NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|119579215|gb|EAW58811|]
View 

SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2, isoform CRA_a [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
SNF2_N super family cl26465
SNF2 family N-terminal domain; This domain is found in proteins involved in a variety of ...
720-1202 7.46e-163

SNF2 family N-terminal domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1).


The actual alignment was detected with superfamily member PLN03142:

Pssm-ID: 331286  Cd Length: 1033  Bit Score: 524.75  E-value: 7.46e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  720 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSV 799
Cdd:PLN03142  166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  800 VKISYKGTPAMRRSLVPQ-LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvapr 875
Cdd:PLN03142  246 RAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  876 RILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGErvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 955
Cdd:PLN03142  322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  956 SQLPEKVEYVIKCDMSALQKILYRHMQAKGI-LLTDGSEKDKkgkggaktLMNTIMQLRKICNHPYMFQHIEESfaehlg 1034
Cdd:PLN03142  392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLNIAMQLRKCCNHPYLFQGAEPG------ 457
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1035 ysNGVINGAELYRASGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNE 1114
Cdd:PLN03142  458 --PPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNK 535
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1115 PGSQYFIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNV 1194
Cdd:PLN03142  536 PGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615

                  ....*...
gi 119579215 1195 DQKVIQAG 1202
Cdd:PLN03142  616 DALVIQQG 623
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1382-1506 1.31e-57

Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 is a global transcriptional activator, which cooperates with nuclear hormone receptors to boost transcriptional activation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


:

Pssm-ID: 99947  Cd Length: 107  Bit Score: 197.26  E-value: 1.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1382 KLTKQMNAIIDTVINYKDrcnvekvpsnsqleiegnSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKY 1461
Cdd:cd05516     1 ELTKKMNKIVDVVIKYKD------------------SDGRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKY 62
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 119579215 1462 RSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQKI 1506
Cdd:cd05516    63 RSLEDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFKSARQKI 107
HSA smart00573
domain in helicases and associated with SANT domains;
436-508 3.81e-23

domain in helicases and associated with SANT domains;


:

Pssm-ID: 214727  Cd Length: 73  Bit Score: 97.47  E-value: 3.81e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119579215    436 QKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQKKETERIEKERMRRLMA 508
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
1259-1326 2.12e-20

Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role in chromatin remodelling for yeast SWI/SNF. It binds histones. It is required for mobilising nucleosomes and lies within the catalytic subunit of the yeast SWI/SNF. It is found to be universally conserved.


:

Pssm-ID: 317068  Cd Length: 75  Bit Score: 89.26  E-value: 2.12e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119579215  1259 DRRREDARN-------PKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKIFGRGSRQRRDVDYSDALTEKQWL 1326
Cdd:pfam14619    1 ERRREEAAEwadgpngKPLPSRLMEESELPEWYLKDIDEEEKEEKEELDEQLYGRGKRARKEVSYSDGLTEEQWL 75
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
590-630 1.40e-13

BRK domain; The function of this domain is unknown. It is often found associated with helicases and transcription factors.


:

Pssm-ID: 311469  Cd Length: 41  Bit Score: 68.68  E-value: 1.40e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 119579215   590 MSDLPVKVTHTETGKVLFGPEAPKASQLDAWLEMNPGYEVA 630
Cdd:pfam07533    1 TGDERVPVINRKTGKKLTGDKAPKLKDLEEWLEENPGYEVD 41
QLQ pfam08880
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ...
173-207 2.83e-12

QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. This domain has thus been postulated to be involved in mediating protein interactions.


:

Pssm-ID: 312430  Cd Length: 35  Bit Score: 65.04  E-value: 2.83e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 119579215   173 PFSPVQLHQLRAQILAYKMLARGQPLPETLQLAVQ 207
Cdd:pfam08880    1 PFTPAQLQELRAQILAFKYLSRNQPVPPELQQAIF 35
Bromodomain super family cl02556
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
1333-1419 1.23e-10

Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.


The actual alignment was detected with superfamily member cd05494:

Pssm-ID: 321986  Cd Length: 114  Bit Score: 62.08  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1333 NLEEMEEEVRLKKRKRRrNVDKDPAKEDVEKAkkRRGRPPAEKLSPNPPKLTKQMNAIIDT-VINYKDRCNVEKVPSNSQ 1411
Cdd:cd05494     1 DYEALERVLRELKRHRR-NEDAWPFLEPVNPP--RRGAPDYRDVIKRPMSFGTKVNNIVETgARDLEDLQIVQEDPADKQ 77

                  ....*...
gi 119579215 1412 LEIEGNSS 1419
Cdd:cd05494    78 IDDEGRRS 85
SOBP super family cl25880
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
44-176 1.71e-05

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 characteristic 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.


The actual alignment was detected with superfamily member pfam15279:

Pssm-ID: 317654  Cd Length: 303  Bit Score: 48.62  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215    44 MGPSPGPPSVSHPMPTMGSTDFPQegMHQMHKPIdgihdkgivedihcgsmkGTGMRPPHPGMgPPQSPMDQHSqgyMSP 123
Cdd:pfam15279  185 MEGSSMPPPFLRPPPSIGNLQGPL--PNQSLPPI------------------GPPPKPPRTLG-PPSNPMHRPP---FSP 240
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 119579215   124 HPSPlgaPEHVSSPmsgggptPPQMPPSQPGALIPGDPQAMSQPNRGPSPFSP 176
Cdd:pfam15279  241 HPPP---PPTPSGN-------PPGLPPPHPRGFPPPFGPPLPPVVMVPPEMNF 283
EBV-NA3 super family cl27975
Epstein-Barr virus nuclear antigen 3 (EBNA-3); This family contains EBNA-3A, -3B, and -3C ...
66-382 5.09e-05

Epstein-Barr virus nuclear antigen 3 (EBNA-3); This family contains EBNA-3A, -3B, and -3C which are latent infection nuclear proteins important for Epstein-Barr virus (EBV)-induced B-cell immortalisation and the immune response to EBV infection.


The actual alignment was detected with superfamily member PHA03378:

Pssm-ID: 332796  Cd Length: 991  Bit Score: 47.75  E-value: 5.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   66 PQEGMHQMHKPIDGIHDKGIVEDIHCGSMKGTGMRPPHPGMGPPQspmdqhsqgyMSPHPSPLGAPEHVSSPMSGGGPTP 145
Cdd:PHA03378  529 PPQPRAGRRAPCVYTEDLDIESDEPASTEPVHDQLLPAPGLGPLQ----------IQPLTSPTTSQLASSAPSYAQTPWP 598
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  146 PQMPPSQPG-----ALIPgdpqAMSQPNRGPSPFSPVQLHQLRAQILAYKMLARGQP--LPETLQLAVQGKRTLPGLQQQ 218
Cdd:PHA03378  599 VPHPSQTPEppttqSHIP----ETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPTPhqPPQVEITPYKPTWTQIGHIPY 674
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  219 QQQQQQQQQQQQQQQQQQQQPQQQP--------PQPQTQQQQQPALVNYNRPSGPGPELSGPSTPQKLPVPAPGGRPSPA 290
Cdd:PHA03378  675 QPSPTGANTMLPIQWAPGTMQPPPRaptpmrppAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRA 754
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  291 PPAAAQPPAAAVPGPSVPQPAPGQP--SPVLQLQQKQSRISPIQKPQGLDPVEILQEREYRLQARIAHRI--QELENLPG 366
Cdd:PHA03378  755 RPPAAAPGRARPPAAAPGAPTPQPPpqAPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQIlrQLLTGGVK 834
                         330
                  ....*....|....*.
gi 119579215  367 SLPPDLRTKATVELKA 382
Cdd:PHA03378  835 RGRPSLKKPAALERQA 850
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
720-1202 7.46e-163

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601  Cd Length: 1033  Bit Score: 524.75  E-value: 7.46e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  720 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSV 799
Cdd:PLN03142  166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  800 VKISYKGTPAMRRSLVPQ-LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvapr 875
Cdd:PLN03142  246 RAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  876 RILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGErvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 955
Cdd:PLN03142  322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  956 SQLPEKVEYVIKCDMSALQKILYRHMQAKGI-LLTDGSEKDKkgkggaktLMNTIMQLRKICNHPYMFQHIEESfaehlg 1034
Cdd:PLN03142  392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLNIAMQLRKCCNHPYLFQGAEPG------ 457
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1035 ysNGVINGAELYRASGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNE 1114
Cdd:PLN03142  458 --PPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNK 535
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1115 PGSQYFIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNV 1194
Cdd:PLN03142  536 PGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615

                  ....*...
gi 119579215 1195 DQKVIQAG 1202
Cdd:PLN03142  616 DALVIQQG 623
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination and ...
708-1209 2.99e-110

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination and repair];


Pssm-ID: 223627  Cd Length: 866  Bit Score: 373.30  E-value: 2.99e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  708 ISERVEKQSALLINGTLKHYQLQGLEWMVS-LYNNNLNGILADEMGLGKTIQTIALITYLME-HKRLNGPYLIIVPLSTL 785
Cdd:COG0553   323 SEDLLNAPEPVDLSAELRPYQLEGVNWLSElLRSNLLGGILADDMGLGKTVQTIALLLSLLEsIKVYLGPALIVVPASLL 402
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  786 SNWTYEFDKWAPSVVKI-SYKGTP-------AMRRSLVPQLRSGKFNVLLTTYEYIIK---DKHILAKIRWKYMIVDEGH 854
Cdd:COG0553   403 SNWKREFEKFAPDLRLVlVYHGEKseldkkrEALRDLLKLHLVIIFDVVITTYELLRRflvDHGGLKKIEWDRVVLDEAH 482
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  855 RMKNHHCKLTQVLNtHYVAPRRILLTGTPLQNKLPELWALLN-FLLPTIFKSC-STFEQWFNAPfaMTGERVDLNEEETI 932
Cdd:COG0553   483 RIKNDQSSEGKALQ-FLKALNRLDLTGTPLENRLGELWSLLQeFLNPGLLGTSfAIFTRLFEKP--IQAEEDIGPLEARE 559
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  933 LIIRRLHKVLRPFLLRRLKKEVE--SQLPEKVEYVIKCDMSALQKILYRHMQAKGI-------LLTDGSEKDKKGKGGAK 1003
Cdd:COG0553   560 LGIELLRKLLSPFILRRTKEDVEvlKELPPKIEKVLECELSEEQRELYEALLEGAEknqqlleDLEKADSDENRIGDSEL 639
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1004 TLMNTIMQLRKICNHPYMFQHIEESFAEHLGYSNGV------INGAELYRASGKFELLDRILP---KLRATNHRVLLFCQ 1074
Cdd:COG0553   640 NILALLTRLRQICNHPALVDEGLEATFDRIVLLLREdkdfdyLKKPLIQLSKGKLQALDELLLdklLEEGHYHKVLIFSQ 719
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1075 MTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNEPgSQYFIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDL 1154
Cdd:COG0553   720 FTPVLDLLEDYLKALGIKYVRLDGSTPAKRRQELIDRFNAD-EEEKVFLLSLKAGGLGLNLTGADTVILFDPWWNPAVEL 798
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119579215 1155 QAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSS 1209
Cdd:COG0553   799 QAIDRAHRIGQKRPVKVYRLITRGTIEEKILELQEKKQELLDSLIDAEGEKELSK 853
SNF2_N pfam00176
SNF2 family N-terminal domain; This domain is found in proteins involved in a variety of ...
727-1022 8.12e-108

SNF2 family N-terminal domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1).


