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Conserved domains on  [gi|1977155862|gb|KAG2471204|]
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SMCA4 protein, partial [Polypterus senegalus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
 714-964 1.06e-172

DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4, also known as transcription activator BRG1) is a component of the CREST-BRG1 complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. Mutation of SMARCA4 (BRG1), the ATPase of BAF (mSWI/SNF) and PBAF complexes, contributes to a range of malignancies and neurologic disorders. SMARCA4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


:

Pssm-ID: 350820 [Multi-domain]  Cd Length: 251  Bit Score: 524.61  E-value: 1.06e-172
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  714 YYSVAHAVTEKVEKQSSLLVNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIV 793
Cdd:cd18062      1 YYAVAHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  794 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHH 873
Cdd:cd18062     81 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  874 CKLTQVLNTHYLAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 953
Cdd:cd18062    161 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 240

                          250
                   ....*....|.
gi 1977155862  954 VLRPFLLRRLK 964
Cdd:cd18062    241 VLRPFLLRRLK 251
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
 1373-1479 1.19e-61

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: 205.74  E-value: 1.19e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1373 LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1452
Cdd:cd05516      2 LTKKMNKIVDVVIKYKDSD-GRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQ 80

                           90       100
                   ....*....|....*....|....*..
gi 1977155862 1453 TFNLEGSLIYEDSIVLQSVFTSVRQKI 1479
Cdd:cd05516     81 TFNLEGSLIYEDSIVLQSVFKSARQKI 107
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 1026-1152 1.77e-57

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


:

Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 195.00  E-value: 1.77e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1026 SGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRNFKYLRLDGTTKAEDRGMLLKAFNDPaSQYFVFLLSTRA 1105
Cdd:cd18793     10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDIRVFLLSTKA 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1977155862 1106 GGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLC 1152
Cdd:cd18793     89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
 1236-1303 4.13e-24

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: 464219 [Multi-domain]  Cd Length: 69  Bit Score: 97.33  E-value: 4.13e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1977155862 1236 DRRREEARNPK-RKPRLMEEDELPTWIMKDDAEVERLTCEEEEEKMFGRGSRQRKEVDYSDSLTEKQWL 1303
Cdd:pfam14619    1 ERRREEAEQLPpLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
HSA smart00573
domain in helicases and associated with SANT domains;
465-537 1.25e-23

domain in helicases and associated with SANT domains;


:

Pssm-ID: 214727 [Multi-domain]  Cd Length: 73  Bit Score: 95.93  E-value: 1.25e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1977155862   465 QKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERMRRLMA 537
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
 599-642 1.19e-16

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


:

Pssm-ID: 462196  Cd Length: 44  Bit Score: 75.24  E-value: 1.19e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1977155862  599 QMSDLPVKVIHVDSGKILTGADAPKAGQLDAWLEMNPGYEVAPR 642
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
QLQ pfam08880
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ...
 165-199 2.05e-14

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: 462622  Cd Length: 35  Bit Score: 68.52  E-value: 2.05e-14
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1977155862  165 PFNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQ 199
Cdd:pfam08880    1 PFTPAQLQELRAQILAYKYLSRNQPVPPELQQAIF 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1676-1710 4.30e-14

Low-density lipoprotein receptor domain class A;


:

Pssm-ID: 395011  Cd Length: 37  Bit Score: 67.66  E-value: 4.30e-14
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1977155862 1676 CSSLEFQCGSGECVHQKWLCDGTNDCRDHSDETNC 1710
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1714-1749 1.70e-13

Low-density lipoprotein receptor domain class A;


:

Pssm-ID: 395011  Cd Length: 37  Bit Score: 66.12  E-value: 1.70e-13
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1977155862 1714 TCRPDEFQCNDGTCIHGSRQCDREYDCKDLSDELGC 1749
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1628-1665 1.39e-12

Low-density lipoprotein receptor domain class A;


:

Pssm-ID: 395011  Cd Length: 37  Bit Score: 63.42  E-value: 1.39e-12
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1977155862 1628 TCGPNMFQCNNSACIPLLWACDGDPECLDQSDEwpQNC 1665
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDE--ENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1590-1624 1.58e-12

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 63.38  E-value: 1.58e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1977155862 1590 CTDDEFRCRSGKCISVQFVCDEEKDCDDGSDEDSC 1624
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1552-1581 2.29e-11

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 59.91  E-value: 2.29e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 1977155862 1552 NYFQCANERCVPYRWICDGTDDCGDGSDEL 1581
Cdd:cd00112      4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEE 33
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 1797-1831 5.24e-10

