQRPRRRAARPTVGSLTSladpPPPPPTPEPAPHALVSATPLPPGpaaarqaspalpaapAPPAVPAGPATPG 2752

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19921138   671 LNASPRDSPITIQSNSASPAKFEV--PVRASPSPAKSDTSSHASTSRTRNSPAPSPGKFSVSDIARNsPSITP 741
Cdd:PHA03247 2753 GPARPARPPTTAGPPAPAPPAAPAagPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALP-PAASP 2824
MPN_like cd08070
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 297-404 2.81e-04

Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); This family contains archaeal and bacterial MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+)-like domains. These domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity for the release of ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. The JAMM proteins likely hydrolyze ubiquitin conjugates in a manner similar to thermolysin, in which the zinc-polarized aqua ligand serves as the nucleophile, compared with the classical DUBs that do so with a cysteine residue in the active site.


Pssm-ID: 163701  Cd Length: 128  Bit Score: 42.24  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138  297 HCHLTV-REVCGYLGGTWDMNTHTlsITKTYPCR------STRF-----DRQRAgeverdiQKMMIQDQLLLVGWYHSHP 364
Cdd:cd08070   10 HAEAEYpEECCGLLLGKGGGVTAI--VTEVYPVRnvaespRRRFeidpaEQLAA-------QREARERGLEVVGIYHSHP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 19921138  365 KFQAEPTLRDCdaqldyqikmRGAsdlTYTPCVSLIISPY 404
Cdd:cd08070   81 DGPARPSETDL----------RLA---WPPGVSYLIVSLA 107
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 604-724 4.51e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 44.71  E-value: 4.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138   604 SGLNMNPVRML-------------SPLATPNPTSLPPVLPnlgAPVLPATPSQLLPPQVPAVTAPPAITPAVTTSALTSA 670
Cdd:PRK14951  352 AALTMVLLRLLafkpaaaaeaaapAEKKTPARPEAAAPAA---APVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAA 428

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19921138   671 LNASPRDSPITIQSNSASPAKFE----------VPVRASPSPAKSDTSSHASTsrtrnSPAPSP 724
Cdd:PRK14951  429 PAAAAPAAAPAAAPAAVALAPAPpaqaapetvaIPVRVAPEPAVASAAPAPAA-----APAAAR 487
Metaviral_G pfam09595
Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. ...
 651-743 5.28e-04

Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. It is high in serine and threonine suggesting it is highly glycosylated.


Pssm-ID: 462833 [Multi-domain]  Cd Length: 183  Bit Score: 42.63  E-value: 5.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138    651 AVTAPPAITPAVTTSALTSALNASPRDSPITIQSNSASP---AKFEVPVRASPSPAKSDTSSHASTSRTRNSPAPSPGKF 727
Cdd:pfam09595   31 ASLILIGESNKEAALIITDIIDININKQHPEQEHHENPPlneAAKEAPSESEDAPDIDPNNQHPSQDRSEAPPLEPAAKT 110

                           90
                   ....*....|....*.
gi 19921138    728 SVSDIARNSPSITPNK 743
Cdd:pfam09595  111 KPSEHEPANPPDASNR 126
JAB pfam01398
JAB1/Mov34/MPN/PAD-1 ubiquitin protease; Members of this family are found in proteasome ...
 285-382 8.41e-04

JAB1/Mov34/MPN/PAD-1 ubiquitin protease; Members of this family are found in proteasome regulatory subunits, eukaryotic initiation factor 3 (eIF3) subunits and regulators of transcription factors. This family is also known as the MPN domain and PAD-1-like domain, JABP1 domain or JAMM domain. These are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signalling and protein turnover pathways in eukaryotes. Versions of the domain in prokaryotic cognates of the ubiquitin-modification pathway are shown to have a similar role, and the archael protein from Haloferax volcanii is found to cleave ubiquitin-like small archaeal modifier proteins (SAMP1/2) from protein conjugates.


Pssm-ID: 396120  Cd Length: 117  Bit Score: 40.41  E-value: 8.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138    285 TVNSSALLLADFHCHLT-----VREVCGYLGGTWDMNThTLSITKTYPcrsTRF--DRQRAGEVERDIQKMMIQDQLLL- 356
Cdd:pfam01398    5 TVIIHPLVLLKILDHANrggkiGEEVMGVLLGKLEGDG-TIEITNSFA---LPQeeTEDDVNAVALDQEYMENMHEMLKk 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 19921138    357 -------VGWYHSHPKFqAEPTLRDCDAQLDYQ 382
Cdd:pfam01398   81 vnrkeevVGWYHTHPGL-CWLSSVDVHTHALYQ 112
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 610-726 1.64e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 42.99  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138   610 PVRMLSPLATPNPTSLPPVLPNLGAPVLPATPSQLLPPQVPAVTAPPaitpavtTSALTSALNASPRDSPITIQSNSASP 689
Cdd:PLN03209  324 PSQRVPPKESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPRP-------LSPYTAYEDLKPPTSPIPTPPSSSPA 396

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 19921138   690 AKFEVPVRASPSPAKSDTSSHASTSRTRNSPAPSPGK 726
Cdd:PLN03209  397 SSKSVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAK 433
PHA03378 PHA03378
EBNA-3B; Provisional
 610-724 1.98e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 42.75  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138   610 PVRMLSPLATPNPTSLPPVLPNLGAPVLPATPSQLLPPQVPAVTAPPAITPAVTTsaltsalnaSPRDSPITIQSNSASP 689
Cdd:PHA03378  691 PGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRAR---------PPAAAPGRARPPAAAP 761

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 19921138   690 AKFEVPVRA--SPSPAKSDTSSHASTSRTRNSPAPSP 724
Cdd:PHA03378  762 GRARPPAAApgAPTPQPPPQAPPAPQQRPRGAPTPQP 798
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 572-703 2.51e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.45  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138    572 SGRKAEEESNAQAEQKASELKVMSLQEQLCMPSGLNMnPVRMLSPLATPNPTSLPPVLPNLGAPvlPATPsqllPPQVPA 651
Cdd:pfam03154  150 SPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSP-PPPGTTQAATAGPTPSAPSVPPQGSP--ATSQ----PPNQTQ 222

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 19921138    652 VTAPPaITPAVTTSALTSALNASPRdSPITIQSNSASPAkfEVPVRASPSPA 703
Cdd:pfam03154  223 STAAP-HTLIQQTPTLHPQRLPSPH-PPLQPMTQPPPPS--QVSPQPLPQPS 270
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 610-741 2.78e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.45  E-value: 2.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138    610 PVRMLSPLATPNPTSLPPVLPNLGAPVLPATPSQLLPPQVPA-VTAPPAITPavtTSALTSALNASPRDSPITIQSNS-- 686
Cdd:pfam03154  347 PAPLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSnLPPPPALKP---LSSLSTHHPPSAHPPPLQLMPQSqq 423

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 19921138    687 --ASPAKFEVPVRASPSPAKSdtSSHASTSRTRNSPAPSPGKfSVSDIARNSPSITP 741
Cdd:pfam03154  424 lpPPPAQPPVLTQSQSLPPPA--ASHPPTSGLHQVPSQSPFP-QHPFVPGGPPPITP 477
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 601-745 3.27e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 41.84  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138   601 CMPSG--LNMNPVRMLSPLATPNPTSLPPVLPNLGA------------PVLP-ATPSQLLPPQVPAVTAPpaiTPAVTTS 665
Cdd:PLN03209  389 TPPSSspASSKSVDAVAKPAEPDVVPSPGSASNVPEvepaqveakktrPLSPyARYEDLKPPTSPSPTAP---TGVSPSV 465

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138   666 ALTSALNASPRDSPITIQSNSASPAKfEVPVRASPSPAKSDTSSHASTSRTRNSPAPSPGKFSVSDIARNSPSITPNKYE 745
Cdd:PLN03209  466 SSTSSVPAVPDTAPATAATDAAAPPP-ANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADE 544
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 578-731 3.36e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 41.72  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138   578 EESNAQAEQKASELKVMSLQEQLCMPSGLNMNpvrmlspLATPNPTSLPPVLPNLGAPVLPATPSQLLPPQVPA---VTA 654
Cdd:PRK14950  309 ADEKAALQKVSQIANLEALTKWVKAFSQLDFQ-------LRTTSYGQLPLELAVIEALLVPVPAPQPAKPTAAApspVRP 381

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19921138   655 PPAITPAVTTSALTSALNASPRDSPITIQSNSASPAKFEVPVRASPSPAKSDTSSHASTSRTRNSPAPSPGKFSVSD 731
Cdd:PRK14950  382 TPAPSTRPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPKLTRAAIPVDEKPKYTPPAPPKEEEKALI 458
PHA03247 PHA03247
large tegument protein UL36; Provisional
 616-745 3.44e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 3.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138   616 PLATPNPTSLPPVLPnlGAPVLPATPSQLLPPQVPAVTAPPAITPAVTTSALTSALNASPRDSPITIQSNSASPAKFEVP 695
Cdd:PHA03247 2722 PPGPAAARQASPALP--AAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLP 2799

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 19921138   696 VRASPSPAKSDTSSHASTSRTRNSPA-PSPGKFSVSDIARNSPSITPNKYE 745
Cdd:PHA03247 2800 SPWDPADPPAAVLAPAAALPPAASPAgPLPPPTSAQPTAPPPPPGPPPPSL 2850
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
604-848 6.03e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.99  E-value: 6.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138   604 SGLNMNPVRML---------SPLATPNPTSLPPVLPNLGAPVLPATPSQLLPPQVPAVTAPP-AITPAVTTSALTSALNA 673
Cdd:PRK07003  346 AGFTMTLLRMLafepavtggGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGaALAPKAAAAAAATRAEA 425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138   674 SP-RDSPITIQSNSASPAkfevpvrASPSPAKSDTSSHASTSRTRNSPAPSPGKFSVSDI--ARNSPSITPNKYEAAAAA 750
Cdd:PRK07003  426 PPaAPAPPATADRGDDAA-------DGDAPVPAKANARASADSRCDERDAQPPADSGSASapASDAPPDAAFEPAPRAAA 498

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138   751 LVPPAAACLPTANDLMAASL---AQLAGQLPPNFLQGDLAALFQQQRKDYGSSSLNQLAAAAAKVGGSKQSNASASSGLN 827
Cdd:PRK07003  499 PSAATPAAVPDARAPAAASRedaPAAAAPPAPEARPPTPAAAAPAARAGGAAAALDVLRNAGMRVSSDRGARAAAAAKPA 578

                         250       260
                  ....*....|....*....|.
gi 19921138   828 DPNVAAAVAAYSNSfNMPLPT 848
Cdd:PRK07003  579 AAPAAAPKPAAPRV-AVQVPT 598
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 609-727 8.22e-03

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: 40.24  E-value: 8.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921138  609 NPVRMLSPLATPNPTSLPPVLPNLGAPVLPATPSQLLPpqVPAVTAPPAITPAVTTSALTSALNASPRDSPITIQSNSAS 688
Cdd:cd23959  117 NPFSASSSTQRETHKTAQVAPPKAEPQTAPVTPFGQLP--MFGQHPPPAKPLPAAAAAQQSSASPGEVASPFASGTVSAS 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 19921138  689 PakFEVPVRASPSPAKSDTS----SHASTSRTRNSPAPSPGKF 727
Cdd:cd23959  195 P--FATATDTAPSSGAPDGFpaeaSAPSPFAAPASAASFPAAP 235
 
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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