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Conserved domains on  [gi|568968636|ref|XP_006514223|]
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R3H domain-containing protein 2 isoform X4 [Mus musculus]

Protein Classification

R3H domain-containing protein( domain architecture ID 11552619)

R3H domain-containing protein with SUZ and Med15 domains, may bind ssDNA or ssRNA in a sequence-specific manner; similar to Mus musculus R3H domain-containing protein 2

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
R3H_encore_like cd02642
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ...
168-229 4.59e-27

R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


:

Pssm-ID: 100071  Cd Length: 63  Bit Score: 104.61  E-value: 4.59e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568968636  168 DRMMLLKLEQEILDFINDNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTG-KAVIINKT 229
Cdd:cd02642     1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
449-766 7.50e-13

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 72.73  E-value: 7.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   449 PALPPTPQHQPPLNNHMISQAEDLSNPFGQMSLSRQGSTEAADPSSALFQPPLISQHPQQASFIMASAGQPLPTSNYSTS 528
Cdd:pfam09606  158 MMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGA 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   529 SHAPPTQQVLPPQGYMQppQQIQVSYYPPGQYPNSNQQYRPLSHPVAYSPQRGQQLPQASQQ--PGLQPMMSNQQQTAYQ 606
Cdd:pfam09606  238 PNQVAMQQQQPQQQGQQ--SQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVmsIGDQNNYQQQQTRQQQ 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   607 GMLGVQQPQNQGLLSNQRSSMGGQMQ---GLVVQYTPLPSYQVPVGSDSQNVVQP---SFQQPMLVPASQSVQG--GLPT 678
Cdd:pfam09606  316 QQQGGNHPAAHQQQMNQSVGQGGQVValgGLNHLETWNPGNFGGLGANPMQRGQPgmmSSPSPVPGQQVRQVTPnqFMRQ 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   679 GGVPVYYSMIPPAQQNGTSPSVGFLQPPGSEQYQMPQSPSPCSPPQMSQQYSGVSPSG-PGVVVMqlNVPNGPQAPQNPS 757
Cdd:pfam09606  396 SPQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQQRTIGQDSPGGSLNtPGQSAV--NSPLNPQEEQLYR 473

                   ....*....
gi 568968636   758 MVQWSHCKY 766
Cdd:pfam09606  474 EKYRQLTKY 482
SUZ pfam12752
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ...
250-303 2.53e-12

SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterized in the C.elegans protein Szy-20 where it has been shown to bind RNA and allow their localization to the centrosome. Warning- the domain has a compositionally biased character.


:

Pssm-ID: 463689 [Multi-domain]  Cd Length: 56  Bit Score: 62.34  E-value: 2.53e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568968636   250 EFQQRFILKRDDASMD--RDDNQMRVPLQDGRRSKSIEEREEEYQRVRERIFARET 303
Cdd:pfam12752    1 PPPKMKILRRPSSGSSssSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
 
Name Accession Description Interval E-value
R3H_encore_like cd02642
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ...
168-229 4.59e-27

R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100071  Cd Length: 63  Bit Score: 104.61  E-value: 4.59e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568968636  168 DRMMLLKLEQEILDFINDNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTG-KAVIINKT 229
Cdd:cd02642     1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
152-229 3.59e-14

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 68.48  E-value: 3.59e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636    152 IDLHEFLVNTLKKNPRDRMMLLKLEQEILDFINdNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTGKA--VIINKT 229
Cdd:smart00393    1 ADFLPVTLDALSYRPRRREELIELELEIARFVK-STKESVELPPMNSYERKIVHELAEKYGLESESFGEGPKrrVVISKK 79
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
449-766 7.50e-13

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 72.73  E-value: 7.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   449 PALPPTPQHQPPLNNHMISQAEDLSNPFGQMSLSRQGSTEAADPSSALFQPPLISQHPQQASFIMASAGQPLPTSNYSTS 528
Cdd:pfam09606  158 MMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGA 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   529 SHAPPTQQVLPPQGYMQppQQIQVSYYPPGQYPNSNQQYRPLSHPVAYSPQRGQQLPQASQQ--PGLQPMMSNQQQTAYQ 606
Cdd:pfam09606  238 PNQVAMQQQQPQQQGQQ--SQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVmsIGDQNNYQQQQTRQQQ 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   607 GMLGVQQPQNQGLLSNQRSSMGGQMQ---GLVVQYTPLPSYQVPVGSDSQNVVQP---SFQQPMLVPASQSVQG--GLPT 678
Cdd:pfam09606  316 QQQGGNHPAAHQQQMNQSVGQGGQVValgGLNHLETWNPGNFGGLGANPMQRGQPgmmSSPSPVPGQQVRQVTPnqFMRQ 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   679 GGVPVYYSMIPPAQQNGTSPSVGFLQPPGSEQYQMPQSPSPCSPPQMSQQYSGVSPSG-PGVVVMqlNVPNGPQAPQNPS 757
Cdd:pfam09606  396 SPQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQQRTIGQDSPGGSLNtPGQSAV--NSPLNPQEEQLYR 473