Pssm-ID: 306645  Cd Length: 305  Bit Score: 346.69  E-value: 8.12e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   727 YQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALIT---YLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 803
Cdd:pfam00176    1 YQIEGVNWMLSRENNQRGGILADEMGLGKTLQTISLLLtlkYLYHIKKLPGPTLIVVPLSLLDNWMNEFERWVPSLRLVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   804 YKGTPAMRRSL----VPQLRSGKFNVLLTTYEYIIKDKHI---LAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPRR 876
Cdd:pfam00176   81 LVGDGGSRMDKmnvrLLPKVLADYDVVITTYETLRRDKKNrslLKKLKWHRVILDEGHRLKNSKSKLSEALS-KLRTRNR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   877 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGervdlneeeTILIIRRLHKVLRPFLLRRLKKEVES 956
Cdd:pfam00176  160 WILTGTPIQNNLEELWALLNFLRPGPFGSLQTFDKWFVRPIERGG---------GEKGVARLHKLLKPFLLRRTKKDVEK 230
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119579215   957 QLPEKVEYVIKCDMSALQKILYRH------------MQAKGILLTDGSEKDKKGKGGaktLMNTIMQLRKICNHPYMF 1022
Cdd:pfam00176  231 SLPPKVEEILFCRLSKGQRKLYQTalqalrgngilkLLIRNRAATKFSSKSFRGKPG---LLNILLRLRKICNHPDLF 305
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1382-1506 1.31e-57

Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 is a global transcriptional activator, which cooperates with nuclear hormone receptors to boost transcriptional activation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99947  Cd Length: 107  Bit Score: 197.26  E-value: 1.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1382 KLTKQMNAIIDTVINYKDrcnvekvpsnsqleiegnSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKY 1461
Cdd:cd05516     1 ELTKKMNKIVDVVIKYKD------------------SDGRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKY 62
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 119579215 1462 RSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQKI 1506
Cdd:cd05516    63 RSLEDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFKSARQKI 107
DEXDc smart00487
DEAD-like helicases superfamily;
723-912 3.43e-30

DEAD-like helicases superfamily;


Pssm-ID: 214692  Cd Length: 201  Bit Score: 121.83  E-value: 3.43e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215    723 TLKHYQLQGLEWMvslYNNNLNGILADEMGLGKTIQ-TIALITYLMEHKrlNGPYLIIVPLSTL-SNWTYEFDKWAPS-V 799
Cdd:smart00487    8 PLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGK--GGRVLVLVPTRELaEQWAEELKKLGPSlG 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215    800 VKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKD--KHILAKIRWKYMIVDEGHRMKN--HHCKLTQVLNTHYVAPR 875
Cdd:smart00487   83 LKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKNVQ 162
                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 119579215    876 RILLTGTPLQNKLPELWALLN--FLLPTIFKSCSTFEQW 912
Cdd:smart00487  163 LLLLSATPPEEIENLLELFLNdpVFIDVGFTPLEPIEQF 201
BROMO smart00297
bromo domain;
1381-1506 2.15e-27

bromo domain;


Pssm-ID: 197636  Cd Length: 107  Bit Score: 110.45  E-value: 2.15e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   1381 PKLTKQMNAIIDTVINYKDRcnvekvpsnsqleiegnssgRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHK 1460
Cdd:smart00297    2 PKLQKKLQELLKAVLDKLDS--------------------HPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGK 61
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 119579215   1461 YRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQKI 1506
Cdd:smart00297   62 YSSVEEFVADFNLMFSNARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
HELICc cd00079
Helicase superfamily c-terminal domain; associated with DEXDc-, DEAD-, and DEAH-box proteins, ...
1040-1172 5.37e-27

Helicase superfamily c-terminal domain; associated with DEXDc-, DEAD-, and DEAH-box proteins, yeast initiation factor 4A, Ski2p, and Hepatitis C virus NS3 helicases; this domain is found in a wide variety of helicases and helicase related proteins; may not be an autonomously folding unit, but an integral part of the helicase; 4 helicase superfamilies at present according to the organization of their signature motifs; all helicases share the ability to unwind nucleic acid duplexes with a distinct directional polarity; they utilize the free energy from nucleoside triphosphate hydrolysis to fuel their translocation along DNA, unwinding the duplex in the process


Pssm-ID: 238034  Cd Length: 131  Bit Score: 110.41  E-value: 5.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1040 INGAELYRASGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNEPGsqy 1119
Cdd:cd00079     2 IKQYVLPVEDEKLEALLELLKEHLKKGGKVLIFCPSKKMLDELAELLRKPGIKVAALHGDGSQEEREEVLKDFREGE--- 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 119579215 1120 FIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVL 1172
Cdd:cd00079    79 IVVLVATDVIARGIDLPNVSVVINYDLPWSPSSYLQRIGRAGRAGQKGTAILL 131
HSA smart00573
domain in helicases and associated with SANT domains;
436-508 3.81e-23

domain in helicases and associated with SANT domains;


Pssm-ID: 214727  Cd Length: 73  Bit Score: 97.47  E-value: 3.81e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119579215    436 QKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQKKETERIEKERMRRLMA 508
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
HSA pfam07529
HSA; This domain is predicted to bind DNA and is often found associated with helicases.
437-507 4.19e-22

HSA; This domain is predicted to bind DNA and is often found associated with helicases.


Pssm-ID: 311466  Cd Length: 71  Bit Score: 94.14  E-value: 4.19e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119579215   437 KIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQKKETERIEKERMRRLM 507
Cdd:pfam07529    1 RQEPERREKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHQNIEKEEQKRIEREEKQRLQALK 71
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
1259-1326 2.12e-20

Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role in chromatin remodelling for yeast SWI/SNF. It binds histones. It is required for mobilising nucleosomes and lies within the catalytic subunit of the yeast SWI/SNF. It is found to be universally conserved.


Pssm-ID: 317068  Cd Length: 75  Bit Score: 89.26  E-value: 2.12e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119579215  1259 DRRREDARN-------PKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKIFGRGSRQRRDVDYSDALTEKQWL 1326
Cdd:pfam14619    1 ERRREEAAEwadgpngKPLPSRLMEESELPEWYLKDIDEEEKEEKEELDEQLYGRGKRARKEVSYSDGLTEEQWL 75
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1412-1492 2.51e-19

Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 306857  Cd Length: 84  Bit Score: 86.60  E-value: 2.51e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  1412 LEIEGNSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYED 1491
Cdd:pfam00439    2 LEILDKLMEHPLAAPFLEPVDPDEYPDYYSVIKRPMDLSTIKKKLENGEYKSLAEFEADVKLMFSNARTYNGPGSVIYKA 81

                   .
gi 119579215  1492 S 1492
Cdd:pfam00439   82 A 82
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1412-1501 4.04e-14

Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227408  Cd Length: 371  Bit Score: 76.00  E-value: 4.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1412 LEIEGNSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYED 1491
Cdd:COG5076   154 KKQLFLRDGRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVD 233
                          90
                  ....*....|
gi 119579215 1492 SIVLQSVFKS 1501
Cdd:COG5076   234 AKELEKYFLK 243
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
590-630 1.40e-13

BRK domain; The function of this domain is unknown. It is often found associated with helicases and transcription factors.


Pssm-ID: 311469  Cd Length: 41  Bit Score: 68.68  E-value: 1.40e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 119579215   590 MSDLPVKVTHTETGKVLFGPEAPKASQLDAWLEMNPGYEVA 630
Cdd:pfam07533    1 TGDERVPVINRKTGKKLTGDKAPKLKDLEEWLEENPGYEVD 41
BRK smart00592
domain in transcription and CHROMO domain helicases;
590-632 1.60e-13

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 68.91  E-value: 1.60e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 119579215    590 MSDLPVKVTHTETGKVLFGPEAPKASQLDAWLEMNPGYEVAPR 632
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPR 43
QLQ pfam08880
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ...
173-207 2.83e-12

QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. This domain has thus been postulated to be involved in mediating protein interactions.


Pssm-ID: 312430  Cd Length: 35  Bit Score: 65.04  E-value: 2.83e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 119579215   173 PFSPVQLHQLRAQILAYKMLARGQPLPETLQLAVQ 207
Cdd:pfam08880    1 PFTPAQLQELRAQILAFKYLSRNQPVPPELQQAIF 35
Bromodomain_1 cd05494
Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated ...
1333-1419 1.23e-10

Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.


Pssm-ID: 99926  Cd Length: 114  Bit Score: 62.08  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1333 NLEEMEEEVRLKKRKRRrNVDKDPAKEDVEKAkkRRGRPPAEKLSPNPPKLTKQMNAIIDT-VINYKDRCNVEKVPSNSQ 1411
Cdd:cd05494     1 DYEALERVLRELKRHRR-NEDAWPFLEPVNPP--RRGAPDYRDVIKRPMSFGTKVNNIVETgARDLEDLQIVQEDPADKQ 77

                  ....*...
gi 119579215 1412 LEIEGNSS 1419
Cdd:cd05494    78 IDDEGRRS 85
QLQ smart00951
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ...
172-206 4.62e-09

QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. QLQ has been postulated to be involved in mediating protein interactions.


Pssm-ID: 214931  Cd Length: 36  Bit Score: 55.62  E-value: 4.62e-09
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 119579215    172 SPFSPVQLHQLRAQILAYK-MLARGQPLPETLQLAV 206
Cdd:smart00951    1 SPFTPAQLELLRAQILAYKyLLARNQPVPPELLQAI 36
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
44-176 1.71e-05

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 characteristic 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: 317654  Cd Length: 303  Bit Score: 48.62  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215    44 MGPSPGPPSVSHPMPTMGSTDFPQegMHQMHKPIdgihdkgivedihcgsmkGTGMRPPHPGMgPPQSPMDQHSqgyMSP 123
Cdd:pfam15279  185 MEGSSMPPPFLRPPPSIGNLQGPL--PNQSLPPI------------------GPPPKPPRTLG-PPSNPMHRPP---FSP 240
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 119579215   124 HPSPlgaPEHVSSPmsgggptPPQMPPSQPGALIPGDPQAMSQPNRGPSPFSP 176
Cdd:pfam15279  241 HPPP---PPTPSGN-------PPGLPPPHPRGFPPPFGPPLPPVVMVPPEMNF 283
PHA03378 PHA03378
EBNA-3B; Provisional
66-382 5.09e-05

EBNA-3B; Provisional


Pssm-ID: 223065  Cd Length: 991  Bit Score: 47.75  E-value: 5.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   66 PQEGMHQMHKPIDGIHDKGIVEDIHCGSMKGTGMRPPHPGMGPPQspmdqhsqgyMSPHPSPLGAPEHVSSPMSGGGPTP 145
Cdd:PHA03378  529 PPQPRAGRRAPCVYTEDLDIESDEPASTEPVHDQLLPAPGLGPLQ----------IQPLTSPTTSQLASSAPSYAQTPWP 598
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  146 PQMPPSQPG-----ALIPgdpqAMSQPNRGPSPFSPVQLHQLRAQILAYKMLARGQP--LPETLQLAVQGKRTLPGLQQQ 218
Cdd:PHA03378  599 VPHPSQTPEppttqSHIP----ETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPTPhqPPQVEITPYKPTWTQIGHIPY 674
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  219 QQQQQQQQQQQQQQQQQQQQPQQQP--------PQPQTQQQQQPALVNYNRPSGPGPELSGPSTPQKLPVPAPGGRPSPA 290
Cdd:PHA03378  675 QPSPTGANTMLPIQWAPGTMQPPPRaptpmrppAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRA 754
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  291 PPAAAQPPAAAVPGPSVPQPAPGQP--SPVLQLQQKQSRISPIQKPQGLDPVEILQEREYRLQARIAHRI--QELENLPG 366
Cdd:PHA03378  755 RPPAAAPGRARPPAAAPGAPTPQPPpqAPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQIlrQLLTGGVK 834
                         330
                  ....*....|....*.
gi 119579215  367 SLPPDLRTKATVELKA 382
Cdd:PHA03378  835 RGRPSLKKPAALERQA 850
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
46-450 2.47e-04

