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Conserved domains on  [gi|530394017|ref|XP_005270045|]
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zinc finger MIZ domain-containing protein 1 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Zmiz1_N pfam18028
Zmiz1 N-terminal tetratricopeptide repeat domain; This is the N-terminal domain found in Zmiz1 ...
8-100 1.92e-53

Zmiz1 N-terminal tetratricopeptide repeat domain; This is the N-terminal domain found in Zmiz1 proteins (Zinc finger MIZ domain-containing protein 1). Zmiz1 is a direct Notch1 cofactor that heterogeneously regulates Notch target genes. Zmiz1 directly interacts with the RAM1 domain of Notch1 through this N-terminal tetratricopeptide repeat (TPR) domain. Furthermore, it has been shown that Zmiz1 and Notch1 cooperatively recruit each other to chromatin through direct interaction via the N-terminal TPR domain resulting in a slight increase in activating histone marks and decrease of repressive histone marks. Functional analysis indicate that the N-Terminal Domain of Zmiz1 is important for driving Myc transcription and proliferation indirectly.


:

Pssm-ID: 375500  Cd Length: 93  Bit Score: 181.23  E-value: 1.92e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017     8 IQQTNDRLQCIKQHLQNPANFHNAATELLDWCGDPRAFQRPFEQSLMGCLTVVSRVAAQQGFDLDLGYRLLAVCAANRDK 87
Cdd:pfam18028    1 VQQNNDRLQSIKQHLQNPANFHNACTELLDWCGDPRAFQRPFEQNLLGCLTVVVRVATQQGFDLDLAYRLLAVCAANRKL 80
                           90
                   ....*....|...
gi 530394017    88 FTPKSAALLSSWC 100
Cdd:pfam18028   81 LSPKSAALINRWC 93
RING_Ubox super family cl17238
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
743-806 1.93e-42

RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enable efficient transfer of ubiquitin from E2 to the substrates.


The actual alignment was detected with superfamily member cd16822:

Pssm-ID: 473075  Cd Length: 64  Bit Score: 148.67  E-value: 1.93e-42
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530394017  743 KVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGLEVDQYMW 806
Cdd:cd16822     1 KVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGLEVDQYMW 64
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
184-468 8.88e-08

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: 56.56  E-value: 8.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   184 NPMANANNPMNPGGNPMASGMTTSNPglNSPQFAGQQQQFSAKAGPAQPYIQQSMYGRPNYPGSGGfGASYPGGPNAPAG 263
Cdd:pfam09606  115 GGPGTASNLLASLGRPQMPMGGAGFP--SQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNG-GPGQGQAGGMNGG 191
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   264 MGIPPHTRPPADFTQPAAAAAAAAVAAAAATATATATATVAALQETQNKDINQYGPVcssfQMGPTQAYNSQFMNQP--- 340
Cdd:pfam09606  192 QQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQP----QQQGQQSQLGMGINQMqqm 267
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   341 -----GPRGPASMGGSMNPASMAAGMTPSGMS--GPPM-----GMNQPRPPGISPFGTHGQRMPQQTYPGPRPQSLPIQN 408
Cdd:pfam09606  268 pqgvgGGAGQGGPGQPMGPPGQQPGAMPNVMSigDQNNyqqqqTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLN 347
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530394017   409 IKRPY--------------PGEPNY--GNQQYGPNSQFPTQPGQYPAPNPPRPLTSPNYPGQRMPSQPSSGQYPPP 468
Cdd:pfam09606  348 HLETWnpgnfgglganpmqRGQPGMmsSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSP 423
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
386-562 2.07e-04

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.46  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  386 THGQRMPQQTYPGPRPQSL------PIQNIKRPYPGEPnygnqQYGPNSQFPTQPGQYPAPNPPRPLTSPNYPGQRMPSQ 459
Cdd:PRK10263  706 TQQQRYSGEQPAGANPFSLddfefsPMKALLDDGPHEP-----LFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQ 780
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  460 PSSGQYPPPtvnmgQYYKPEQFNGQNNTFSGSSYSNYSQGNVNRPPRpvPVANYPHSPVPGNPTPPMTPGSSIPPYLSPS 539
Cdd:PRK10263  781 PQQPVAPQP-----QYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQ--PVAPQPQYQQPQQPVAPQPQDTLLHPLLMRN 853
                         170       180
                  ....*....|....*....|....
gi 530394017  540 QDVKPPFPPDIK-PNMSALPPPPA 562
Cdd:PRK10263  854 GDSRPLHKPTTPlPSLDLLTPPPS 877
 
Name Accession Description Interval E-value
Zmiz1_N pfam18028
Zmiz1 N-terminal tetratricopeptide repeat domain; This is the N-terminal domain found in Zmiz1 ...
8-100 1.92e-53

Zmiz1 N-terminal tetratricopeptide repeat domain; This is the N-terminal domain found in Zmiz1 proteins (Zinc finger MIZ domain-containing protein 1). Zmiz1 is a direct Notch1 cofactor that heterogeneously regulates Notch target genes. Zmiz1 directly interacts with the RAM1 domain of Notch1 through this N-terminal tetratricopeptide repeat (TPR) domain. Furthermore, it has been shown that Zmiz1 and Notch1 cooperatively recruit each other to chromatin through direct interaction via the N-terminal TPR domain resulting in a slight increase in activating histone marks and decrease of repressive histone marks. Functional analysis indicate that the N-Terminal Domain of Zmiz1 is important for driving Myc transcription and proliferation indirectly.


Pssm-ID: 375500  Cd Length: 93  Bit Score: 181.23  E-value: 1.92e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017     8 IQQTNDRLQCIKQHLQNPANFHNAATELLDWCGDPRAFQRPFEQSLMGCLTVVSRVAAQQGFDLDLGYRLLAVCAANRDK 87
Cdd:pfam18028    1 VQQNNDRLQSIKQHLQNPANFHNACTELLDWCGDPRAFQRPFEQNLLGCLTVVVRVATQQGFDLDLAYRLLAVCAANRKL 80
                           90
                   ....*....|...
gi 530394017    88 FTPKSAALLSSWC 100
Cdd:pfam18028   81 LSPKSAALINRWC 93
SP-RING_ZMIZ1 cd16822
SP-RING finger found in zinc finger MIZ domain-containing protein 1 (Zmiz1) and similar ...
743-806 1.93e-42

SP-RING finger found in zinc finger MIZ domain-containing protein 1 (Zmiz1) and similar proteins; Zmiz1, also known as PIAS-like protein Zimp10 (zinc finger-containing, Miz1, PIAS-like protein on chromosome 10) or retinoic acid-induced protein 17, is a novel PIAS-like protein that was initially identified as an androgen receptor (AR) interacting protein and functions as a transcriptional co-activator. It co-localizes with AR and small ubiquitin-like modifier SUMO-1, forms a protein complex at replication foci in the nucleus, and augments AR-mediated transcription. It also functions as a transcriptional co-activator of the p53 tumor suppressor that plays a critical role in cell cycle progression, DNA repair, and apoptosis. Moreover, Zmiz1 dysfunction may be associated with multiple autoimmune diseases and it has been implicated in the development, function, and survival of melanocytes. Zmiz1 also interacts with Smad3/4 proteins and augments Smad-mediated transcription, suggesting it is important in the regulation of the transforming growth factor beta (TGF-beta)/Smad signaling pathway and may have an inhibitory effect on the immune system. Zmiz1 is overexpressed in a significant percentage of human cutaneous squamous cell carcinoma (SCC), breast, ovarian, and colon cancers, suggesting it may play a broader role in epithelial cancers. It functionally interacts with NOTCH1 to promote C-MYC transcription and activity, and thus is involved in a variety of C-MYC-driven cancers. Zmiz1 contains a PAT domain, a highly conserved Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, also known as msx-interacting zinc finger (Miz domain), and a putative nuclear localization sequence (NLS), as well as a strong intrinsic transactivation domain within the C-terminus. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438471  Cd Length: 64  Bit Score: 148.67  E-value: 1.93e-42
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530394017  743 KVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGLEVDQYMW 806
Cdd:cd16822     1 KVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGLEVDQYMW 64
zf-MIZ pfam02891
MIZ/SP-RING zinc finger; This domain has SUMO (small ubiquitin-like modifier) ligase activity ...
744-792 2.94e-22

MIZ/SP-RING zinc finger; This domain has SUMO (small ubiquitin-like modifier) ligase activity and is involved in DNA repair and chromosome organization.