                   ....*....
gi 568968636   758 MVQWSHCKY 766
Cdd:pfam09606  474 EKYRQLTKY 482
SUZ pfam12752
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ...
250-303 2.53e-12

SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterized in the C.elegans protein Szy-20 where it has been shown to bind RNA and allow their localization to the centrosome. Warning- the domain has a compositionally biased character.


Pssm-ID: 463689 [Multi-domain]  Cd Length: 56  Bit Score: 62.34  E-value: 2.53e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568968636   250 EFQQRFILKRDDASMD--RDDNQMRVPLQDGRRSKSIEEREEEYQRVRERIFARET 303
Cdd:pfam12752    1 PPPKMKILRRPSSGSSssSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
170-228 2.67e-10

R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.


Pssm-ID: 460206  Cd Length: 60  Bit Score: 56.73  E-value: 2.67e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568968636   170 MMLLKLEQEILDFINDNNNQFKkFPQMTSYHRMLLHRVAAYFGMDHNV--DQTGKAVIINK 228
Cdd:pfam01424    1 EFLEQLAEKLAEFVKDTGKSLE-LPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 60
PRK10263 PRK10263
DNA translocase FtsK; Provisional
492-643 4.06e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 47.77  E-value: 4.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  492 PSSALFQPPLI-SQHPQQasfimasagQPLPTSNYSTSSH-APPTQQVLPPQGYMQPPQQiqvsYYPPGQYPNSNQQYRP 569
Cdd:PRK10263  740 PHEPLFTPIVEpVQQPQQ---------PVAPQQQYQQPQQpVAPQPQYQQPQQPVAPQPQ----YQQPQQPVAPQPQYQQ 806
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568968636  570 LSHPVAYSPQRGQ-QLPQASQQPGLQPmmsnQQQTAyqgmlgvqqPQNQGLLSNQRSSMGGQMQGLVVQYTPLPS 643
Cdd:PRK10263  807 PQQPVAPQPQYQQpQQPVAPQPQYQQP----QQPVA---------PQPQDTLLHPLLMRNGDSRPLHKPTTPLPS 868
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
472-641 1.51e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 45.57  E-value: 1.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   472 LSNPFGQMSLSRQGSTEAADPSSALFQPPLISQHPQQASfimasAGQPLptsNYstsshaPPTQQVLPPQGYMQPPQQIQ 551
Cdd:TIGR01628  371 LQDQFMQLQPRMRQLPMGSPMGGAMGQPPYYGQGPQQQF-----NGQPL---GW------PRMSMMPTPMGPGGPLRPNG 436
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   552 VSYYPPGQYPNSNQQYRPLSHPVA---YSPQ-RGQQLPQASQQPGLQPMMSNQQQTAYQgMLGVQQPQnqgllsNQRSSM 627
Cdd:TIGR01628  437 LAPMNAVRAPSRNAQNAAQKPPMQpvmYPPNyQSLPLSQDLPQPQSTASQGGQNKKLAQ-VLASATPQ------MQKQVL 509
                          170
                   ....*....|....
gi 568968636   628 GGQMQGLVVQYTPL 641
Cdd:TIGR01628  510 GERLFPLVEAIEPA 523
Amelin smart00817
Ameloblastin precursor (Amelin); This family consists of several mammalian Ameloblastin ...
483-618 1.85e-03

Ameloblastin precursor (Amelin); This family consists of several mammalian Ameloblastin precursor (Amelin) proteins. Matrix proteins of tooth enamel consist mainly of amelogenin but also of non-amelogenin proteins, which, although their volumetric percentage is low, have an important role in enamel mineralisation. One of the non-amelogenin proteins is ameloblastin, also known as amelin and sheathlin. Ameloblastin (AMBN) is one of the enamel sheath proteins which is though to have a role in determining the prismatic structure of growing enamel crystals.