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


Pssm-ID: 308660  Cd Length: 938  Bit Score: 45.86  E-value: 2.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215    46 PSPGPPSVSHPMPTMGSTDFPQEGM-HQMHKPIDGIHDkgivediHCGSMKGTGMRPPHPGMGPPQSPMDQHSQGYMSPH 124
Cdd:pfam03154  232 PNPDPPSIIAPQSAQRGPEGPPTPQpHSLQGPPSFPGP-------AQGPGQGQGQSPPPPSLYPPHPNQLQSHPPSQGPH 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   125 PSPLGAPEHVSSPmsgggPTPPQMPPSQPGALIPGDPQAMSQPNRGPSPFspVQLHQLRAQILAYKMLAR--------GQ 196
Cdd:pfam03154  305 PTHSFPPKPVPLP-----PPPASAPQIKPPPTTPIPSSHKHPPHLSASPF--PQMPSNLPPPPALKPLASlpsqhppcAQ 377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   197 PLPetLQLAVQGKRTLPglqqqqqqqqqqqqqqqqqqqqqqQPQQQPPQPQTQQQQQPALVNYNRPSGPGPELSGPSTPq 276
Cdd:pfam03154  378 PPP--LQLMPQPHQLQP------------------------PPAQPPVLTQSQSHQVKGHHASPPPTTAASHPSLSSTA- 430
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   277 klPVPapggrpspappaaaqppaaAVPGPSVPQPAPGQPSPvlqlqqkQSRISPIQKPQG--------LDPVEILQErey 348
Cdd:pfam03154  431 --PFP-------------------LSSASSVPGAVGPVPSP-------VPAMSGPQPSSSsalsvstvPPQLTIKEE--- 479
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   349 rlqariahRIQELENlPGSLPPDLR------TKATVELKALRLLNFQRQLRQEVVACMRRDTTLETALNSK-------AY 415
Cdd:pfam03154  480 --------PLDEEEE-CESPPPPRRspspepTIVNIASHASQSARFIKHLDRGYNSCARTDLYFTPLASSKlakkreeAA 550
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 119579215   416 KRSKRQTLREARMTEKLEKQQKIEQERKR-RQKHQE 450
Cdd:pfam03154  551 EKARREAEQSARQEREREREREREREREReREREAD 586
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
332-525 5.82e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009  Cd Length: 1164  Bit Score: 44.67  E-value: 5.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   332 QKPQGLDPVEILQEREYRLQARIAHRIQELENLpgslppdlrtkATVELKALRLLNFQRQLRQevvacmRRDTTLetALN 411
Cdd:TIGR02169  171 KKEKALEELEEVEENIERLDLIIDEKRQQLERL-----------RREREKAERYQALLKEKRE------YEGYEL--LKE 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   412 SKAYKRSKRQTLRE-ARMTEKLEK-QQKIEQERKRRQKHQEYLNSILQHAKD--------FKEYHRSVAGKIQKLSKAVA 481
Cdd:TIGR02169  232 KEALERQKEAIERQlASLEEELEKlTEEISELEKRLEEIEQLLEELNKKIKDlgeeeqlrVKEKIGELEAEIASLERSIA 311
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 119579215   482 TwhANTEREQKKETERIEKERMRRLMAEDEEGYRKLIDQKKDRR 525
Cdd:TIGR02169  312 E--KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD 353
PTZ00121 PTZ00121
MAEBL; Provisional
413-524 1.95e-03

MAEBL; Provisional


Pssm-ID: 173412  Cd Length: 2084  Bit Score: 42.82  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  413 KAYKRSKRQTLREARMTEKLEKQQKIEQERKRrqkhQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHAntEREQK 492
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKA----EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA--EEAKK 1614
                          90       100       110
                  ....*....|....*....|....*....|..
gi 119579215  493 KETERIEKERMRRlmaedEEGYRKLIDQKKDR 524
Cdd:PTZ00121 1615 AEEAKIKAEELKK-----AEEEKKKVEQLKKK 1641
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
98-199 2.45e-03

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891  Cd Length: 165  Bit Score: 40.16  E-value: 2.45e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215     98 GMRPPH--PGMGPPQSPMDQHSQGYMSPHPSPLGAPEHVSSPMsgggptPPQMPPSQPGALIPGDPQAMSQPNrgpspfS 175
Cdd:smart00818   51 TLQPHHhiPVLPAQQPVVPQQPLMPVPGQHSMTPTQHHQPNLP------QPAQQPFQPQPLQPPQPQQPMQPQ------P 118
                            90       100
                    ....*....|....*....|....
gi 119579215    176 PVQLHQLRAQILAYKMLARGQPLP 199
Cdd:smart00818  119 PVHPIPPLPPQPPLPPMFPMQPLP 142
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
720-1202 7.46e-163

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601  Cd Length: 1033  Bit Score: 524.75  E-value: 7.46e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  720 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSV 799
Cdd:PLN03142  166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  800 VKISYKGTPAMRRSLVPQ-LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvapr 875
Cdd:PLN03142  246 RAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  876 RILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGErvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 955
Cdd:PLN03142  322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  956 SQLPEKVEYVIKCDMSALQKILYRHMQAKGI-LLTDGSEKDKkgkggaktLMNTIMQLRKICNHPYMFQHIEESfaehlg 1034
Cdd:PLN03142  392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLNIAMQLRKCCNHPYLFQGAEPG------ 457
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1035 ysNGVINGAELYRASGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNE 1114
Cdd:PLN03142  458 --PPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNK 535
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1115 PGSQYFIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNV 1194
Cdd:PLN03142  536 PGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615

                  ....*...
gi 119579215 1195 DQKVIQAG 1202
Cdd:PLN03142  616 DALVIQQG 623
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination and ...
708-1209 2.99e-110

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination and repair];


Pssm-ID: 223627  Cd Length: 866  Bit Score: 373.30  E-value: 2.99e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  708 ISERVEKQSALLINGTLKHYQLQGLEWMVS-LYNNNLNGILADEMGLGKTIQTIALITYLME-HKRLNGPYLIIVPLSTL 785
Cdd:COG0553   323 SEDLLNAPEPVDLSAELRPYQLEGVNWLSElLRSNLLGGILADDMGLGKTVQTIALLLSLLEsIKVYLGPALIVVPASLL 402
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  786 SNWTYEFDKWAPSVVKI-SYKGTP-------AMRRSLVPQLRSGKFNVLLTTYEYIIK---DKHILAKIRWKYMIVDEGH 854
Cdd:COG0553   403 SNWKREFEKFAPDLRLVlVYHGEKseldkkrEALRDLLKLHLVIIFDVVITTYELLRRflvDHGGLKKIEWDRVVLDEAH 482
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  855 RMKNHHCKLTQVLNtHYVAPRRILLTGTPLQNKLPELWALLN-FLLPTIFKSC-STFEQWFNAPfaMTGERVDLNEEETI 932
Cdd:COG0553   483 RIKNDQSSEGKALQ-FLKALNRLDLTGTPLENRLGELWSLLQeFLNPGLLGTSfAIFTRLFEKP--IQAEEDIGPLEARE 559
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  933 LIIRRLHKVLRPFLLRRLKKEVE--SQLPEKVEYVIKCDMSALQKILYRHMQAKGI-------LLTDGSEKDKKGKGGAK 1003
Cdd:COG0553   560 LGIELLRKLLSPFILRRTKEDVEvlKELPPKIEKVLECELSEEQRELYEALLEGAEknqqlleDLEKADSDENRIGDSEL 639
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1004 TLMNTIMQLRKICNHPYMFQHIEESFAEHLGYSNGV------INGAELYRASGKFELLDRILP---KLRATNHRVLLFCQ 1074
Cdd:COG0553   640 NILALLTRLRQICNHPALVDEGLEATFDRIVLLLREdkdfdyLKKPLIQLSKGKLQALDELLLdklLEEGHYHKVLIFSQ 719
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1075 MTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNEPgSQYFIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDL 1154
Cdd:COG0553   720 FTPVLDLLEDYLKALGIKYVRLDGSTPAKRRQELIDRFNAD-EEEKVFLLSLKAGGLGLNLTGADTVILFDPWWNPAVEL 798
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119579215 1155 QAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSS 1209
Cdd:COG0553   799 QAIDRAHRIGQKRPVKVYRLITRGTIEEKILELQEKKQELLDSLIDAEGEKELSK 853
SNF2_N pfam00176
SNF2 family N-terminal domain; This domain is found in proteins involved in a variety of ...
727-1022 8.12e-108

SNF2 family N-terminal domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1).


Pssm-ID: 306645  Cd Length: 305  Bit Score: 346.69  E-value: 8.12e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   727 YQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALIT---YLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 803
Cdd:pfam00176    1 YQIEGVNWMLSRENNQRGGILADEMGLGKTLQTISLLLtlkYLYHIKKLPGPTLIVVPLSLLDNWMNEFERWVPSLRLVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   804 YKGTPAMRRSL----VPQLRSGKFNVLLTTYEYIIKDKHI---LAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPRR 876
Cdd:pfam00176   81 LVGDGGSRMDKmnvrLLPKVLADYDVVITTYETLRRDKKNrslLKKLKWHRVILDEGHRLKNSKSKLSEALS-KLRTRNR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   877 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGervdlneeeTILIIRRLHKVLRPFLLRRLKKEVES 956
Cdd:pfam00176  160 WILTGTPIQNNLEELWALLNFLRPGPFGSLQTFDKWFVRPIERGG---------GEKGVARLHKLLKPFLLRRTKKDVEK 230
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119579215   957 QLPEKVEYVIKCDMSALQKILYRH------------MQAKGILLTDGSEKDKKGKGGaktLMNTIMQLRKICNHPYMF 1022
Cdd:pfam00176  231 SLPPKVEEILFCRLSKGQRKLYQTalqalrgngilkLLIRNRAATKFSSKSFRGKPG---LLNILLRLRKICNHPDLF 305
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1382-1506 1.31e-57

Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 is a global transcriptional activator, which cooperates with nuclear hormone receptors to boost transcriptional activation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99947  Cd Length: 107  Bit Score: 197.26  E-value: 1.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1382 KLTKQMNAIIDTVINYKDrcnvekvpsnsqleiegnSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKY 1461
Cdd:cd05516     1 ELTKKMNKIVDVVIKYKD------------------SDGRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKY 62
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 119579215 1462 RSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQKI 1506
Cdd:cd05516    63 RSLEDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFKSARQKI 107
DEXDc smart00487
DEAD-like helicases superfamily;
723-912 3.43e-30

DEAD-like helicases superfamily;


Pssm-ID: 214692  Cd Length: 201  Bit Score: 121.83  E-value: 3.43e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215    723 TLKHYQLQGLEWMvslYNNNLNGILADEMGLGKTIQ-TIALITYLMEHKrlNGPYLIIVPLSTL-SNWTYEFDKWAPS-V 799
Cdd:smart00487    8 PLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGK--GGRVLVLVPTRELaEQWAEELKKLGPSlG 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215    800 VKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKD--KHILAKIRWKYMIVDEGHRMKN--HHCKLTQVLNTHYVAPR 875
Cdd:smart00487   83 LKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKNVQ 162
                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 119579215    876 RILLTGTPLQNKLPELWALLN--FLLPTIFKSCSTFEQW 912
Cdd:smart00487  163 LLLLSATPPEEIENLLELFLNdpVFIDVGFTPLEPIEQF 201
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
1383-1504 2.26e-28

Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99946  Cd Length: 105  Bit Score: 113.55  E-value: 2.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1383 LTKQMNAIIDTVINYKDrcnvekvpsnsqleiegnSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYR 1462
Cdd:cd05515     1 MQQKLWELYNAVKNYTD------------------GRGRRLSLIFMRLPSKSEYPDYYDVIKKPIDMEKIRSKIEGNQYQ 62
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 119579215 1463 SLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQ 1504
Cdd:cd05515    63 SLDDMVSDFVLMFDNACKYNEPDSQIYKDALTLQKVLLETKR 104
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1050-1164 1.13e-27

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 306726  Cd Length: 110  Bit Score: 111.53  E-value: 1.13e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  1050 GKFELLDRILpKLRATNHRVLLFCQMTSlmTIMEDYFAFR-NFLYLRLDGTTKSEDRAALLKKFNEPGsqyFIFLLSTRA 1128
Cdd:pfam00271    1 EKLEALLELL-KKKERGGKVLIFSQTKK--RLEAELLLEKeGIKVARLHGDLSQEEREEILEDFRNGK---IDVLVATDV 74
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 119579215  1129 GGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIG 1164
Cdd:pfam00271   75 AGRGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 110
BROMO smart00297
bromo domain;
1381-1506 2.15e-27

bromo domain;


Pssm-ID: 197636  Cd Length: 107  Bit Score: 110.45  E-value: 2.15e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   1381 PKLTKQMNAIIDTVINYKDRcnvekvpsnsqleiegnssgRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHK 1460
Cdd:smart00297    2 PKLQKKLQELLKAVLDKLDS--------------------HPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGK 61
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 119579215   1461 YRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQKI 1506
Cdd:smart00297   62 YSSVEEFVADFNLMFSNARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
HELICc cd00079
Helicase superfamily c-terminal domain; associated with DEXDc-, DEAD-, and DEAH-box proteins, ...
1040-1172 5.37e-27

Helicase superfamily c-terminal domain; associated with DEXDc-, DEAD-, and DEAH-box proteins, yeast initiation factor 4A, Ski2p, and Hepatitis C virus NS3 helicases; this domain is found in a wide variety of helicases and helicase related proteins; may not be an autonomously folding unit, but an integral part of the helicase; 4 helicase superfamilies at present according to the organization of their signature motifs; all helicases share the ability to unwind nucleic acid duplexes with a distinct directional polarity; they utilize the free energy from nucleoside triphosphate hydrolysis to fuel their translocation along DNA, unwinding the duplex in the process


Pssm-ID: 238034  Cd Length: 131  Bit Score: 110.41  E-value: 5.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1040 INGAELYRASGKFELLDRILPKLRATNHRVLLFCQMTSLMTIMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNEPGsqy 1119
Cdd:cd00079     2 IKQYVLPVEDEKLEALLELLKEHLKKGGKVLIFCPSKKMLDELAELLRKPGIKVAALHGDGSQEEREEVLKDFREGE--- 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 119579215 1120 FIFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVL 1172
Cdd:cd00079    79 IVVLVATDVIARGIDLPNVSVVINYDLPWSPSSYLQRIGRAGRAGQKGTAILL 131
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
1383-1500 6.88e-26

Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in transcriptional activation, it is the catalytic component of the SWI/SNF ATP-dependent chromatin remodeling complex. The protein is essential for the regulation of gene expression (both positive and negative) of a large number of genes. The SWI/SNF complex changes chromatin structure by altering DNA-histone contacts within the nucleosome, which results in a re-positioning of the nucleosome and facilitates or represses the binding of gene-specific transcription factors. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99950  Cd Length: 103  Bit Score: 106.27  E-value: 6.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1383 LTKQMNAIIDTVINYKDrcnvekvpsnsqleiegnSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYR 1462
Cdd:cd05519     1 LKAAMLEIYDAVLNCED------------------ETGRKLSELFLEKPSKKLYPDYYVIIKRPIALDQIKRRIEGRAYK 62
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 119579215 1463 SLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFK 1500
Cdd:cd05519    63 SLEEFLEDFHLMFANARTYNQEGSIVYEDAVEMEKAFK 100
DEXDc cd00046
DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or ...
744-883 9.26e-26

DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 238005  Cd Length: 144  Bit Score: 107.04  E-value: 9.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  744 NGILADEMGLGKTIQTIALITYLMEHKRlNGPYLIIVPLSTLSNWTYEFDKWAPSV---VKISYKGTPAMRRslvPQLRS 820
Cdd:cd00046     2 DVLLAAPTGSGKTLAALLPILELLDSLK-GGQVLVLAPTRELANQVAERLKELFGEgikVGYLIGGTSIKQQ---EKLLS 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119579215  821 GKFNVLLTTYEYIIKDKHILA--KIRWKYMIVDEGHRMKNHHCKLTQ--VLNTHYVAPRRILLTGTP 883
Cdd:cd00046    78 GKTDIVVGTPGRLLDELERLKlsLKKLDLLILDEAHRLLNQGFGLLGlkILLKLPKDRQVLLLSATP 144
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
1421-1501 8.76e-25

Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.


Pssm-ID: 99922  Cd Length: 99  Bit Score: 102.84  E-value: 8.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1421 RQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFK 1500
Cdd:cd04369    17 RDLSEPFLEPVDPKEAPDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYNGPGSPIYKDAKKLEKLFE 96

                  .
gi 119579215 1501 S 1501
Cdd:cd04369    97 K 97
HSA smart00573
domain in helicases and associated with SANT domains;
436-508 3.81e-23

domain in helicases and associated with SANT domains;


Pssm-ID: 214727  Cd Length: 73  Bit Score: 97.47  E-value: 3.81e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119579215    436 QKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQKKETERIEKERMRRLMA 508
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
1417-1503 7.44e-23

Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99948  Cd Length: 103  Bit Score: 97.51  E-value: 7.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1417 NSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQ 1496
Cdd:cd05517    17 DPSGRLISELFQKLPSKVLYPDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFNEPGSQVYKDANAIK 96

                  ....*..
gi 119579215 1497 SVFKSAR 1503
Cdd:cd05517    97 KIFTAKK 103
HSA pfam07529
HSA; This domain is predicted to bind DNA and is often found associated with helicases.
437-507 4.19e-22

HSA; This domain is predicted to bind DNA and is often found associated with helicases.


Pssm-ID: 311466  Cd Length: 71  Bit Score: 94.14  E-value: 4.19e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119579215   437 KIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQKKETERIEKERMRRLM 507
Cdd:pfam07529    1 RQEPERREKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHQNIEKEEQKRIEREEKQRLQALK 71
HELICc smart00490
helicase superfamily c-terminal domain;
1081-1164 6.12e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757  Cd Length: 82  Bit Score: 91.12  E-value: 6.12e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   1081 IMEDYFAFRNFLYLRLDGTTKSEDRAALLKKFNEPGSQyfiFLLSTRAGGLGLNLQAADTVVIFDSDWNPHQDLQAQDRA 1160
Cdd:smart00490    2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 119579215   1161 HRIG 1164
Cdd:smart00490   79 GRAG 82
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
1419-1503 1.29e-20

Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99949  Cd Length: 103  Bit Score: 90.97  E-value: 1.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1419 SGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSV 1498
Cdd:cd05518    19 SGRRLCDLFMEKPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHYNEEGSQVYEDANILEKV 98

                  ....*
gi 119579215 1499 FKSAR 1503
Cdd:cd05518    99 LKEKR 103
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
1417-1506 1.39e-20

Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99954  Cd Length: 113  Bit Score: 91.24  E-value: 1.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1417 NSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQ 1496
Cdd:cd05524    19 SEDGRILCESFIRVPKRRNEPEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDSPEHKDACKLW 98
                          90
                  ....*....|
gi 119579215 1497 SVFKSARQKI 1506
Cdd:cd05524    99 ELFLSARNEV 108
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
1259-1326 2.12e-20

Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role in chromatin remodelling for yeast SWI/SNF. It binds histones. It is required for mobilising nucleosomes and lies within the catalytic subunit of the yeast SWI/SNF. It is found to be universally conserved.


Pssm-ID: 317068  Cd Length: 75  Bit Score: 89.26  E-value: 2.12e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119579215  1259 DRRREDARN-------PKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKIFGRGSRQRRDVDYSDALTEKQWL 1326
Cdd:pfam14619    1 ERRREEAAEwadgpngKPLPSRLMEESELPEWYLKDIDEEEKEEKEELDEQLYGRGKRARKEVSYSDGLTEEQWL 75
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
1417-1501 2.77e-20

Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99951  Cd Length: 103  Bit Score: 90.09  E-value: 2.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1417 NSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQ 1496
Cdd:cd05520    17 NNQGQLLAEPFLKLPSKRKYPDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIYKDAEKLQ 96

                  ....*
gi 119579215 1497 SVFKS 1501
Cdd:cd05520    97 KLMQA 101
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1412-1492 2.51e-19

Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 306857  Cd Length: 84  Bit Score: 86.60  E-value: 2.51e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  1412 LEIEGNSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYED 1491
Cdd:pfam00439    2 LEILDKLMEHPLAAPFLEPVDPDEYPDYYSVIKRPMDLSTIKKKLENGEYKSLAEFEADVKLMFSNARTYNGPGSVIYKA 81

                   .
gi 119579215  1492 S 1492
Cdd:pfam00439   82 A 82
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1417-1499 9.83e-15

Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are components of the RSC complex (remodeling the structure of chromatin), are essential for transcriptional control, and have a specific domain architecture including two bromodomains. The RSC complex has also been linked to homologous recombination and nonhomologous end-joining repair of DNA double strand breaks. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99953  Cd Length: 104  Bit Score: 73.81  E-value: 9.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1417 NSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQ 1496
Cdd:cd05522    18 DENGRLLTLHFEKLPDKAREPEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYNENDSQEYKDAVLLE 97

                  ...
gi 119579215 1497 SVF 1499
Cdd:cd05522    98 KEA 100
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1412-1501 4.04e-14

Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227408  Cd Length: 371  Bit Score: 76.00  E-value: 4.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1412 LEIEGNSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYED 1491
Cdd:COG5076   154 KKQLFLRDGRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVD 233
                          90
                  ....*....|
gi 119579215 1492 SIVLQSVFKS 1501
Cdd:COG5076   234 AKELEKYFLK 243
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
590-630 1.40e-13

BRK domain; The function of this domain is unknown. It is often found associated with helicases and transcription factors.