Pssm-ID: 460741  Cd Length: 50  Bit Score: 90.40  E-value: 2.94e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 530394017   744 VSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNK 792
Cdd:pfam02891    1 VSLKCPISYLRISIPVRGRFCKHLQCFDLLSYLESNERTPTWNCPVCDK 49
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
184-468 8.88e-08

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: 56.56  E-value: 8.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   184 NPMANANNPMNPGGNPMASGMTTSNPglNSPQFAGQQQQFSAKAGPAQPYIQQSMYGRPNYPGSGGfGASYPGGPNAPAG 263
Cdd:pfam09606  115 GGPGTASNLLASLGRPQMPMGGAGFP--SQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNG-GPGQGQAGGMNGG 191
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   264 MGIPPHTRPPADFTQPAAAAAAAAVAAAAATATATATATVAALQETQNKDINQYGPVcssfQMGPTQAYNSQFMNQP--- 340
Cdd:pfam09606  192 QQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQP----QQQGQQSQLGMGINQMqqm 267
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   341 -----GPRGPASMGGSMNPASMAAGMTPSGMS--GPPM-----GMNQPRPPGISPFGTHGQRMPQQTYPGPRPQSLPIQN 408
Cdd:pfam09606  268 pqgvgGGAGQGGPGQPMGPPGQQPGAMPNVMSigDQNNyqqqqTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLN 347
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530394017   409 IKRPY--------------PGEPNY--GNQQYGPNSQFPTQPGQYPAPNPPRPLTSPNYPGQRMPSQPSSGQYPPP 468
Cdd:pfam09606  348 HLETWnpgnfgglganpmqRGQPGMmsSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSP 423
PHA03247 PHA03247
large tegument protein UL36; Provisional
119-527 5.75e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.17  E-value: 5.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  119 PPGKLPMQPPLSSMSsmkPTLSHSDGSFPYDSVPWQQNTNQPPG---SLSVVTTVWGVTNTSQSQVLG----------NP 185
Cdd:PHA03247 2618 PPDTHAPDPPPPSPS---PAANEPDPHPPPTVPPPERPRDDPAPgrvSRPRRARRLGRAAQASSPPQRprrraarptvGS 2694
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  186 MANANNPMNPGGNPmASGMTTSNPGLNSPQFAGQQQQfSAKAGPAQPYIQQSMYGrPNYPGSGGFGAS--YPGGPNAPAG 263
Cdd:PHA03247 2695 LTSLADPPPPPPTP-EPAPHALVSATPLPPGPAAARQ-ASPALPAAPAPPAVPAG-PATPGGPARPARppTTAGPPAPAP 2771
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  264 MGIPPHTRPPADFTQPAAAAAAAAVAAAAATATATATATVAALQETQNKDINQYGPVCSsfqmgPTQAYNSQFMNQPGPR 343
Cdd:PHA03247 2772 PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP-----PTSAQPTAPPPPPGPP 2846
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  344 GPA-SMGGSMNPASMAAGMTPSGmSGPPMGMNQPRPPgispfgthGQRMPQ-QTYPGPRPQSLPIQNIKRPYPgepnygn 421
Cdd:PHA03247 2847 PPSlPLGGSVAPGGDVRRRPPSR-SPAAKPAAPARPP--------VRRLARpAVSRSTESFALPPDQPERPPQ------- 2910
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  422 qqygPNSQFPTQPgQYPAPNPPRPLTSPNYPGQrmPSQPSSGQYPPPTVNMGQYYKPEQFNGQnntfsgssysnYSQGNV 501
Cdd:PHA03247 2911 ----PQAPPPPQP-QPQPPPPPQPQPPPPPPPR--PQPPLAPTTDPAGAGEPSGAVPQPWLGA-----------LVPGRV 2972
                         410       420
                  ....*....|....*....|....*.
gi 530394017  502 NRPPRPVPvANYPHSPVPGNPTPPMT 527
Cdd:PHA03247 2973 AVPRFRVP-QPAPSREAPASSTPPLT 2997
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
386-515 2.86e-05

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: 47.88  E-value: 2.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   386 THGQRMPQQTYPGPRPQSLPIQNIkrPYPGEPNYGNQqyGPNSQFPTQPGQYPApnpprpltSPNYPGQRMPSQPSSGQY 465
Cdd:TIGR01628  369 AHLQDQFMQLQPRMRQLPMGSPMG--GAMGQPPYYGQ--GPQQQFNGQPLGWPR--------MSMMPTPMGPGGPLRPNG 436
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 530394017   466 PPPTVNMGQYYKPEQFNGQNNTFSGSSYSNYSQGNVNRPPRPVPVANYPH 515
Cdd:TIGR01628  437 LAPMNAVRAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQ 486
PRK10263 PRK10263
DNA translocase FtsK; Provisional
386-562 2.07e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.46  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  386 THGQRMPQQTYPGPRPQSL------PIQNIKRPYPGEPnygnqQYGPNSQFPTQPGQYPAPNPPRPLTSPNYPGQRMPSQ 459
Cdd:PRK10263  706 TQQQRYSGEQPAGANPFSLddfefsPMKALLDDGPHEP-----LFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQ 780
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  460 PSSGQYPPPtvnmgQYYKPEQFNGQNNTFSGSSYSNYSQGNVNRPPRpvPVANYPHSPVPGNPTPPMTPGSSIPPYLSPS 539
Cdd:PRK10263  781 PQQPVAPQP-----QYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQ--PVAPQPQYQQPQQPVAPQPQDTLLHPLLMRN 853
                         170       180
                  ....*....|....*....|....
gi 530394017  540 QDVKPPFPPDIK-PNMSALPPPPA 562
Cdd:PRK10263  854 GDSRPLHKPTTPlPSLDLLTPPPS 877
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
452-571 2.76e-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: 41.72  E-value: 2.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   452 PGQRMPSQPSSGQypPPTVNMGQYykpEQFNGQNNTFSGSSYSNYSQGNvNRPPRPVPVANYPHSPVPGNPTPPMTPGSS 531
Cdd:TIGR01628  385 LPMGSPMGGAMGQ--PPYYGQGPQ---QQFNGQPLGWPRMSMMPTPMGP-GGPLRPNGLAPMNAVRAPSRNAQNAAQKPP 458
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 530394017   532 IPPYLSPSQDVKPPFPPDiKPNmsalPPPPANHNDELRLT 571
Cdd:TIGR01628  459 MQPVMYPPNYQSLPLSQD-LPQ----PQSTASQGGQNKKL 493
ARG80 COG5068
Regulator of arginine metabolism and related MADS box-containing transcription factors ...
324-541 2.93e-03

Regulator of arginine metabolism and related MADS box-containing transcription factors [Transcription];


Pssm-ID: 227400 [Multi-domain]  Cd Length: 412  Bit Score: 41.15  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  324 FQMGPTQAYnsQFMNQPGPRGPASMGGSMNPASMAAGMTPSGMSGPPMGMNQPRPPGISPFGTHGQR-------MPQQTY 396
Cdd:COG5068   202 LQNPQTQQY--QQHSSRKDHPTVPHSNTNNGRPPAKFMIPELHSSHSTLDLPSDFISDSGFPNQSSTsifpldsAIIQIT 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  397 PGPRPQSLPIQNIKRPYPGEPNYGNQQYGPNSQFPTQPGQYPAPNPPRPLtspnypgqrmPSQPSSGQYPPPTVNmgqyy 476
Cdd:COG5068   280 PPHLPNNPPQENRHELYSNDSSMVSETPPPKNLPNGSPNQSPLNNLSRGN----------PASPNSIIRENNQVE----- 344
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530394017  477 kPEQFNGQNNTFSGSSYSNYSQGNVNRPP-RPVPVANYPHSPVPGN--PTPPMTPGSSIPPYLSPSQD 541
Cdd:COG5068   345 -DESFNGRQGSAIWNALISTTQPNSGLHTeASTAPSSTIPADPLKNaaQTNSGTRNNNFSDNLYGQLN 411
 
Name Accession Description Interval E-value
Zmiz1_N pfam18028
Zmiz1 N-terminal tetratricopeptide repeat domain; This is the N-terminal domain found in Zmiz1 ...
8-100 1.92e-53

Zmiz1 N-terminal tetratricopeptide repeat domain; This is the N-terminal domain found in Zmiz1 proteins (Zinc finger MIZ domain-containing protein 1). Zmiz1 is a direct Notch1 cofactor that heterogeneously regulates Notch target genes. Zmiz1 directly interacts with the RAM1 domain of Notch1 through this N-terminal tetratricopeptide repeat (TPR) domain. Furthermore, it has been shown that Zmiz1 and Notch1 cooperatively recruit each other to chromatin through direct interaction via the N-terminal TPR domain resulting in a slight increase in activating histone marks and decrease of repressive histone marks. Functional analysis indicate that the N-Terminal Domain of Zmiz1 is important for driving Myc transcription and proliferation indirectly.