Pssm-ID: 214832 [Multi-domain]  Cd Length: 411  Bit Score: 41.80  E-value: 1.85e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636    483 RQGSTEAADPSSALFQPPLISQHPQQAsfimasagqPLPTSNYSTSSHAPPTQQVLPPQGYMQPPQQIQVSYYPPGQYPN 562
Cdd:smart00817   82 REHETQQYEYSLPVHPPPLPSQPSLQP---------QQPGLKPFLQPTALPTNQATPQKNGPQPPMHLGQPPLQQAELPM 152
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568968636    563 SNQQYRPLSHP-------VAYSPQRGQQLPQASQQPGLQPMMSNQQQTAYQGMLGVQQPQNQG 618
Cdd:smart00817  153 IPPQVAPSDKPpqtelplYDFADPQNPLLFQIAHLMSRGPMPQNKQQHLYPGLFYMSYGANQL 215
PRK06462 PRK06462
asparagine synthetase A; Reviewed
140-306 4.21e-03

asparagine synthetase A; Reviewed


Pssm-ID: 235808 [Multi-domain]  Cd Length: 335  Bit Score: 40.39  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  140 RDSSQEYTDSTGIDLHEFLVNTLKKnprdrmmllKLEQEILDFINDNNNQFKKFPQMTsyhrmllHRVAAYFGMDHNVDQ 219
Cdd:PRK06462  136 EGADLDEVMDLIEDLIKYLVKELLE---------EHEDELEFFGRDLPHLKRPFKRIT-------HKEAVEILNEEGCRG 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  220 TGKAVIinktssTRIPEQRFSEHIKD--------EKNTEFQQRFILKRDDASMDRDdnqMRVPLQDGRRSkSIEEREEEY 291
Cdd:PRK06462  200 IDLEEL------GSEGEKSLSEHFEEpfwiidipKGSREFYDREDPERPGVLRNYD---LLLPEGYGEAV-SGGEREYEY 269
                         170
                  ....*....|....*
gi 568968636  292 QRVRERIfaRETGQN 306
Cdd:PRK06462  270 EEIVERI--REHGVD 282
 
Name Accession Description Interval E-value
R3H_encore_like cd02642
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ...
168-229 4.59e-27

R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100071  Cd Length: 63  Bit Score: 104.61  E-value: 4.59e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568968636  168 DRMMLLKLEQEILDFINDNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTG-KAVIINKT 229
Cdd:cd02642     1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
152-229 3.59e-14

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 68.48  E-value: 3.59e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636    152 IDLHEFLVNTLKKNPRDRMMLLKLEQEILDFINdNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTGKA--VIINKT 229
Cdd:smart00393    1 ADFLPVTLDALSYRPRRREELIELELEIARFVK-STKESVELPPMNSYERKIVHELAEKYGLESESFGEGPKrrVVISKK 79
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
449-766 7.50e-13

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 72.73  E-value: 7.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   449 PALPPTPQHQPPLNNHMISQAEDLSNPFGQMSLSRQGSTEAADPSSALFQPPLISQHPQQASFIMASAGQPLPTSNYSTS 528
Cdd:pfam09606  158 MMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGA 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   529 SHAPPTQQVLPPQGYMQppQQIQVSYYPPGQYPNSNQQYRPLSHPVAYSPQRGQQLPQASQQ--PGLQPMMSNQQQTAYQ 606
Cdd:pfam09606  238 PNQVAMQQQQPQQQGQQ--SQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVmsIGDQNNYQQQQTRQQQ 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   607 GMLGVQQPQNQGLLSNQRSSMGGQMQ---GLVVQYTPLPSYQVPVGSDSQNVVQP---SFQQPMLVPASQSVQG--GLPT 678
Cdd:pfam09606  316 QQQGGNHPAAHQQQMNQSVGQGGQVValgGLNHLETWNPGNFGGLGANPMQRGQPgmmSSPSPVPGQQVRQVTPnqFMRQ 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   679 GGVPVYYSMIPPAQQNGTSPSVGFLQPPGSEQYQMPQSPSPCSPPQMSQQYSGVSPSG-PGVVVMqlNVPNGPQAPQNPS 757
Cdd:pfam09606  396 SPQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQQRTIGQDSPGGSLNtPGQSAV--NSPLNPQEEQLYR 473

                   ....*....
gi 568968636   758 MVQWSHCKY 766
Cdd:pfam09606  474 EKYRQLTKY 482
SUZ pfam12752
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ...
250-303 2.53e-12

SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterized in the C.elegans protein Szy-20 where it has been shown to bind RNA and allow their localization to the centrosome. Warning- the domain has a compositionally biased character.