Pssm-ID: 311469  Cd Length: 41  Bit Score: 68.68  E-value: 1.40e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 119579215   590 MSDLPVKVTHTETGKVLFGPEAPKASQLDAWLEMNPGYEVA 630
Cdd:pfam07533    1 TGDERVPVINRKTGKKLTGDKAPKLKDLEEWLEENPGYEVD 41
BRK smart00592
domain in transcription and CHROMO domain helicases;
590-632 1.60e-13

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 68.91  E-value: 1.60e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 119579215    590 MSDLPVKVTHTETGKVLFGPEAPKASQLDAWLEMNPGYEVAPR 632
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPR 43
Bromo_Rsc1_2_I cd05521
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1417-1497 1.04e-12

Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are components of the RSC complex (remodeling the structure of chromatin), are essential for transcriptional control, and have a specific domain architecture including two bromodomains. The RSC complex has also been linked to homologous recombination and nonhomologous end-joining repair of DNA double strand breaks. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99952  Cd Length: 106  Bit Score: 68.12  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1417 NSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNhkYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQ 1496
Cdd:cd05521    18 EENGIEIHPIFNVLPLRKDYPDYYKIIKNPLSLNTVKKRLPH--YTNAQEFVNDLAQIPWNARLYNTKGSVIYKYALILE 95

                  .
gi 119579215 1497 S 1497
Cdd:cd05521    96 K 96
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
1427-1508 1.25e-12

Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was identified as a novel human bromodomain gene by cDNA library screening. The Drosophila homologue, Acf1, is part of the CHRAC (chromatin accessibility complex) and regulates ISWI-induced nucleosome remodeling. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99936  Cd Length: 115  Bit Score: 67.81  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1427 FIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQKI 1506
Cdd:cd05504    33 FLRPVSKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVFSNCFLYNPEHTSVYKAGTRLQRFFIKRCRKL 112

                  ..
gi 119579215 1507 AK 1508
Cdd:cd05504   113 GL 114
QLQ pfam08880
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ...
173-207 2.83e-12

QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. This domain has thus been postulated to be involved in mediating protein interactions.


Pssm-ID: 312430  Cd Length: 35  Bit Score: 65.04  E-value: 2.83e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 119579215   173 PFSPVQLHQLRAQILAYKMLARGQPLPETLQLAVQ 207
Cdd:pfam08880    1 PFTPAQLQELRAQILAFKYLSRNQPVPPELQQAIF 35
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
1427-1506 3.33e-12

Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates acetylation of histones at lysine residues; such acetylation is generally correlated with the activation of transcription. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99941  Cd Length: 101  Bit Score: 66.42  E-value: 3.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1427 FIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQKI 1506
Cdd:cd05509    22 FLEPVDKEEAPDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYNGPDTEYYKCANKLEKFFWKKLKEL 101
Bromodomain_1 cd05494
Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated ...
1333-1419 1.23e-10

Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.


Pssm-ID: 99926  Cd Length: 114  Bit Score: 62.08  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1333 NLEEMEEEVRLKKRKRRrNVDKDPAKEDVEKAkkRRGRPPAEKLSPNPPKLTKQMNAIIDT-VINYKDRCNVEKVPSNSQ 1411
Cdd:cd05494     1 DYEALERVLRELKRHRR-NEDAWPFLEPVNPP--RRGAPDYRDVIKRPMSFGTKVNNIVETgARDLEDLQIVQEDPADKQ 77

                  ....*...
gi 119579215 1412 LEIEGNSS 1419
Cdd:cd05494    78 IDDEGRRS 85
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
1431-1501 1.87e-10

Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast transcription factors involved in the expression of a wide range of genes, including snRNAs; they are required for sporulation and DNA repair and protect histone H4 from deacetylation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99931  Cd Length: 102  Bit Score: 61.15  E-value: 1.87e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119579215 1431 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKS 1501
Cdd:cd05499    30 PVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVFND 100
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
1435-1482 1.84e-09

Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. The structure(2DKW) in this alignment is an uncharacterized protein predicted from analysis of cDNA clones from human fetal liver


Pssm-ID: 99957  Cd Length: 112  Bit Score: 58.52  E-value: 1.84e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 119579215 1435 ELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFN 1482
Cdd:cd05528    32 EVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYN 79
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1430-1488 2.86e-09

Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome critical region-2 of chromosome 21. It encodes for a nuclear protein containing WD40 repeats and two bromodomains, which may function as a transcriptional regulator involved in chromatin remodeling and play a role in embryonic development. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99958  Cd Length: 128  Bit Score: 58.12  E-value: 2.86e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119579215 1430 LPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQI 1488
Cdd:cd05529    52 VDLRAWYPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILSNAETFNEPNSEI 110
QLQ smart00951
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ...
172-206 4.62e-09

QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. QLQ has been postulated to be involved in mediating protein interactions.


Pssm-ID: 214931  Cd Length: 36  Bit Score: 55.62  E-value: 4.62e-09
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 119579215    172 SPFSPVQLHQLRAQILAYK-MLARGQPLPETLQLAV 206
Cdd:smart00951    1 SPFTPAQLELLRAQILAYKyLLARNQPVPPELLQAI 36
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
1382-1504 7.05e-09

Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the trithorax-group in Drosophila melanogaster, an epigenetic transcriptional regulator of HOX genes. Drosophila ASH1 has been shown to methylate specific lysines in histones H3 and H4. Mammalian ASH1 has been shown to methylate histone H3. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99955  Cd Length: 106  Bit Score: 56.63  E-value: 7.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1382 KLTKQMNAIIDTVINYKDrcnvekvpsnsqleiegnSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKY 1461
Cdd:cd05525     2 RLAQVLKEICDAIITYKD------------------SNGQSLAIPFINLPSKKKNPDYYERITDPVDLSTIEKQILTGYY 63
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 119579215 1462 RSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQ 1504
Cdd:cd05525    64 KTPEAFDSDMLKVFRNAEKYYGRKSPIGRDVCRLRKAYYQAKH 106
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
1434-1501 7.15e-09

Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B (BAZ2B) were identified as a novel human bromodomain gene by cDNA library screening. BAZ2A is also known as Tip5 (Transcription termination factor I-interacting protein 5) and hWALp3. The proteins may play roles in transcriptional regulation. Human Tip5 is part of a complex termed NoRC (nucleolar remodeling complex), which induces nucleosome sliding and may play a role in the regulation of the rDNA locus. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99935  Cd Length: 97  Bit Score: 56.23  E-value: 7.15e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119579215 1434 KELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKS 1501
Cdd:cd05503    28 KLVPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEVGRAGHNMRKFFEK 95
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
1421-1506 4.50e-08

Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of the tripartite motif (TRIM) protein family, which is characterized by a particular domain architecture. It functions by recruiting coactivators and/or corepressors to modulate transcription. Vertebrate Tif1-gamma, also labeled E3 ubiquitin-protein ligase TRIM33, plays a role in the control of hematopoiesis. Its homologue in Xenopus laevis, Ectodermin, has been shown to function in germ-layer specification and control of cell growth during embryogenesis. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99934  Cd Length: 109  Bit Score: 54.22  E-value: 4.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1421 RQLSEVFIQLPSR-------KELPEYYELIRKPVDFKKIKERIR----NHkYRSLGDLEKDVMLLCHNAQTFNLEGSQIY 1489
Cdd:cd05502    11 RLLLELYCHELSLpfhepvsPSVPNYYKIIKTPMDLSLIRKKLQpkspQH-YSSPEEFVADVRLMFKNCYKFNEEDSEVA 89
                          90
                  ....*....|....*..
gi 119579215 1490 EDSIVLQSVFKSARQKI 1506
Cdd:cd05502    90 QAGKELELFFEEQLKEI 106
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
1437-1482 8.16e-08

Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown to inhibit cell growth and the progression of the cell cycle by regulating cell-cycle genes at the transcriptional level. BRD7 has been identified as a gene involved in nasopharyngeal carcinoma. The protein interacts with acetylated histone H3 via its bromodomain. Bromodomains are 110 amino acid long domains that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99945  Cd Length: 98  Bit Score: 53.18  E-value: 8.16e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 119579215 1437 PEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFN 1482
Cdd:cd05513    32 PGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYN 77
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
1434-1507 9.19e-08

Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, a large multi-domain complex, which initiates the assembly of the transcription machinery. TAFII250 contains two bromodomains that specifically bind to acetylated histone H4. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99943  Cd Length: 112  Bit Score: 53.42  E-value: 9.19e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119579215 1434 KELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIyedSIVLQSVFKSARQKIA 1507
Cdd:cd05511    28 KKVPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSVY---TKKAKEMLELAEELLA 98
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
1431-1500 9.38e-08

Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET subfamily of bromodomain proteins; the first bromodomain in Brdt has been shown to be essential for male germ cell differentiation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99930  Cd Length: 102  Bit Score: 53.05  E-value: 9.38e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1431 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFK 1500
Cdd:cd05498    30 PEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHPVHAMARKLQDVFE 99
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
1425-1482 4.55e-07

Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein assumed to be a transcriptional regulator. BRD1 has been implicated with brain development and susceptibility to schizophrenia and bipolar affective disorder. Bromodomains are 110 amino acid long domains that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99944  Cd Length: 98  Bit Score: 50.86  E-value: 4.55e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 119579215 1425 EVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFN 1482
Cdd:cd05512    20 EIFSEPVDLSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYN 77
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
1435-1507 5.35e-07

Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET subfamily of bromodomain proteins; the first bromodomain in Brdt has been shown to be essential for male germ cell differentiation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99929  Cd Length: 107  Bit Score: 50.88  E-value: 5.35e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119579215 1435 ELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGsqiyeDSIVL--QSVFKSARQKIA 1507
Cdd:cd05497    36 NLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKPG-----DDVVLmaQTLEKLFLQKLA 105
ResIII pfam04851
Type III restriction enzyme, res subunit;
723-883 8.39e-07

Type III restriction enzyme, res subunit;


Pssm-ID: 309815  Cd Length: 162  Bit Score: 50.75  E-value: 8.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   723 TLKHYQLQGLE-WMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEhKRLNGPYLIIVP-LSTLSNWTYEFDKWAPSVV 800
Cdd:pfam04851    3 ELRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFK-KGPIKKVLFLVPrKDLLEQALEEFKKFLPNYV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   801 KIS--YKGtpamrRSLVPQLRSGKfnVLLTTYEYIIKD----KHILAKIRWKYMIVDEGHRM--KNHhcklTQVLNtHYV 872
Cdd:pfam04851   82 EIGeiISG-----DKKDESVDDNK--IVVTTIQSLYKAlelaSLELLPDFFDVIIIDEAHRSgaSSY----RNILE-YFK 149
                          170
                   ....*....|.
gi 119579215   873 APRRILLTGTP 883
Cdd:pfam04851  150 PAFLLGLTATP 160
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
1431-1501 2.12e-06

Bromodomain, uncharacterized subfamily specific to plants. Might function as a global transcription factor. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99938  Cd Length: 99  Bit Score: 48.87  E-value: 2.12e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119579215 1431 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKS 1501
Cdd:cd05506    27 VVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTMAKELLKIFET 97
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1431-1501 2.36e-06

Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase acting on histone, which gives a specific tag for transcriptional activation and also acetylates non-histone proteins. CREBBP binds specifically to phosphorylated CREB protein and augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99927  Cd Length: 108  Bit Score: 48.98  E-value: 2.36e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119579215 1431 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKS 1501
Cdd:cd05495    31 PKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWLYNRKTSRVYKYCTKLAEVFEQ 101
Bromo_WDR9_II cd05496
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1424-1508 4.03e-06

Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome critical region-2 of chromosome 21. It encodes for a nuclear protein containing WD40 repeats and two bromodomains, which may function as a transcriptional regulator involved in chromatin remodeling and play a role in embryonic development. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99928  Cd Length: 119  Bit Score: 48.22  E-value: 4.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1424 SEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNL-EGSQIYEDSIVLQSVFKSA 1502
Cdd:cd05496    23 SEPFRQPVDLLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYTPnKRSRIYSMTLRLSALFEEH 102

                  ....*.
gi 119579215 1503 RQKIAK 1508
Cdd:cd05496   103 IKKIIS 108
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
1431-1499 5.02e-06

Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast transcription factors involved in the expression of a wide range of genes, including snRNAs; they are required for sporulation and DNA repair and protect histone H4 from deacetylation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99932  Cd Length: 103  Bit Score: 47.69  E-value: 5.02e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119579215 1431 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVF 1499
Cdd:cd05500    31 PVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQMGKRLQAAF 99
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
1424-1482 1.45e-05

Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with the thyroid hormone receptor in a ligand-dependent fashion and enhances thyroid hormone-dependent activation from thyroid response elements. Brd8 is thought to be a nuclear receptor coactivator. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99939  Cd Length: 104  Bit Score: 46.20  E-value: 1.45e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1424 SEVFIQ-LPSRKElPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFN 1482
Cdd:cd05507    21 ASVFLKpVTEDIA-PGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYN 79
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
44-176 1.71e-05

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 characteristic 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: 317654  Cd Length: 303  Bit Score: 48.62  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215    44 MGPSPGPPSVSHPMPTMGSTDFPQegMHQMHKPIdgihdkgivedihcgsmkGTGMRPPHPGMgPPQSPMDQHSqgyMSP 123
Cdd:pfam15279  185 MEGSSMPPPFLRPPPSIGNLQGPL--PNQSLPPI------------------GPPPKPPRTLG-PPSNPMHRPP---FSP 240
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 119579215   124 HPSPlgaPEHVSSPmsgggptPPQMPPSQPGALIPGDPQAMSQPNRGPSPFSP 176
Cdd:pfam15279  241 HPPP---PPTPSGN-------PPGLPPPHPRGFPPPFGPPLPPVVMVPPEMNF 283
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
752-883 2.82e-05

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 306725  Cd Length: 165  Bit Score: 46.08  E-value: 2.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   752 GLGKTIqtIALITYL-MEHKRLNGPY-LIIVPLSTLSNWTYE-FDKWAPSV---VKISYKGTPamRRSLVPQLRSGkfNV 825
Cdd:pfam00270   24 GSGKTL--AFLLPALeALDKLDGGPQaLVLAPTRELAEQIYEeLKKLGKPLglkVASLLGGDS--RKEQLEKLKGP--DI 97
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119579215   826 LLTTYE---YIIKDKHILAKIrwKYMIVDEGHRM--KNHHCKLTQVLNTHYVAPRRILLTGTP 883
Cdd:pfam00270   98 LVGTPGrllDLLQERKLLKNL--KLLVLDEAHRLldMGFGPDLEEILRRLPKKRQILLLSATL 158
DUF4207 pfam13904
Domain of unknown function (DUF4207); This family is found in eukaryotes; it has several ...
413-522 3.51e-05

Domain of unknown function (DUF4207); This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 316426  Cd Length: 250  Bit Score: 47.05  E-value: 3.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   413 KAYKRSKRQTLREARMTEKLEKQQKIEQ-------------ERKRRQKHQEYLNSILQHAKdfKEYHRSVAGKIQKLSKA 479
Cdd:pfam13904   90 LAAKRRQRQQKLLAEKREREEREQEAAErkrlakekyqewlQRKARQQKKKREQSHKQKAA--EKASSSLSSSVRNVSKE 167
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 119579215   480 VATWHANtEREQKK---ETERIEKERMRRLMAEDEEGYRKLIDQKK 522
Cdd:pfam13904  168 EIKRRLQ-EWELKKleqQQRKREEEQREQLKKEEEEQERKQLAEKA 212
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
1424-1482 3.59e-05

Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA, and SLIK. SAGA is involved in the RNA polymerase II-dependent transcriptional regulation of about 10% of all yeast genes. The SPT7 bromodomain has been shown to weakly interact with acetylated histone H3, but not H4. The human representative of this subfamily is cat eye syndrome critical region protein 2 (CECR2). Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99942  Cd Length: 112  Bit Score: 45.12  E-value: 3.59e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119579215 1424 SEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFN 1482
Cdd:cd05510    26 STPFLTKVSKREAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLYN 84
Bromo_polybromo_VI cd05526
Bromodomain, polybromo repeat VI. Polybromo is a nuclear protein of unknown function, which ...
1418-1508 3.99e-05

Bromodomain, polybromo repeat VI. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99956  Cd Length: 110  Bit Score: 45.05  E-value: 3.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1418 SSGRQLSEVFIQLPSRKELPEyyELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQS 1497
Cdd:cd05526    21 EEGRCYSDSLAELPELAVDGV--GPKKIPLTLDIIKRNVDKGRYRRLDKFQEDMFEVLERARRLSRTDSEIYEDAVELQQ 98
                          90
                  ....*....|.
gi 119579215 1498 VFKSARQKIAK 1508
Cdd:cd05526    99 FFIKIRDELCK 109
PHA03378 PHA03378
EBNA-3B; Provisional
66-382 5.09e-05

EBNA-3B; Provisional


Pssm-ID: 223065  Cd Length: 991  Bit Score: 47.75  E-value: 5.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   66 PQEGMHQMHKPIDGIHDKGIVEDIHCGSMKGTGMRPPHPGMGPPQspmdqhsqgyMSPHPSPLGAPEHVSSPMSGGGPTP 145
Cdd:PHA03378  529 PPQPRAGRRAPCVYTEDLDIESDEPASTEPVHDQLLPAPGLGPLQ----------IQPLTSPTTSQLASSAPSYAQTPWP 598
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  146 PQMPPSQPG-----ALIPgdpqAMSQPNRGPSPFSPVQLHQLRAQILAYKMLARGQP--LPETLQLAVQGKRTLPGLQQQ 218
Cdd:PHA03378  599 VPHPSQTPEppttqSHIP----ETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPTPhqPPQVEITPYKPTWTQIGHIPY 674
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  219 QQQQQQQQQQQQQQQQQQQQPQQQP--------PQPQTQQQQQPALVNYNRPSGPGPELSGPSTPQKLPVPAPGGRPSPA 290
Cdd:PHA03378  675 QPSPTGANTMLPIQWAPGTMQPPPRaptpmrppAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRA 754
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  291 PPAAAQPPAAAVPGPSVPQPAPGQP--SPVLQLQQKQSRISPIQKPQGLDPVEILQEREYRLQARIAHRI--QELENLPG 366
Cdd:PHA03378  755 RPPAAAPGRARPPAAAPGAPTPQPPpqAPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQIlrQLLTGGVK 834
                         330
                  ....*....|....*.
gi 119579215  367 SLPPDLRTKATVELKA 382
Cdd:PHA03378  835 RGRPSLKKPAALERQA 850
MISS pfam15822
MAPK-interacting and spindle-stabilizing protein-like; MISS is a family of eukaryotic ...
45-162 6.04e-05

MAPK-interacting and spindle-stabilizing protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilizing protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.


Pssm-ID: 318115  Cd Length: 238  Bit Score: 46.13  E-value: 6.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215    45 GPSPGPPSVSHPMPTM---GST-DFPQEGMH--QMHKPIDGIHDKGIVEDIHC-GSMK----GTGM-----------RP- 101
Cdd:pfam15822   88 GPSCPPPGGPYPAPTVpgpGPIgPYPTPNMPfpELPRPYGAPTDPAAAAPSGPwGSMSsgpwAPGMggqypapnmpyPSp 167
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119579215   102 -PHPGMGPPQSP----------MDQHSQGYMSPHPSPLGapehvSSPMSGGGPTPP---QMPPSQPGA-LIPGDPQ 162
Cdd:pfam15822  168 gPYPAVPPPQSPgaappvpwgtVPPGPWGPPAPYPDPTG-----SYPMPGLYPTPNnpfQVPSGPSGApPMPGGPH 238
Pro-rich pfam15240
Proline-rich; This family includes several eukaryotic proline-rich proteins.
100-181 6.57e-05

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


Pssm-ID: 291893  Cd Length: 160  Bit Score: 44.98  E-value: 6.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   100 RPPHPGM-----GPPQSPMDQHS--QGYMSPHPSPLGAPEHVSSPMSGGGPtPPQMPPSQPGALIPGDPQAMSQPNRGPS 172
Cdd:pfam15240   47 GPPPGGFppqppGPPPQGGPQQPppQGGNPQGPPPQGGPQRPPGPGNQQGP-PPQGGNQQQRPPPPGKPQGPPPQGGGPP 125

                   ....*....
gi 119579215   173 PFSPVQLHQ 181
Cdd:pfam15240  126 PPQGGNQQG 134
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
320-527 1.06e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227278  Cd Length: 420  Bit Score: 46.25  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  320 QLQQKQSRISPIQKP--QGLDPVEILQEREYRLQARIAHRIQELENLPGSLPPDLRTKATVELKALRLLNFQRQL---RQ 394
Cdd:COG4942    81 QLIETADDLKKLRKQiaDLNARLNALEVQEREQRRRLAEQLAALQRSGRNPPPALLVSPEDAQRSVRLAIYYGALnpaRA 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  395 EVVACMRRDTTLETALNSKAykRSKRQTLREArMTEKLEKQQKIEQERKRRQKHQEYLNS-ILQHAKDFKEyhrsVAGKI 473
Cdd:COG4942   161 ERIDALKATLKQLAAVRAEI--AAEQAELTTL-LSEQRAQQAKLAQLLEERKKTLAQLNSeLSADQKKLEE----LRANE 233
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119579215  474 QKLSKAVATWHANTEREQKKEtERIEKERMRRLMAEDE-EGYRKLIDQKKDRRLA 527
Cdd:COG4942   234 SRLKNEIASAEAAAAKAREAA-AAAEAAAARARAAEAKrTGETYKPTAPEKMLIS 287
Forkhead_N pfam08430
Forkhead N-terminal region; The region described in this family is found towards the ...
40-174 1.19e-04

Forkhead N-terminal region; The region described in this family is found towards the N-terminus of various eukaryotic forkhead/HNF-3-related transcription factors (which contain the pfam00250 domain). These proteins play key roles in embryogenesis, maintenance of differentiated cell states, and tumorigenesis.


Pssm-ID: 312062  Cd Length: 139  Bit Score: 43.87  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215    40 VHSMMGPSPGPPSVSHPMPTMGSTDFPQEGMHQMhkpidgihdkgivedihcGSMKGTGMRPPHPGMGPPQSPMDQHSqg 119
Cdd:pfam08430   21 MNSMNTYMPMNTMSTSTSSMNMSGYAGPGAMNGM------------------SSSSMNGMSPGYGGAGSPMGMMGMSS-- 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 119579215   120 yMSPHPSPLG--APEHVSSPMSgGGPTPPQMPPSQPgalIPGDPQAMSQPNRGPSPF 174
Cdd:pfam08430   81 -MGTSLSPSGtmGAMGPQPAGS-MGSLSPNQSMSRA---SNQYGQSNLNRARDPKTY 132
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
389-523 1.20e-04

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 318010  Cd Length: 520  Bit Score: 46.53  E-value: 1.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   389 QRQLRQEVvacMRRDTTLETALNSKAYKRSKRQTLREARMTEklEKQQKIEQERKRRQKhqeyLNSILQHAKDFKEYHRS 468
Cdd:pfam15709  358 QRRLQQEQ---LERAEKMKEELELEQQRRAEEIRLRKQRLEE--EQQRQEEEERKQRLQ----LQAAQERARQQQEEFRR 428
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 119579215   469 VAGKIQKLSKAVATWHANTEREQKKETERIEKERMRRLMAEDEEGYRKLIDQKKD 523
Cdd:pfam15709  429 KLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQE 483
Bromo_ZMYND11 cd05492
Bromodomain; ZMYND11_like sub-family. ZMYND11 or BS69 is a ubiquitously expressed nuclear ...
1436-1490 2.17e-04