Pssm-ID: 375500  Cd Length: 93  Bit Score: 181.23  E-value: 1.92e-53
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gi 530394017     8 IQQTNDRLQCIKQHLQNPANFHNAATELLDWCGDPRAFQRPFEQSLMGCLTVVSRVAAQQGFDLDLGYRLLAVCAANRDK 87
Cdd:pfam18028    1 VQQNNDRLQSIKQHLQNPANFHNACTELLDWCGDPRAFQRPFEQNLLGCLTVVVRVATQQGFDLDLAYRLLAVCAANRKL 80
                           90
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gi 530394017    88 FTPKSAALLSSWC 100
Cdd:pfam18028   81 LSPKSAALINRWC 93
SP-RING_ZMIZ1 cd16822
SP-RING finger found in zinc finger MIZ domain-containing protein 1 (Zmiz1) and similar ...
743-806 1.93e-42

SP-RING finger found in zinc finger MIZ domain-containing protein 1 (Zmiz1) and similar proteins; Zmiz1, also known as PIAS-like protein Zimp10 (zinc finger-containing, Miz1, PIAS-like protein on chromosome 10) or retinoic acid-induced protein 17, is a novel PIAS-like protein that was initially identified as an androgen receptor (AR) interacting protein and functions as a transcriptional co-activator. It co-localizes with AR and small ubiquitin-like modifier SUMO-1, forms a protein complex at replication foci in the nucleus, and augments AR-mediated transcription. It also functions as a transcriptional co-activator of the p53 tumor suppressor that plays a critical role in cell cycle progression, DNA repair, and apoptosis. Moreover, Zmiz1 dysfunction may be associated with multiple autoimmune diseases and it has been implicated in the development, function, and survival of melanocytes. Zmiz1 also interacts with Smad3/4 proteins and augments Smad-mediated transcription, suggesting it is important in the regulation of the transforming growth factor beta (TGF-beta)/Smad signaling pathway and may have an inhibitory effect on the immune system. Zmiz1 is overexpressed in a significant percentage of human cutaneous squamous cell carcinoma (SCC), breast, ovarian, and colon cancers, suggesting it may play a broader role in epithelial cancers. It functionally interacts with NOTCH1 to promote C-MYC transcription and activity, and thus is involved in a variety of C-MYC-driven cancers. Zmiz1 contains a PAT domain, a highly conserved Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, also known as msx-interacting zinc finger (Miz domain), and a putative nuclear localization sequence (NLS), as well as a strong intrinsic transactivation domain within the C-terminus. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438471  Cd Length: 64  Bit Score: 148.67  E-value: 1.93e-42
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gi 530394017  743 KVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGLEVDQYMW 806
Cdd:cd16822     1 KVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGLEVDQYMW 64
SP-RING_ZMIZ2 cd16823
SP-RING finger found in zinc finger MIZ domain-containing protein 2 (Zmiz2) and similar ...
738-798 1.33e-38

SP-RING finger found in zinc finger MIZ domain-containing protein 2 (Zmiz2) and similar proteins; Zmiz2, also known as PIAS-like protein Zimp7 (zinc finger-containing, Miz1, PIAS-like protein on chromosome 7), is a novel PIAS-like protein that was initially identified as an androgen receptor (AR) interacting protein and functions as a transcriptional co-activator. It interacts with beta-catenin and enhances Wnt/beta-catenin-mediated transcription. It also associates with BRG1 and BAF57, components of the ATP-dependent mammalian SWI/SNF-like BAF chromatin-remodeling complexes, and thus plays a potential role in modulation of AR and/or other nuclear receptor-mediated transcription. For instance, it can increase the effects of BRG1 on AR-mediated transcriptional activity. Moreover, Zmiz2 physically interacts with PIAS proteins, especially PIAS3. Through this interaction, PIAS3 augments Zmiz2-mediated transcription, suggesting PIAS proteins may play a regulatory role in Zmiz-mediated transcription. Furthermore, Zmiz2 is involved in transcriptional regulation of factors essential for patterning in the dorsoventral axis. It is required for the restriction of the zebrafish organizer and mesoderm development. Zmiz2 contains a PAT domain, a highly conserved Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, also known as msx-interacting zinc finger (Miz domain), and a strong intrinsic transactivation domain within the C-terminus. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438472  Cd Length: 61  Bit Score: 137.49  E-value: 1.33e-38
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gi 530394017  738 EQTAIKVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEG 798
Cdd:cd16823     1 EQTAIKVSLKCPITFRRIQLPARGHDCRHIQCFDLESYLQLNCERGTWRCPVCNKTALLEG 61
SP-RING_ZMIZ cd16791
SP-RING finger found in zinc finger MIZ domain-containing protein Zmiz1, Zmiz2, and similar ...
745-792 9.13e-33

SP-RING finger found in zinc finger MIZ domain-containing protein Zmiz1, Zmiz2, and similar proteins; This subfamily includes Zmiz1 (Zimp10) and its homolog Zmiz2 (Zimp7), both initially identified in humans as androgen receptor (AR) interacting proteins which function as transcriptional co-activators. They interact with BRG1, the catalytic subunit of the SWI-SNF remodeling complex. They also associate with other hormone nuclear receptors and transcription factors, such as p53 and Smad3/Smad4, and regulate transcription of specific target genes by altering their chromatin structure. This subfamily also includes tonalli (Tna), an ortholog identified in Drosophila. It genetically interacts with the ATP-dependent SWI/SNF and Mediator complexes, suggesting a potential role for the Zmiz proteins in chromatin remodeling. Zmiz proteins contain a highly conserved Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, also known as msx-interacting zinc finger (Miz domain), and a strong transactivation domain within the C-terminus. The SP-RING/Miz domain is highly conserved in members of the PIAS family and confers SUMO-conjugating activity. It is a variant of the RING finger, and lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers. The strong intrinsic transactivation domain facilitates Zmiz proteins to augment the transcriptional activity of nuclear hormone receptors and other transcriptional factors. They may act as transcriptional co-regulators.


Pssm-ID: 438445  Cd Length: 48  Bit Score: 120.68  E-value: 9.13e-33
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gi 530394017  745 SLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNK 792
Cdd:cd16791     1 SLKCPITFRRITLPARGHDCKHIQCFDLESYLQLNCERGTWRCPVCNK 48
SP-RING_PIAS-like cd16650
SP-RING finger found in the Siz/PIAS RING (SP-RING) family of SUMO E3 ligases; The SP-RING ...
745-792 2.81e-25

SP-RING finger found in the Siz/PIAS RING (SP-RING) family of SUMO E3 ligases; The SP-RING family includes PIAS (protein inhibitor of activated STAT) proteins, Zmiz proteins, and Siz proteins from plants and fungi. PIAS proteins modulate the activity of several transcription factors and act as E3 ubiquitin ligases in the sumoylation pathway. There are four members: PIAS1, PIAS2 (also known as PIASx), PIAS3, and PIAS4 (also known as PIASy). PIAS proteins were initially identified as inhibitors of activated STAT only, but are now known to interact with and modulate several other proteins, including androgen receptor (AR), tumor suppressor p53, and the transforming growth factor-beta (TGF-beta) signaling protein SMAD. They interact with STATs in a cytokine-dependent manner. PIAS proteins have SUMO E3-ligase activity and interaction of PIAS proteins with transcription factors often results in sumoylation of that protein. Zmiz1 (Zimp10) and its homolog Zmiz2 (Zimp7) were initially identified in humans as androgen receptor (AR) interacting proteins that function as transcriptional co-activators. They interact with BRG1, the catalytic subunit of the SWI-SNF remodeling complex. They also associate with other hormone nuclear receptors and transcription factors such as p53 and Smad3/Smad4, and regulate transcription of specific target genes by altering their chromatin structure. SIZ1 proteins from plants and fungi are also founding members of this family. SIZ1-mediated conjugation of SUMO1 and SUMO2 to other intracellular proteins is essential in Arabidopsis. Yeast SIZ proteins are SUMO E3 ligases involved in a novel pathway of chromosome maintenance. They enhance SUMO modification to many substrates in vivo, but also exhibit unique substrate specificity. PIAS proteins contain a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, which is essential for SUMO ligase activity. The SP-RING finger is a variant of the RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438312  Cd Length: 48  Bit Score: 99.27  E-value: 2.81e-25
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gi 530394017  745 SLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNK 792
Cdd:cd16650     1 SLRCPLSLKRIKTPARGKHCKHLQCFDLDSYLEFNKRKPTWKCPICDK 48
zf-MIZ pfam02891
MIZ/SP-RING zinc finger; This domain has SUMO (small ubiquitin-like modifier) ligase activity ...
744-792 2.94e-22

MIZ/SP-RING zinc finger; This domain has SUMO (small ubiquitin-like modifier) ligase activity and is involved in DNA repair and chromosome organization.