Pssm-ID: 463689 [Multi-domain]  Cd Length: 56  Bit Score: 62.34  E-value: 2.53e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568968636   250 EFQQRFILKRDDASMD--RDDNQMRVPLQDGRRSKSIEEREEEYQRVRERIFARET 303
Cdd:pfam12752    1 PPPKMKILRRPSSGSSssSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
R3H cd02325
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ...
172-228 3.73e-11

R3H domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. R3H domains are found in proteins together with ATPase domains, SF1 helicase domains, SF2 DEAH helicase domains, Cys-rich repeats, ring-type zinc fingers, and KH domains. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100064  Cd Length: 59  Bit Score: 59.16  E-value: 3.73e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568968636  172 LLKLEQEILDFINDNNNQFKKFPQMTSYHRMLLHRVAAYFGMDHNVDQTG--KAVIINK 228
Cdd:cd02325     1 REEREEELEAFAKDAAGKSLELPPMNSYERKLIHDLAEYYGLKSESEGEGpnRRVVITK 59
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
170-228 2.67e-10

R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.


Pssm-ID: 460206  Cd Length: 60  Bit Score: 56.73  E-value: 2.67e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568968636   170 MMLLKLEQEILDFINDNNNQFKkFPQMTSYHRMLLHRVAAYFGMDHNV--DQTGKAVIINK 228
Cdd:pfam01424    1 EFLEQLAEKLAEFVKDTGKSLE-LPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 60
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
485-665 2.86e-06

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 51.58  E-value: 2.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   485 GSTEAADPSSALFQPPLISQHPQQASFIM------------ASAGQPLPTSNYSTSSHAPPTQQVLPPQGYMQPPQQIQv 552
Cdd:pfam09770  166 APKKAAAPAPAPQPAAQPASLPAPSRKMMsleeveaamraqAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQ- 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   553 syyPPGQYPNSNQQYRPLSHPVAYspqrgQQLPQASQQPGLQPMMSNQQQTAYQGMLGV-QQP----QNQGLLSNQRSSM 627
Cdd:pfam09770  245 ---QPQQQPQQPQQHPGQGHPVTI-----LQRPQSPQPDPAQPSIQPQAQQFHQQPPPVpVQPtqilQNPNRLSAARVGY 316
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 568968636   628 GGQMQGlVVQYTPLPSYQVPVGSDSQNVVQPSFQQPML 665
Cdd:pfam09770  317 PQNPQP-GVQPAPAHQAHRQQGSFGRQAPIITHPQQLA 353
PRK10263 PRK10263
DNA translocase FtsK; Provisional
492-643 4.06e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 47.77  E-value: 4.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  492 PSSALFQPPLI-SQHPQQasfimasagQPLPTSNYSTSSH-APPTQQVLPPQGYMQPPQQiqvsYYPPGQYPNSNQQYRP 569
Cdd:PRK10263  740 PHEPLFTPIVEpVQQPQQ---------PVAPQQQYQQPQQpVAPQPQYQQPQQPVAPQPQ----YQQPQQPVAPQPQYQQ 806
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568968636  570 LSHPVAYSPQRGQ-QLPQASQQPGLQPmmsnQQQTAyqgmlgvqqPQNQGLLSNQRSSMGGQMQGLVVQYTPLPS 643
Cdd:PRK10263  807 PQQPVAPQPQYQQpQQPVAPQPQYQQP----QQPVA---------PQPQDTLLHPLLMRNGDSRPLHKPTTPLPS 868
PRK10263 PRK10263
DNA translocase FtsK; Provisional
452-685 8.78e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 46.62  E-value: 8.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  452 PPTPQHQPPLNNHMISQAEDLSNPFGQMSLSRQGSTEAADPSSALFQPPLISQHPQqasfimaSAGQPLPTSNYSTSSHA 531
Cdd:PRK10263  302 PEYDEYDPLLNGAPITEPVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPT-------VAWQPVPGPQTGEPVIA 374
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  532 PPtqqvlpPQGYMQPPQ--QIQVSYYPPGQYPNSNQQyrPLSHPVAYSPQRGQQLPQASQQPGLQPMMSNQQQTAYQGML 609
Cdd:PRK10263  375 PA------PEGYPQQSQyaQPAVQYNEPLQQPVQPQQ--PYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNA 446
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568968636  610 GVQQPQNQgLLSNQRSsmggqmqglvvqYTPLPSYQVPVGSDSQNVVQPSFQQPMLVPASQSVQGGLPTGGvPVYY 685
Cdd:PRK10263  447 WQAEEQQS-TFAPQST------------YQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARP-PLYY 508
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
472-641 1.51e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 45.57  E-value: 1.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   472 LSNPFGQMSLSRQGSTEAADPSSALFQPPLISQHPQQASfimasAGQPLptsNYstsshaPPTQQVLPPQGYMQPPQQIQ 551
Cdd:TIGR01628  371 LQDQFMQLQPRMRQLPMGSPMGGAMGQPPYYGQGPQQQF-----NGQPL---GW------PRMSMMPTPMGPGGPLRPNG 436
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   552 VSYYPPGQYPNSNQQYRPLSHPVA---YSPQ-RGQQLPQASQQPGLQPMMSNQQQTAYQgMLGVQQPQnqgllsNQRSSM 627
Cdd:TIGR01628  437 LAPMNAVRAPSRNAQNAAQKPPMQpvmYPPNyQSLPLSQDLPQPQSTASQGGQNKKLAQ-VLASATPQ------MQKQVL 509
                          170
                   ....*....|....
gi 568968636   628 GGQMQGLVVQYTPL 641
Cdd:TIGR01628  510 GERLFPLVEAIEPA 523
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
420-708 1.82e-04

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: 45.53  E-value: 1.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   420 QVTSPQSVRGLLPCTAQQQQQQQQQQQQLPALPPT---PQHQPPlnNHMISQAEDLSNPFGQMSLSRQGSTEAADPSSAL 496
Cdd:pfam03154  175 QAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQgspATSQPP--NQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPM 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   497 FQPPLISQHPQQA--SFIMASAGQPLPTSNYSTSSHAPptqQVLPPQGYMQPPQ--QIQVSYYPPGQYPNSNQQ--YRPL 570
Cdd:pfam03154  253 TQPPPPSQVSPQPlpQPSLHGQMPPMPHSLQTGPSHMQ---HPVPPQPFPLTPQssQSQVPPGPSPAAPGQSQQriHTPP 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   571 SHPVAYSPQ--RGQQLPQASQQ------------PGLQPMMSNQQQTAYQGMLGVQQPQN----------QGLLSNQRSS 626
Cdd:pfam03154  330 SQSQLQSQQppREQPLPPAPLSmphikpppttpiPQLPNPQSHKHPPHLSGPSPFQMNSNlppppalkplSSLSTHHPPS 409
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   627 MGGQMQGLVVQYTPLPS--YQVPVGSDSQNVVQPSFQQPmlvPASQSVQGG----------LPTGGVPVYYSMIPPAQqn 694
Cdd:pfam03154  410 AHPPPLQLMPQSQQLPPppAQPPVLTQSQSLPPPAASHP---PTSGLHQVPsqspfpqhpfVPGGPPPITPPSGPPTS-- 484
                          330
                   ....*....|....
gi 568968636   695 gTSPSVGFLQPPGS 708
Cdd:pfam03154  485 -TSSAMPGIQPPSS 497
PHA03379 PHA03379
EBNA-3A; Provisional
408-814 5.88e-04

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 43.89  E-value: 5.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  408 PGMALGAPEVCNQVTSPQSVRGLLPCTAQQQQQQQQQQQQLPALPPTPQHQPPLNNHMISQAEDLSNPF--------GQM 479
Cdd:PHA03379  409 SEPTYGTPRPPVEKPRPEVPQSLETATSHGSAQVPEPPPVHDLEPGPLHDQHSMAPCPVAQLPPGPLQDlepgdqlpGVV 488
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  480 SLSRQGSTEAADPSSALFQP--PLISQHPQQASFI-----MASAGQPLPTSNYSTSSHAPPTQQVLPPQGYMQPPQQIQV 552
Cdd:PHA03379  489 QDGRPACAPVPAPAGPIVRPweASLSQVPGVAFAPvmpqpMPVEPVPVPTVALERPVCPAPPLIAMQGPGETSGIVRVRE 568
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  553 SYYPPGQYPNSNQQYRPLshPVAYSPQRGQQLPQASQQP-GLQPMMSNQQQTayqgmlgvQQPQNQGLLSNQRSSMGGQM 631
Cdd:PHA03379  569 RWRPAPWTPNPPRSPSQM--SVRDRLARLRAEAQPYQASvEVQPPQLTQVSP--------QQPMEYPLEPEQQMFPGSPF 638
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  632 QGL--VVQYTPLPSYQVPvgSDSQNVVQPSFQQPMLVPASQSVQGGLPTGGVPVYYSMIPPAQQ--NGTSPSVGFLQPPG 707
Cdd:PHA03379  639 SQVadVMRAGGVPAMQPQ--YFDLPLQQPISQGAPLAPLRASMGPVPPVPATQPQYFDIPLTEPinQGASAAHFLPQQPM 716
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  708 S-------EQYQMPQSPSPCSPPQMSQQYSGVSPSGPgvvvMQLNVPNGPQAPQNPSMVQWshckyysVEQRGQKPGDLY 780
Cdd:PHA03379  717 EgplvperWMFQGATLSQSVRPGVAQSQYFDLPLTQP----INHGAPAAHFLHQPPMEGPW-------VPEQWMFQGAPP 785
                         410       420       430
                  ....*....|....*....|....*....|....
gi 568968636  781 SPdGSPQANAQMGSSPVTSPTQSPAPSPVTSLSN 814
Cdd:PHA03379  786 SQ-GTDVVQHQLDALGYVLHVLNHPGVPVSPAVN 818
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
450-597 1.08e-03