Bromodomain; ZMYND11_like sub-family. ZMYND11 or BS69 is a ubiquitously expressed nuclear protein that has been shown to associate with chromatin. It interacts with chromatin remodeling factors and might play a role in chromatin remodeling and gene expression. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99924  Cd Length: 109  Bit Score: 42.75  E-value: 2.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119579215 1436 LPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYE 1490
Cdd:cd05492    36 LPKRRRLIHTHLDVADIQEKINSEKYTSLEEFKADALLLLHNTAIFHGADSEQYD 90
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
46-450 2.47e-04

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


Pssm-ID: 308660  Cd Length: 938  Bit Score: 45.86  E-value: 2.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215    46 PSPGPPSVSHPMPTMGSTDFPQEGM-HQMHKPIDGIHDkgivediHCGSMKGTGMRPPHPGMGPPQSPMDQHSQGYMSPH 124
Cdd:pfam03154  232 PNPDPPSIIAPQSAQRGPEGPPTPQpHSLQGPPSFPGP-------AQGPGQGQGQSPPPPSLYPPHPNQLQSHPPSQGPH 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   125 PSPLGAPEHVSSPmsgggPTPPQMPPSQPGALIPGDPQAMSQPNRGPSPFspVQLHQLRAQILAYKMLAR--------GQ 196
Cdd:pfam03154  305 PTHSFPPKPVPLP-----PPPASAPQIKPPPTTPIPSSHKHPPHLSASPF--PQMPSNLPPPPALKPLASlpsqhppcAQ 377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   197 PLPetLQLAVQGKRTLPglqqqqqqqqqqqqqqqqqqqqqqQPQQQPPQPQTQQQQQPALVNYNRPSGPGPELSGPSTPq 276
Cdd:pfam03154  378 PPP--LQLMPQPHQLQP------------------------PPAQPPVLTQSQSHQVKGHHASPPPTTAASHPSLSSTA- 430
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   277 klPVPapggrpspappaaaqppaaAVPGPSVPQPAPGQPSPvlqlqqkQSRISPIQKPQG--------LDPVEILQErey 348
Cdd:pfam03154  431 --PFP-------------------LSSASSVPGAVGPVPSP-------VPAMSGPQPSSSsalsvstvPPQLTIKEE--- 479
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   349 rlqariahRIQELENlPGSLPPDLR------TKATVELKALRLLNFQRQLRQEVVACMRRDTTLETALNSK-------AY 415
Cdd:pfam03154  480 --------PLDEEEE-CESPPPPRRspspepTIVNIASHASQSARFIKHLDRGYNSCARTDLYFTPLASSKlakkreeAA 550
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 119579215   416 KRSKRQTLREARMTEKLEKQQKIEQERKR-RQKHQE 450
Cdd:pfam03154  551 EKARREAEQSARQEREREREREREREREReREREAD 586
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
1424-1488 2.48e-04

Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The Williams-Beuren syndrome deletion transcript 9 is a putative transcriptional regulator. WSTF was found to play a role in vitamin D-mediated transcription as part of two chromatin remodeling complexes, WINAC and WICH. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99937  Cd Length: 97  Bit Score: 42.52  E-value: 2.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119579215 1424 SEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQI 1488
Cdd:cd05505    18 SWPFREPVTADEAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAEKYYENGSYV 82
Cytadhesin_P30 pfam07271
Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 ...
40-177 2.63e-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.


Pssm-ID: 284643  Cd Length: 308  Bit Score: 44.84  E-value: 2.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215    40 VHSMMGPSPGPPSVSHPmPTMGSTDfPQEGMHQMHKPIDGIHDKGIVEDIHCGSM---KGTGMRPPHPGMGPPQSpmdqh 116
Cdd:pfam07271  142 AHAEAETEPAGQNVANN-PQMGINQ-PQININFGPNPQQRINPQCFGFPMQPGQMamrPGFNQMPPHMGGAPPNQ----- 214
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119579215   117 sqgyMSPHPSPLGAPehvssPMSGGGPTPPQMPPSQPGALIPgDPQAMSQPNRGPSPFSPV 177
Cdd:pfam07271  215 ----MGMRPGFNQMP-----PQMGGMAPRPGFPNHMPGMNAP-RPGFPPQPGMAPRGGMPM 265
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination and repair];
721-987 3.11e-04

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination and repair];


Pssm-ID: 223989  Cd Length: 442  Bit Score: 44.74  E-value: 3.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  721 NGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALItylmehKRLNGPYLIIVPLSTL-SNWTYEFDKW--AP 797
Cdd:COG1061    34 EFELRPYQEEALDALVKNRRTERRGVIVLPTGAGKTVVAAEAI------AELKRSTLVLVPTKELlDQWAEALKKFllLN 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  798 SVVKISYKGTPAMRrslvpqlrsgKFNVLLTTYEYIIKDKHILAKI--RWKYMIVDEGHRMKNHhcKLTQVLNtHYVAPR 875
Cdd:COG1061   108 DEIGIYGGGEKELE----------PAKVTVATVQTLARRQLLDEFLgnEFGLIIFDEVHHLPAP--SYRRILE-LLSAAY 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  876 RIL-LTGTP---LQNKLPELWALLNFLLPTIFKScSTFEQWFNAPFAMTGERVDLNEEEtILIIRRLHKVLRPFLLRRLK 951
Cdd:COG1061   175 PRLgLTATPereDGGRIGDLFDLIGPIVYEVSLK-ELIDEGYLAPYKYVEIKVTLTEDE-EREYAKESARFRELLRARGT 252
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 119579215  952 KEVESQLpEKVEYVIKCDMSALQKILYRHMQAKGIL 987
Cdd:COG1061   253 LRAENEA-RRIAIASERKIAAVRGLLLKHARGDKTL 287
Pro-rich pfam15240
Proline-rich; This family includes several eukaryotic proline-rich proteins.
45-178 3.71e-04

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


Pssm-ID: 291893  Cd Length: 160  Bit Score: 42.67  E-value: 3.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215    45 GPSPGPPSVSHPMPtmgstdfPQEGMHQmHKPIDGIHDKGivedihcGSMKGTGMRPPHPGmgPPQSPMDQhsQGYMSPH 124
Cdd:pfam15240   47 GPPPGGFPPQPPGP-------PPQGGPQ-QPPPQGGNPQG-------PPPQGGPQRPPGPG--NQQGPPPQ--GGNQQQR 107
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 119579215   125 PSPLGAPEhvSSPMSGGGPTPPQM-PPSQPGALIPGDPQAMSQPNRGPSPFSPVQ 178
Cdd:pfam15240  108 PPPPGKPQ--GPPPQGGGPPPPQGgNQQGPPPPPPGNPQGPPRPPQPGNPQGPPQ 160
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
332-525 5.82e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009  Cd Length: 1164  Bit Score: 44.67  E-value: 5.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   332 QKPQGLDPVEILQEREYRLQARIAHRIQELENLpgslppdlrtkATVELKALRLLNFQRQLRQevvacmRRDTTLetALN 411
Cdd:TIGR02169  171 KKEKALEELEEVEENIERLDLIIDEKRQQLERL-----------RREREKAERYQALLKEKRE------YEGYEL--LKE 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   412 SKAYKRSKRQTLRE-ARMTEKLEK-QQKIEQERKRRQKHQEYLNSILQHAKD--------FKEYHRSVAGKIQKLSKAVA 481
Cdd:TIGR02169  232 KEALERQKEAIERQlASLEEELEKlTEEISELEKRLEEIEQLLEELNKKIKDlgeeeqlrVKEKIGELEAEIASLERSIA 311
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 119579215   482 TwhANTEREQKKETERIEKERMRRLMAEDEEGYRKLIDQKKDRR 525
Cdd:TIGR02169  312 E--KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD 353
Cytadhesin_P30 pfam07271
Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 ...
44-154 9.71e-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.


Pssm-ID: 284643  Cd Length: 308  Bit Score: 42.91  E-value: 9.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215    44 MGPSPGPPSVShpmPTMGSTDFPQEGM----HQMHKPIDGIHDKGIVEDIHCGSMKGTGMRPPHPGMGP-PQSPMDQHSQ 118
Cdd:pfam07271  194 MAMRPGFNQMP---PHMGGAPPNQMGMrpgfNQMPPQMGGMAPRPGFPNHMPGMNAPRPGFPPQPGMAPrGGMPMGNKAG 270
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 119579215   119 GYMsPHPSPLGAPEHVSSPMSGGGPTPPQMPPSQPG 154
Cdd:pfam07271  271 GGF-NHPGTPMAPNRMGFPNQPGMAPPPGMAGPRAG 305
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
1011-1201 1.09e-03

Class II histone deacetylase complex subunits 2 and 3; This family of class II histone deacetylase complex subunits HDA2 and HDA3 is found in fungi, The member from S. pombe is referred to as Ccq1 (coiled-coil quantitatively-enriched protein 1). These proteins associate with HDA1 to generate the activity of the HDA1 histone deacetylase complex. HDA1 interacts with itself and with the HDA2-HDA3 subcomplex to form a probable tetramer and these interactions are necessary for catalytic activity. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. HDA2 and HDA3 have a conserved coiled-coil domain towards their C-terminus.


Pssm-ID: 314413  Cd Length: 279  Bit Score: 42.70  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  1011 QLRKICNHPYMF-QHIEES------FAEHLGYSngvingaelyraSGKFELLDRILPKL----RATNHRVLLFCQMTSLM 1079
Cdd:pfam11496   57 NLSLVATHPYLLiDHYMPKslllkdEPEKLAET------------SGKFLVLNDLINLLierdRKRPINVAIVARSVKTL 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  1080 TIMEDYFAFRNFLYLRLDGTTKSEDRAAllKKFNEPGSQYFIFLLSTRA---GGLGLNLQAADTVVIFDSDWNPHQDLQA 1156
Cdd:pfam11496  125 DLVEALLLGKGLSYKRYSGEMLKGENKE--VPDLKISSTVIHLLSTTGQltnDYSLLENYKFDLIIAFDSSVDTSSPSIE 202
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 119579215  1157 QDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVD--QKVIQA 1201
Cdd:pfam11496  203 HLRTQNRRQGNLAPIIRLVPINSIEHVELCFPKPRDSPDylEKVIAA 249
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
341-537 1.43e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 316391  Cd Length: 352  Bit Score: 42.58  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   341 EILQEREyRLQARIAHRIQELENlpgslppdlrTKAtvELKALRLlnfqrQLRQEVVACMRRDTTLETALNskayKRSKR 420
Cdd:pfam13868  177 EIEEEKE-REIARLRAQQEKAQD----------EKA--ERDELRA-----KLYQEEAERKWRQKEKEEAEK----KARQR 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   421 QTLREARMTEKLEKQQKIEQERKRRQkhQEYLNSILQHAKDFKEYHRSVAGKIQKLSKavatwHAN------TEREQKKE 494
Cdd:pfam13868  235 EELKQAREEQIELKERRLAEEAEREE--EEFERMLRKQAEDERIEQEEAEKRREKRLE-----HRRelekqiEERERQRE 307
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 119579215   495 TERIEKERMRRLMAEDEEGYRKLIDQKKDRRLAYLLQQTDEYV 537
Cdd:pfam13868  308 AEREEEFEEGEALREEEAERRERIEEERQKKLKEHLRELLGGL 350
Bromo_RACK7 cd05508
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ...
1424-1506 1.44e-03

Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) was identified as a potential tumor suppressor genes, it shares domain architecture with BS69/ZMYND11; both have been implicated in the regulation of cellular proliferation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99940  Cd Length: 99  Bit Score: 40.06  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215 1424 SEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSivlQSVFKSAR 1503
Cdd:cd05508    20 AEPFLKPVDLEQFPDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWILHNAIIYNGGDHKLTQAA---KAIVKICE 96