Pssm-ID: 460741  Cd Length: 50  Bit Score: 90.40  E-value: 2.94e-22
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gi 530394017   744 VSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNK 792
Cdd:pfam02891    1 VSLKCPISYLRISIPVRGRFCKHLQCFDLLSYLESNERTPTWNCPVCDK 49
SP-RING_Siz-like cd16792
SP-RING finger found in Arabidopsis thaliana E3 SUMO-protein ligase SIZ1 (AtSIZ1) and similar ...
745-793 1.35e-19

SP-RING finger found in Arabidopsis thaliana E3 SUMO-protein ligase SIZ1 (AtSIZ1) and similar proteins; SIZ1-mediated conjugation of SUMO1 and SUMO2 to other intracellular proteins is essential in Arabidopsis. AtSIZ1 negatively regulates abscisic acid (ABA) signaling through the sumoylation of bZIP transcripton factor ABI5. It also mediates sumoylation of bromodomain GTE proteins. Moreover, AtSIZ1 regulates flowering by controlling a salicylic acid-mediated floral promotion pathway and through affecting on FLOWERING LOCUS C (FLC) chromatin structure. It also plays a role in drought stress response likely through the regulation of gene expression. Members of this subfamily contain an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box, a plant homeodomain (PHD) finger, and a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438446  Cd Length: 50  Bit Score: 82.84  E-value: 1.35e-19
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gi 530394017  745 SLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKT 793
Cdd:cd16792     1 SLKCPLSYSRIKVPCRSIKCTHIQCFDLDSFLQLNEQTPSWQCPICNKN 49
SP-RING-like cd16452
SP-RING finger and SPL-RING finger, variants of RING fingers; This family corresponds to a ...
746-791 1.02e-15

SP-RING finger and SPL-RING finger, variants of RING fingers; This family corresponds to a group of proteins with variants of RING fingers that are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues compared with the classic C3H2C3-/C3HC4-type RING fingers. They include SP-RING finger found in the Siz/PIAS RING (SP-RING) family of SUMO E3 ligases and SPL-RING finger found in E3 SUMO-protein ligase NSE2. The SP-RING family includes PIAS (protein inhibitor of activated STAT) proteins, Zmiz proteins, and Siz proteins from plants and fungi. The PIAS (protein inhibitor of activated STAT) protein family modulates the activity of several transcription factors and acts as an E3 ubiquitin ligase in the sumoylation pathway. NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress.


Pssm-ID: 438116 [Multi-domain]  Cd Length: 45  Bit Score: 71.90  E-value: 1.02e-15
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gi 530394017  746 LKCPITFRRIQLPARGHDCKHvqCFDLESYLQLNCER-GTWRCPVCN 791
Cdd:cd16452     1 LKCPITQKRMKDPVRGKHCGH--CFDLEAILQYLKRRkKKWKCPVCS 45
SP-RING_PIAS2 cd16819
SP-RING finger found in protein inhibitor of activated STAT protein 2 (PIAS2) and similar ...
740-799 1.07e-13

SP-RING finger found in protein inhibitor of activated STAT protein 2 (PIAS2) and similar proteins; PIAS2, also known as androgen receptor-interacting protein 3 (ARIP3), DAB2-interacting protein (DIP), Msx-interacting zinc finger protein (Miz1), PIAS-NY protein, protein inhibitor of activated STAT x, protein inhibitor of activated STAT2, is an E3 SUMO-protein ligase highly expressed in the testis. It functions as a transcriptional activator of BCL2 and is essential for blocking c-MYC-induced apoptosis. It also acts as a negative regulator of cell proliferation, induces expression of the cell-cycle inhibitors p15(Ink4b) and p21(Cip1), and activates transcription of the p21(Cip1) gene in response to UV irradiation. Moreover, PIAS2 associates with topoisomerase II binding protein 1 (TopBP1), an essential activator of the Atr kinase. It thus affects the activity of the Atr checkpoint. Receptor of activated C kinase 1 (RACK1), glucocorticoid receptor (GR)-interacting protein 1 (GRIP1), friend leukemia integration-I (FLI-1), and ubiquitously expressed transcript (UXT) are binding partners of PIAS2. The interaction between UXT and PIAS2 may be important for the transcriptional activation of androgen receptor (AR). PIAS2 contains an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus, and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and an acidic C-terminal domain. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438468  Cd Length: 60  Bit Score: 66.65  E-value: 1.07e-13
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gi 530394017  740 TAIKVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGL 799
Cdd:cd16819     1 TSLRVSLMCPLGKMRLTIPCRAVTCSHLQCFDAALYLQMNEKKPTWICPVCDKKAAYESL 60
SP-RING_PIAS4 cd16821
SP-RING finger found in protein inhibitor of activated STAT protein 4 (PIAS4) and similar ...
740-797 1.33e-12

SP-RING finger found in protein inhibitor of activated STAT protein 4 (PIAS4) and similar proteins; PIAS4, also known as PIASy or protein inhibitor of activated STAT protein gamma (PIAS-gamma), is an E3 SUMO-protein ligase that interacts with the androgen receptor (AR) and is involved in ubiquitin signaling pathways. It is associated with macro/microcephaly in the novel interstitial 19p13.3 microdeletion/microduplication syndrome. It also regulates the hypoxia signalling pathway by interacting with the tumor suppressor von Hippel-Lindau (VHL), which leads to VHL sumoylation, oligomerization, and impaired function during growth of pancreatic cancer cells. Moreover, PIAS4 acts as a direct binding partner for vitamin D receptor (VDR) and facilitates its modification with SUMO2. The process of SUMOylation modulates VDR-mediated signaling. As components of the DNA-damage response (DDR), PIAS4 together with PIAS1 promote responses to DNA double-strand breaks (DSBs). They are required for effective ubiquitin-adduct formation mediated by RNF8, RNF168, and BRCA1 at sites of DNA damage. PIAS4 contains an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and an acidic C-terminal domain. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438470  Cd Length: 58  Bit Score: 63.54  E-value: 1.33e-12
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gi 530394017  740 TAIKVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLE 797
Cdd:cd16821     1 TGVRVSLICPLVKMRLSVPCRAETCAHLQCFDAVFYLQMNEKKPTWTCPVCDKPAPYD 58
SP-RING_PIAS3 cd16820
SP-RING finger found in protein inhibitor of activated STAT protein 3 (PIAS3) and similar ...
740-799 2.98e-12

SP-RING finger found in protein inhibitor of activated STAT protein 3 (PIAS3) and similar proteins; PIAS3 is an E3 SUMO-protein ligase that was initially identified as an interleukin-6 (IL-6)-dependent repressor of signal transducer and activator of transcription 3 (STAT3) and has anti-proliferative properties. It binds specifically to phosphorylated STAT3 and inhibits its transcriptional activity by blocking its binding to DNA. It regulates STAT3-mediated induction of Snail expression, as well as suppresses acute graft-versus-host disease (GVHD) by modulating effector T and B cell subsets through inhibition of STAT3 activation. It activates the intrinsic apoptotic pathway in non-small cell lung cancer cells independent of p53 status. When overexpressed, it can interact with STAT5 to regulate prolactin-induced STAT5-mediated gene expression. Moreover, PIAS3 binds to and activates Smad3 transcriptional activity, resulting in the enhancement of transforming growth factor-beta (TGF-beta) signaling. It functions as a transcriptional corepressor of Erythroid Kruppel-like factor (EKLF or KLF1) and thus plays an important role in erythropoiesis. It also plays a significant role in the DNA damage response (DDR) pathway by promoting homologous recombination (HR)- and non-homologous end joining (NHEJ)-mediated DNA double-strand break (DSB) repair. Furthermore, PIAS3 preferentially interacts with and enhances the SUMOylation of TAK1-binding protein 2 (TAB2), an upstream adaptor protein in the IL-1 signaling pathway. It also promotes SUMOylation and nuclear sequestration of ErbB4 receptor tyrosine kinase. In addition, PIAS3 may form a complex with microphthalmia-associated transcription factor, nuclear factor-kappaB, Smad, and estrogen receptor. Its other transcription factor binding partners include: ETS, EGR1, NR1I2, and GATA1. PIAS3 contains an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and an acidic C-terminal domain. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438469  Cd Length: 62  Bit Score: 62.75  E-value: 2.98e-12
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gi 530394017  740 TAIKVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGL 799
Cdd:cd16820     1 TSLRVSLMCPLGKMRLTVPCRAITCTHLQCFDAALYLQMNEKKPTWTCPVCDKKAPYESL 60
SP-RING_PIAS1 cd16818
SP-RING finger found in protein inhibitor of activated STAT protein 1 (PIAS1) and similar ...
740-799 3.32e-12

SP-RING finger found in protein inhibitor of activated STAT protein 1 (PIAS1) and similar proteins; PIAS1, also known as DEAD/H box-binding protein 1, Gu-binding protein (GBP), or RNA helicase II-binding protein, was initially identified as an inhibitor of STAT1 that blocks the DNA-binding activity of STAT1 and specifically inhibits STAT1-mediated gene transcription in response to cytokine stimulation. It selectively inhibits interferon-inducible gene expression and plays an important role in the IFN-gamma- or IFN-beta-mediated innate immune response through negative regulation of STAT1. It also regulates the activity of other transcription factors to regulate immune response, such as NF-kappaB and Smad4. Moreover, PIAS1 functions as an E3 small ubiquitin-like modifier (SUMO)-protein ligase specifying target proteins for SUMO conjugation by Ubc9. The sumoylation activity of PIAS1 can suppress cytokine transforming growth factor beta (TGFbeta)-induced epithelial mesenchymal transition (EMT) in non-transformed epithelial cells to promote activation of the matrix metalloproteinase 2 (MMP2). It thus regulates TGFbeta-induced cancer cell invasion and metastasis. PIAS1 may also be involved in spatial learning and memory formation through its SUMOylation of cAMP-responsive element binding protein (CREB). In addition, PIAS1 is the E3 ligase responsible for SUMOylation of High mobility group nucleosomal binding domain 2 (HMGN2), which is a small and unique non-histone protein that has many functions in a variety of cellular processes, including regulation of chromatin structure, transcription, and DNA repair, as well as antimicrobial activity, cell homing, and regulating cytokine release. Furthermore, PIAS1 is a genuine chromatin-bound androgen receptor (AR) co-regulator that functions in a target gene selective fashion to regulate prostate cancer cell growth. It also mediates the SUMOylation of c-Myc, which is the most frequently overexpressed oncogene in tumors, including breast cancer, colon cancer, and lung cancer. Necdin, a pleiotropic protein that promotes differentiation and survival of mammalian neurons, can suppress PIAS1 both by inhibiting SUMO E3 ligase activity and by promoting ubiquitin-dependent degradation. PIAS1 contains an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and the acidic C-terminal domain. The SP-RING finger mediates the interaction of PIAS1 with the SUMO E2 conjugating enzyme Ubc9. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438467  Cd Length: 60  Bit Score: 62.38  E-value: 3.32e-12
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gi 530394017  740 TAIKVSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNKTALLEGL 799
Cdd:cd16818     1 TSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHL 60
SP-RING_PIAS cd16790
SP-RING finger found in protein inhibitor of activated signal transducer and activator of ...
745-792 6.58e-12

SP-RING finger found in protein inhibitor of activated signal transducer and activator of transcription (PIAS) proteins; The PIAS (protein inhibitor of activated STAT) protein family modulates the activity of several transcription factors and acts as an E3 ubiquitin ligase in the sumoylation pathway. It consists of four members: PIAS1, PIAS2 (also known as PIASx), PIAS3, and PIAS4 (also known as PIASy). PIAS proteins were initially identified as inhibitors of activated STAT only, but are now known to interact with and modulate several other proteins, including androgen receptor (AR), tumor suppressor p53, and the transforming growth factor-beta (TGF-beta) signaling protein SMAD. They interact with STATs in a cytokine-dependent manner. PIAS1, PIAS2, and PIAS3 interact with STAT1, STAT3, and STAT4, respectively. In addition, PIAS4 is associated with STAT1. PIAS proteins have SUMO E3-ligase activity and interaction of PIAS proteins with transcription factors often results in sumoylation of that protein. PIAS proteins contain an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, which is required for the trans-repression of STAT1 activity by PIAS2, a PINT motif, which is essential for nuclear retention of PIAS3L (the long form of PIAS3), a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, which is essential for SUMO ligase activity, and the acidic C-terminal domain, which is involved in binding of PIAS3 to the nuclear coactivator TIF2. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438444  Cd Length: 48  Bit Score: 60.98  E-value: 6.58e-12
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gi 530394017  745 SLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVCNK 792
Cdd:cd16790     1 SLMCPLGKMRLTIPCRALTCSHLQCFDAALYLQMNEKKPTWICPVCDK 48
SP-RING_ScSiz-like cd16793
SP-RING finger found in Saccharomyces cerevisiae E3 SUMO-protein ligase SIZ1, SIZ2, and ...
744-790 2.76e-10

SP-RING finger found in Saccharomyces cerevisiae E3 SUMO-protein ligase SIZ1, SIZ2, and similar proteins; Saccharomyces cerevisiae SIZ proteins, also known as SAP and Miz-finger domain-containing proteins, are Siz/PIAS RING (SP-RING) family SUMO E3 ligases, and may be involved in a novel pathway of chromosome maintenance. They enhance SUMO modification with many substrates in vivo, but also exhibit unique substrate specificity. SIZ1, also known as ubiquitin-like protein ligase 1 (Ull1), modifies both cytoplasmic and nuclear proteins. It functions as an E3 factor specific for septin components. SIZ1-dependent substrates include Cdc3 and Cdc11 (septin subunits), Prp45 (a splicing factor), and the proliferating cell nuclear antigen (PCNA). SIZ2, also known as NFI1, interacts with Smt3, SUMO/Smt3 conjugating enzyme Ubc9, and a septin component Cdc3. Members of this subfamily contain an N-terminal SAP (scaffold attachment factor A/B (SAF-A/B), acinus and PIAS) box with the LXXLL signature, a PINT motif, a specific RING finger known as Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING (SP-RING) finger, and an acidic C-terminal domain. The SP-RING finger is a variant of RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It binds a single Zn ion, instead of two ions bound by typical RING fingers.


Pssm-ID: 438447  Cd Length: 56  Bit Score: 57.00  E-value: 2.76e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 530394017  744 VSLKCPITFRRIQLPARGHDCKHVQCFDLESYLQLNCERGTWRCPVC 790
Cdd:cd16793     4 MSLQCPISYTRMKYPSKSINCKHLQCFDALWFLHSQLQIPTWQCPVC 50
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
184-468 8.88e-08

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: 56.56  E-value: 8.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   184 NPMANANNPMNPGGNPMASGMTTSNPglNSPQFAGQQQQFSAKAGPAQPYIQQSMYGRPNYPGSGGfGASYPGGPNAPAG 263
Cdd:pfam09606  115 GGPGTASNLLASLGRPQMPMGGAGFP--SQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNG-GPGQGQAGGMNGG 191
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   264 MGIPPHTRPPADFTQPAAAAAAAAVAAAAATATATATATVAALQETQNKDINQYGPVcssfQMGPTQAYNSQFMNQP--- 340
Cdd:pfam09606  192 QQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQP----QQQGQQSQLGMGINQMqqm 267
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   341 -----GPRGPASMGGSMNPASMAAGMTPSGMS--GPPM-----GMNQPRPPGISPFGTHGQRMPQQTYPGPRPQSLPIQN 408
Cdd:pfam09606  268 pqgvgGGAGQGGPGQPMGPPGQQPGAMPNVMSigDQNNyqqqqTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLN 347
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530394017   409 IKRPY--------------PGEPNY--GNQQYGPNSQFPTQPGQYPAPNPPRPLTSPNYPGQRMPSQPSSGQYPPP 468
Cdd:pfam09606  348 HLETWnpgnfgglganpmqRGQPGMmsSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSP 423
SPL-RING_NSE2 cd16651
SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as ...
746-806 1.05e-07

SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress. Moreover, NSE2 together with its partner proteins SMC6 and SMC5 form a tight subcomplex of the structural maintenance of chromosomes SMC5-6 complex, which includes another two subcomplexes, NSE1-NSE3-NSE4 and NSE5-NSE6. SMC6 and NSE3 are sumoylated in an NSE2-dependent manner, but SMC5 and NSE1 are not. NSE2-dependent E3 SUMO ligase activity is required for efficient DNA repair, but not for SMC5-6 complex stability. NSE2 contains a RING variant known as a Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription)-like RING (SPL-RING) finger that is likely shared by the SP-RING type SUMO E3 ligases, such as PIAS family proteins. The SPL-RING finger is a variant of the RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It harbors only one Zn binding site and is required for the sumoylating activity.


Pssm-ID: 438313 [Multi-domain]  Cd Length: 67  Bit Score: 49.95  E-value: 1.05e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530394017  746 LKCPITFRRIQLPARGHDCKHVqcFDLESYLQ-LNCERGTWRCPV--CNKTALLEGLEVDQYMW 806
Cdd:cd16651     1 LKCPITQQLMVDPVRNKKCGHT--YEKAAILQyLQSRKKKAKCPVagCRNTVSKSDLVPDPELK 62
PHA03247 PHA03247
large tegument protein UL36; Provisional
119-527 5.75e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.17  E-value: 5.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  119 PPGKLPMQPPLSSMSsmkPTLSHSDGSFPYDSVPWQQNTNQPPG---SLSVVTTVWGVTNTSQSQVLG----------NP 185
Cdd:PHA03247 2618 PPDTHAPDPPPPSPS---PAANEPDPHPPPTVPPPERPRDDPAPgrvSRPRRARRLGRAAQASSPPQRprrraarptvGS 2694
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  186 MANANNPMNPGGNPmASGMTTSNPGLNSPQFAGQQQQfSAKAGPAQPYIQQSMYGrPNYPGSGGFGAS--YPGGPNAPAG 263
Cdd:PHA03247 2695 LTSLADPPPPPPTP-EPAPHALVSATPLPPGPAAARQ-ASPALPAAPAPPAVPAG-PATPGGPARPARppTTAGPPAPAP 2771
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  264 MGIPPHTRPPADFTQPAAAAAAAAVAAAAATATATATATVAALQETQNKDINQYGPVCSsfqmgPTQAYNSQFMNQPGPR 343
Cdd:PHA03247 2772 PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP-----PTSAQPTAPPPPPGPP 2846
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  344 GPA-SMGGSMNPASMAAGMTPSGmSGPPMGMNQPRPPgispfgthGQRMPQ-QTYPGPRPQSLPIQNIKRPYPgepnygn 421
Cdd:PHA03247 2847 PPSlPLGGSVAPGGDVRRRPPSR-SPAAKPAAPARPP--------VRRLARpAVSRSTESFALPPDQPERPPQ------- 2910
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  422 qqygPNSQFPTQPgQYPAPNPPRPLTSPNYPGQrmPSQPSSGQYPPPTVNMGQYYKPEQFNGQnntfsgssysnYSQGNV 501
Cdd:PHA03247 2911 ----PQAPPPPQP-QPQPPPPPQPQPPPPPPPR--PQPPLAPTTDPAGAGEPSGAVPQPWLGA-----------LVPGRV 2972
                         410       420
                  ....*....|....*....|....*.
gi 530394017  502 NRPPRPVPvANYPHSPVPGNPTPPMT 527
Cdd:PHA03247 2973 AVPRFRVP-QPAPSREAPASSTPPLT 2997
PHA03247 PHA03247
large tegument protein UL36; Provisional
185-579 6.98e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.79  E-value: 6.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  185 PMANANNPMNPGGNPMASGMTTSNPGLNSPQfagQQQQFSAKAGPAQPYIQQSMYGRPNYPgsggfgASYPGGPNAPAgm 264
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPP---ERPRDDPAPGRVSRPRRARRLGRAAQA------SSPPQRPRRRA-- 2687
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  265 gIPPHTRPPADFTQPAAAAAAAAVAAAAATATATAtatvaalqetqnkdinqygPVCSSFQMGPTQAYNSQFMNQPGPRG 344
Cdd:PHA03247 2688 -ARPTVGSLTSLADPPPPPPTPEPAPHALVSATPL-------------------PPGPAAARQASPALPAAPAPPAVPAG 2747
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  345 PASMGGSMNPASMAAGMTPSGMSGP--PMGMNQPR--PPGISPFGTHGQRMPQQTYPGPRPQSLPIQNIKRPYPGEPNYG 420
Cdd:PHA03247 2748 PATPGGPARPARPPTTAGPPAPAPPaaPAAGPPRRltRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP 2827
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  421 NQQygPNSQFPTQPGQYPAPNPPR-PLTSPNYPGQRMPSQPSSGQyPPPTVNMGQYYKPEQFNGQNNTFSGSSYSnysqg 499
Cdd:PHA03247 2828 LPP--PTSAQPTAPPPPPGPPPPSlPLGGSVAPGGDVRRRPPSRS-PAAKPAAPARPPVRRLARPAVSRSTESFA----- 2899
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  500 nvnRPPRPVPVANYPHSPVPGNPTPPMTPGSSIPPYLSPSQDVKPPFPPDIKPnMSALPPPPANHNDELRLTFPVRDGVV 579
Cdd:PHA03247 2900 ---LPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDP-AGAGEPSGAVPQPWLGALVPGRVAVP 2975
PHA03247 PHA03247
large tegument protein UL36; Provisional
185-562 3.27e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 3.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  185 PMANANNPmnPGGNPMASGMTTSNPGLNSPQFAGQQQQFSAKAGPAQPYIQQSMYGRPNYPGSGGFGASYPGGPNAPAGM 264
Cdd:PHA03247 2631 PSPAANEP--DPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTP 2708
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  265 GIPPHTRPPADFTQPAAAAAAAAVAAAAATATATATATVAALQETQNKDINQ---YGPVCSSFQMGPTQAynsqfmnqPG 341
Cdd:PHA03247 2709 EPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPpttAGPPAPAPPAAPAAG--------PP 2780
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  342 PRGPASMGGSMNPASMAAGmTPSGMSGPPMGMNQP--------RPPGISPFGTHGQRMPQQTYPGPRPQSLPIQNikRPY 413
Cdd:PHA03247 2781 RRLTRPAVASLSESRESLP-SPWDPADPPAAVLAPaaalppaaSPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGG--SVA 2857
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  414 PGEPNygnQQYGPNSQFPTQPGQYPAPnPPRPLTSPNYPGQRMP-SQPSSGQYPPPTVNMGQYYKPeqfngqnntfsgss 492
Cdd:PHA03247 2858 PGGDV---RRRPPSRSPAAKPAAPARP-PVRRLARPAVSRSTESfALPPDQPERPPQPQAPPPPQP-------------- 2919
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530394017  493 ysnysQGNVNRPPRPVPvanypHSPVPGNPTPPMTPGSSIPPYLSPSQDVKPPFPPDIKPNMSALP----PPPA 562
Cdd:PHA03247 2920 -----QPQPPPPPQPQP-----PPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPrfrvPQPA 2983
PHA03378 PHA03378
EBNA-3B; Provisional
342-577 7.09e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 50.45  E-value: 7.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  342 PRGPASMggSMNPASMAAGMTPSGMSGPPMGMNQPRPpgiSPFGTHGQRMPQQTypgPRPQSLPIQNiKRPYPGEPNYGN 421
Cdd:PHA03378  606 PEPPTTQ--SHIPETSAPRQWPMPLRPIPMRPLRMQP---ITFNVLVFPTPHQP---PQVEITPYKP-TWTQIGHIPYQP 676
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  422 QQYGPNSQFPTQ--PGQY-PAPNPPRPLTSPNY-PGQRMPSQPSSGQYPPPTVNMGQYYKPEQFNGQNNTFSGSSysnys 497
Cdd:PHA03378  677 SPTGANTMLPIQwaPGTMqPPPRAPTPMRPPAApPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAP----- 751
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  498 qgNVNRPPRPVPVANYPHSPVPGNPTPPMTPGSSIPPYLSPSQDVKPPFPPDIKPNMSALPPP-------PANHNDELRL 570
Cdd:PHA03378  752 --GRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRaapgqqgPTKQILRQLL 829

                  ....*..
gi 530394017  571 TFPVRDG 577
Cdd:PHA03378  830 TGGVKRG 836
zf-Nse pfam11789
Zinc-finger of the MIZ type in Nse subunit; Nse1 and Nse2 are novel non-SMC subunits of the ...
743-789 9.13e-06

Zinc-finger of the MIZ type in Nse subunit; Nse1 and Nse2 are novel non-SMC subunits of the fission yeast Smc5-6 DNA repair complex. This family is the zinc-finger domain similar to the MIZ type of zinc-finger.


Pssm-ID: 403098 [Multi-domain]  Cd Length: 57  Bit Score: 43.82  E-value: 9.13e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 530394017   743 KVSLKCPITFRRIQLPARGHDCKHVqcFDLESYLQLNCERGTWRCPV 789
Cdd:pfam11789    9 TISLTCPLTLQPFVEPVTSKKCNHV--FEKDAILEMLKRNPTVKCPV 53
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
322-561 1.22e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 49.69  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  322 SSFQMGPTQAYNSQFMNQPgPRGPASMGgsMNPASMAAGMTPSGMSGPPMGMNQPR---PPGISPFGTHGQRmpqqtyPG 398
Cdd:PTZ00449  492 SKKKLAPIEEEDSDKHDEP-PEGPEASG--LPPKAPGDKEGEEGEHEDSKESDEPKeggKPGETKEGEVGKK------PG 562
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  399 P----RPQSLPIQNIKRPYPGEPNYGNQQYGPNS----QFPTQPGQYPAPNPPRPLTSPNYPgqRMPSQPSSGQYPPPTV 470
Cdd:PTZ00449  563 PakehKPSKIPTLSKKPEFPKDPKHPKDPEEPKKpkrpRSAQRPTRPKSPKLPELLDIPKSP--KRPESPKSPKRPPPPQ 640
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  471 NMGQYYKPEQFNGQNNTFSGSS-------------YSNYSQG------NVNRPPRPVPVANYPHSPVPGNPTPPMTPGSS 531
Cdd:PTZ00449  641 RPSSPERPEGPKIIKSPKPPKSpkppfdpkfkekfYDDYLDAaakskeTKTTVVLDESFESILKETLPETPGTPFTTPRP 720
                         250       260       270
                  ....*....|....*....|....*....|...
gi 530394017  532 IPPYL--SPSQDVKPPFPPDI-KPNMSALPPPP 561
Cdd:PTZ00449  721 LPPKLprDEEFPFEPIGDPDAeQPDDIEFFTPP 753
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
319-529 1.97e-05

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: 48.85  E-value: 1.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   319 PVCSSFQMGPTQAYNSQFMNQ----PGPRGPASMGGSMNPASM-----AAGMTPSGMSGPPMGMNQPRPPGISPFGTHGQ 389
Cdd:pfam09606   81 DPINALQNLAGQGTRPQMMGPmgpgPGGPMGQQMGGPGTASNLlaslgRPQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQ 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   390 RMPQQTYPGPRPQSLPIQNIKRPYPGEPNYGnQQYGPNSQfptQPGQYPAPNPPRPLTSPNYPGQRMPS----QPSSGQY 465
Cdd:pfam09606  161 PSSGQPGSGTPNQMGPNGGPGQGQAGGMNGG-QQGPMGGQ---MPPQMGVPGMPGPADAGAQMGQQAQAnggmNPQQMGG 236
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530394017   466 PPPTVNMGQYYKPEQFNGQNNTFSGSSYSNYSQGNVNRPPRPVPVANY-PHSPVPGNPTPPMTPG 529
Cdd:pfam09606  237 APNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMgPPGQQPGAMPNVMSIG 301
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
386-515 2.86e-05

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: 47.88  E-value: 2.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   386 THGQRMPQQTYPGPRPQSLPIQNIkrPYPGEPNYGNQqyGPNSQFPTQPGQYPApnpprpltSPNYPGQRMPSQPSSGQY 465
Cdd:TIGR01628  369 AHLQDQFMQLQPRMRQLPMGSPMG--GAMGQPPYYGQ--GPQQQFNGQPLGWPR--------MSMMPTPMGPGGPLRPNG 436
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 530394017   466 PPPTVNMGQYYKPEQFNGQNNTFSGSSYSNYSQGNVNRPPRPVPVANYPH 515
Cdd:TIGR01628  437 LAPMNAVRAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQ 486
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
335-442 1.79e-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: 1.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   335 QFMnQPGPRGPASMGGSMNPASMAA----GMTPSGMSGPPMGMNQPRPPGISPFGTHGQRMPQqTYPGPRPQSLPIQNiK 410
Cdd:TIGR01628  374 QFM-QLQPRMRQLPMGSPMGGAMGQppyyGQGPQQQFNGQPLGWPRMSMMPTPMGPGGPLRPN-GLAPMNAVRAPSRN-A 450
                           90       100       110
                   ....*....|....*....|....*....|..
gi 530394017   411 RPYPGEPNYGNQQYGPNSQFPTQPGQYPAPNP 442
Cdd:TIGR01628  451 QNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQS 482
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
328-564 1.91e-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: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   328 PTQAYNSQFMNQPGPRGPASMGGSMNPASMAAGMTPSGMSGPPMGMNQPRPPGISPFGTHGQRMPQ----QTYPGPRPQS 403
Cdd:pfam03154  213 ATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMphslQTGPSHMQHP 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   404 LPIQnikrPYPGEPNYGNQQY--GPNSQFPTQPGQYPAPNPPRPLTSPNYPGQRMPSQPSSGQY----PPPTVNMGQYYK 477
Cdd:pfam03154  293 VPPQ----PFPLTPQSSQSQVppGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMphikPPPTTPIPQLPN 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   478 PEQFNGQNNTFSGSSYsnysQGNVNRPPRPV--PVANYPHSPVPGNPTPP---MTPGSSIPPylspsqdvkPPFPPDIKP 552
Cdd:pfam03154  369 PQSHKHPPHLSGPSPF----QMNSNLPPPPAlkPLSSLSTHHPPSAHPPPlqlMPQSQQLPP---------PPAQPPVLT 435
                          250
                   ....*....|..
gi 530394017   553 NMSALPPPPANH 564
Cdd:pfam03154  436 QSQSLPPPAASH 447
PRK10263 PRK10263
DNA translocase FtsK; Provisional
386-562 2.07e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.46  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  386 THGQRMPQQTYPGPRPQSL------PIQNIKRPYPGEPnygnqQYGPNSQFPTQPGQYPAPNPPRPLTSPNYPGQRMPSQ 459
Cdd:PRK10263  706 TQQQRYSGEQPAGANPFSLddfefsPMKALLDDGPHEP-----LFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQ 780
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  460 PSSGQYPPPtvnmgQYYKPEQFNGQNNTFSGSSYSNYSQGNVNRPPRpvPVANYPHSPVPGNPTPPMTPGSSIPPYLSPS 539
Cdd:PRK10263  781 PQQPVAPQP-----QYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQ--PVAPQPQYQQPQQPVAPQPQDTLLHPLLMRN 853
                         170       180
                  ....*....|....*....|....
gi 530394017  540 QDVKPPFPPDIK-PNMSALPPPPA 562
Cdd:PRK10263  854 GDSRPLHKPTTPlPSLDLLTPPPS 877
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
111-472 2.37e-04

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: 45.38  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   111 HQKSRQSDPPGKLPMQPPLSSMSSMKPTLSHSDGSFPYDSVPWQQNTNQP-----PGSLSVVTTVWGVTNTSQSQvlgNP 185
Cdd:pfam09606  125 ASLGRPQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMgpnggPGQGQAGGMNGGQQGPMGGQ---MP 201
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   186 MA----NANNPMNPGGN-----PMASGMTTSNPGLNSPQFAGQQQQFSAKAGPAQPYIQQSMYGRPNYPGSGGFGASYPG 256
Cdd:pfam09606  202 PQmgvpGMPGPADAGAQmgqqaQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPG 281
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   257 GPNAPAGMGipPHTRPPADFTQPAAAAAAAAVAAAAATATATATATVAALQETQNKDINQYGPVCSSFQMGPTQAYNSQF 336
Cdd:pfam09606  282 QPMGPPGQQ--PGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGG 359
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   337 MNQPGP-RGPASMGGSMNPASMAAGMTPSGMSGPPMGMNQPRPPGISPFGTHGQRMPQQTYPGPRPQSLPIQNIKRPYPG 415
Cdd:pfam09606  360 LGANPMqRGQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQ 439
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 530394017   416 EPNYGnqQYGPNSQFPTqPGQYPAPNPPRPLTSPNYpgqrMPSQPSSGQYPPPTVNM 472
Cdd:pfam09606  440 QRTIG--QDSPGGSLNT-PGQSAVNSPLNPQEEQLY----REKYRQLTKYIEPLKRM 489
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
371-470 5.34e-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: 44.03  E-value: 5.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   371 MGMNQPrpPGISPF-GTHGQRM-----PQQTYPGpRPQSLPIQNiKRPYPGEPNYGNQ-----QYGPNSQFPTQPGQYPA 439
Cdd:TIGR01628  380 PRMRQL--PMGSPMgGAMGQPPyygqgPQQQFNG-QPLGWPRMS-MMPTPMGPGGPLRpnglaPMNAVRAPSRNAQNAAQ 455
                           90       100       110
                   ....*....|....*....|....*....|.
gi 530394017   440 PNPPRPLTSPnyPGQRMPSQPSSGQYPPPTV 470
Cdd:TIGR01628  456 KPPMQPVMYP--PNYQSLPLSQDLPQPQSTA 484
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
327-456 7.71e-04

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: 43.49  E-value: 7.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   327 GPTQAYNSQFMnQPGPRGPASMGGSMNPASMAAGMTPSGMSGPPM-----GMNQPRPPGISPFGTHGQRMPQQTYPGPRP 401
Cdd:pfam09770  220 QPPAAPPAQQA-QQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVtilqrPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQ 298
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 530394017   402 QSLPIQNIKRPYPGEPNYGNQQYGPNSQFPTQPGQYPAPNPPRPLTSPNYPGQRM 456
Cdd:pfam09770  299 PTQILQNPNRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITHPQQLA 353
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
354-467 1.09e-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: 43.10  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   354 PASMAAGMTPSGMSGPPMGMNQPRPPGIS---PFGTHGQRMPQQTYPGPRPQSLPIQNIKRPYPGEPNYGN------QQY 424
Cdd:pfam09770  213 QPAPAPAQPPAAPPAQQAQQQQQFPPQIQqqqQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQPSIQPqaqqfhQQP 292
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 530394017   425 GPNSQFPTQ---------PGQYPAPNPPRPLTSPNYPGQRMPSQPSSGQYPP 467
Cdd:pfam09770  293 PPVPVQPTQilqnpnrlsAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAP 344
dnaA PRK14086
chromosomal replication initiator protein DnaA;
392-564 1.75e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 42.51  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  392 PQQTYPGPRPQSLPiqniKRPYPGepnygnqqYGPNSQFPTQPGqyPAPNPPRPLTSPNYPGQRMPSQPssGQYPPPTVN 471
Cdd:PRK14086  101 HARRTSEPELPRPG----RRPYEG--------YGGPRADDRPPG--LPRQDQLPTARPAYPAYQQRPEP--GAWPRAADD 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  472 MGQYYKPEQFNGQNNTFSGSSYS--------NYSQGNVNRPPR------PVPVANYPHS-------PVPGNPTPPMTPGS 530
Cdd:PRK14086  165 YGWQQQRLGFPPRAPYASPASYApeqerdrePYDAGRPEYDQRrrdydhPRPDWDRPRRdrtdrpePPPGAGHVHRGGPG 244
                         170       180       190
                  ....*....|....*....|....*....|....
gi 530394017  531 SIPPYLSPSQDVKPPFPPDIKPNMSALPPPPANH 564
Cdd:PRK14086  245 PPERDDAPVVPIRPSAPGPLAAQPAPAPGPGEPT 278
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
505-582 1.92e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 42.10  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  505 PRPVPVANYPHSPVP----GNPTP---PMTPGSSIPPYLSPSQDVKPPFPPDIKPNMSALPPPPANHNDELRLTFPVRDG 577
Cdd:PRK14950  362 PVPAPQPAKPTAAAPspvrPTPAPstrPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPKLTRAAIPVDEK 441

                  ....*
gi 530394017  578 VVLEP 582
Cdd:PRK14950  442 PKYTP 446
PHA03369 PHA03369
capsid maturational protease; Provisional
392-469 2.15e-03

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 41.91  E-value: 2.15e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530394017  392 PQQTYPGPRPQSLPIQNIKRPYPGEPNYGNQQYGPNSQFPTQPGqypapnpPRPLTSPNYPGQRMPSQPSSGQYPPPT 469
Cdd:PHA03369  371 APQTHTGPADRQRPQRPDGIPYSVPARSPMTAYPPVPQFCGDPG-------LVSPYNPQSPGTSYGPEPVGPVPPQPT 441
PHA03247 PHA03247
large tegument protein UL36; Provisional
358-562 2.68e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  358 AAGMTPSGMSGPPMGMNQPRPPG-----ISPFGTHGQ----RM------------------------------PQQTYPG 398
Cdd:PHA03247 2491 AAGAAPDPGGGGPPDPDAPPAPSrlapaILPDEPVGEpvhpRMltwirgleelasddagdpppplppaappaaPDRSVPP 2570
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  399 PRPQSLPIQ-----NIKRP-YPGEPNYGNQQYGPNSQFPTQPGQYPAP---NPPRPLTSPNYPGQRMPSQPSSGQYPPPT 469
Cdd:PHA03247 2571 PRPAPRPSEpavtsRARRPdAPPQSARPRAPVDDRGDPRGPAPPSPLPpdtHAPDPPPPSPSPAANEPDPHPPPTVPPPE 2650
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  470 VNM-----GQYYKPEQFNGQNNTFSGSSysnYSQGNVNRPPRPV--PVANY----PHSPVPGNPTPPMTPGSSIPPYLSP 538
Cdd:PHA03247 2651 RPRddpapGRVSRPRRARRLGRAAQASS---PPQRPRRRAARPTvgSLTSLadppPPPPTPEPAPHALVSATPLPPGPAA 2727
                         250       260
                  ....*....|....*....|....
gi 530394017  539 SQDVKPPFPPDIKPnmsalPPPPA 562
Cdd:PHA03247 2728 ARQASPALPAAPAP-----PAVPA 2746
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
452-571 2.76e-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: 41.72  E-value: 2.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   452 PGQRMPSQPSSGQypPPTVNMGQYykpEQFNGQNNTFSGSSYSNYSQGNvNRPPRPVPVANYPHSPVPGNPTPPMTPGSS 531
Cdd:TIGR01628  385 LPMGSPMGGAMGQ--PPYYGQGPQ---QQFNGQPLGWPRMSMMPTPMGP-GGPLRPNGLAPMNAVRAPSRNAQNAAQKPP 458
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 530394017   532 IPPYLSPSQDVKPPFPPDiKPNmsalPPPPANHNDELRLT 571
Cdd:TIGR01628  459 MQPVMYPPNYQSLPLSQD-LPQ----PQSTASQGGQNKKL 493
ARG80 COG5068
Regulator of arginine metabolism and related MADS box-containing transcription factors ...
324-541 2.93e-03

Regulator of arginine metabolism and related MADS box-containing transcription factors [Transcription];


Pssm-ID: 227400 [Multi-domain]  Cd Length: 412  Bit Score: 41.15  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  324 FQMGPTQAYnsQFMNQPGPRGPASMGGSMNPASMAAGMTPSGMSGPPMGMNQPRPPGISPFGTHGQR-------MPQQTY 396
Cdd:COG5068   202 LQNPQTQQY--QQHSSRKDHPTVPHSNTNNGRPPAKFMIPELHSSHSTLDLPSDFISDSGFPNQSSTsifpldsAIIQIT 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  397 PGPRPQSLPIQNIKRPYPGEPNYGNQQYGPNSQFPTQPGQYPAPNPPRPLtspnypgqrmPSQPSSGQYPPPTVNmgqyy 476
Cdd:COG5068   280 PPHLPNNPPQENRHELYSNDSSMVSETPPPKNLPNGSPNQSPLNNLSRGN----------PASPNSIIRENNQVE----- 344
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530394017  477 kPEQFNGQNNTFSGSSYSNYSQGNVNRPP-RPVPVANYPHSPVPGN--PTPPMTPGSSIPPYLSPSQD 541
Cdd:COG5068   345 -DESFNGRQGSAIWNALISTTQPNSGLHTeASTAPSSTIPADPLKNaaQTNSGTRNNNFSDNLYGQLN 411
PHA03377 PHA03377
EBNA-3C; Provisional
376-568 3.72e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 41.58  E-value: 3.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  376 PRPPGISPFGTHGQ-RMPQQTYPG---PRPQSLPIQNIKRPypgepnygNQQYGPNSQFPTQPGQYPA-PNPPRPLTS-- 448
Cdd:PHA03377  740 PPPSHQAPYSGHEEpQAQQAPYPGywePRPPQAPYLGYQEP--------QAQGVQVSSYPGYAGPWGLrAQHPRYRHSwa 811
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  449 --PNYPGQRMPSQP--SSGQYPPPTvnmgqyykpeqfngqnntFSGSSYSNYSQGNVNRPPRPVPVANYPH-SPVPGNPT 523
Cdd:PHA03377  812 ywSQYPGHGHPQGPwaPRPPHLPPQ------------------WDGSAGHGQDQVSQFPHLQSETGPPRLQlSQVPQLPY 873
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 530394017  524 PPMTPGSSIPPYLSPsqdvkPPFPPdIKPNMSALPPPPANHNDEL 568
Cdd:PHA03377  874 SQTLVSSSAPSWSSP-----QPRAP-IRPIPTRFPPPPMPLQDSM 912
PHA03379 PHA03379
EBNA-3A; Provisional
318-549 7.45e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 40.43  E-value: 7.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  318 GPVCSSFQMGPTQAYNSQFmnqpGPRGPASMGGSMNPASMAAGMTPSGMSGPPMGMNQPRPPGISPFGTHGQRMPQQTYP 397
Cdd:PHA03379  503 GPIVRPWEASLSQVPGVAF----APVMPQPMPVEPVPVPTVALERPVCPAPPLIAMQGPGETSGIVRVRERWRPAPWTPN 578
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  398 GPRPQSlPIQNIKRPYPGEPnygnQQYGPNSQFPTQPGQYPAPNPPRPLTSPNYPGQRM-PSQPSSGQYPPPTVNMGQYY 476
Cdd:PHA03379  579 PPRSPS-QMSVRDRLARLRA----EAQPYQASVEVQPPQLTQVSPQQPMEYPLEPEQQMfPGSPFSQVADVMRAGGVPAM 653
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530394017  477 KPEQFNG--QNNTFSGSSYSNYSQGNVNRPPRPVPVANYPHSPVpgnpTPPMTPGSSIPPYLsPSQDVKPPFPPD 549
Cdd:PHA03379  654 QPQYFDLplQQPISQGAPLAPLRASMGPVPPVPATQPQYFDIPL----TEPINQGASAAHFL-PQQPMEGPLVPE 723
PRK10263 PRK10263
DNA translocase FtsK; Provisional
340-534 8.94e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.07  E-value: 8.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  340 PGPRG--PASMGGSMNPASMAAGMTPSGMSGPPMGMNQPRPPGISPFGTHGQRMPQQTYPGPRPQSLPIQNIKRPYPGEP 417
Cdd:PRK10263  375 PAPEGypQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQS 454
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017  418 NYGNQQYgpnsQFPTQPGQYPAPNPPRPLTSPnypgqrmPSQPSSGQYPPPTVNMGQYYKPEQFNGQNNTFSGSSYSNYS 497
Cdd:PRK10263  455 TFAPQST----YQTEQTYQQPAAQEPLYQQPQ-------PVEQQPVVEPEPVVEETKPARPPLYYFEEVEEKRAREREQL 523
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 530394017  498 QGNVNRPPRPV--PVANYPHSPVPGNPT-PPMTPGSSIPP 534
Cdd:PRK10263  524 AAWYQPIPEPVkePEPIKSSLKAPSVAAvPPVEAAAAVSP 563
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
322-589 9.34e-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: 40.14  E-value: 9.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   322 SSFQMGPTQAYNSQFMNQPGPRGPASMGGSMNPASMAAGMTPSGMSGPPmgmnQPRPPGISPfgthgqrmPQQTYPGPRP 401
Cdd:pfam03154  160 SSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPP----QGSPATSQP--------PNQTQSTAAP 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   402 QSLpIQNIKRPYPgepnygnqQYGPNSQFPTQPgqypAPNPPRPltsPNYPGQRMPsQPSSGQYPPPTVNMGQYYKPE-Q 480
Cdd:pfam03154  228 HTL-IQQTPTLHP--------QRLPSPHPPLQP----MTQPPPP---SQVSPQPLP-QPSLHGQMPPMPHSLQTGPSHmQ 290
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530394017   481 FNGQNNTFSGSSYSNYSQGnvnrPPRPVPVANYPHSPVPGNPTPPMTPGSSIPPYLSPSQDVKPPFPPDIKPNMSALP-- 558
Cdd:pfam03154  291 HPVPPQPFPLTPQSSQSQV----PPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPql 366
                          250       260       270
                   ....*....|....*....|....*....|.
gi 530394017   559 PPPANHNDELRLTFPvrdgvvlEPFRLEHNL 589
Cdd:pfam03154  367 PNPQSHKHPPHLSGP-------SPFQMNSNL 390
 
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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