G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.


Pssm-ID: 464961 [Multi-domain]  Cd Length: 272  Bit Score: 42.22  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   450 ALPPTPQHQPPLNNHMISQAEDLSnPFGQMSLSRQGSTEAADPSSALFQPPLISQHPQQASFIMASAGQPLPTSNYSTSS 529
Cdd:pfam15991  117 SMQGQPHHQQHPGPQVGVLKRTRS-PSPPVQQQAYYKQPAFSPGYAEHGQQKHDDGRRGYDVARFGSWNKSTAQYPPSGQ 195
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568968636   530 HAPPTQQVLPP-QGYMQPPQQIQVSYYPPGQYPNSNQQYRPLSHPVAY---SPQRGQQLPQA--SQQPGLQPMM 597
Cdd:pfam15991  196 LFYPTHQYLPPpQTQGQADARLQTIYPQPGYALPLQQQYEHANQPSPFvssSPLKQMQSPKAgpGPQPMQLSVL 269
PRK10263 PRK10263
DNA translocase FtsK; Provisional
468-709 1.20e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.15  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  468 QAEDLSNPFGQMSLSRQGST-------EAADPSSALfQPPLISQ--HPQQASFimaSAGQPLPTSNYSTSSHAPPTQQVL 538
Cdd:PRK10263  660 QQDELARQFAQTQQQRYGEQyqhdvpvNAEDADAAA-EAELARQfaQTQQQRY---SGEQPAGANPFSLDDFEFSPMKAL 735
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  539 PPQGYMQPpqqiqvsYYPPGQYPNSNQQYRPLSHPVAYSPQRgqqlPQASQQPGLQPMMSNQQQTAYQGMLGVQQPQNQG 618
Cdd:PRK10263  736 LDDGPHEP-------LFTPIVEPVQQPQQPVAPQQQYQQPQQ----PVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQY 804
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  619 LLSNQrssmggqmqglvvQYTPLPSYQVPvgsDSQNVVQPSFQQPMLVPASQSVQgglptggvpvyySMIPP-AQQNGTS 697
Cdd:PRK10263  805 QQPQQ-------------PVAPQPQYQQP---QQPVAPQPQYQQPQQPVAPQPQD------------TLLHPlLMRNGDS 856
                         250       260
                  ....*....|....*....|..
gi 568968636  698 ----------PSVGFLQPPGSE 709
Cdd:PRK10263  857 rplhkpttplPSLDLLTPPPSE 878
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
498-834 1.21e-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: 42.83  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   498 QPPLIsqHPQQASFIMASAGQPLPTSnySTSSHAPPTQQVLPPQGY---MQPPQQIQVSYYPPG---QYPNSNQQYRPLS 571
Cdd:pfam03154  170 QPPVL--QAQSGAASPPSPPPPGTTQ--AATAGPTPSAPSVPPQGSpatSQPPNQTQSTAAPHTliqQTPTLHPQRLPSP 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   572 HP----VAYSPQRGQQLPQASQQPGLQPMMSNQQQTAYQGMLGVQQP-QNQGLLSNQRSSMGgqmqglvvQYTPLPSYQV 646
Cdd:pfam03154  246 HPplqpMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPvPPQPFPLTPQSSQS--------QVPPGPSPAA 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   647 PVGSDSQNVVQPSfqQPMLVPASQSVQGGLPTGGVPVYYSMIPPaqqngTSPsVGFLQPPGSEQYQMPQspspcsppqms 726
Cdd:pfam03154  318 PGQSQQRIHTPPS--QSQLQSQQPPREQPLPPAPLSMPHIKPPP-----TTP-IPQLPNPQSHKHPPHL----------- 378
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   727 qqysgvspSGPGVVVMQLNVPNgPQAPQNPSMVQWSHckyysveqrgqkPGDLYSPDGS--PQANaQMGSSPVTSP--TQ 802
Cdd:pfam03154  379 --------SGPSPFQMNSNLPP-PPALKPLSSLSTHH------------PPSAHPPPLQlmPQSQ-QLPPPPAQPPvlTQ 436
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 568968636   803 SPAPSPVTSLSNVCTGLSPLPVLTPFPR----PGGP 834
Cdd:pfam03154  437 SQSLPPPAASHPPTSGLHQVPSQSPFPQhpfvPGGP 472
Amelin smart00817
Ameloblastin precursor (Amelin); This family consists of several mammalian Ameloblastin ...
483-618 1.85e-03

Ameloblastin precursor (Amelin); This family consists of several mammalian Ameloblastin precursor (Amelin) proteins. Matrix proteins of tooth enamel consist mainly of amelogenin but also of non-amelogenin proteins, which, although their volumetric percentage is low, have an important role in enamel mineralisation. One of the non-amelogenin proteins is ameloblastin, also known as amelin and sheathlin. Ameloblastin (AMBN) is one of the enamel sheath proteins which is though to have a role in determining the prismatic structure of growing enamel crystals.


Pssm-ID: 214832 [Multi-domain]  Cd Length: 411  Bit Score: 41.80  E-value: 1.85e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636    483 RQGSTEAADPSSALFQPPLISQHPQQAsfimasagqPLPTSNYSTSSHAPPTQQVLPPQGYMQPPQQIQVSYYPPGQYPN 562
Cdd:smart00817   82 REHETQQYEYSLPVHPPPLPSQPSLQP---------QQPGLKPFLQPTALPTNQATPQKNGPQPPMHLGQPPLQQAELPM 152
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568968636    563 SNQQYRPLSHP-------VAYSPQRGQQLPQASQQPGLQPMMSNQQQTAYQGMLGVQQPQNQG 618
Cdd:smart00817  153 IPPQVAPSDKPpqtelplYDFADPQNPLLFQIAHLMSRGPMPQNKQQHLYPGLFYMSYGANQL 215
PHA03377 PHA03377
EBNA-3C; Provisional
449-702 2.97e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 41.58  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  449 PALPPTPQHQPPLNNHMISQAEDLSNPfGQMSLSRQGSTEAADPSSALFQP-------PL-ISQHPQQAsfimasagqPL 520
Cdd:PHA03377  672 PATQSTPPRPSWLPSVFVLPSVDAGRA-QPSEESHLSSMSPTQPISHEEQPryedpddPLdLSLHPDQA---------PP 741
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  521 PTSNYSTSSHAPPTQQVLPPQGYMQPP--------------QQIQVSYYPPGQYP-NSNQQYRPLSHPVAYSPQR----G 581
Cdd:PHA03377  742 PSHQAPYSGHEEPQAQQAPYPGYWEPRppqapylgyqepqaQGVQVSSYPGYAGPwGLRAQHPRYRHSWAYWSQYpghgH 821
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  582 QQLPQASQQPGLQPmmsnqqqtAYQGMLGVQQPQNQGLLSNQRSSMGGQMQGLVVQYTPLPsyQVPVGSDSQNVVQPSFQ 661
Cdd:PHA03377  822 PQGPWAPRPPHLPP--------QWDGSAGHGQDQVSQFPHLQSETGPPRLQLSQVPQLPYS--QTLVSSSAPSWSSPQPR 891
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 568968636  662 QPMlvpasQSVQGGLPTGGVPVYYSMIPPAQQNGTS-PSVGF 702
Cdd:PHA03377  892 API-----RPIPTRFPPPPMPLQDSMAVGCDSSGTAcPSMPF 928
PHA03377 PHA03377
EBNA-3C; Provisional
452-708 3.15e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 41.58  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  452 PPT--PQHQPPLNNHMISQAEDLSNPFG-------QMSLSRQGSTEAADPSSALfQPPLISQHPQQA--------SFIMA 514
Cdd:PHA03377  617 PPSsaPRDMAPSVVRMFLRERLLEQSTGpkpksfwEMRAGRDGSGIQQEPSSRR-QPATQSTPPRPSwlpsvfvlPSVDA 695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  515 SAGQPLPTSNYSTSSHAPPTQQVLPPQgYMQPPQQIQVSYYPPGQYPNSNQqyrplshpvaySPQRGQQLPQASQQPGLQ 594
Cdd:PHA03377  696 GRAQPSEESHLSSMSPTQPISHEEQPR-YEDPDDPLDLSLHPDQAPPPSHQ-----------APYSGHEEPQAQQAPYPG 763
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  595 PMMSNQQQTAYQGmlgVQQPQNQGLLSNQRSSMGGQMqGLVVQYtplPSYQVPVGSDSQNVV----------QPSFQQPM 664
Cdd:PHA03377  764 YWEPRPPQAPYLG---YQEPQAQGVQVSSYPGYAGPW-GLRAQH---PRYRHSWAYWSQYPGhghpqgpwapRPPHLPPQ 836
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 568968636  665 LVPASQSVQGGLpTGGVPVYYSMIPPAQQNGTSPSVGFLQPPGS 708
Cdd:PHA03377  837 WDGSAGHGQDQV-SQFPHLQSETGPPRLQLSQVPQLPYSQTLVS 879
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
478-706 3.80e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 41.17  E-value: 3.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   478 QMSLSRQGSTEAADPSSALfQPPLISQHPQQASFIMASAGQPLPTS--NYSTSSHAPPTQ--QVL---PPQGYMQPPQQI 550
Cdd:pfam09770   99 QVRFNRQQPAARAAQSSAQ-PPASSLPQYQYASQQSQQPSKPVRTGyeKYKEPEPIPDLQvdASLwgvAPKKAAAPAPAP 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   551 QVSYYPPGQYPNSNQ---------QYRplshpvAYSPQRGQQLPQASQQP--GLQPMMSNQQQTAYQGMLGVQQPQNQGL 619
Cdd:pfam09770  178 QPAAQPASLPAPSRKmmsleeveaAMR------AQAKKPAQQPAPAPAQPpaAPPAQQAQQQQQFPPQIQQQQQPQQQPQ 251
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   620 LSNQRSSMGGQMQGL---------VVQYTPLPSYQVPVGSDSQNVVQPS--FQQPMLVPASQSVQGGLPTGGVPVyysmi 688
Cdd:pfam09770  252 QPQQHPGQGHPVTILqrpqspqpdPAQPSIQPQAQQFHQQPPPVPVQPTqiLQNPNRLSAARVGYPQNPQPGVQP----- 326
                          250
                   ....*....|....*...
gi 568968636   689 PPAQQNGTSPSVGFLQPP 706
Cdd:pfam09770  327 APAHQAHRQQGSFGRQAP 344
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
579-709 3.81e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 40.95  E-value: 3.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636   579 QRGQQLPQASQQPGLQPMMSNQQQTAYQGMLGVQQ----PQNQGLLSNQRSSMGGQMQGLVVQYTPLPSYQVPvGSDSQN 654
Cdd:TIGR01628  374 QFMQLQPRMRQLPMGSPMGGAMGQPPYYGQGPQQQfngqPLGWPRMSMMPTPMGPGGPLRPNGLAPMNAVRAP-SRNAQN 452
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568968636   655 VVQPSFQQPMlvPASQSVQGGLPTGGVPVYYSMIPPAQQNGTSPSVGFLQPPGSE 709
Cdd:TIGR01628  453 AAQKPPMQPV--MYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVLASATPQMQ 505
PRK06462 PRK06462
asparagine synthetase A; Reviewed
140-306 4.21e-03

asparagine synthetase A; Reviewed


Pssm-ID: 235808 [Multi-domain]  Cd Length: 335  Bit Score: 40.39  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  140 RDSSQEYTDSTGIDLHEFLVNTLKKnprdrmmllKLEQEILDFINDNNNQFKKFPQMTsyhrmllHRVAAYFGMDHNVDQ 219
Cdd:PRK06462  136 EGADLDEVMDLIEDLIKYLVKELLE---------EHEDELEFFGRDLPHLKRPFKRIT-------HKEAVEILNEEGCRG 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968636  220 TGKAVIinktssTRIPEQRFSEHIKD--------EKNTEFQQRFILKRDDASMDRDdnqMRVPLQDGRRSkSIEEREEEY 291
Cdd:PRK06462  200 IDLEEL------GSEGEKSLSEHFEEpfwiidipKGSREFYDREDPERPGVLRNYD---LLLPEGYGEAV-SGGEREYEY 269
                         170
                  ....*....|....*
gi 568968636  292 QRVRERIfaRETGQN 306
Cdd:PRK06462  270 EEIVERI--REHGVD 282
 
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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