                  ...
gi 119579215 1504 QKI 1506
Cdd:cd05508    97 QEM 99
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
344-541 1.45e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705  Cd Length: 1042  Bit Score: 43.03  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   344 QEREYRLQARIAHRIQELENLPGSLPpDLRTKATVELKALRLLNFQRQlrQEVVACMRRDTTLETAlnskAYKRSKRQTL 423
Cdd:TIGR00618  721 NEIENASSSLGSDLAAREDALNQSLK-ELMHQARTVLKARTEAHFNNN--EEVTAALQTGAELSHL----AAEIQFFNRL 793
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   424 REARMTEKLEKQQKIEQERKrrQKHQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHANTEREQKKETERIEKERM 503
Cdd:TIGR00618  794 REEDTHLLKTLEAEIGQEIP--SDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKI 871
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 119579215   504 RRLMaEDEEGYRKLIDQKKDRRLAYLLQQTDEYVANLT 541
Cdd:TIGR00618  872 IQLS-DKLNGINQIKIQFDGDALIKFLHEITLYANVRL 908
PTZ00121 PTZ00121
MAEBL; Provisional
413-524 1.95e-03

MAEBL; Provisional


Pssm-ID: 173412  Cd Length: 2084  Bit Score: 42.82  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  413 KAYKRSKRQTLREARMTEKLEKQQKIEQERKRrqkhQEYLNSILQHAKDFKEYHRSVAGKIQKLSKAVATWHAntEREQK 492
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKA----EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA--EEAKK 1614
                          90       100       110
                  ....*....|....*....|....*....|..
gi 119579215  493 KETERIEKERMRRlmaedEEGYRKLIDQKKDR 524
Cdd:PTZ00121 1615 AEEAKIKAEELKK-----AEEEKKKVEQLKKK 1641
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
352-548 2.07e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009  Cd Length: 1164  Bit Score: 42.75  E-value: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   352 ARIAHRIQELENLPGSLPPDLR----------------TKATVEL--KALRLLNFQRQLRQEVVACMRRDTTLETALnsk 413
Cdd:TIGR02169  677 QRLRERLEGLKRELSSLQSELRrienrldelsqelsdaSRKIGEIekEIEQLEQEEEKLKERLEELEEDLSSLEQEI--- 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   414 AYKRSKRQTLRE--ARMTEKLEKQQKIEQERKRRQKHQEyLNSILQHAKDFKEYHRSVAGKIQKLSKAVatwHANTEREQ 491
Cdd:TIGR02169  754 ENVKSELKELEAriEELEEDLHKLEEALNDLEARLSHSR-IPEIQAELSKLEEEVSRIEARLREIEQKL---NRLTLEKE 829
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 119579215   492 KKETERIEKERMRRLMAEDEEGYRKLIDQKKdRRLAYLLQQTDEYVANLTNLVWEHK 548
Cdd:TIGR02169  830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLN-GKKEELEEELEELEAALRDLESRLG 885
PRK09401 PRK09401
reverse gyrase; Reviewed
752-851 2.07e-03

reverse gyrase; Reviewed


Pssm-ID: 236498  Cd Length: 1176  Bit Score: 42.61  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  752 GLGKTIQTIALITYLmehKRLNGPYLIIVPLSTLSNWTYE-----FDKWAPSVVKISYKG--TPAMRRSLVPQLRSGKFN 824
Cdd:PRK09401  105 GVGKTTFGLVMSLYL---AKKGKKSYIIFPTRLLVEQVVEklekfGEKVGCGVKILYYHSslKKKEKEEFLERLKEGDFD 181
                          90       100
                  ....*....|....*....|....*..
gi 119579215  825 VLLTTYEYIIKDKHILAKIRWKYMIVD 851
Cdd:PRK09401  182 ILVTTSQFLSKNFDELPKKKFDFVFVD 208
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
98-199 2.45e-03

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891  Cd Length: 165  Bit Score: 40.16  E-value: 2.45e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215     98 GMRPPH--PGMGPPQSPMDQHSQGYMSPHPSPLGAPEHVSSPMsgggptPPQMPPSQPGALIPGDPQAMSQPNrgpspfS 175
Cdd:smart00818   51 TLQPHHhiPVLPAQQPVVPQQPLMPVPGQHSMTPTQHHQPNLP------QPAQQPFQPQPLQPPQPQQPMQPQ------P 118
                            90       100
                    ....*....|....*....|....
gi 119579215    176 PVQLHQLRAQILAYKMLARGQPLP 199
Cdd:smart00818  119 PVHPIPPLPPQPPLPPMFPMQPLP 142
DUF1720 pfam08226
Domain of unknown function (DUF1720); This domain is found in different combinations with ...
96-167 2.76e-03

Domain of unknown function (DUF1720); This domain is found in different combinations with cortical patch components EF hand, SH3 and ENTH and is therefore likely to be involved in cytoskeletal processes. This family contains many hypothetical proteins.


Pssm-ID: 311924  Cd Length: 76  Bit Score: 38.98  E-value: 2.76e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119579215    96 GTGMRPPHPGM-GPPQSPMDQHSQGYMSPHPSPLGAPEHvsspMSGGGPTPPQMPPSQPGALIPGDPQAMSQP 167
Cdd:pfam08226    5 QTGFMPPQQQQpQQTQQPLQPQPTGFMPQQQTGQGLQPQ----PTGFGGQVQPLQPQQTGFQPQAQQGLQPQA 73
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
46-174 3.08e-03

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 283903  Cd Length: 152  Bit Score: 39.88  E-value: 3.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215    46 PSPGPPSVSHPMPTMGSTDFPQEgmhqmhKPIDGIhdkgivedihcgsmkgTGMRPPHP-----GMGPPQSPMDQHSQgy 120
Cdd:pfam06346   45 PLPGGTSIPPPPPLPGGTSIPPP------PPLPGS----------------TGIPPPPPlpggaGIPPPPPPLPGGAG-- 100
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 119579215   121 MSPHPSPLGapehvsspmsgGGPTPPQMPPSQPGALIPGDPQAMSQPNrgPSPF 174
Cdd:pfam06346  101 IPPPPPPLP-----------GGPGIPPPPPFPGGPGIPPPPPGMGMPP--PPPF 141
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
67-203 3.12e-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  Cd Length: 732  Bit Score: 41.92  E-value: 3.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215    67 QEGMHQMHKPIDGIHDKGIVEDihcgsmkgTGMRP-PHPGMGPPQSPMDQHSQGYMS-PHPSPLGAPEHvsSPMSGGGPT 144
Cdd:pfam09606  369 QPGMMSSPSPVPGQQVRQVTPN--------QFMRQsPQPSVPSPQGPGSQPPQSHPGgMIPSPALIPSP--SPQMSQQPA 438
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 119579215   145 PPQMPPSQPGALIPGDPQAMSqpnrGPSPFSPVQLHQLRAQilaYKMLargQPLPETLQ 203
Cdd:pfam09606  439 QQRTIGQDSPGGSLNTPGQSA----VNSPLNPQEEQLYREK---YRQL---TKYIEPLK 487
FliJ pfam02050
Flagellar FliJ protein;
420-538 3.39e-03

Flagellar FliJ protein;


Pssm-ID: 307944  Cd Length: 123  Bit Score: 39.19  E-value: 3.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   420 RQTLREARmTEKLEKQQKIEQERKRRQKHQEYLNSILQH--AKDFKEYHR---SVAGKIQKLSKAVATWHANTEREQKKE 494
Cdd:pfam02050    4 ARQLAEAQ-RELQQAEEQLEELEQYRQEYQQQLSGSGQGlsAAELRNYQAfisQLDEAIAQQQQELAQAEQQVEQAREEW 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 119579215   495 TE-RIEKERMRRLMAEDEEGYRKLIDqKKDRRlayllqQTDEYVA 538
Cdd:pfam02050   83 QEaRQERKKLEKLKEREKKEEQKEEN-RREQK------QLDEIAA 120
PHA03247 PHA03247
large tegument protein UL36; Provisional
45-315 4.57e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021  Cd Length: 3151  Bit Score: 41.85  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215   45 GPSPG---------PPSVSHPMPTMGSTDFPQEGMH-QMHKPIDGIHDkgivedihCGSMKGTGMRPPHPGMGPPQSPmD 114
Cdd:PHA03247 2495 APDPGgggppdpdaPPAPSRLAPAILPDEPVGEPVHpRMLTWIRGLEE--------LASDDAGDPPPPLPPAAPPAAP-D 2565
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  115 QHSqgymsPHPSPLGAPehvSSPMSGGGPTPPQMPPSQPGALIPGDPqamSQPNRGPSPFSPVQLHQLRAQILAYKMLAR 194
Cdd:PHA03247 2566 RSV-----PPPRPAPRP---SEPAVTSRARRPDAPPQSARPRAPVDD---RGDPRGPAPPSPLPPDTHAPDPPPPSPSPA 2634
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215  195 GQPLPETLQLAVQgKRTLPGLQQQQQQQQQQQQQQQQQQQQQQQPQQQPPQPQTQQQQQPALVNYNRPSGPGPELSGPST 274
Cdd:PHA03247 2635 ANEPDPHPPPTVP-PPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPH 2713
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 119579215  275 PQKLPVPAPGGrpspapPAAAQPPAAAVPGPSVPQPAPGQP 315
Cdd:PHA03247 2714 ALVSATPLPPG------PAAARQASPALPAAPAPPAVPAGP 2748
GGN pfam15685
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ...
45-176 9.23e-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: 317988  Cd Length: 648  Bit Score: 40.42  E-value: 9.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215    45 GPSPGPPSVSHPMPtmgSTDFPQEGMhqMHKPIDGIHDKGIVEDIHCG--SMKGTGMRPPHPGMGPPQSPMDQhsQGYMS 122
Cdd:pfam15685  389 GSPPPPPGQKHPAP---GPRRPAPAL--LAPPMFIFPAPTNGEPVRPGppGQQELPPMPPPVPPPTPQPPALQ--PTPLP 461
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 119579215   123 PHPSPLGAPEHVSSPMSG--GGPTPPQMPPSQPGALIPGDPQAMSQPNRGPSPFSP 176
Cdd:pfam15685  462 VAPPPTPGPGHAESALAPppAPALPPALAADQTPAPAPAPSPAPAPTTAEPLPPAP 517
SSDP pfam04503
Single-stranded DNA binding protein, SSDP; This is a family of eukaryotic single-stranded DNA ...
41-175 9.44e-03

Single-stranded DNA binding protein, SSDP; This is a family of eukaryotic single-stranded DNA binding proteins with specificity to a pyrimidine-rich element found in the promoter region of the alpha2(I) collagen gene.


Pssm-ID: 309585  Cd Length: 293  Bit Score: 39.60  E-value: 9.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579215    41 HSMMGPS---------PGPPSVSHPMPTMG-STDFPQEGMHQMHKpidgihdkgivedihcGSMKGTgmRPPHPGMGPPQ 110
Cdd:pfam04503   67 ATMMGPHsqpfmgpryPGGPRPGVRMPQQGnDFNGPGPGQQPMMP----------------NSMDPT--RQGGHGMGGMM 128
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119579215   111 SPMDQHSQGYMSP-HPSPLGAPEHVSSPMSGGGPTPpqMPPSQPGaliPGDPQAMSQPNRG-PSPFS 175
Cdd:pfam04503  129 PRMNPPRGPGMGPmGPGSYGPGMRGPPPNSTDGPGG--MPPMNMG---PGGRRPWPQPNASnPLNYS 190
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH