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Conserved domains on  [gi|1028725279|ref|XP_016664324|]
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trithorax group protein osa isoform X4 [Acyrthosiphon pisum]

Protein Classification

ARID/BRIGHT DNA-binding domain-containing protein( domain architecture ID 13013628)

ARID (AT-rich interactive domain)/BRIGHT DNA-binding domain-containing protein similar to Arabidopsis thaliana AT-rich interactive domain-containing protein 1 (ARID1) that is specifically required for sperm cell formation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BAF250_C pfam12031
SWI/SNF-like complex subunit BAF250/Osa; This entry represents the mammalian BAF250a/b and its ...
1368-1633 7.75e-146

SWI/SNF-like complex subunit BAF250/Osa; This entry represents the mammalian BAF250a/b and its homolog osa from fruit flies. They are part of the SWI/SNF-like ATP-dependent chromatin remodelling complex that regulates gene expression through regulating nucleosome remodelling. In humans there are two BAF250 isoforms, BAF250a/ARID1a and BAF250b/ARID1b. BAF250a/b may be E3 ubiquitin ligases that target histone H2B.


:

Pssm-ID: 463439  Cd Length: 257  Bit Score: 448.32  E-value: 7.75e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279 1368 SIGKRCVCISNILRNLSFVPGNELEFAKSGPFLGLVGKLLLTHHEHPLRSSKTRNYDKADDDTESLFNCTTttdadtiep 1447
Cdd:pfam12031    1 SLARRCLCVSNILRSLSFVPGNDLEMAKHPGLLLILGRLLLLHHEHPERSSAPRTYDKEEDEDFGLSCSRD--------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279 1448 gndaKWWWDYLDVVRENLLVSLANIAGYVDLSTFNEDISRPILDGLLHWAICPAAAGQDPFPS----APLSPQRLALESL 1523
Cdd:pfam12031   72 ----EWWWDCLEVLRENALVTLANISGQLDLSPYPESICLPILDGLLHWAVCPSAEAQDPFPSagpnSPLSPQRLVLEAL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279 1524 CKLCVTDNNVDLVIATPPYSRLEKLANVLTRLLCRTEEQVLREFAVNLLHYLAAADSGMARTIALQSPCVSLLVAFIEQT 1603
Cdd:pfam12031  148 CKLSVIDNNVDLILATPPFSRLEKLFHILVRLLGRREEQVCREFAVVLLSYLAQADSAAARAIAMQKPCISNLISFIEDA 227
                          250       260       270
                   ....*....|....*....|....*....|
gi 1028725279 1604 EQNALSVVNTHGLNALRDNPDSMGTSLDML 1633
Cdd:pfam12031  228 EQNAQYVQSQHGLNALRDNPELMGTSVDML 257
ARID_ARID1A-like cd16865
ARID/BRIGHT DNA binding domain found in AT-rich interactive domain-containing proteins ARID1A, ...
605-700 1.27e-53

ARID/BRIGHT DNA binding domain found in AT-rich interactive domain-containing proteins ARID1A, ARID1B and similar proteins; This subfamily contains ARID1A and its paralog ARID1B. They are mutually exclusive components of human SWItch/Sucrose NonFermentable (SWI/SNF) chromatin remodeling protein complexes, but display different functions in development and cell-cycle control. SWI/SNF complexes containing ARID1A have an antiproliferative function, whereas the one harboring ARID1B shows a pro-proliferative function. ARID1A functions as an important tumor suppressor in various tumor types. It has been implicated in cell-cycle arrest, as well as in the interactions with p53 and BRG1/BRM and with topoisomerase II alpha. ARID1B may be considered as a potential therapeutic target for ARID1A-mutant cancers. Moreover, mutations in the ARID1B gene cause Coffin-Siris syndrome, exhibiting developmental defects, and haplo-insufficiency of ARID1B is a frequent cause of intellectual disability. Mutations in the ARID1B gene also have been found in many cancers. Both ARID1A and ARID1B contain an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), which binds DNA in a non-sequence-specific manner.


:

Pssm-ID: 350629  Cd Length: 93  Bit Score: 182.09  E-value: 1.27e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  605 PERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEvckVTKNKIWKDVAGLLGIGASSSAAYTLRK 684
Cdd:cd16865      1 PERRPFLDRLLRFMEERGSPITNCPQISKQPLDLFRLYVTVKERGGVAE---VTKNKKWKEICTELNIGASSSAAFTLRK 77
                           90
                   ....*....|....*.
gi 1028725279  685 HYTKNLLPYECHFDRG 700
Cdd:cd16865     78 NYIKYLLAYECRFDRG 93
PHA03247 super family cl33720
large tegument protein UL36; Provisional
726-1104 4.07e-10

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 65.34  E-value: 4.07e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  726 PSPGSAGSNSQDSLPSAPTAPGPGHVDGYPGYGGYSGPQDYNSPQR-----PPHPPHGTQGSYQGQGGYSQQYPGGneqy 800
Cdd:PHA03247  2690 PTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALpaapaPPAVPAGPATPGGPARPARPPTTAG---- 2765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  801 gqhyPPASTPVGYPSGPVRPPLYPP--YSNDADRNYGGSVPPPQGPPNTPQGPGNGQDPYGR--GPVPPPSgyqqppRFP 876
Cdd:PHA03247  2766 ----PPAPAPPAAPAAGPPRRLTRPavASLSESRESLPSPWDPADPPAAVLAPAAALPPAASpaGPLPPPT------SAQ 2835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  877 GPPPPQNSSPATVNQTQGGSVStPGYPpgqqpqpdyYRQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPD-FAK--DQQ 953
Cdd:PHA03247  2836 PTAPPPPPGPPPPSLPLGGSVA-PGGD---------VRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTEsFALppDQP 2905
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  954 AGPPQPAgypgygPQQRPMYPgpgwtgtpnaasnqyPRPGYPPGSQPPQnwsQGPPRSMPPSHPGQPPQweqhrypPQGQ 1033
Cdd:PHA03247  2906 ERPPQPQ------APPPPQPQ---------------PQPPPPPQPQPPP---PPPPRPQPPLAPTTDPA-------GAGE 2954
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028725279 1034 PYGAQQNHW-GPMAQAQMRMPRhgYRPDGSKPYGPHGPMAPPPHMKAGMPGQPMFQGSSLMKREVIFPPDSI 1104
Cdd:PHA03247  2955 PSGAVPQPWlGALVPGRVAVPR--FRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSL 3024
 
Name Accession Description Interval E-value
BAF250_C pfam12031
SWI/SNF-like complex subunit BAF250/Osa; This entry represents the mammalian BAF250a/b and its ...
1368-1633 7.75e-146

SWI/SNF-like complex subunit BAF250/Osa; This entry represents the mammalian BAF250a/b and its homolog osa from fruit flies. They are part of the SWI/SNF-like ATP-dependent chromatin remodelling complex that regulates gene expression through regulating nucleosome remodelling. In humans there are two BAF250 isoforms, BAF250a/ARID1a and BAF250b/ARID1b. BAF250a/b may be E3 ubiquitin ligases that target histone H2B.


Pssm-ID: 463439  Cd Length: 257  Bit Score: 448.32  E-value: 7.75e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279 1368 SIGKRCVCISNILRNLSFVPGNELEFAKSGPFLGLVGKLLLTHHEHPLRSSKTRNYDKADDDTESLFNCTTttdadtiep 1447
Cdd:pfam12031    1 SLARRCLCVSNILRSLSFVPGNDLEMAKHPGLLLILGRLLLLHHEHPERSSAPRTYDKEEDEDFGLSCSRD--------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279 1448 gndaKWWWDYLDVVRENLLVSLANIAGYVDLSTFNEDISRPILDGLLHWAICPAAAGQDPFPS----APLSPQRLALESL 1523
Cdd:pfam12031   72 ----EWWWDCLEVLRENALVTLANISGQLDLSPYPESICLPILDGLLHWAVCPSAEAQDPFPSagpnSPLSPQRLVLEAL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279 1524 CKLCVTDNNVDLVIATPPYSRLEKLANVLTRLLCRTEEQVLREFAVNLLHYLAAADSGMARTIALQSPCVSLLVAFIEQT 1603
Cdd:pfam12031  148 CKLSVIDNNVDLILATPPFSRLEKLFHILVRLLGRREEQVCREFAVVLLSYLAQADSAAARAIAMQKPCISNLISFIEDA 227
                          250       260       270
                   ....*....|....*....|....*....|
gi 1028725279 1604 EQNALSVVNTHGLNALRDNPDSMGTSLDML 1633
Cdd:pfam12031  228 EQNAQYVQSQHGLNALRDNPELMGTSVDML 257
ARID_ARID1A-like cd16865
ARID/BRIGHT DNA binding domain found in AT-rich interactive domain-containing proteins ARID1A, ...
605-700 1.27e-53

ARID/BRIGHT DNA binding domain found in AT-rich interactive domain-containing proteins ARID1A, ARID1B and similar proteins; This subfamily contains ARID1A and its paralog ARID1B. They are mutually exclusive components of human SWItch/Sucrose NonFermentable (SWI/SNF) chromatin remodeling protein complexes, but display different functions in development and cell-cycle control. SWI/SNF complexes containing ARID1A have an antiproliferative function, whereas the one harboring ARID1B shows a pro-proliferative function. ARID1A functions as an important tumor suppressor in various tumor types. It has been implicated in cell-cycle arrest, as well as in the interactions with p53 and BRG1/BRM and with topoisomerase II alpha. ARID1B may be considered as a potential therapeutic target for ARID1A-mutant cancers. Moreover, mutations in the ARID1B gene cause Coffin-Siris syndrome, exhibiting developmental defects, and haplo-insufficiency of ARID1B is a frequent cause of intellectual disability. Mutations in the ARID1B gene also have been found in many cancers. Both ARID1A and ARID1B contain an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), which binds DNA in a non-sequence-specific manner.


Pssm-ID: 350629  Cd Length: 93  Bit Score: 182.09  E-value: 1.27e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  605 PERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEvckVTKNKIWKDVAGLLGIGASSSAAYTLRK 684
Cdd:cd16865      1 PERRPFLDRLLRFMEERGSPITNCPQISKQPLDLFRLYVTVKERGGVAE---VTKNKKWKEICTELNIGASSSAAFTLRK 77
                           90
                   ....*....|....*.
gi 1028725279  685 HYTKNLLPYECHFDRG 700
Cdd:cd16865     78 NYIKYLLAYECRFDRG 93
BRIGHT smart00501
BRIGHT, ARID (A/T-rich interaction domain) domain; DNA-binding domain containing a ...
605-699 4.70e-32

BRIGHT, ARID (A/T-rich interaction domain) domain; DNA-binding domain containing a helix-turn-helix structure


Pssm-ID: 128777 [Multi-domain]  Cd Length: 93  Bit Score: 120.46  E-value: 4.70e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279   605 PERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEVCkvtKNKIWKDVAGLLGIGA-SSSAAYTLR 683
Cdd:smart00501    1 RERVLFLDRLYKFMEERGSPLKKIPVIGGKPLDLYRLYRLVQERGGYDQVT---KDKKWKEIARELGIPDtSTSAASSLR 77
                            90
                    ....*....|....*.
gi 1028725279   684 KHYTKNLLPYECHFDR 699
Cdd:smart00501   78 KHYERYLLPYERFLRG 93
ARID pfam01388
ARID/BRIGHT DNA binding domain; This domain is know as ARID for AT-Rich Interaction Domain, ...
606-694 1.61e-28

ARID/BRIGHT DNA binding domain; This domain is know as ARID for AT-Rich Interaction Domain, and also known as the BRIGHT domain.


Pssm-ID: 460187  Cd Length: 87  Bit Score: 110.41  E-value: 1.61e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  606 ERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMevcKVTKNKIWKDVAGLLGIGAS-SSAAYTLRK 684
Cdd:pfam01388    1 EKELFLKSLRKFHEKRGTPLKQIPVIGGKPVDLYKLYKAVQKLGGYD---KVTEKNLWREVAEKLGFPPSaASAATQLKQ 77
                           90
                   ....*....|
gi 1028725279  685 HYTKNLLPYE 694
Cdd:pfam01388   78 IYEKYLLPYE 87
PHA03247 PHA03247
large tegument protein UL36; Provisional
726-1104 4.07e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 65.34  E-value: 4.07e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  726 PSPGSAGSNSQDSLPSAPTAPGPGHVDGYPGYGGYSGPQDYNSPQR-----PPHPPHGTQGSYQGQGGYSQQYPGGneqy 800
Cdd:PHA03247  2690 PTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALpaapaPPAVPAGPATPGGPARPARPPTTAG---- 2765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  801 gqhyPPASTPVGYPSGPVRPPLYPP--YSNDADRNYGGSVPPPQGPPNTPQGPGNGQDPYGR--GPVPPPSgyqqppRFP 876
Cdd:PHA03247  2766 ----PPAPAPPAAPAAGPPRRLTRPavASLSESRESLPSPWDPADPPAAVLAPAAALPPAASpaGPLPPPT------SAQ 2835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  877 GPPPPQNSSPATVNQTQGGSVStPGYPpgqqpqpdyYRQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPD-FAK--DQQ 953
Cdd:PHA03247  2836 PTAPPPPPGPPPPSLPLGGSVA-PGGD---------VRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTEsFALppDQP 2905
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  954 AGPPQPAgypgygPQQRPMYPgpgwtgtpnaasnqyPRPGYPPGSQPPQnwsQGPPRSMPPSHPGQPPQweqhrypPQGQ 1033
Cdd:PHA03247  2906 ERPPQPQ------APPPPQPQ---------------PQPPPPPQPQPPP---PPPPRPQPPLAPTTDPA-------GAGE 2954
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028725279 1034 PYGAQQNHW-GPMAQAQMRMPRhgYRPDGSKPYGPHGPMAPPPHMKAGMPGQPMFQGSSLMKREVIFPPDSI 1104
Cdd:PHA03247  2955 PSGAVPQPWlGALVPGRVAVPR--FRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSL 3024
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
735-1083 7.08e-10

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: 64.02  E-value: 7.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  735 SQDSLPSAPTAPGPGHVDGYPGYGGYSGPQDYNSPQRPPHPPHGTQGSYQGQGGYSQQYPggnEQYGQHYPPASTPVGYP 814
Cdd:pfam03154  176 AQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTP---TLHPQRLPSPHPPLQPM 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  815 SGPVRPPLYPPYSNDADRNYGgsvPPPQGPPNTPQGPGNGQDPYgrgpvpPPSGYQQPPRFPGPPPPQNSSPATVNQTQG 894
Cdd:pfam03154  253 TQPPPPSQVSPQPLPQPSLHG---QMPPMPHSLQTGPSHMQHPV------PPQPFPLTPQSSQSQVPPGPSPAAPGQSQQ 323
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  895 GSVSTPGYPPGQQPQPDYYRQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPdfakdQQAGPPQPAGYPGYGPQQRPMYP 974
Cdd:pfam03154  324 RIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHP-----PHLSGPSPFQMNSNLPPPPALKP 398
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  975 gpgwtgtPNAASNQYPRPGYPPgsqPPQNWSQGPPRSMPPSHPGQPPQWEQHRYPPQGQPyGAQQNHWGPmaqAQMRMPR 1054
Cdd:pfam03154  399 -------LSSLSTHHPPSAHPP---PLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHP-PTSGLHQVP---SQSPFPQ 464
                          330       340
                   ....*....|....*....|....*....
gi 1028725279 1055 HGYRPDGSKPYGPhgPMAPPPHMKAGMPG 1083
Cdd:pfam03154  465 HPFVPGGPPPITP--PSGPPTSTSSAMPG 491
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
919-1051 7.76e-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: 7.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  919 ASPGYPPTSAPGTYPGKGMPPPQPRRHPdfakdQQAGPPQPAGYPGYGPQQRPMYPGpgwtgTPNAAsnQYPRPgYPPGS 998
Cdd:TIGR01628  378 LQPRMRQLPMGSPMGGAMGQPPYYGQGP-----QQQFNGQPLGWPRMSMMPTPMGPG-----GPLRP--NGLAP-MNAVR 444
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1028725279  999 QPPQNWSQGPPRSMPPSHPgQPPQWEQHRYPPQGQPYGAQQNHWGPMAQ-AQMR 1051
Cdd:TIGR01628  445 APSRNAQNAAQKPPMQPVM-YPPNYQSLPLSQDLPQPQSTASQGGQNKKlAQVL 497
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
904-1091 9.61e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 40.43  E-value: 9.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  904 PGQQPQPDYYRQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPDfakDQQAGPPQPAGYPGYGPQqrpmypgpgwtGTPN 983
Cdd:COG5180    260 DAKERRRAAIGDTPAAEPPGLPVLEAGSEPQSDAPEAETARPID---VKGVASAPPATRPVRPPG-----------GARD 325
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  984 AASNQYPRPGYPPGSQPPQNWSQGPprsmPPSHPgQPPQWEQHRYP-PQGQPYGAQQNHWGPMAQAQMRMPRHGYRPDGS 1062
Cdd:COG5180    326 PGTPRPGQPTERPAGVPEAASDAGQ----PPSAY-PPAEEAVPGKPlEQGAPRPGSSGGDGAPFQPPNGAPQPGLGRRGA 400
                          170       180       190
                   ....*....|....*....|....*....|
gi 1028725279 1063 KPYG-PHGPMAPPPHMKAGMPGQPMFQGSS 1091
Cdd:COG5180    401 PGPPmGAGDLVQAALDGGGRETASLGGAAG 430
 
Name Accession Description Interval E-value
BAF250_C pfam12031
SWI/SNF-like complex subunit BAF250/Osa; This entry represents the mammalian BAF250a/b and its ...
1368-1633 7.75e-146

SWI/SNF-like complex subunit BAF250/Osa; This entry represents the mammalian BAF250a/b and its homolog osa from fruit flies. They are part of the SWI/SNF-like ATP-dependent chromatin remodelling complex that regulates gene expression through regulating nucleosome remodelling. In humans there are two BAF250 isoforms, BAF250a/ARID1a and BAF250b/ARID1b. BAF250a/b may be E3 ubiquitin ligases that target histone H2B.


Pssm-ID: 463439  Cd Length: 257  Bit Score: 448.32  E-value: 7.75e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279 1368 SIGKRCVCISNILRNLSFVPGNELEFAKSGPFLGLVGKLLLTHHEHPLRSSKTRNYDKADDDTESLFNCTTttdadtiep 1447
Cdd:pfam12031    1 SLARRCLCVSNILRSLSFVPGNDLEMAKHPGLLLILGRLLLLHHEHPERSSAPRTYDKEEDEDFGLSCSRD--------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279 1448 gndaKWWWDYLDVVRENLLVSLANIAGYVDLSTFNEDISRPILDGLLHWAICPAAAGQDPFPS----APLSPQRLALESL 1523
Cdd:pfam12031   72 ----EWWWDCLEVLRENALVTLANISGQLDLSPYPESICLPILDGLLHWAVCPSAEAQDPFPSagpnSPLSPQRLVLEAL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279 1524 CKLCVTDNNVDLVIATPPYSRLEKLANVLTRLLCRTEEQVLREFAVNLLHYLAAADSGMARTIALQSPCVSLLVAFIEQT 1603
Cdd:pfam12031  148 CKLSVIDNNVDLILATPPFSRLEKLFHILVRLLGRREEQVCREFAVVLLSYLAQADSAAARAIAMQKPCISNLISFIEDA 227
                          250       260       270
                   ....*....|....*....|....*....|
gi 1028725279 1604 EQNALSVVNTHGLNALRDNPDSMGTSLDML 1633
Cdd:pfam12031  228 EQNAQYVQSQHGLNALRDNPELMGTSVDML 257
ARID_ARID1A-like cd16865
ARID/BRIGHT DNA binding domain found in AT-rich interactive domain-containing proteins ARID1A, ...
605-700 1.27e-53

ARID/BRIGHT DNA binding domain found in AT-rich interactive domain-containing proteins ARID1A, ARID1B and similar proteins; This subfamily contains ARID1A and its paralog ARID1B. They are mutually exclusive components of human SWItch/Sucrose NonFermentable (SWI/SNF) chromatin remodeling protein complexes, but display different functions in development and cell-cycle control. SWI/SNF complexes containing ARID1A have an antiproliferative function, whereas the one harboring ARID1B shows a pro-proliferative function. ARID1A functions as an important tumor suppressor in various tumor types. It has been implicated in cell-cycle arrest, as well as in the interactions with p53 and BRG1/BRM and with topoisomerase II alpha. ARID1B may be considered as a potential therapeutic target for ARID1A-mutant cancers. Moreover, mutations in the ARID1B gene cause Coffin-Siris syndrome, exhibiting developmental defects, and haplo-insufficiency of ARID1B is a frequent cause of intellectual disability. Mutations in the ARID1B gene also have been found in many cancers. Both ARID1A and ARID1B contain an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), which binds DNA in a non-sequence-specific manner.


Pssm-ID: 350629  Cd Length: 93  Bit Score: 182.09  E-value: 1.27e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  605 PERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEvckVTKNKIWKDVAGLLGIGASSSAAYTLRK 684
Cdd:cd16865      1 PERRPFLDRLLRFMEERGSPITNCPQISKQPLDLFRLYVTVKERGGVAE---VTKNKKWKEICTELNIGASSSAAFTLRK 77
                           90
                   ....*....|....*.
gi 1028725279  685 HYTKNLLPYECHFDRG 700
Cdd:cd16865     78 NYIKYLLAYECRFDRG 93
ARID_ARID1B cd16877
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 1B (ARID1B) ...
605-700 2.60e-32

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 1B (ARID1B) and similar proteins; ARID1B, also called BRG1-associated factor 250b (BAF250B), BRG1-binding protein ELD/OSA1, Osa homolog 2 (Osa2), or p250R, is the largest subunit of ATP-dependent SWItch/sucrose nonfermentable (SWI/SNF) chromatin remodeling complex, which plays a critical role in transcriptional control and gene expression. ARID1B exhibits tumour-suppressor activities in pancreatic cancer cell lines. Mutations in the ARID1B gene cause Coffin-Siris syndrome, exhibiting developmental defects, and haplo-insufficiency of ARID1B is a frequent cause of intellectual disability. Moreover, mutations in the ARID1B gene have been found in many cancers. ARID1B contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), which binds DNA in a non-sequence-specific manner similar to ARID1A.


Pssm-ID: 350641  Cd Length: 93  Bit Score: 121.25  E-value: 2.60e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  605 PERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGfmeVCKVTKNKIWKDVAGLLGIGASSSAAYTLRK 684
Cdd:cd16877      1 PERKLWVDRYLTFMEERGTPVASLPAVGKKPLDLFRLYVCVKEIGG---LAQVNKNKKWRELATNLNVGTSSSAASSLKK 77
                           90
                   ....*....|....*.
gi 1028725279  685 HYTKNLLPYECHFDRG 700
Cdd:cd16877     78 QYIQYLFAFECKIERG 93
BRIGHT smart00501
BRIGHT, ARID (A/T-rich interaction domain) domain; DNA-binding domain containing a ...
605-699 4.70e-32

BRIGHT, ARID (A/T-rich interaction domain) domain; DNA-binding domain containing a helix-turn-helix structure


Pssm-ID: 128777 [Multi-domain]  Cd Length: 93  Bit Score: 120.46  E-value: 4.70e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279   605 PERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEVCkvtKNKIWKDVAGLLGIGA-SSSAAYTLR 683
Cdd:smart00501    1 RERVLFLDRLYKFMEERGSPLKKIPVIGGKPLDLYRLYRLVQERGGYDQVT---KDKKWKEIARELGIPDtSTSAASSLR 77
                            90
                    ....*....|....*.
gi 1028725279   684 KHYTKNLLPYECHFDR 699
Cdd:smart00501   78 KHYERYLLPYERFLRG 93
ARID smart01014
ARID/BRIGHT DNA binding domain; Members of the recently discovered ARID (AT-rich interaction ...
605-694 3.60e-29

ARID/BRIGHT DNA binding domain; Members of the recently discovered ARID (AT-rich interaction domain) family of DNA-binding proteins are found in fungi and invertebrate and vertebrate metazoans. ARID-encoding genes are involved in a variety of biological processes including embryonic development, cell lineage gene regulation and cell cycle control. Although the specific roles of this domain and of ARID-containing proteins in transcriptional regulation are yet to be elucidated, they include both positive and negative transcriptional regulation and a likely involvement in the modification of chromatin structure. The basic structure of the ARID domain domain appears to be a series of six alpha-helices separated by beta-strands, loops, or turns, but the structured region may extend to an additional helix at either or both ends of the basic six. Based on primary sequence homology, they can be partitioned into three structural classes: Minimal ARID proteins that consist of a core domain formed by six alpha helices; ARID proteins that supplement the core domain with an N-terminal alpha-helix; and Extended-ARID proteins, which contain the core domain and additional alpha-helices at their N- and C-termini.


Pssm-ID: 198082 [Multi-domain]  Cd Length: 88  Bit Score: 112.32  E-value: 3.60e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279   605 PERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMevcKVTKNKIWKDVAGLLGI-GASSSAAYTLR 683
Cdd:smart01014    1 RERELFLDRLRKFMEKRGTPLDKIPVIGGKPLDLYRLYRAVQKRGGFD---KVTKKKKWKQVARELGIpPSATSAGTSLR 77
                            90
                    ....*....|.
gi 1028725279   684 KHYTKNLLPYE 694
Cdd:smart01014   78 KHYEKYLLPYE 88
ARID pfam01388
ARID/BRIGHT DNA binding domain; This domain is know as ARID for AT-Rich Interaction Domain, ...
606-694 1.61e-28

ARID/BRIGHT DNA binding domain; This domain is know as ARID for AT-Rich Interaction Domain, and also known as the BRIGHT domain.


Pssm-ID: 460187  Cd Length: 87  Bit Score: 110.41  E-value: 1.61e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  606 ERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMevcKVTKNKIWKDVAGLLGIGAS-SSAAYTLRK 684
Cdd:pfam01388    1 EKELFLKSLRKFHEKRGTPLKQIPVIGGKPVDLYKLYKAVQKLGGYD---KVTEKNLWREVAEKLGFPPSaASAATQLKQ 77
                           90
                   ....*....|
gi 1028725279  685 HYTKNLLPYE 694
Cdd:pfam01388   78 IYEKYLLPYE 87
ARID_ARID3 cd16867
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing proteins ARID3A, ...
597-695 1.67e-28

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing proteins ARID3A, ARID3B, ARID3C, dead ringer (Dri) from Drosophila melanogaster, and similar proteins; The ARID3 subfamily includes AT-rich interactive domain (ARID, also known as BRIGHT)-containing proteins ARID3A, ARID3B and ARID3C, which are the most direct mammalian counterparts of the Drosophila "dead ringer" protein Dri. They consist of an acidic N-terminal region of unknown function, the central ARID matrix association (or attachment) region (MAR)-DNA binding domain, a SUMO-I conjugation (SUMO) motif, and a multifunctional homomerization/nuclear export REKLES domain in the C-terminal third of the molecule. The ARID domain in this subfamily has been described as the "extended" or e-ARID due to additional conserved sequences at both the N and C termini of the core ARID region. The REKLES domain is found only in the ARID3 subfamily. It has co-evolved with and regulates functional properties of the ARID DNA-binding domain.


Pssm-ID: 350631  Cd Length: 118  Bit Score: 111.42  E-value: 1.67e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  597 KLYEMDDNPERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEvckVTKNKIWKDVAGLLGIGAS- 675
Cdd:cd16867      3 QLYELSDDPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLYELYRLVVEKGGLVE---VINKKIWREITKGLNLPSSi 79
                           90       100
                   ....*....|....*....|
gi 1028725279  676 SSAAYTLRKHYTKNLLPYEC 695
Cdd:cd16867     80 TSAAFTLRTQYMKYLYPYEC 99
ARID_ARID1A cd16876
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 1A (ARID1A) ...
605-700 7.19e-27

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 1A (ARID1A) and similar proteins; ARID1A, also called B120, BRG1-associated factor 250a (BAF250A), Osa homolog 1(OSA1), SWI-like protein, SWI/SNF complex protein p270, or SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1 (SWI1), has been identified as a novel tumor suppressor in various tumor types. It interacts with BRG1 adenosine triphosphatase to form a SWItch/Sucrose NonFermentable (SWI/SNF) chromatin remodeling protein complex, which plays a critical role in transcriptional control and gene expression. ARID1A contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), and Eld/Osa homology domains (EHD) 1 and 2 within the C-terminus. The ARID in ARID1A binds nonspecific DNA in general and plays an important role in targeting SWI/SNF to chromatin. The EHD1 may be capable of mediating an intramolecular association with EHD2, and/or an intermolecular association resulting in homo- or hetero-dimerization. The EHD2 binds Swi2/Brahma homologue Brahma-related gene 1 (BRG1, also known as Snf2b), a human homologue of yeast Swi2.


Pssm-ID: 350640  Cd Length: 93  Bit Score: 105.90  E-value: 7.19e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  605 PERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEvckVTKNKIWKDVAGLLGIGASSSAAYTLRK 684
Cdd:cd16876      1 PERKMWVDRYLAFTEEKAMGMTNLPAVGRKPLDLYRLYVSVKEIGGLTQ---VNKNKKWRELATNLNVGTSSSAASSLKK 77
                           90
                   ....*....|....*.
gi 1028725279  685 HYTKNLLPYECHFDRG 700
Cdd:cd16876     78 QYIQCLYAFECKIERG 93
ARID cd16100
ARID/BRIGHT DNA binding domain family; The AT-rich interaction domain (ARID) family of ...
606-694 2.04e-25

ARID/BRIGHT DNA binding domain family; The AT-rich interaction domain (ARID) family of transcription factors, found in a broad array of organisms from fungi to mammals, is characterized by a highly conserved, helix-turn-helix DNA binding domain that binds to the major groove of DNA. The ARID domain, also called BRIGHT, was first identified in the mouse B-cell-specific transcription factor Bright and in the product of the dead ringer (dri) gene of Drosophila melanogaster. ARID family members are implicated in normal development, differentiation, cell cycle regulation, transcriptional activation and chromatin remodeling. Different family members exhibit different DNA-binding properties. Drosophila Dri, mammalian ARID3A/3B/3C and ARID5A/5B, selectively bind AT-rich sites. However, ARID1A/1B, Drosophila Osa, yeast SWI1, ARID2, ARID4A/4B, JARID1A/1B/1C/1D, and JARID2, bind DNA without sequence specificity.


Pssm-ID: 350627  Cd Length: 87  Bit Score: 101.28  E-value: 2.04e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  606 ERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMevcKVTKNKIWKDVAGLLGIGAS-SSAAYTLRK 684
Cdd:cd16100      1 EREEFLEQLRAFLESRGTPLLKPPTIGGKPLDLYKLYRAVVSRGGYE---KVTEKKLWKEVARKLGLPTSsTSAAQALKR 77
                           90
                   ....*....|
gi 1028725279  685 HYTKNLLPYE 694
Cdd:cd16100     78 IYEKYLLPFE 87
ARID_ARID3B cd16879
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 3B (ARID3B) ...
595-695 1.28e-24

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 3B (ARID3B) and similar proteins; ARID3B, also called Bright and dead ringer protein, or Bright-Dri-like protein (Bdp), is a DNA binding protein involved in cellular immortalization, epithelial-mesenchymal transition (EMT), and tumorigenesis. Its expression is differentially regulated in normal and malignant tissues. It is required for heart development by regulating the motility and differentiation of heart progenitors. ARID3B is overexpressed in neuroblastoma and ovarian cancer. It acts as a novel target with roles in cell motility in breast cancer cells, promotes migration of mouse embryo fibroblasts (MEFs) and breast cancer cells, and induces tumor necrosis factor alpha (TNFalpha)-mediated apoptosis. ARID3B contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a SUMO-I conjugation (SUMO) motif and a multifunctional homomerization/nuclear export REKLES domain, which consists of two subdomains: a modestly conserved N-terminal REKLES alpha and a highly conserved (among ARID3 orthologous proteins) C-terminal REKLES beta.


Pssm-ID: 350643  Cd Length: 126  Bit Score: 100.47  E-value: 1.28e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  595 LSKLYEMDDNPERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEvckVTKNKIWKDVAGLLGIGA 674
Cdd:cd16879      3 FAKLYELDNDPKRKEFLDDLFAFMQKRGTPINRIPIMAKQVLDLYMLYKLVTEKGGLVE---VINKKIWREITKGLNLPT 79
                           90       100
                   ....*....|....*....|..
gi 1028725279  675 S-SSAAYTLRKHYTKNLLPYEC 695
Cdd:cd16879     80 SiTSAAFTLRTQYMKYLYPYEC 101
ARID_ARID3C cd16880
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 3C (ARID3C) ...
593-695 6.51e-24

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 3C (ARID3C) and similar proteins; ARID3C, also called Brightlike, is a new ARID3 family transcription factor that co-activates ARID3A-mediated immunoglobulin gene transcription. It also functions as a potential regulator of early events in B cell antigen receptor (BCR) signaling. ARID3C contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a SUMO-I conjugation (SUMO) motif and a multifunctional homomerization/nuclear export REKLES domain, which consists of two subdomains: a modestly conserved N-terminal REKLES alpha and a highly conserved (among ARID3 orthologous proteins) C-terminal REKLES beta.


Pssm-ID: 350644  Cd Length: 127  Bit Score: 98.57  E-value: 6.51e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  593 DSLSKLYEMDDNPERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEvckVTKNKIWKDVAGLLGI 672
Cdd:cd16880      2 EQFKQLYELDDDPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLYTLYRLVTDKGGLVE---VINKKIWREITKGLSL 78
                           90       100
                   ....*....|....*....|....
gi 1028725279  673 GAS-SSAAYTLRKHYTKNLLPYEC 695
Cdd:cd16880     79 PTSiTSAAFTLRTQYMKYLYPYEC 102
ARID_ARID3A cd16878
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 3A (ARID3A) ...
593-704 1.59e-23

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 3A (ARID3A) and similar proteins; ARID3A, also called B-cell regulator of IgH transcription (Bright), dead ringer-like protein 1 (Dril1), or E2F-binding protein 1 (E2FBP1), is an ubiquitously expressed DNA-binding protein that has been implicated in embryonic patterning, cell lineage gene regulation, and cell cycle control, chromatin remodeling and transcriptional regulation. It was originally identified as a B cell-specific trans-activator of immunoglobulin heavy-chain (IgH) transcription, which increases immunoglobulin transcription in antigen-activated B cells and plays regulatory roles in hematopoiesis. It also functions as an E2F transcription regulator, inducing promyelocytic leukemia protein (PML) reduction and suppressing the formation of PML-nuclear bodies. It antagonizes the p16(INK4A)-Rb tumor suppressor machinery by regulating PML stability. ARID3A transcriptional activity can be modulated by SUMO (Small Ubiquitin-related Modifier) modification through the interaction with the SUMO-conjugating enzyme Ubc9. ARID3A also plays an important role in marginal zone B lymphocyte development and autoantibody production. Furthermore, ARID3A is a direct p53 target gene. It controls cell growth in a p53-dependent manner. ARID3A contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a SUMO-I conjugation (SUMO) motif and a multifunctional homomerization/nuclear export REKLES domain, which consists of two subdomains: a modestly conserved N-terminal REKLES alpha and a highly conserved (among ARID3 orthologous proteins) C-terminal REKLES beta.


Pssm-ID: 350642  Cd Length: 133  Bit Score: 97.83  E-value: 1.59e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  593 DSLSKLYEMDDNPERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEvckVTKNKIWKDVAGLLGI 672
Cdd:cd16878      9 EQFKQLYELDGDPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLYMLYVLVTEKGGLVE---VINKKLWREITKGLNL 85
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1028725279  673 GAS-SSAAYTLRKHYTKNLLPYECHfDRGGIDP 704
Cdd:cd16878     86 PTSiTSAAFTLRTQYMKYLYPYECE-KRGLSNP 117
ARID_Dri-like cd16881
ARID/BRIGHT DNA binding domain of dead ringer (Dri) from Drosophila melanogaster and similar ...
596-695 1.78e-23

ARID/BRIGHT DNA binding domain of dead ringer (Dri) from Drosophila melanogaster and similar proteins; Dri, also termed retained (retn), is a nuclear protein with a sequence-specific DNA-binding domain termed AT-rich DNA-interacting domain (ARID, also known as BRIGHT). It is a founding member of the ARID family. Sequence comparison shows that DRI belongs to the "extended" or e-ARID subfamily, which exhibits an extended region of similarity either side of the ARID. Dri plays an important role in embryogenesis. It functions as an essential transcription factor involved in aspects of dorsal/ventral and anterior/posterior axis patterning, as well as myogenesis and hindgut development.


Pssm-ID: 350645  Cd Length: 125  Bit Score: 97.27  E-value: 1.78e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  596 SKLYEMDDNPERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEvckVTKNKIWKDVAGLLGIGAS 675
Cdd:cd16881      9 KQLYEISDDPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLYELYNLVVARGGLVE---VINKKLWREITKGLHLPSS 85
                           90       100
                   ....*....|....*....|.
gi 1028725279  676 -SSAAYTLRKHYTKNLLPYEC 695
Cdd:cd16881     86 iTSAAFTLRTQYMKYLYPYEC 106
ARID_ARID5 cd16869
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing proteins ARID5A, ...
606-694 4.20e-17

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing proteins ARID5A, ARID5B, and similar proteins; This subfamily contains ARID5A and its paralog ARID5B. ARID5A, also called modulator recognition factor 1 (MRF-1), is an estrogen receptor alpha (ER alpha)-interacting protein that is expressed abundantly in cardiovascular tissues and suppresses ER alpha-induced transactivation. It also plays an important role in the promotion of inflammatory processes and autoimmune diseases. ARID5B, also called MRF1-like protein or modulator recognition factor 2 (MRF-2), is a DNA-binding protein that directly interacts with plant homeodomain (PHD) finger 2 (PHF2) to form a protein kinase A (PKA)-dependent PHF2-ARID5B histone H3K9Me2 demethylase complex. It also functions as a transcriptional co-regulator for the transcription factor sex determining region Y (SRY)-box protein 9 (Sox9) and promotes chondrogenesis through histone modification. Moreover, ARID5B is highly expressed in the cardiovascular system and may play essential roles in the phenotypic change of smooth muscle cells (SMCs) through its regulation of SMC differentiation. Both ARID5A and ARID5B contain an AT-rich DNA-interacting domain (ARID, also known as BRIGHT).


Pssm-ID: 350633  Cd Length: 87  Bit Score: 77.72  E-value: 4.20e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  606 ERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMEvckVTKNKIWKDVAGLLGIGASS-SAAYTLRK 684
Cdd:cd16869      1 EEQAFLKLLYKFMKDRGTPIERIPHLGFKQIDLYTFFKLVQKLGGYEQ---VTAKRLWKHVYDELGGNPSStSAATCTRR 77
                           90
                   ....*....|
gi 1028725279  685 HYTKNLLPYE 694
Cdd:cd16869     78 HYEKLLLPYE 87
ARID_HMGB9-like cd16872
ARID/BRIGHT DNA binding domain of Arabidopsis thaliana high mobility group B proteins HMGB9, ...
606-694 2.50e-16

ARID/BRIGHT DNA binding domain of Arabidopsis thaliana high mobility group B proteins HMGB9, HMGB10, HMGB11, HMGB15 and similar proteins; This subfamily includes a group of conserved plant DNA-binding proteins, including HMGB9 (or ARID-HMG1), HMGB10 (or ARID-HMG2), HMGB11, and HMGB15. They have been termed ARID-HMG proteins, due to containing two DNA-binding domains, an N-terminal AT-rich DNA-interacting domain (ARID, also known as BRIGHT), and a C-terminal high mobility group (HMG)-box domain. They are widely expressed in Arabidopsis and localize primarily to the nucleus. HMGB9/ARID-HMG1 binds specifically to A/T-rich DNA. HMGB15 is a transcription factor predominantly expressed in mature pollen grains and pollen tubes. It may work in the form of a homodimer, or interact with HMGB9, HMGB10 and HMGB11 to form heteromultimers in plant cells. HMGB15 is required for pollen tube growth in Arabidopsis and is involved in transcriptional regulation through the interaction with AGL66 and AGL104.


Pssm-ID: 350636  Cd Length: 86  Bit Score: 75.38  E-value: 2.50e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  606 ERRIWLDKLLHFMEERGSPiSTCPTISKNPLDLFRLYIYVKERGGfMEvcKVTKNKIWKDVAGLLGIGAS-SSAAYTLRK 684
Cdd:cd16872      1 DPDLFWETLRKFHESLGTK-FRIPIVGGKELDLHRLYKEVTSRGG-LE--KVIKDRKWKEVAAVFNFPPTiTNASFVLRK 76
                           90
                   ....*....|
gi 1028725279  685 HYTKNLLPYE 694
Cdd:cd16872     77 YYLSLLHHYE 86
ARID_ARID4 cd16868
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing proteins ARID4A, ...
606-694 8.61e-16

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing proteins ARID4A, ARID4B and similar proteins; This subfamily contains ARID4A and its paralog ARID4B, both of which are retinoblastoma (Rb)-binding proteins that function as coactivators to enhance the androgen receptor (AR) and Rb transcriptional activity, and play important roles in the AR and Rb pathways to control male fertility. They also act as the leukemia and tumor suppressors involved in epigenetic regulation in leukemia and Prader-Willi/Angelman syndrome. Moreover, they associate with the mSIN3A histone deacetylase (HDAC) chromatin remodeling complex through the interaction with each other, as well as with the breast cancer associated tumor suppressor ING1 and the breast cancer metastasis suppressor BRMS1. Both ARID4A and ARID4B contain a Tudor domain, a PWWP domain (also known as HATH domain or RBB1NT domain), an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a chromobarrel domain, and a C-terminal R2 domain.


Pssm-ID: 350632  Cd Length: 87  Bit Score: 73.96  E-value: 8.61e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  606 ERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMevcKVTKNKIWKDVAGLLGIGA-SSSAAYTLRK 684
Cdd:cd16868      1 EKENFLEQLYKFMEDRGTPINKPPVLGYKDLDLFKLYKLVQELGGME---RVSQGAKWRSIYQQLGIPVlNSAASHNIKQ 77
                           90
                   ....*....|
gi 1028725279  685 HYTKNLLPYE 694
Cdd:cd16868     78 AYKKYLYAFE 87
ARID_JARID cd16864
ARID/BRIGHT DNA binding domain of JARID proteins; The JARID subfamily within the JmjC protein ...
611-694 6.17e-13

ARID/BRIGHT DNA binding domain of JARID proteins; The JARID subfamily within the JmjC protein family includes lysine-specific demethylase KDM5A, KDM5B, KDM5C, KDM5D and a Drosophila homolog, protein little imaginal discs (Lid). KDM5A was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5B has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. Both KDM5A and KDM5B function as trimethylated histone H3 lysine 4 (H3K4me3) demethylases. KDM5C is a H3K4 trimethyl-histone demethylase that catalyzes demethylation of H3K4me3 and H3K4me2 to H3K4me1. It plays a role in neuronal survival and dendrite development. KDM5C defects are associated with X-linked mental retardation (XLMR). KDM5D is a male-specific antigen that shows a demethylase activity specific for di- and tri-methylated histone H3K4 (H3K4me3 and H3K4me2), and has a male-specific function as a histone H3K4 demethylase by recruiting a meiosis-regulatory protein, MSH5, to condensed DNA. KDM5D directly interacts with a polycomb-like protein Ring6a/MBLR, and plays a role in regulation of transcriptional initiation through H3K4 demethylation. The family also includes Drosophila melanogaster protein little imaginal discs (Lid) that functions as a JmjC-dependent trimethyl histone H3K4 (H3K4me3) demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Members of this subfamily contain the catalytic JmjC domain, JmjN, the AT-rich domain interacting domain (ARID)/BRIGHT domain, a C5HC2 zinc finger, as well as two or three plant homeodomain (PHD) fingers.


Pssm-ID: 350628  Cd Length: 87  Bit Score: 65.79  E-value: 6.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  611 LDKLLHFMEERGSPISTcPTISKNPLDLFRLYIYVKERGGFMEVCKVTKnkiWKDVAGLLGIGASSSAAYTLRKHYTKNL 690
Cdd:cd16864      8 LDQIAKFWELQGSSLKI-PNVERKALDLFTLHKIVQEEGGFEEVTKERK---WSKVARRLGYPPGKGVGSLLRGHYERIL 83

                   ....
gi 1028725279  691 LPYE 694
Cdd:cd16864     84 YPYD 87
ARID_Swi1p-like cd16871
ARID/BRIGHT DNA binding domain of yeast SWI/SNF chromatin-remodeling complex subunit Swi1p and ...
611-694 2.66e-12

ARID/BRIGHT DNA binding domain of yeast SWI/SNF chromatin-remodeling complex subunit Swi1p and similar proteins; Saccharomyces cerevisiae Swi1p, also called SWI/SNF chromatin-remodeling complex subunit SWI1, regulatory protein GAM3, or transcription regulatory protein ADR6, is a transcription regulatory protein that is a subunit of the SWI/SNF complex, which plays critical roles in the regulation of gene transcription and expression. It can exist as a prion, [SWI(+)], which demonstrates a link between prionogenesis and global transcriptional regulation. Swi1p contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT) that binds DNA nonspecifically. This subfamily also includes Schizosaccharomyces pombe SWI/SNF chromatin-remodeling complex subunit sol1 (sol1p, also known as switch one-like protein). sol1p is a homolog of S. cerevisiae Swi1p and is also a part of SWI/SNF chromatin-remodeling complex.


Pssm-ID: 350635  Cd Length: 90  Bit Score: 64.19  E-value: 2.66e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  611 LDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMevcKVTKNKIWKDVAGLLGI--GASSSAAYTLRKHYTK 688
Cdd:cd16871      7 MKSLREFMAKRGTPIEQQPVIGGRPVNLFRLYQLVQKLGGSR---QVTQNNQWPRVAQKLGFppEQNPQVAQQLAQIYQR 83

                   ....*.
gi 1028725279  689 NLLPYE 694
Cdd:cd16871     84 YLLPYE 89
ARID_ARID5A cd16884
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 5A (ARID5A) ...
606-694 1.19e-11

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 5A (ARID5A) and similar proteins; ARID5A, also called modulator recognition factor 1 (MRF-1), is an estrogen receptor alpha (ER alpha)-interacting protein that is expressed abundantly in cardiovascular tissues and suppresses ER alpha-induced transactivation. It also associates with thyroid receptor alpha (TR alpha) and retinoid X receptor alpha (RXR alpha) in a ligand-dependent manner, and with ER beta, androgen receptor (AR), and the retinoic acid receptor (RAR) in a ligand-independent manner. ARID5A functions as a negative regulator of RORgamma-induced Th17 cell differentiation and may be involved in the pathogenesis of rheumatoid arthritis (RA). Moreover, it is an important transcriptional partner of the transcription factor sex determining region Y (SRY)-box protein 9 (Sox9) in stimulation of chondrocyte-specific transcription. Meanwhile, ARID5A plays an important role in promotion of inflammatory processes and autoimmune diseases. It works as a unique RNA binding protein, which stabilizes interleukin-6 (IL-6) but not tumor necrosis factor-alpha (TNF-alpha) mRNA through binding to the 3' untranslated region (UTR) of IL-6 mRNA, and inhibits the destabilizing effect of regnase-1 on IL-6 mRNA. ARID5A contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT).


Pssm-ID: 350648  Cd Length: 87  Bit Score: 62.33  E-value: 1.19e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  606 ERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMevcKVTKNKIWKDVAGLLGIG-ASSSAAYTLRK 684
Cdd:cd16884      1 EEQAFLVNLYKFMKERNTPIERIPHLGFKQINLWKIYKAVEKLGGYE---LVTARRLWKNVYDELGGSpGSTSAATCTRR 77
                           90
                   ....*....|
gi 1028725279  685 HYTKNLLPYE 694
Cdd:cd16884     78 HYERLVLPYV 87
ARID_ARID2 cd16866
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 2 (ARID2) and ...
606-694 5.02e-11

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 2 (ARID2) and similar proteins; ARID2, also called BRG1-associated factor 200 (BAF200) or zinc finger protein with activation potential (Zipzap/p200), is a novel serum response factor (SRF)-binding protein with multiple conserved domains, including an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), RFX DNA-binding domain, a glutamine-rich domain, and two C2H2 zinc fingers. It binds DNA without sequence specificity. ARID2 is an intrinsic subunit of PBAF (SWI/SNF-B) remodeling complex, which needs ARID2 to play an essential role in promoting osteoblast differentiation, maintaining cellular identity and activating tissue-specific gene expression. Moreover, ARID2 may function as a tumor suppressor in many cancers. It may also serve as a transcription co-activator for the regulation of cardiac gene expression, and is required for heart morphogenesis and coronary artery development.


Pssm-ID: 350630  Cd Length: 88  Bit Score: 60.36  E-value: 5.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  606 ERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMevcKVTKNKIWKDVAGLLGIGAS-SSAAYTLRK 684
Cdd:cd16866      1 EYDAFLNELRQFHASRGTPFKKIPVVGGKELDLYLLYSKVTALGGWA---KVTDKNKWEEILEDFNFPRGcSNAAFALKQ 77
                           90
                   ....*....|
gi 1028725279  685 HYTKNLLPYE 694
Cdd:cd16866     78 IYLRYLEAYE 87
ARID_ARID4B cd16883
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 4B (ARID4B) ...
606-694 7.27e-11

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 4B (ARID4B) and similar proteins; ARID4B, also called 180 kDa Sin3-associated polypeptide (p180), breast cancer-associated antigen BRCAA1, histone deacetylase complex subunit SAP180, or retinoblastoma-binding protein 1-like 1 (RBP1L1, or RBBP1L1), is a tumor suppressor involved in epigenetic regulation in leukemia and Prader-Willi/Angelman syndrome. It associates with the mSIN3A histone deacetylase (HDAC) chromatin remodeling complex through the interaction with the breast cancer associated tumor suppressor ING1, the breast cancer metastasis suppressor BRMS1, and the ARID4 family homolog ARID4A ( also known as RBP1). ARID4B plays a causative role in metastatic progression of breast cancer. It may also be associated with regulating cell cycle. ARID4B contains a Tudor domain, a PWWP domain (also known as HATH domain or RBB1NT domain), an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a chromobarrel domain, and a C-terminal R2 domain.


Pssm-ID: 350647  Cd Length: 92  Bit Score: 60.37  E-value: 7.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  606 ERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFMevcKVTKNKIWKDVAGLLGIGASSSAA-YTLRK 684
Cdd:cd16883      1 ERENFLQQLYKFMEDRGTPINKRPVLGYRNLNLFKLFRLVHKLGGFD---NIESGAVWKQVYQDLGIPVLNSAAgYNVKC 77
                           90
                   ....*....|
gi 1028725279  685 HYTKNLLPYE 694
Cdd:cd16883     78 AYRKYLYGFE 87
PHA03247 PHA03247
large tegument protein UL36; Provisional
726-1104 4.07e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 65.34  E-value: 4.07e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  726 PSPGSAGSNSQDSLPSAPTAPGPGHVDGYPGYGGYSGPQDYNSPQR-----PPHPPHGTQGSYQGQGGYSQQYPGGneqy 800
Cdd:PHA03247  2690 PTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALpaapaPPAVPAGPATPGGPARPARPPTTAG---- 2765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  801 gqhyPPASTPVGYPSGPVRPPLYPP--YSNDADRNYGGSVPPPQGPPNTPQGPGNGQDPYGR--GPVPPPSgyqqppRFP 876
Cdd:PHA03247  2766 ----PPAPAPPAAPAAGPPRRLTRPavASLSESRESLPSPWDPADPPAAVLAPAAALPPAASpaGPLPPPT------SAQ 2835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  877 GPPPPQNSSPATVNQTQGGSVStPGYPpgqqpqpdyYRQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPD-FAK--DQQ 953
Cdd:PHA03247  2836 PTAPPPPPGPPPPSLPLGGSVA-PGGD---------VRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTEsFALppDQP 2905
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  954 AGPPQPAgypgygPQQRPMYPgpgwtgtpnaasnqyPRPGYPPGSQPPQnwsQGPPRSMPPSHPGQPPQweqhrypPQGQ 1033
Cdd:PHA03247  2906 ERPPQPQ------APPPPQPQ---------------PQPPPPPQPQPPP---PPPPRPQPPLAPTTDPA-------GAGE 2954
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028725279 1034 PYGAQQNHW-GPMAQAQMRMPRhgYRPDGSKPYGPHGPMAPPPHMKAGMPGQPMFQGSSLMKREVIFPPDSI 1104
Cdd:PHA03247  2955 PSGAVPQPWlGALVPGRVAVPR--FRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSL 3024
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
735-1083 7.08e-10

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: 64.02  E-value: 7.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  735 SQDSLPSAPTAPGPGHVDGYPGYGGYSGPQDYNSPQRPPHPPHGTQGSYQGQGGYSQQYPggnEQYGQHYPPASTPVGYP 814
Cdd:pfam03154  176 AQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTP---TLHPQRLPSPHPPLQPM 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  815 SGPVRPPLYPPYSNDADRNYGgsvPPPQGPPNTPQGPGNGQDPYgrgpvpPPSGYQQPPRFPGPPPPQNSSPATVNQTQG 894
Cdd:pfam03154  253 TQPPPPSQVSPQPLPQPSLHG---QMPPMPHSLQTGPSHMQHPV------PPQPFPLTPQSSQSQVPPGPSPAAPGQSQQ 323
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  895 GSVSTPGYPPGQQPQPDYYRQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPdfakdQQAGPPQPAGYPGYGPQQRPMYP 974
Cdd:pfam03154  324 RIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHP-----PHLSGPSPFQMNSNLPPPPALKP 398
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  975 gpgwtgtPNAASNQYPRPGYPPgsqPPQNWSQGPPRSMPPSHPGQPPQWEQHRYPPQGQPyGAQQNHWGPmaqAQMRMPR 1054
Cdd:pfam03154  399 -------LSSLSTHHPPSAHPP---PLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHP-PTSGLHQVP---SQSPFPQ 464
                          330       340
                   ....*....|....*....|....*....
gi 1028725279 1055 HGYRPDGSKPYGPhgPMAPPPHMKAGMPG 1083
Cdd:pfam03154  465 HPFVPGGPPPITP--PSGPPTSTSSAMPG 491
ARID_KDM5C_5D cd16875
ARID/BRIGHT DNA binding domain of lysine-specific demethylase KDM5C and KDM5D; This group ...
610-694 3.47e-09

ARID/BRIGHT DNA binding domain of lysine-specific demethylase KDM5C and KDM5D; This group includes KDM5C and KDM5D, both of which belong to the JARID subfamily within the JmjC proteins. KDM5C, also called histone demethylase JARID1C, Jumonji/ARID domain-containing protein 1C, protein SmcX, or protein Xe169, is a H3K4 trimethyl-histone demethylase that catalyzes demethylation of H3K4me3 and H3K4me2 to H3K4me1. It plays a role in neuronal survival and dendrite development. KDM5C defects are associated with X-linked mental retardation (XLMR). KDM5D, also called histocompatibility Y antigen (H-Y), histone demethylase JARID1D, Jumonji/ARID domain-containing protein 1D, or protein SmcY, is a male-specific antigen that shows a demethylase activity specific for di- and tri-methylated histone H3K4 (H3K4me3 and H3K4me2), and has a male-specific function as a histone H3K4 demethylase by recruiting a meiosis-regulatory protein, MSH5, to condensed DNA. KDM5D directly interacts with a polycomb-like protein Ring6a/MBLR, and plays a role in regulation of transcriptional initiation through H3K4 demethylation. Both KDM5C and KDM5D contain the catalytic JmjC domain, a JmjN domain, an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a C5HC2 zinc finger, as well as two plant homeodomain (PHD) fingers.


Pssm-ID: 350639  Cd Length: 92  Bit Score: 55.31  E-value: 3.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  610 WLDKLLHFMEERGSPISTcPTISKNPLDLFRLYIYVKERGGFMEVCkvtKNKIWKDVAGLLGIGASSSAAYTLRKHYTKN 689
Cdd:cd16875      7 YLDQIAKFWEIQGSSLKI-PNVERRILDLYSLSKIVQEEGGYEAIC---KDRRWARVAQRLGYPPGKNIGSLLRSHYERI 82

                   ....*
gi 1028725279  690 LLPYE 694
Cdd:cd16875     83 IYPYE 87
ARID_KDM5A cd16873
ARID/BRIGHT DNA binding domain of lysine-specific demethylase 5A (KDM5A); KDM5A, also called ...
610-694 5.87e-09

ARID/BRIGHT DNA binding domain of lysine-specific demethylase 5A (KDM5A); KDM5A, also called histone demethylase JARID1A, Jumonji/ARID domain-containing protein 1A, or Retinoblastoma-binding protein 2 (RBBP-2 or RBP2), was originally identified as a retinoblastoma protein (Rb)-binding partner; its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5A functions as the trimethylated histone H3 lysine 4 (H3K4me3) demethylase that belongs to the JARID subfamily within the JmjC proteins. It also displays DNA-binding activities that can recognize the specific DNA sequence CCGCCC. KDM5A contains the catalytic JmjC domain, a JmjN domain, an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a C5HC2 zinc finger, as well as three plant homeodomain (PHD) fingers.


Pssm-ID: 350637  Cd Length: 92  Bit Score: 54.89  E-value: 5.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  610 WLDKLLHFMEERGSPISTcPTISKNPLDLFRLYIYVKERGGFMEVCKvtkNKIWKDVAGLLGIGASSSAAYTLRKHYTKN 689
Cdd:cd16873      7 FLDQLAKFWELQGSTLKI-PVVERKILDLYALSKIVASEGGFEMVTK---EKKWSKVGSRMGYLPGKGTGSLLKSHYERI 82

                   ....*
gi 1028725279  690 LLPYE 694
Cdd:cd16873     83 LYPYE 87
dnaA PRK14086
chromosomal replication initiator protein DnaA;
887-1075 9.78e-09

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 60.22  E-value: 9.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  887 ATVNQTQGGSVSTPGYPPgQQPQPDYYRQEPPASPGYPPTSA----PGTYPGKGMPPPQPRrHPDFAKDQQAGPPQPAGY 962
Cdd:PRK14086    86 ITVDPSAGEPAPPPPHAR-RTSEPELPRPGRRPYEGYGGPRAddrpPGLPRQDQLPTARPA-YPAYQQRPEPGAWPRAAD 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  963 PgYGPQQRPMYPGPgwtGTPNAASNQYPRPGYPPGSQPPQNWSQGPPRSMPPSHPG----QPPQWEQHRypPQGQPYGAQ 1038
Cdd:PRK14086   164 D-YGWQQQRLGFPP---RAPYASPASYAPEQERDREPYDAGRPEYDQRRRDYDHPRpdwdRPRRDRTDR--PEPPPGAGH 237
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1028725279 1039 QNHWGPMAQAQMRMPRHGYRPDGSKPYGPHGPMAPPP 1075
Cdd:PRK14086   238 VHRGGPGPPERDDAPVVPIRPSAPGPLAAQPAPAPGP 274
PHA03247 PHA03247
large tegument protein UL36; Provisional
726-1134 1.82e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.95  E-value: 1.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  726 PSPGSAGSNSQDSLPSAPTAPGPGHVDGYPGYGGYSGPQDYNSP----QRPPHPPHGTQGSYQGQGGYSQQYPGGNEQYG 801
Cdd:PHA03247  2575 PRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPpdthAPDPPPPSPSPAANEPDPHPPPTVPPPERPRD 2654
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  802 QHYPP----------------ASTPVGYPSGPVRPPLYPPYSNDADRNYGGSVPPPQGPPNTPQGPGNGQDPYGRG--PV 863
Cdd:PHA03247  2655 DPAPGrvsrprrarrlgraaqASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQasPA 2734
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  864 PPPSGYQQPPRFPGPPPPQNSSPATVNQTQGGSVSTPGYPPGQQPQP----------DYYRQEPPASPGYPPTSAPGTYP 933
Cdd:PHA03247  2735 LPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRrltrpavaslSESRESLPSPWDPADPPAAVLAP 2814
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  934 GKGMPP---PQPRRHPDFAKDQQAGPPQPAGYPGYGPQQRPMYPG-----PGWTGTPNAASNQYPRP-----GYPPGSQP 1000
Cdd:PHA03247  2815 AAALPPaasPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvrrRPPSRSPAAKPAAPARPpvrrlARPAVSRS 2894
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279 1001 PQNWSQGPPRSMPPSHPGQPPqweqhryPPQGQPYGAQQNHWGPMAQAQMRMPRHGYRPDGSKPYGPHGPMAPPPHMKAG 1080
Cdd:PHA03247  2895 TESFALPPDQPERPPQPQAPP-------PPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL 2967
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1028725279 1081 MPGQpmfqgSSLMKREVIFPPDSIEAVTPILYKRRrmmRHDVAPVDAWRLMMSL 1134
Cdd:PHA03247  2968 VPGR-----VAVPRFRVPQPAPSREAPASSTPPLT---GHSLSRVSSWASSLAL 3013
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
728-1085 3.42e-08

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 58.42  E-value: 3.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  728 PGSAGSNSQDSLPSAPTAPGPGHVDGYPGYGGYSGPQDYNSPQRPPHPPHGTQGSYQGQGGYsqqYPGGNEQYGQ----H 803
Cdd:pfam03157  221 GQQPERGQQGQQPGQGQQPGQGQQGQQPGQPQQLGQGQQGYYPISPQQPRQWQQSGQGQQGY---YPTSLQQPGQgqsgY 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  804 YPPASTPVGYPSGPVRPPLYPPYSNDADRNYGGSVPPPQGPPNTPQG--PGNGQDP-YGRGPVPPPSGYQQPPRFPGPPP 880
Cdd:pfam03157  298 YPTSQQQAGQLQQEQQLGQEQQDQQPGQGRQGQQPGQGQQGQQPAQGqqPGQGQPGyYPTSPQQPGQGQPGYYPTSQQQP 377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  881 PQNSSPATVNQTQGGSVSTPGYPPGQQPQPDYYRQ-EPPASPGYPPTSAPGTYP------GKGMPPPQPRR--HPDFAKD 951
Cdd:pfam03157  378 QQGQQPEQGQQGQQQGQGQQGQQPGQGQQPGQGQPgYYPTSPQQSGQGQPGYYPtspqqsGQGQQPGQGQQpgQEQPGQG 457
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  952 QQAGPPQPAGYPGYGPQ-QRPMYPGPGWTGTPNAASNQYPRPGYP-------PGSQP--PQNWSQGPPRSMP--PSHPGQ 1019
Cdd:pfam03157  458 QQPGQGQQGQQPGQPEQgQQPGQGQPGYYPTSPQQSGQGQQLGQWqqqgqgqPGYYPtsPLQPGQGQPGYYPtsPQQPGQ 537
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028725279 1020 PPQWEQHRYPPQGQP-----YGAQQNHWGPMAQAQMR-------MPRHGYRPDGSKP-YGPHGPMAPPPHMKAGMPGQP 1085
Cdd:pfam03157  538 GQQLGQLQQPTQGQQgqqsgQGQQGQQPGQGQQGQQPgqgqqgqQPGQGQQPGQGQPgYYPTSPQQSGQGQQPGQWQQP 616
ARID_KDM5B cd16874
ARID/BRIGHT DNA binding domain of lysine-specific demethylase 5B (KDM5B); KDM5B, also called ...
610-693 7.02e-08

ARID/BRIGHT DNA binding domain of lysine-specific demethylase 5B (KDM5B); KDM5B, also called cancer/testis antigen 31 (CT31), histone demethylase JARID1B, Jumonji/ARID domain-containing protein 1B (JARID1B), PLU-1, or retinoblastoma-binding protein 2 homolog 1 (RBP2-H1 or RBBP2H1A), is a member of the JARID subfamily within the JmjC proteins. It has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. KDM5B acts as a histone demethylase that catalyzes the removal of trimethylation of lysine 4 on histone H3 (H3K4me3), induced by polychlorinated biphenyls (PCBs). It also mediates demethylation of H3K4me2 and H3K4me1. Moreover, KDM5B functions as a negative regulator of hematopoietic stem cell (HSC) self-renewal and progenitor cell activity. KDM5B has also been shown to interact with the DNA binding transcription factors BF-1 and PAX9, as well as TIEG1/KLF10 (transforming growth factor-beta inducible earlygene-1/Kruppel-like transcription factor 10), and possibly function as a transcriptional corepressor. KDM5B contains the catalytic JmjC domain, a JmjN domain, an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a C5HC2 zinc finger, as well as three plant homeodomain (PHD) fingers.


Pssm-ID: 350638  Cd Length: 90  Bit Score: 51.86  E-value: 7.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  610 WLDKLLHFMEERGSPISTcPTISKNPLDLFRLYIYVKERGGFMEVCKVTKnkiWKDVAGLLGIGASSSAAYTLRKHYTKN 689
Cdd:cd16874     10 FLDQIAKFWELQGCTLKI-PHVERKILDLFQLNKLVAEEGGFDLVCKERK---WTKIATKMGFAPGKAVGSHIRAHYERI 85

                   ....
gi 1028725279  690 LLPY 693
Cdd:cd16874     86 LYPY 89
ARID_ARID4A cd16882
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 4A (ARID4A) ...
606-694 1.08e-07

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 4A (ARID4A) and similar proteins; ARID4A, also called retinoblastoma-binding protein 1 (RBBP1, or RBP1), is a leukemia and tumor suppressor involved in epigenetic regulation in leukemia and Prader-Willi/Angelman syndrome. It associates with the mSIN3A histone deacetylase (HDAC) chromatin remodeling complex through the interaction with the breast cancer associated tumor suppressor ING1, the breast cancer metastasis suppressor BRMS1, and the ARID4 family homolog ARID4B (also known as RBP1L1). ARID4A specifically interacts with retinoblastoma protein (pRb) and shows both HDAC-dependent and -independent repression activities. It is also involved in the pocket domain of pRb-mediated repression of E2F-dependent transcription and cellular proliferation. Moreover, it acts as a Runx2 coactivator and is involved in the regulation of osteoblastic differentiation in Runx2-osterix transcriptional cascade. ARID4A contains a Tudor domain, a PWWP domain (also known as HATH domain or RBB1NT domain), an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), a chromobarrel domain, and a C-terminal R2 domain. The ARID and R2 domains are responsible for the repression activities. The Tudor, PWWP, and chromobarrel domains are all Royal Family domains, but only chromobarrel domain of ARID4A is responsible for recognizing both dsDNA and methylated histone tails, particularly H4K20me3, in chromatin remodeling and epigenetic regulation.


Pssm-ID: 350646  Cd Length: 87  Bit Score: 51.13  E-value: 1.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  606 ERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGfmevC-KVTKNKIWKDVAGLLGIGA-SSSAAYTLR 683
Cdd:cd16882      1 ERDNFLQQLYKFMEDRGTPINKPPVLGYKDLNLFKLFRLVYQQGG----CdNIESGSVWKQIYMDLGIPIlNSAASYNVK 76
                           90
                   ....*....|.
gi 1028725279  684 KHYTKNLLPYE 694
Cdd:cd16882     77 TAYRKYLYGFE 87
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
727-1049 1.27e-07

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 56.49  E-value: 1.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  727 SPGSAGSNSQDSLPSAPTAPGPGHVDGYPGYGGYSGPQDYNSP---QRPPHPPHGTQGSYQGQG--GY---SQQYPGGNE 798
Cdd:pfam03157  418 SPQQSGQGQPGYYPTSPQQSGQGQQPGQGQQPGQEQPGQGQQPgqgQQGQQPGQPEQGQQPGQGqpGYyptSPQQSGQGQ 497
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  799 QYGQHYPPASTPVG-YPSGPVRP----PLYPPYSndadrnyggsvpppqgppntPQGPGNGQDP-YGRGPVPPPSGYQQP 872
Cdd:pfam03157  498 QLGQWQQQGQGQPGyYPTSPLQPgqgqPGYYPTS--------------------PQQPGQGQQLgQLQQPTQGQQGQQSG 557
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  873 PRFPGPPPPQNSSPATVNQTQGGSVSTPGYPPGQQpQPDYYrQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPDFAKDQ 952
Cdd:pfam03157  558 QGQQGQQPGQGQQGQQPGQGQQGQQPGQGQQPGQG-QPGYY-PTSPQQSGQGQQPGQWQQPGQGQPGYYPTSSLQLGQGQ 635
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  953 QAGPPQPAGYPGYGPQ-QRPMYPGPGWTGTPNAASNQYPRPGYPPGSQPPQNWSQgPPRSMPPSHPGQPPQWEQHRYPPQ 1031
Cdd:pfam03157  636 QGYYPTSPQQPGQGQQpGQWQQSGQGQQGYYPTSPQQSGQAQQPGQGQQPGQWLQ-PGQGQQGYYPTSPQQPGQGQQLGQ 714
                          330
                   ....*....|....*...
gi 1028725279 1032 GQPYGAQQNHWGPMAQAQ 1049
Cdd:pfam03157  715 GQQSGQGQQGYYPTSPGQ 732
ARID_ARID5B cd16885
ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 5B (ARID5B) ...
606-694 2.31e-07

ARID/BRIGHT DNA binding domain of AT-rich interactive domain-containing protein 5B (ARID5B) and similar proteins; ARID5B, also called MRF1-like protein or modulator recognition factor 2 (MRF-2), is a DNA-binding protein that directly interacts with plant homeodomain (PHD) finger 2 (PHF2) to form a protein kinase A (PKA)-dependent PHF2-ARID5B histone H3K9Me2 demethylase complex, which is a signal-sensing modulator of histone methylation and gene transcription. It also functions as a transcriptional co-regulator for the transcription factor sex determining region Y (SRY)-box protein 9 (Sox9) and promotes chondrogenesis through histone modification. Moreover, ARID5B is highly expressed in the cardiovascular system and may play essential roles in the phenotypic change of smooth muscle cells (SMCs) through its regulation of SMC differentiation. Its polymorphism has been associated with risk for pediatric acute lymphoblastic leukemia (ALL). ARID5B contains an AT-rich DNA-interacting domain (ARID, also known as BRIGHT), which can bind both the major and minor grooves of its target sequences.


Pssm-ID: 350649  Cd Length: 95  Bit Score: 50.46  E-value: 2.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  606 ERRIWLDKLLHFMEERGSPISTCPTISKNPLDLFRLYIYVKERGGFmEVckVTKNKIWKDVAGLLGIG-ASSSAAYTLRK 684
Cdd:cd16885      1 DEQAFLVALYKYMKERKTPIERIPYLGFKQINLWTMFQAAQKLGGY-ET--ITARRQWKHIYDELGGNpGSTSAATCTRR 77
                           90
                   ....*....|
gi 1028725279  685 HYTKNLLPYE 694
Cdd:cd16885     78 HYERLILPYE 87
PHA03378 PHA03378
EBNA-3B; Provisional
886-1085 2.69e-07

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 55.84  E-value: 2.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  886 PATVNQTQGGSVSTPGYP--PGQQPQPDYYRQEPPASPGYPPTSAPGTYPGKGMP-PPQPRRHPDFAKDQQAGPPqpagy 962
Cdd:PHA03378   576 PLTSPTTSQLASSAPSYAqtPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPiPMRPLRMQPITFNVLVFPT----- 650
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  963 PGYGPQQRPMYPGPGWTGTPNAASNqyPRPGYPPGSQPPQnWS----QGPPRS---MPPSH----PGQPPQWEQHRY-PP 1030
Cdd:PHA03378   651 PHQPPQVEITPYKPTWTQIGHIPYQ--PSPTGANTMLPIQ-WApgtmQPPPRAptpMRPPAappgRAQRPAAATGRArPP 727
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1028725279 1031 QGQPYGAQqnhwgPMAQAQMRMPRHGYRPDGSK-PYGPHGPMAPPphmkAGMPGQP 1085
Cdd:PHA03378   728 AAAPGRAR-----PPAAAPGRARPPAAAPGRARpPAAAPGRARPP----AAAPGAP 774
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
859-1039 5.34e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 54.61  E-value: 5.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  859 GRGPVPPPSGYQQPPRFPGPPPPQNSSPATVNQTQGGSVSTPGYPPGQQPQPdyyrqepPASPGYPPTSAPGTYPGKGmP 938
Cdd:PRK07764   595 AGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPG-------VAAPEHHPKHVAVPDASDG-G 666
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  939 PPQPRRHPDFAKDQQAGPPQPAGYPG-YGPQQRPMYPGPGWT---GTPNAASNQYPRPGYPPGSQPPQNWSQGPPRSMPP 1014
Cdd:PRK07764   667 DGWPAKAGGAAPAAPPPAPAPAAPAApAGAAPAQPAPAPAATppaGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD 746
                          170       180
                   ....*....|....*....|....*
gi 1028725279 1015 SHPGQPPQWEQHRYPPQGQPYGAQQ 1039
Cdd:PRK07764   747 DPPDPAGAPAQPPPPPAPAPAAAPA 771
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
805-1027 7.76e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 54.22  E-value: 7.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  805 PPASTPVGYPSGPVRPPLYPPYSNDADrnyggsvpppqgpPNTPQGPGNGQDPYGRGPVPPPSGYQQPPRFPGPPPPQNS 884
Cdd:PRK07764   600 PPAPASSGPPEEAARPAAPAAPAAPAA-------------PAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGG 666
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  885 SPATVNQTQGGSVSTPGYPPGQQPQPDYYRQEPPASPGYPPTSAPGTYPGKGMPPPQPRrhpdfakdQQAGPPQPAGYPG 964
Cdd:PRK07764   667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAA--------QGASAPSPAADDP 738
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1028725279  965 YGPQQRPMYPGPGWTGTPNAASNQYPRPGYPPGSQPPqnWSQGPPRSMPPSHPGQPPQWEQHR 1027
Cdd:PRK07764   739 VPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPP--PSPPSEEEEMAEDDAPSMDDEDRR 799
PHA03378 PHA03378
EBNA-3B; Provisional
805-1075 1.62e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 53.15  E-value: 1.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  805 PPASTPvgypsGPVRPPLYPPYSNDADRNYGGSVPPPQGPpntpqgPGNGQDPYGR-GPVPPPSGYQQPPRFPGPPPPQN 883
Cdd:PHA03378   696 PPPRAP-----TPMRPPAAPPGRAQRPAAATGRARPPAAA------PGRARPPAAApGRARPPAAAPGRARPPAAAPGRA 764
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  884 SSPATvnqTQGGSVSTP----GYPPGQQPQPDYYRQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPDFAKDQQAGPpqP 959
Cdd:PHA03378   765 RPPAA---APGAPTPQPppqaPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTGGVKRGRP--S 839
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  960 AGYPGYGPQQRPMYPGPGWTGTPNAASNQYPrPGYPPGSQPPQ-NWSQGPPRSMPPSHPGQPPqweqhryppqgQPYGAQ 1038
Cdd:PHA03378   840 LKKPAALERQAAAGPTPSPGSGTSDKIVQAP-VFYPPVLQPIQvMRQLGSVRAAAASTVTQAP-----------TEYTGE 907
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1028725279 1039 QNHWGPMAQAQMRMPRHGYRPDGSKPYGPHGPMAPPP 1075
Cdd:PHA03378   908 RRGVGPMHPTDIPPSKRAKTDAYVESQPPHGGQSHSF 944
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
850-1034 1.94e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 52.68  E-value: 1.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  850 GPGNGQDPYGRGPVPPPSGYQQPprfpgppppqNSSPATVNQTQGGSVSTPGYPPGQQPQPDYYRQEPPASPGYPPTSAP 929
Cdd:PRK07764   620 APAAPAAPAPAGAAAAPAEASAA----------PAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAA 689
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  930 GTyPGKGMPPPQPrrhpdfakdQQAGPPQPAGYPGYGPQQRPMYPGPGWTGTPNAASNQYPRPGYPPgsqPPQNWSQGPP 1009
Cdd:PRK07764   690 PA-APAGAAPAQP---------APAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD---DPPDPAGAPA 756
                          170       180
                   ....*....|....*....|....*
gi 1028725279 1010 RSMPPSHPGQPPQWEQHRYPPQGQP 1034
Cdd:PRK07764   757 QPPPPPAPAPAAAPAAAPPPSPPSE 781
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
894-1102 2.28e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 52.68  E-value: 2.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  894 GGSVSTPGYPPGQQPQPdyyrQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPDFAKDQQAGPPQPAGYPGYGPQQRPMY 973
Cdd:PRK07764   599 GPPAPASSGPPEEAARP----AAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAG 674
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  974 PGPGWTGTPNAASNQYPRPGYPPGSQPpqnwsqGPPRSMPPSHPGQPPQWEQHRYPPQGQpygaqqnhWGPMAQAQMRMP 1053
Cdd:PRK07764   675 GAAPAAPPPAPAPAAPAAPAGAAPAQP------APAPAATPPAGQADDPAAQPPQAAQGA--------SAPSPAADDPVP 740
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1028725279 1054 RHGYRPDGSKPYGPHGPMAPPPHMKAGMPGQPMFQGSSLMKREVIFPPD 1102
Cdd:PRK07764   741 LPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDD 789
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
909-1114 3.42e-06

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


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 51.96  E-value: 3.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  909 QPDYYRQEPPASPGYPPTSapgtypgkgmPPPQPRRHPDFAKDQQAGPPQPA--GY-----PGYGPQQRPMYPGPGWTGT 981
Cdd:pfam09770   99 QVRFNRQQPAARAAQSSAQ----------PPASSLPQYQYASQQSQQPSKPVrtGYekykePEPIPDLQVDASLWGVAPK 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  982 PNAASNQYPRPGYPPGSQPPQN---------------WSQGPPRSMPPSHPGQPPQWEQHRYPPQGQ--PYGAQQNHWGP 1044
Cdd:pfam09770  169 KAAAPAPAPQPAAQPASLPAPSrkmmsleeveaamraQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQfpPQIQQQQQPQQ 248
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028725279 1045 MAQAQMRMPRHGY------RPDGSKPYGPHGPMAPPPHMKAGMPGQPMFQGSSLMKREVIFPPDSIEAVTPILYKR 1114
Cdd:pfam09770  249 QPQQPQQHPGQGHpvtilqRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQILQNPNRLSAARVGYPQNPQPGV 324
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
883-1090 3.64e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 51.80  E-value: 3.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  883 NSSPATVNQTQGGSVSTPGYPP-GQQPQPDYYRQEPPASPGY-PPTSAPGTYPGKGMPPP---QPRRHPDFAKDQQAGPP 957
Cdd:PRK12323   371 GAGPATAAAAPVAQPAPAAAAPaAAAPAPAAPPAAPAAAPAAaAAARAVAAAPARRSPAPealAAARQASARGPGGAPAP 450
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  958 QPAGYPGYGPQQRPMYPGPgwtGTPNAASNQYPRPGYPPGSQPPQNWSQGPPRSMPPSHPGQPPqweqhrYPPQGQPYGA 1037
Cdd:PRK12323   451 APAPAAAPAAAARPAAAGP---RPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAP------AQPDAAPAGW 521
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1028725279 1038 QQNHWGPMAQAQMRMPRHGYRPDGSKPYGPHGPMAPPPHMKAGMPGQ------PMFQGS 1090
Cdd:PRK12323   522 VAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRAsasglpDMFDGD 580
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
893-1052 5.06e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 51.53  E-value: 5.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  893 QGGSVSTPGYPPGQQPQPDyyRQEPPAspgypPTSAPGTYPGKGMPPPQPRRHPdfakdQQAGPPQPAGypgyGPQQRPM 972
Cdd:PRK07764   383 RRLGVAGGAGAPAAAAPSA--AAAAPA-----AAPAPAAAAPAAAAAPAPAAAP-----QPAPAPAPAP----APPSPAG 446
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  973 YPGPGWTGTPNAASNQYPRPGypPGSQPPQNWSQGPPRSMPPSHPGQPPqweqhryPPQGQPYGAQQnhwGPMAQAQMRM 1052
Cdd:PRK07764   447 NAPAGGAPSPPPAAAPSAQPA--PAPAAAPEPTAAPAPAPPAAPAPAAA-------PAAPAAPAAPA---GADDAATLRE 514
PHA03247 PHA03247
large tegument protein UL36; Provisional
851-1109 1.15e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  851 PGNGQDPYGRGP----VPPPSGYQQPPRFPGPPPPQNSSPATVNQTQG---------GSVSTPGYPPGQQPQPDyyRQEP 917
Cdd:PHA03247  2492 AGAAPDPGGGGPpdpdAPPAPSRLAPAILPDEPVGEPVHPRMLTWIRGleelasddaGDPPPPLPPAAPPAAPD--RSVP 2569
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  918 PASPG-YPPTSAPGTYPGKGMPPPQPR--RHPDFAKDQQAGPPQPAGYPGYGPQQRPmyPGPGwtgtPNAASNQYPRPGY 994
Cdd:PHA03247  2570 PPRPApRPSEPAVTSRARRPDAPPQSArpRAPVDDRGDPRGPAPPSPLPPDTHAPDP--PPPS----PSPAANEPDPHPP 2643
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  995 PPGSQPPQNWSQ-GPPRSMPPSHPGQPPQWEQHRYPPQGQPYGAQQNHWGPMAqaqmrmprhgyrpDGSKPYGPHGPMAP 1073
Cdd:PHA03247  2644 PTVPPPERPRDDpAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLT-------------SLADPPPPPPTPEP 2710
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1028725279 1074 PPHmkAGMPGQPMFQGSSLMKREviFPPDSIEAVTP 1109
Cdd:PHA03247  2711 APH--ALVSATPLPPGPAAARQA--SPALPAAPAPP 2742
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
899-1098 1.19e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 50.37  E-value: 1.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  899 TPGYPPGQQPQPdyyRQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPDFAKDQQAGPPQPAGYPGYGPQQRPMYPGPGW 978
Cdd:PRK07764   616 AAPAAPAAPAAP---APAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAA 692
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  979 TGTPNAASNQYPRPGYPPGSQPPQNWSQgPPRSMPPSHPGQPPQWEQHRYPPQGQPYGAQQNHWGPMAQAQmrMPRHGYR 1058
Cdd:PRK07764   693 PAGAAPAQPAPAPAATPPAGQADDPAAQ-PPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPP--APAPAAA 769
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1028725279 1059 PDGSKPYGPHGPMAPPPHMKAGMPGQPMFQGSSLMKREVI 1098
Cdd:PRK07764   770 PAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVAMELL 809
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
917-1085 1.47e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.98  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  917 PPASPGYPPTSAPGTYPGKGMPPPQPRRHPDFAKDQQAGPPQPAGYP--GYGPQQRPMYPGPGWTGTPNAASNQYPRPGy 994
Cdd:PRK07764   593 GAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEAsaAPAPGVAAPEHHPKHVAVPDASDGGDGWPA- 671
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  995 PPGSQPPQNWSQGPPRSMPPSHPGQPPQWEQHRYPPQGQPYGAQQNHWGPMAQAQMRMPRHGYRPDG-SKPYGPHGPMAP 1073
Cdd:PRK07764   672 KAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPvPLPPEPDDPPDP 751
                          170
                   ....*....|..
gi 1028725279 1074 PPHMKAGMPGQP 1085
Cdd:PRK07764   752 AGAPAQPPPPPA 763
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
885-1085 1.51e-05

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: 50.03  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  885 SPATVNQTQGGSVSTPGYPPGQQPQPDYYRQEPPASPGYPP-----TSAPGTYPGKgmpPPQPRRHPDFAKdQQAGPPQP 959
Cdd:pfam09770  114 SSAQPPASSLPQYQYASQQSQQPSKPVRTGYEKYKEPEPIPdlqvdASLWGVAPKK---AAAPAPAPQPAA-QPASLPAP 189
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  960 ---------------AGYPGYGPQQRPMYPGPGWTGTPNAASNQYPRPGYPPGSQPPQNWSQGPPRSMPPSHPGQPPQWE 1024
Cdd:pfam09770  190 srkmmsleeveaamrAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRP 269
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028725279 1025 QHRYPPQGQPYGAQQNHWGPMAQAQMRM---------PRHGYRPDGSKPYGPHGPMAPPPHM----KAGMPGQP 1085
Cdd:pfam09770  270 QSPQPDPAQPSIQPQAQQFHQQPPPVPVqptqilqnpNRLSAARVGYPQNPQPGVQPAPAHQahrqQGSFGRQA 343
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
895-1049 1.74e-05

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: 49.65  E-value: 1.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  895 GSVSTPGYPPGQQPQPdyyrqePPASPGYPPTSAPGTYPGKGMPPPQPRRHPDFAkdQQAGPPQPAgypgYGPQQRPMYP 974
Cdd:pfam09770  209 KPAQQPAPAPAQPPAA------PPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHP--GQGHPVTIL----QRPQSPQPDP 276
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028725279  975 GPGWTGTPNAASNQYPRPGYPPGSQPPQNwsqgpPRSMPPSHPGQPPQWEQHRYPPQGQPYGAQQNHWGPMAQAQ 1049
Cdd:pfam09770  277 AQPSIQPQAQQFHQQPPPVPVQPTQILQN-----PNRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPII 346
PRK10263 PRK10263
DNA translocase FtsK; Provisional
892-1034 5.04e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 48.54  E-value: 5.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  892 TQGGSVSTPGYPPGQ-----QPQPDYYRQEP---PASPGYPPTSAPGTYPGKGMPP---PQPRRHPDFAKDQQAGPPQPA 960
Cdd:PRK10263   341 TQTPPVASVDVPPAQptvawQPVPGPQTGEPviaPAPEGYPQQSQYAQPAVQYNEPlqqPVQPQQPYYAPAAEQPAQQPY 420
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028725279  961 GYPGYGPQQRPMYPGPGWTGTPNAASNQYPRPGYPPGSQPPQNWSQGPPRSMPPSHPGQPPQWEQHRYPPQGQP 1034
Cdd:PRK10263   421 YAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEP 494
PRK10263 PRK10263
DNA translocase FtsK; Provisional
916-1034 5.44e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 48.16  E-value: 5.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  916 EPPASPGYPPTSAPgTYPGKGMPPPQPRRHPDFAKDQQAGPPQPAGypgygPQQRPMYPGPgwtgtPNAASNQYPRPGYP 995
Cdd:PRK10263   742 EPLFTPIVEPVQQP-QQPVAPQQQYQQPQQPVAPQPQYQQPQQPVA-----PQPQYQQPQQ-----PVAPQPQYQQPQQP 810
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1028725279  996 pgsQPPQNWSQGPPRSMPPshpgqPPQWEQHRYPPQGQP 1034
Cdd:PRK10263   811 ---VAPQPQYQQPQQPVAP-----QPQYQQPQQPVAPQP 841
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
722-1001 1.04e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.47  E-value: 1.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  722 ATSVPSPGSAGSNSQDSLPSAPTAPGPGHVDGYPGYGGYSGPqdynSPQRPPHPPHGTQGSYQGQGGYSQQYPGGNEQYG 801
Cdd:PHA03307   163 ASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASP----RPPRRSSPISASASSPAPAPGRSAADDAGASSSD 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  802 QHYPPASTPVGYPSGpvRPPLYPPYSNDADRNYGGSVPPPQGPPNTPQGPGNGQDPyGRGPVPPPSGYQQPPRFPGPPPP 881
Cdd:PHA03307   239 SSSSESSGCGWGPEN--ECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPR-ERSPSPSPSSPGSGPAPSSPRAS 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  882 QN---------SSPATVNQTQGGSVSTPGYPPGQQPQPDyyRQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPDFAKDQ 952
Cdd:PHA03307   316 SSssssresssSSTSSSSESSRGAAVSPGPSPSRSPSPS--RPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAA 393
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1028725279  953 QAGPPQPAGYPGYGPQQRPMYPGPGWTGTPNAASNQYPrPGYP-----PGSQPP 1001
Cdd:PHA03307   394 VAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYP-LLTPsgepwPGSPPP 446
ARID_JARD2 cd16870
ARID/BRIGHT DNA binding domain of Jumonji/ARID domain-containing protein 2 (JARID2) and ...
618-693 1.35e-04

ARID/BRIGHT DNA binding domain of Jumonji/ARID domain-containing protein 2 (JARID2) and similar proteins; JARID2, also called protein Jumonji, is a DNA-binding protein that contains both the Jumonji C (JmjC) domain and AT-rich DNA-interacting domain (ARID, also known as BRIGHT). It is an interacting component of Polycomb repressive complex-2 (PRC2) that catalyzes methylation of lysine 27 of histone H3 (H3K27) and regulates important gene expression patterns during development. It exhibits nucleosome-binding activity that contributes to PRC2 stimulation. However, unlike other JmjC domain-containing proteins, JARID2 is catalytically inactive due to the lack of conserved residues essential for histone demethylase activity. JARID2 is also involved in transforming growth factor-beta (TGF-beta)-induced epithelial-mesenchymal transition (EMT) of lung and colon cancer cell lines through the modulation of histone H3K27 methylation. Moreover, JARID2 is a part of GLP- and G9a-containing protein complex that promotes lysine 9 on histone H3 (H3K9) methylation on the cyclin D1 promoter and silences the expression of cyclin D1 and other cell cycle genes. It functions as a transcriptional repressor that plays critical roles in embryonic development including heart development in mice, and regulates cardiomyocyte proliferation via interaction with retinoblastoma protein (Rb), one of the master regulatory genes of the cell cycle. Furthermore, JARID2 acts as a transcriptional repressor of target genes, including Notch1. It directly binds to SETDB1 (SET domain, bifurcated 1) to form a complex that plays an important role in a novel process involving the modification of H3K9 methylation during heart development. Meanwhile, JARID2 is a key transcriptional repressor that plays a role in invariant natural killer T (iNKT) cell maturation. It regulates promyelocytic leukemia zinc finger (PLZF) expression by linking T-cell receptor (TCR) signaling to H3K9me3. JARID2 polymorphisms are associated with non-syndromic orofacial clefts (NSOC) susceptibility.


Pssm-ID: 350634  Cd Length: 112  Bit Score: 42.98  E-value: 1.35e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028725279  618 MEERGSPISTCPTISKNPLDLFRLYIYVKERGGfMEvcKVTKNKIWKDVAGLLGIGASSSAAYT-LRKHYTKNLLPY 693
Cdd:cd16870     16 LESQGINLTPPPLIGGCELDLPRLYHLVQELGG-MQ--QVTDKKKWNKVADHLNIPKTAQDRPSkLQDAYCKYLLSY 89
Cytadhesin_P30 pfam07271
Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 ...
907-1051 1.38e-04

Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 and P30 proteins. P30 has been found to be membrane associated and localized on the tip organelle. It is thought that it is important in cytadherence and virulence. The N-terminus contains two predicted transmembrane helices followed by a long region of a short 6 residue proline rich repeat.


Pssm-ID: 429374 [Multi-domain]  Cd Length: 275  Bit Score: 45.73  E-value: 1.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  907 QPQPDYYRQEPPASPGYPPTSAPGtypgkgMPPPQPRRHPDFAKDQQ---AGPPQP--AGYPGYGPQQR--PMYPGPGWT 979
Cdd:pfam07271  126 EPTEQQNTAEPTQPAGVNVANQPQ------MGINQPQINPQFGPNPQqriGFPMQPnmGMRPGFNQMPGmpPNQMRPGFN 199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  980 GTPNAAsnqyPRPGYP---PGSQP-----PQNWSQGPPRSMPPSHPGQPPQWEQHRYPPQGQPYGAQQNHWGPMAQAQMR 1051
Cdd:pfam07271  200 QMPGMP----PRPGFPnpmPNMQPrpgfrPQPGPMGNRPGGGFPHPGTPMGPNRMPNPGMNQRPGMAPPRPGFPPQNGPR 275
PHA03264 PHA03264
envelope glycoprotein D; Provisional
899-1020 2.17e-04

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 45.77  E-value: 2.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  899 TPGYP-PGQQPQPDYY-----RQEPP---ASPGYPPTSAPGTYPGKGMPPPQPRRHPDFAKDQQAGPPQPAGYPGYGPQq 969
Cdd:PHA03264   231 TQYYPqEAHKAIVDYWfmrhgGVVPPyfeESKGYEPPPAPSGGSPAPPGDDRPEAKPEPGPVEDGAPGRETGGEGEGPE- 309
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1028725279  970 rpmypgpgwTGTPNAASNQYPRPGyPPGSQP----PQNWSQGPPRSMPPSHPGQP 1020
Cdd:PHA03264   310 ---------PAGRDGAAGGEPKPG-PPRPAPdadrPEGWPSLEAITFPPPTPATP 354
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
724-1020 4.54e-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: 45.00  E-value: 4.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  724 SVPSPGSA------GSNSQDSLPSAPTAPGPGHVDGYPGYGGYSGPQDYNSPQRPPHPPHGTQGSYQGQGGYSQQYPGGN 797
Cdd:pfam09606  138 GFPSQMSRvgrmqpGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGA 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  798 EQYGQHYPPASTPVGYPSG--PVRPPLYPPYSNDADRNYGGSVPPPQGPPNTPQGPGNGQD-PYGRGPVPPPSGYQQPPR 874
Cdd:pfam09606  218 QMGQQAQANGGMNPQQMGGapNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGgPGQPMGPPGQQPGAMPNV 297
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  875 FPGPPPPQNSSPATVNQTQGGSVSTPGYPPGQQPQP--DYYRQEPPASPGYPPTSAPGTYPGKGMPPPQP-----RRHPD 947
Cdd:pfam09606  298 MSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSvgQGGQVVALGGLNHLETWNPGNFGGLGANPMQRgqpgmMSSPS 377
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028725279  948 FAKDQQAGPPQPAGYPGYGPQQRPMYP-GPGWTGTPNAASNQYPRPGYPPGSQPPQNWSQGPPRSMPPSHPGQP 1020
Cdd:pfam09606  378 PVPGQQVRQVTPNQFMRQSPQPSVPSPqGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQQRTIGQDSPGGS 451
PRK10263 PRK10263
DNA translocase FtsK; Provisional
955-1150 6.72e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 44.69  E-value: 6.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  955 GPPQPAGYPGYGPQQRPMypgpgwtgTPNAASNQYPRPGYPPgsqPPQNWSQGPPRSMPPSHPGQPPQWEQHRYPPQGQP 1034
Cdd:PRK10263   739 GPHEPLFTPIVEPVQQPQ--------QPVAPQQQYQQPQQPV---APQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQP 807
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279 1035 ygaQQnhwgPMA-QAQMRMPRHGYRPdgSKPYG-PHGPMAPPPHMKAGMPgQPMFQGSSLMKREVIFPPDSIEAVTPily 1112
Cdd:PRK10263   808 ---QQ----PVApQPQYQQPQQPVAP--QPQYQqPQQPVAPQPQDTLLHP-LLMRNGDSRPLHKPTTPLPSLDLLTP--- 874
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1028725279 1113 krrrmMRHDVAPVDAWRL--MMSLRSGLLAESTWALDVLN 1150
Cdd:PRK10263   875 -----PPSEVEPVDTFALeqMARLVEARLADFRIKADVVN 909
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
919-1051 7.76e-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: 7.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  919 ASPGYPPTSAPGTYPGKGMPPPQPRRHPdfakdQQAGPPQPAGYPGYGPQQRPMYPGpgwtgTPNAAsnQYPRPgYPPGS 998
Cdd:TIGR01628  378 LQPRMRQLPMGSPMGGAMGQPPYYGQGP-----QQQFNGQPLGWPRMSMMPTPMGPG-----GPLRP--NGLAP-MNAVR 444
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1028725279  999 QPPQNWSQGPPRSMPPSHPgQPPQWEQHRYPPQGQPYGAQQNHWGPMAQ-AQMR 1051
Cdd:TIGR01628  445 APSRNAQNAAQKPPMQPVM-YPPNYQSLPLSQDLPQPQSTASQGGQNKKlAQVL 497
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
892-1039 8.77e-04

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 41.95  E-value: 8.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  892 TQGGSVSTPGYPPGQQPQPDYYRQEPPASPGYPPTSAPGTYPGKGMP-PPQPRRHPDFAKDQQAGPPQPAGYPGYGPQQR 970
Cdd:pfam15240   24 SQEDSPSLISEEEGQSQQGGQGPQGPPPGGFPPQPPASDDPPGPPPPgGPQQPPPQGGKQKPQGPPPQGGPRPPPGKPQG 103
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028725279  971 PmypgpgwtgtPNAASNQYPRPGYPPGSQPPQNWSQGPPRSMPPSHPGQPPQWEQHRYPPQGQPYGAQQ 1039
Cdd:pfam15240  104 P----------PPQGGNQQQGPPPPGKPQGPPPQGGGPPPQGGNQQGPPPPPPGNPQGPPQRPPQPGNP 162
PRK10263 PRK10263
DNA translocase FtsK; Provisional
919-1075 1.03e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.92  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  919 ASPGYPPTSAPgTYPGKGMPPPQPRRHPDFAKDQQAGPPQPAGYP-GYGPQQRPMYPGPGWTGTPNAASNQYPRPGYPPG 997
Cdd:PRK10263   334 AAPVEPVTQTP-PVASVDVPPAQPTVAWQPVPGPQTGEPVIAPAPeGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAA 412
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028725279  998 SQPPQNWSQGPPRSMPPSHPGQPPQWEQHRYPPQGQPyGAQQNHWGPMAQAQmrmPRHGYRPDGSKPYGPHGPMAPPP 1075
Cdd:PRK10263   413 EQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQA-EEQQSTFAPQSTYQ---TEQTYQQPAAQEPLYQQPQPVEQ 486
GGN pfam15685
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ...
857-1021 1.11e-03

Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the maturation of sperm and is expressed virtually only in the testis. It is found to be associated with the intracellular membrane, binds with GGNBP1 and may be involved in vesicular trafficking.


Pssm-ID: 434857 [Multi-domain]  Cd Length: 668  Bit Score: 43.60  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  857 PYGrGPVPPPSGYQQPPRFPGPPPPQNSSPATVNQTQGGSVSTPGYPPGqqPQPDYYRQEPPASPGYPPTSAPgtyPGKG 936
Cdd:pfam15685  389 PWG-SPPPPPGKAHPIPGPRRPAPALLAPPMFIFPAPTNGEPVRPGPPA--PQALLPRPPPPTPPATPPPVPP---PIPQ 462
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  937 MPPPQPRRHPdfakdqQAGPPQPAgyPGYGPQQRPMYPGPGWTGTPNAASNQYPRPGYPPGSQPpqnwSQGP-PRSMPPS 1015
Cdd:pfam15685  463 LPALQPMPLA------AARPPTPR--PCPGHGESALAPAPTAPLPPALAADQAPAPALAAAPAP----SPAPaPATADPL 530

                   ....*.
gi 1028725279 1016 HPGQPP 1021
Cdd:pfam15685  531 PPAPAP 536
PRK10263 PRK10263
DNA translocase FtsK; Provisional
899-1000 1.31e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.54  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  899 TPGYPPGQQPQpdyyrQEPPASPGYPPTSAPGTYPGKGMPPPQPrrhpdFAKDQQAGPPQP--AGYPGYGPQQRPMYPGP 976
Cdd:PRK10263   746 TPIVEPVQQPQ-----QPVAPQQQYQQPQQPVAPQPQYQQPQQP-----VAPQPQYQQPQQpvAPQPQYQQPQQPVAPQP 815
                           90       100
                   ....*....|....*....|....*.
gi 1028725279  977 GWTG--TPNAASNQYPRPGYPPGSQP 1000
Cdd:PRK10263   816 QYQQpqQPVAPQPQYQQPQQPVAPQP 841
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
785-1030 1.46e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.33  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  785 GQGGYSQQYPGGNEQYGQHYPPASTPVGYPSGPVRPPLYPPysndadrnyggsVPPPQGPPNTPQGPGNGQDPYGRGPVP 864
Cdd:PRK12323   367 QSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPA------------AAPAAAAAARAVAAAPARRSPAPEALA 434
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  865 PPSGYQQPprfpgppppqnsspatvnqtQGGSVSTPGYPPGQQPQPdyyRQEPPASPGYPPTSAPGTYPGKGMPPPQPRR 944
Cdd:PRK12323   435 AARQASAR--------------------GPGGAPAPAPAPAAAPAA---AARPAAAGPRPVAAAAAAAPARAAPAAAPAP 491
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  945 HPDFAKDQQAGPPQPAGYPGYgpQQRPMYPGPGWTGTPNAASNQYPRPGYPPGSQPPQNWSQGPPRSMPPSHPGQPPQWE 1024
Cdd:PRK12323   492 ADDDPPPWEELPPEFASPAPA--QPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRAS 569

                   ....*.
gi 1028725279 1025 QHRYPP 1030
Cdd:PRK12323   570 ASGLPD 575
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
722-922 1.49e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  722 ATSVPSPGSAGSNSQDSLPSAPTAPGPGhvDGYPGYGGYSGPQDYNSPQRPPHPPHGTQGSYQGQGGYSQQYPGGNEQYG 801
Cdd:PRK07764   597 GEGPPAPASSGPPEEAARPAAPAAPAAP--AAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAG 674
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  802 QHYPPASTPVGYPSGPVRPPLYPPYSNDADRNYGGSVPPPQGPPNTPQGPGNGQ---DPYGRGPVPPPSGyqqPPRFPGP 878
Cdd:PRK07764   675 GAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGAsapSPAADDPVPLPPE---PDDPPDP 751
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1028725279  879 PPPQNSSPA-TVNQTQGGSVSTPGYPPGQQPQPDYYRQEPPASPG 922
Cdd:PRK07764   752 AGAPAQPPPpPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDE 796
PRK13729 PRK13729
conjugal transfer pilus assembly protein TraB; Provisional
924-1001 1.74e-03

conjugal transfer pilus assembly protein TraB; Provisional


Pssm-ID: 184281 [Multi-domain]  Cd Length: 475  Bit Score: 42.89  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  924 PPTSAPGTYPGKGMPPPQPRRHPDFAKDQQAGPPQpagYPGYGPQQRPMYPGPGWTGTPNAASNQYPRPG--------YP 995
Cdd:PRK13729   127 PVTATGEPVPQMPASPPGPEGEPQPGNTPVSFPPQ---GSVAVPPPTAFYPGNGVTPPPQVTYQSVPVPNriqrktftYN 203

                   ....*.
gi 1028725279  996 PGSQPP 1001
Cdd:PRK13729   204 EGKKGP 209
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
805-1022 2.62e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 2.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  805 PPASTPVGYPSGPVRPPLYPPYSNDADRNYGGSVPPPQGPPNTPQGPGNGQDPYGRGPVPPP--SGYQQPPRFPGPPPPQ 882
Cdd:PHA03307    71 PPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPdlSEMLRPVGSPGPPPAA 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  883 NSSPATVNQTQGGSvSTPGYPPGQQPQPdyYRQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPDFAKDQQAGPPQPAGY 962
Cdd:PHA03307   151 SPPAAGASPAAVAS-DAASSRQAALPLS--SPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRS 227
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028725279  963 PGYGPQQRPM-YPGPGWTGTPNAASNQYPRPGYPPGSQPPQNWSQGPPRSMPPSHPGQPPQ 1022
Cdd:PHA03307   228 AADDAGASSSdSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSS 288
dnaA PRK14086
chromosomal replication initiator protein DnaA;
769-1002 3.00e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 42.12  E-value: 3.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  769 PQRPPHPPHGTQGSyQGQGGYSQQYPGgneqYGQHyPPASTPVGYPSGPVRPPLYPPYSNDADRnyggsvpppqgppntp 848
Cdd:PRK14086    95 PAPPPPHARRTSEP-ELPRPGRRPYEG----YGGP-RADDRPPGLPRQDQLPTARPAYPAYQQR---------------- 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  849 qgpgngQDPygrGPVPPPSgyqqpprfpgppppqnsSPATVNQTQGGSVSTPGYPPGQQPQPDYYRQEPPAS---PGYPP 925
Cdd:PRK14086   153 ------PEP---GAWPRAA-----------------DDYGWQQQRLGFPPRAPYASPASYAPEQERDREPYDagrPEYDQ 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  926 TSAPGTYPGKGMPPP------QPRRHPDFAKDQQAGPPQPAGYPGYGPQQRPMYPGPgwtgtPNAASNQYPRPGYPPGSQ 999
Cdd:PRK14086   207 RRRDYDHPRPDWDRPrrdrtdRPEPPPGAGHVHRGGPGPPERDDAPVVPIRPSAPGP-----LAAQPAPAPGPGEPTARL 281

                   ...
gi 1028725279 1000 PPQ 1002
Cdd:PRK14086   282 NPK 284
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
954-1091 3.06e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 3.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  954 AGPPQPAGYPGYGPQQRPMYPGPGWTGTPNAASNQYPRPGYPPGSQPPQNWS-QGPPRSMPPSHPGQPPQWEQHRYPPQG 1032
Cdd:PRK07764   589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASaAPAPGVAAPEHHPKHVAVPDASDGGDG 668
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1028725279 1033 QPYGAQQNHWGPMAQAQMRMPRHGYRPDGSKPYGPHGPMAPPPHMKAGMPGQPMFQGSS 1091
Cdd:PRK07764   669 WPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQG 727
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
770-1134 3.25e-03

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: 42.30  E-value: 3.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  770 QRPPHPPHGTQGSYQGQGGYSQQYPGGNEQYGQhyPPASTPVGYPSGPV--RPPLYPPYSNDADRNYGGSVPPPQGPPNT 847
Cdd:pfam09606  150 QPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQ--GQAGGMNGGQQGPMggQMPPQMGVPGMPGPADAGAQMGQQAQANG 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  848 PQGPGNGQDPYGRGPVP--PPSGYQQPPRFPGPPPPQNSSPATVNQTQG-GSVSTPGYPPGQQP-----------QPDYY 913
Cdd:pfam09606  228 GMNPQQMGGAPNQVAMQqqQPQQQGQQSQLGMGINQMQQMPQGVGGGAGqGGPGQPMGPPGQQPgampnvmsigdQNNYQ 307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  914 RQEPPASPGYPPTSAPGTYPGKGMPPPQPRR------HPDFAKDQQAGPPQPAGYPGYGPQQRPMYPGPgwTGTPNAASN 987
Cdd:pfam09606  308 QQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGqvvalgGLNHLETWNPGNFGGLGANPMQRGQPGMMSSP--SPVPGQQVR 385
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  988 QYPRPGYPPGSQPPQNWSQGPPRSMPP-SHPGQPPQweqhryPPQGQPYGAQQNHWGPmaqAQMRMPRHgyrpdgskpYG 1066
Cdd:pfam09606  386 QVTPNQFMRQSPQPSVPSPQGPGSQPPqSHPGGMIP------SPALIPSPSPQMSQQP---AQQRTIGQ---------DS 447
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028725279 1067 PHGPMAPPPHMKAGMPGQPmfqgsslmkREVIFPPDSIEAVTPILYKRRRMMR---HDVAPVDAWRLMMSL 1134
Cdd:pfam09606  448 PGGSLNTPGQSAVNSPLNP---------QEEQLYREKYRQLTKYIEPLKRMIAkmeNDPGDIDKMNKMKRL 509
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
905-1088 3.33e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 42.37  E-value: 3.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  905 GQQPQPDYYRQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPDFAKDQQAGPPqpagypgygpqqrpmyPGPGWTGTPNA 984
Cdd:PTZ00449   508 DEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKK----------------PGPAKEHKPSK 571
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  985 ASNQYPRPGYPPGSQPPQN--WSQGPPRSMPPSHPGQPPQweqhryPPQGQPYGAQQNHWGPMAQAQMRMPRHGYRPDG- 1061
Cdd:PTZ00449   572 IPTLSKKPEFPKDPKHPKDpeEPKKPKRPRSAQRPTRPKS------PKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSp 645
                          170       180
                   ....*....|....*....|....*..
gi 1028725279 1062 SKPYGPHGPMAPPPHMKAGMPGQPMFQ 1088
Cdd:PTZ00449   646 ERPEGPKIIKSPKPPKSPKPPFDPKFK 672
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
885-1022 5.91e-03

Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteriztic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.


Pssm-ID: 464609 [Multi-domain]  Cd Length: 325  Bit Score: 40.95  E-value: 5.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  885 SPATVNQTQGGSVSTPGYPPGQQPQPDYYRQEPPASPGYPPTSA-PGTYPGKGMPPPQPRRHPDFAKDQQAGPPQPAgyP 963
Cdd:pfam15279  142 PPKKGRRHRPGLHPPLGRPPGSPPMSMTPRGLLGKPQQHPPPSPlPAFMEPSSMPPPFLRPPPSIPQPNSPLSNPML--P 219
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028725279  964 GYGPQQRPMYP-GPGWTG------TPNAASNQYPRPGYPPGSQPPqnwsqGPPRSMPPSHPGQPPQ 1022
Cdd:pfam15279  220 GIGPPPKPPRNlGPPSNPmhrppfSPHHPPPPPTPPGPPPGLPPP-----PPRGFTPPFGPPFPPV 280
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
966-1085 7.11e-03

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 39.25  E-value: 7.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  966 GPQQRPMYPGPGWTGTPNAASNQYPRPGYPPGSQPPQNWSQGPPRSMPPSHPGQPPQWEQHRYPP---QGQPYGAQQNHW 1042
Cdd:pfam15240   34 EEEGQSQQGGQGPQGPPPGGFPPQPPASDDPPGPPPPGGPQQPPPQGGKQKPQGPPPQGGPRPPPgkpQGPPPQGGNQQQ 113
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1028725279 1043 GPMAQAQMRMPRHGYRPDGSKPYGPHGPMAPPPHMKAGMPGQP 1085
Cdd:pfam15240  114 GPPPPGKPQGPPPQGGGPPPQGGNQQGPPPPPPGNPQGPPQRP 156
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
884-1020 7.34e-03

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


Pssm-ID: 464961 [Multi-domain]  Cd Length: 272  Bit Score: 40.29  E-value: 7.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  884 SSPATVNQTQGGSVSTPGYPPGQQPQPDYYRQEPPASPGYPPTSAPGTYPGKGmpppqprrHPDFAKDQQAGPPQPAGYP 963
Cdd:pfam15991  142 SPPVQQQAYYKQPAFSPGYAEHGQQKHDDGRRGYDVARFGSWNKSTAQYPPSG--------QLFYPTHQYLPPPQTQGQA 213
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1028725279  964 GYGPQqrPMYPGPGWtGTPnaASNQYPRPGYPPGSQPPQNWSQGP-PRSMPPSHPGQP 1020
Cdd:pfam15991  214 DARLQ--TIYPQPGY-ALP--LQQQYEHANQPSPFVSSSPLKQMQsPKAGPGPQPMQL 266
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
939-1075 7.39e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 7.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  939 PPQPRRHPDFAKDQQAGPPQPagyPGYGPQQRPMYPGPGWTGTPNAASNQYPRPGYPPGSQPPQnwsQGPPRSMPPSHPG 1018
Cdd:PRK07764   379 ERLERRLGVAGGAGAPAAAAP---SAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAP---APPSPAGNAPAGG 452
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1028725279 1019 QPPQWEQHRYPPQGQPYGAQQNHWGPMAQAQmrmPRHGYRPDGSkPYGPHGPMAPPP 1075
Cdd:PRK07764   453 APSPPPAAAPSAQPAPAPAAAPEPTAAPAPA---PPAAPAPAAA-PAAPAAPAAPAG 505
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
769-976 8.25e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 8.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  769 PQRPPHPPHGTQGSYQGQGGYSQQYPGGNEQYGQhyPPASTPVGYPSGPVRPPLYPPYSNDADRNYGGSVPPPQGPPNTP 848
Cdd:PRK07764   590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAA--PAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  849 QGPGNGQDPYGRGPVPPPsgyqqpprfpGPPPPQNSSPATVNQTQGGSVSTPGYPPGQQPQPdyyrqePPASPGYPPTSA 928
Cdd:PRK07764   668 GWPAKAGGAAPAAPPPAP----------APAAPAAPAGAAPAQPAPAPAATPPAGQADDPAA------QPPQAAQGASAP 731
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1028725279  929 PGTYPGKGMPPPQPRRHPDFAKDQQAGPPQPAGYPGYGPQQRPMYPGP 976
Cdd:PRK07764   732 SPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPP 779
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
907-1032 9.21e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 9.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  907 QPQPDYYRQEPPASP-GYPPTSAPGTYPGKGMPPPQPRRHPDFAKDQQAGPPQPAGYPGYGPQQRPMYPGPGWTGTPNAA 985
Cdd:PHA03307   812 ASRTASKRKSRSHTPdGGSESSGPARPPGAAARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKA 891
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1028725279  986 SNQYPRPGYPPGSQPPQnwsqgPPRSMPPSHPGQPPQWEQHRYPPQG 1032
Cdd:PHA03307   892 AAAAPPAGAPAPRPRPA-----PRVKLGPMPPGGPDPRGGFRRVPPG 933
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
904-1091 9.61e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 40.43  E-value: 9.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  904 PGQQPQPDYYRQEPPASPGYPPTSAPGTYPGKGMPPPQPRRHPDfakDQQAGPPQPAGYPGYGPQqrpmypgpgwtGTPN 983
Cdd:COG5180    260 DAKERRRAAIGDTPAAEPPGLPVLEAGSEPQSDAPEAETARPID---VKGVASAPPATRPVRPPG-----------GARD 325
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028725279  984 AASNQYPRPGYPPGSQPPQNWSQGPprsmPPSHPgQPPQWEQHRYP-PQGQPYGAQQNHWGPMAQAQMRMPRHGYRPDGS 1062
Cdd:COG5180    326 PGTPRPGQPTERPAGVPEAASDAGQ----PPSAY-PPAEEAVPGKPlEQGAPRPGSSGGDGAPFQPPNGAPQPGLGRRGA 400
                          170       180       190
                   ....*....|....*....|....*....|
gi 1028725279 1063 KPYG-PHGPMAPPPHMKAGMPGQPMFQGSS 1091
Cdd:COG5180    401 PGPPmGAGDLVQAALDGGGRETASLGGAAG 430
 
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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