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


:

Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 56.10  E-value: 5.24e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1977155862 1797 CLYNNGGCSHTCNDLKVGFECLCPSGFQLA-DKKRC 1831
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQdDGRTC 36
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1757-1787 1.74e-09

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


:

Pssm-ID: 197566  Cd Length: 33  Bit Score: 54.56  E-value: 1.74e-09
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1977155862  1757 GPDKFQCKSGECIKMAQVCDKQRDCRDWSDE 1787
Cdd:smart00192    3 PPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
EGF_CA smart00179
Calcium-binding EGF-like domain;
1833-1863 2.17e-09

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 54.56  E-value: 2.17e-09
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1977155862  1833 DIDECQNPDACSQ--ICINLEGGYKCECREGYH 1863
Cdd:smart00179    1 DIDECASGNPCQNggTCVNTVGSYRCECPPGYT 33
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 369-582 3.19e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 3.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  369 VEILQEREYRLQARIA-------HRIQELENLpgslpgdLRTKANIELKALRLLNFQRQLRQEVVvcmRRDTALETALNA 441
Cdd:COG1196    283 LEEAQAEEYELLAELArleqdiaRLEERRREL-------EERLEELEEELAELEEELEELEEELE---ELEEELEEAEEE 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  442 KAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQK 521
Cdd:COG1196    353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1977155862  522 KENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAyLLQQTDEYVANLTELVRAHKAAQAL 582
Cdd:COG1196    433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE-LLEEAALLEAALAELLEELAEAAAR 492
TYA super family cl03073
Ty transposon capsid protein; Ty are yeast transposons. A 5.7kb transcript codes for p3 a ...
 42-130 1.18e-04

Ty transposon capsid protein; Ty are yeast transposons. A 5.7kb transcript codes for p3 a fusion protein of TYA and TYB. The TYA protein is analogous to the gag protein of retroviruses. TYA a is cleaved to form 46kd protein which can form mature virion like particles. This entry corresponds to the capsid protein from Ty1 and Ty2 transposons.


The actual alignment was detected with superfamily member pfam01021:

Pssm-ID: 425992  Cd Length: 384  Bit Score: 46.87  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862   42 PPAAGHPLPPQGPsgYPQenmHQMHKPmdamhEKAMPDD-PRYGQMKGMGMRPAGHSGMGPPPSPMDQHSQgYPSPLGGS 120
Cdd:pfam01021   56 PQPASVPPPQNGP--YSQ---QCMMTP-----NQANPSGwPFYGHPSMMPYTPYQMSPMYFPPGPQSQFPQ-YPSSVGTP 124

                           90
                   ....*....|
gi 1977155862  121 EHAPSPVPAN 130
Cdd:pfam01021  125 LSTPSPESGN 134
 
Name Accession Description Interval E-value
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
 714-964 1.06e-172

DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4, also known as transcription activator BRG1) is a component of the CREST-BRG1 complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. Mutation of SMARCA4 (BRG1), the ATPase of BAF (mSWI/SNF) and PBAF complexes, contributes to a range of malignancies and neurologic disorders. SMARCA4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350820 [Multi-domain]  Cd Length: 251  Bit Score: 524.61  E-value: 1.06e-172
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  714 YYSVAHAVTEKVEKQSSLLVNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIV 793
Cdd:cd18062      1 YYAVAHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  794 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHH 873
Cdd:cd18062     81 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  874 CKLTQVLNTHYLAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 953
Cdd:cd18062    161 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 240

                          250
                   ....*....|.
gi 1977155862  954 VLRPFLLRRLK 964
Cdd:cd18062    241 VLRPFLLRRLK 251
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 733-1179 8.73e-154

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 502.41  E-value: 8.73e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  733 VNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIVPLSTLSNWVYEFDKWAPSV 812
Cdd:PLN03142   166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  813 VKVSYKGSPAARRAFVPQ-LRSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYlapr 888
Cdd:PLN03142   246 RAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  889 RILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGEkvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 968
Cdd:PLN03142   322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  969 AQLPEK-----------------------------GKGGTKTLMNTIMQLRKICNHPYMFQHIEESfsehlgftGGIVQG 1019
Cdd:PLN03142   392 KGLPPKketilkvgmsqmqkqyykallqkdldvvnAGGERKRLLNIAMQLRKCCNHPYLFQGAEPG--------PPYTTG 463

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1020 PDLYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRNFKYLRLDGTTKAEDRGMLLKAFNDPASQYFVF 1099
Cdd:PLN03142   464 EHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVF 543

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1100 LLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAG 1179
Cdd:PLN03142   544 LLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQG 623
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 733-1163 1.65e-116

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 386.12  E-value: 1.65e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  733 VNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEyKRINGPFLIIVPLSTLSNWVYEFDKWAPSV 812
Cdd:COG0553    238 LKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQRELAKFAPGL 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  813 VKVSYKGSPAARRAFVPqlrSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLNThyL-APRRIL 891
Cdd:COG0553    317 RVLVLDGTRERAKGANP---FEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRA--LkARHRLA 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  892 LTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPfamtGEKVDLNEEEtiliirRLHKVLRPFLLRRLKKEVEAQL 971
Cdd:COG0553    392 LTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP----IEKGDEEALE------RLRRLLRPFLLRRTKEDVLKDL 461

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  972 PEK-----------------------------GKGGTKTLMN---TIMQLRKICNHPYMFQHIEESFSEHlgftggivqg 1019
Cdd:COG0553    462 PEKteetlyveltpeqralyeavleylrreleGAEGIRRRGLilaALTRLRQICSHPALLLEEGAELSGR---------- 531

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1020 pdlyraSGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRNFKYLRLDGTTKAEDRGMLLKAFNDPASqYFVF 1099
Cdd:COG0553    532 ------SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPE-APVF 604

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1977155862 1100 LLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILA 1163
Cdd:COG0553    605 LISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 740-999 4.38e-101

SNF2-related 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). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 326.56  E-value: 4.38e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  740 YQIKGLEWLVSLYNN-NLNGILADEMGLGKTIQTIALITYLMEYKRI-NGPFLIIVPLSTLSNWVYEFDKWA--PSVVKV 815
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNwGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  816 SYKGSPAAR-RAFVPQLRSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYLAPRRILLTG 894
Cdd:pfam00176   81 VLHGNKRPQeRWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK-SLKTRNRWILTG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  895 TPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetiLIIRRLHKVLRPFLLRRLKKEVEAQLP-- 972
Cdd:pfam00176  160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK---------KGVSRLHKLLKPFLLRRTKKDVEKSLPpk 230

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1977155862  973 --------------------------------EKGKGGTKTLMNTIMQLRKICNHPYMF 999
Cdd:pfam00176  231 veyilfcrlsklqrklyqtfllkkdlnaiktgEGGREIKASLLNILMRLRKICNHPGLI 289
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
 1373-1479 1.19e-61

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: 205.74  E-value: 1.19e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1373 LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1452
Cdd:cd05516      2 LTKKMNKIVDVVIKYKDSD-GRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQ 80

                           90       100
                   ....*....|....*....|....*..
gi 1977155862 1453 TFNLEGSLIYEDSIVLQSVFTSVRQKI 1479
Cdd:cd05516     81 TFNLEGSLIYEDSIVLQSVFKSARQKI 107
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 1026-1152 1.77e-57

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 195.00  E-value: 1.77e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1026 SGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRNFKYLRLDGTTKAEDRGMLLKAFNDPaSQYFVFLLSTRA 1105
Cdd:cd18793     10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDIRVFLLSTKA 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1977155862 1106 GGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLC 1152
Cdd:cd18793     89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
BROMO smart00297
bromo domain;
1371-1479 2.22e-31

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 119.31  E-value: 2.22e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  1371 PNLTKKMKKIVDAVIKYKDSssgRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQN 1450
Cdd:smart00297    2 PKLQKKLQELLKAVLDKLDS---HPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78

                            90       100
                    ....*....|....*....|....*....
gi 1977155862  1451 AQTFNLEGSLIYEDSIVLQSVFTSVRQKI 1479
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
DEXDc smart00487
DEAD-like helicases superfamily;
736-925 3.12e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 122.60  E-value: 3.12e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862   736 QLKQYQIKGLEWLvslYNNNLNGILADEMGLGKTIQ-TIALITYLMEYKriNGPFLIIVPLSTL-SNWVYEFDKWAPS-V 812
Cdd:smart00487    8 PLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGK--GGRVLVLVPTRELaEQWAEELKKLGPSlG 82

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862   813 VKVSYKGSPAARRAFVPQLRSGKFNALLTTYEYIIKD--KQVLAKIRWKYMIVDEGHRMKN--HHCKLTQVLNTHYLAPR 888
Cdd:smart00487   83 LKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKNVQ 162

                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 1977155862   889 RILLTGTPLQNKLPELWALLN--FLLPTIFKSCSTFEQW 925
Cdd:smart00487  163 LLLLSATPPEEIENLLELFLNdpVFIDVGFTPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 1027-1141 1.37e-28

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: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 111.53  E-value: 1.37e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1027 GKFELLDRILPKLRatNHKVLLFCQMTSlmTIMEDYFAYR-NFKYLRLDGTTKAEDRGMLLKAFNDPASQyfvFLLSTRA 1105
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKK--TLEAELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1977155862 1106 GGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIG 1141
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
 1236-1303 4.13e-24

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: 464219 [Multi-domain]  Cd Length: 69  Bit Score: 97.33  E-value: 4.13e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1977155862 1236 DRRREEARNPK-RKPRLMEEDELPTWIMKDDAEVERLTCEEEEEKMFGRGSRQRKEVDYSDSLTEKQWL 1303
Cdd:pfam14619    1 ERRREEAEQLPpLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
HSA smart00573
domain in helicases and associated with SANT domains;
465-537 1.25e-23

domain in helicases and associated with SANT domains;


Pssm-ID: 214727 [Multi-domain]  Cd Length: 73  Bit Score: 95.93  E-value: 1.25e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1977155862   465 QKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERMRRLMA 537
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
HELICc smart00490
helicase superfamily c-terminal domain;
1058-1141 2.56e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 92.66  E-value: 2.56e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  1058 IMEDYFAYRNFKYLRLDGTTKAEDRGMLLKAFNDPASQyfvFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRA 1137
Cdd:smart00490    2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78


                    ....
gi 1977155862  1138 HRIG 1141
Cdd:smart00490   79 GRAG 82
HSA pfam07529
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ...
 466-532 6.96e-21

HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. This region does not form a compact domain in the known structures.


Pssm-ID: 462194 [Multi-domain]  Cd Length: 67  Bit Score: 88.01  E-value: 6.96e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1977155862  466 KIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERM 532
Cdd:pfam07529    1 RDEPERREKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQKRIEREEKQRL 67
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
 1377-1465 2.77e-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: 425683 [Multi-domain]  Cd Length: 84  Bit Score: 83.90  E-value: 2.77e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1377 MKKIVDAVIKykdsssgRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNL 1456
Cdd:pfam00439    1 CLEILDKLME-------HPIAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNG 73


                   ....*....
gi 1977155862 1457 EGSLIYEDS 1465
Cdd:pfam00439   74 PGSVIYKAA 82
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
 1345-1479 2.50e-17

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 86.01  E-value: 2.50e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1345 SREKDDENKKQKKRGRPPAEKLSPNPPN--LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDF 1422
Cdd:COG5076    113 TPESGLGSLLMAHLKTSVKKRKTPKIEDelLYADNKAIAKFKKQLFLRD-GRFLSSIFLGLPSKREYPDYYEIIKSPMDL 191

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1977155862 1423 KKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKI 1479
Cdd:COG5076    192 LTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEI 248
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
 599-642 1.19e-16

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


Pssm-ID: 462196  Cd Length: 44  Bit Score: 75.24  E-value: 1.19e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1977155862  599 QMSDLPVKVIHVDSGKILTGADAPKAGQLDAWLEMNPGYEVAPR 642
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
BRK smart00592
domain in transcription and CHROMO domain helicases;
600-644 2.85e-16

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 74.31  E-value: 2.85e-16
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 1977155862   600 MSDLPVKVIHVDSGKILTGADAPKAGQLDAWLEMNPGYEVAPRSD 644
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
QLQ pfam08880
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ...
 165-199 2.05e-14

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: 462622  Cd Length: 35  Bit Score: 68.52  E-value: 2.05e-14
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1977155862  165 PFNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQ 199
Cdd:pfam08880    1 PFTPAQLQELRAQILAYKYLSRNQPVPPELQQAIF 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1676-1710 4.30e-14

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 67.66  E-value: 4.30e-14
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1977155862 1676 CSSLEFQCGSGECVHQKWLCDGTNDCRDHSDETNC 1710
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1676-1710 1.00e-13

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 66.46  E-value: 1.00e-13
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1977155862 1676 CSSLEFQCGSGECVHQKWLCDGTNDCRDHSDETNC 1710
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1714-1749 1.70e-13

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 66.12  E-value: 1.70e-13
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1977155862 1714 TCRPDEFQCNDGTCIHGSRQCDREYDCKDLSDELGC 1749
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1628-1665 1.39e-12

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 63.42  E-value: 1.39e-12
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1977155862 1628 TCGPNMFQCNNSACIPLLWACDGDPECLDQSDEwpQNC 1665
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDE--ENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1590-1624 1.58e-12

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 63.38  E-value: 1.58e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1977155862 1590 CTDDEFRCRSGKCISVQFVCDEEKDCDDGSDEDSC 1624
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1715-1749 6.12e-12

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 61.45  E-value: 6.12e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1977155862 1715 CRPDEFQCNDGTCIHGSRQCDREYDCKDLSDELGC 1749
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
QLQ smart00951
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ...
 165-198 7.98e-12

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: 61.39  E-value: 7.98e-12
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1977155862   165 PFNQNQLHQLRAQIMAYK-MLARGQPLPDHLQMAV 198
Cdd:smart00951    2 PFTPAQLELLRAQILAYKyLLARNQPVPPELLQAI 36
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1676-1707 9.81e-12

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 61.11  E-value: 9.81e-12
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1977155862  1676 CSSLEFQCGSGECVHQKWLCDGTNDCRDHSDE 1707
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1552-1581 2.29e-11

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 59.91  E-value: 2.29e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 1977155862 1552 NYFQCANERCVPYRWICDGTDDCGDGSDEL 1581
Cdd:cd00112      4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1628-1660 2.71e-11

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 59.57  E-value: 2.71e-11
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1977155862  1628 TCGPNMFQCNNSACIPLLWACDGDPECLDQSDE 1660
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1588-1624 3.01e-11

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 59.57  E-value: 3.01e-11
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1977155862 1588 KNCTDDEFRCRSGKCISVQFVCDEEKDCDDGSDEDSC 1624
Cdd:pfam00057    1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1590-1621 3.89e-11

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 59.18  E-value: 3.89e-11
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1977155862  1590 CTDDEFRCRSGKCISVQFVCDEEKDCDDGSDE 1621
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1552-1580 4.68e-11

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 59.18  E-value: 4.68e-11
                            10        20
                    ....*....|....*....|....*....
gi 1977155862  1552 NYFQCANERCVPYRWICDGTDDCGDGSDE 1580
Cdd:smart00192    5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1629-1665 7.68e-11

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 58.37  E-value: 7.68e-11
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1977155862 1629 CGPNMFQCNNSACIPLLWACDGDPECLDQSDEWpqNC 1665
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEE--NC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1714-1746 1.39e-10

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 57.64  E-value: 1.39e-10
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1977155862  1714 TCRPDEFQCNDGTCIHGSRQCDREYDCKDLSDE 1746
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 1797-1831 5.24e-10

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 56.10  E-value: 5.24e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1977155862 1797 CLYNNGGCSHTCNDLKVGFECLCPSGFQLA-DKKRC 1831
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQdDGRTC 36
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1757-1787 1.74e-09

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 54.56  E-value: 1.74e-09
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1977155862  1757 GPDKFQCKSGECIKMAQVCDKQRDCRDWSDE 1787
Cdd:smart00192    3 PPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1757-1787 1.84e-09

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 54.52  E-value: 1.84e-09
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1977155862 1757 GPDKFQCKSGECIKMAQVCDKQRDCRDWSDE 1787
Cdd:cd00112      2 PPNEFRCANGRCIPSSWVCDGEDDCGDGSDE 32
EGF_CA smart00179
Calcium-binding EGF-like domain;
1833-1863 2.17e-09

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 54.56  E-value: 2.17e-09
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1977155862  1833 DIDECQNPDACSQ--ICINLEGGYKCECREGYH 1863
Cdd:smart00179    1 DIDECASGNPCQNggTCVNTVGSYRCECPPGYT 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1757-1787 2.29e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 54.18  E-value: 2.29e-09
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1977155862 1757 GPDKFQCKSGECIKMAQVCDKQRDCRDWSDE 1787
Cdd:pfam00057    4 SPNEFQCGSGECIPRSWVCDGDPDCGDGSDE 34
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1833-1865 5.96e-09

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 53.02  E-value: 5.96e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1977155862 1833 DIDECQNPDACS--QICINLEGGYKCECREGYHLD 1865
Cdd:cd00054      1 DIDECASGNPCQngGTCVNTVGSYRCSCPPGYTGR 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1552-1581 5.97e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 53.02  E-value: 5.97e-09
                           10        20        30
                   ....*....|....*....|....*....|
gi 1977155862 1552 NYFQCANERCVPYRWICDGTDDCGDGSDEL 1581
Cdd:pfam00057    6 NEFQCGSGECIPRSWVCDGDPDCGDGSDEE 35
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 1838-1871 7.85e-08

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 49.93  E-value: 7.85e-08
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1977155862 1838 QNPDACSQICINLEGGYKCECREGYHLDPVNKSC 1871
Cdd:pfam14670    3 VNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 369-582 3.19e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 3.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  369 VEILQEREYRLQARIA-------HRIQELENLpgslpgdLRTKANIELKALRLLNFQRQLRQEVVvcmRRDTALETALNA 441
Cdd:COG1196    283 LEEAQAEEYELLAELArleqdiaRLEERRREL-------EERLEELEEELAELEEELEELEEELE---ELEEELEEAEEE 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  442 KAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQK 521
Cdd:COG1196    353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1977155862  522 KENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAyLLQQTDEYVANLTELVRAHKAAQAL 582
Cdd:COG1196    433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE-LLEEAALLEAALAELLEELAEAAAR 492
TYA pfam01021
Ty transposon capsid protein; Ty are yeast transposons. A 5.7kb transcript codes for p3 a ...
 42-130 1.18e-04

Ty transposon capsid protein; Ty are yeast transposons. A 5.7kb transcript codes for p3 a fusion protein of TYA and TYB. The TYA protein is analogous to the gag protein of retroviruses. TYA a is cleaved to form 46kd protein which can form mature virion like particles. This entry corresponds to the capsid protein from Ty1 and Ty2 transposons.


Pssm-ID: 425992  Cd Length: 384  Bit Score: 46.87  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862   42 PPAAGHPLPPQGPsgYPQenmHQMHKPmdamhEKAMPDD-PRYGQMKGMGMRPAGHSGMGPPPSPMDQHSQgYPSPLGGS 120
Cdd:pfam01021   56 PQPASVPPPQNGP--YSQ---QCMMTP-----NQANPSGwPFYGHPSMMPYTPYQMSPMYFPPGPQSQFPQ-YPSSVGTP 124

                           90
                   ....*....|
gi 1977155862  121 EHAPSPVPAN 130
Cdd:pfam01021  125 LSTPSPESGN 134
PHA03378 PHA03378
EBNA-3B; Provisional
 38-209 3.07e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.83  E-value: 3.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862   38 PSPGPPAAGHPLPPQGPSGYPQENMHQMHKPMDAMHEKAMPDDPRYGQ-MKGMGMRPAGHSGMGPPPspmdQHSQGYPSP 116
Cdd:PHA03378   701 PTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAaAPGRARPPAAAPGRARPP----AAAPGAPTP 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  117 LGGSEHAPSPVpangppsgplmppgpggvpqdnadpqtlgQQNRGGPTPFNQNQLHQLRAQIMAYKMLARGQPLPDHLQM 196
Cdd:PHA03378   777 QPPPQAPPAPQ-----------------------------QRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQ 827

                          170       180
                   ....*....|....*....|..
gi 1977155862  197 AVQG---------KRPMAGMQQ 209
Cdd:PHA03378   828 LLTGgvkrgrpslKKPAALERQ 849
EGF_CA smart00179
Calcium-binding EGF-like domain;
1795-1832 5.08e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.15  E-value: 5.08e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1977155862  1795 NECLYNNGgCSH--TCNDLKVGFECLCPSGFQlaDKKRCQ 1832
Cdd:smart00179    3 DECASGNP-CQNggTCVNTVGSYRCECPPGYT--DGRNCE 39
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 370-555 1.31e-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: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 43.37  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  370 EILQEREyRLQARIAHRIQELEnlpgslpgdlRTKANIElkALRLlnfqrQLRQEVVVCMRRDTALETALNakayKRSKR 449
Cdd:pfam13868  177 EIEEEKE-REIARLRAQQEKAQ----------DEKAERD--ELRA-----KLYQEEQERKERQKEREEAEK----KARQR 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  450 QSLREARITEKLEKQQKIEQERKRRQkhQEYLNSILQHAKDFKEYHRSVTGKIQKLTK-AVATYHANTEREQKKENERIE 528
Cdd:pfam13868  235 QELQQAREEQIELKERRLAEEAEREE--EEFERMLRKQAEDEEIEQEEAEKRRMKRLEhRRELEKQIEEREEQRAAEREE 312

                          170       180
                   ....*....|....*....|....*..
gi 1977155862  529 KERMRRLMAEDEEGYRKLIDQKKDKRL 555
Cdd:pfam13868  313 ELEEGERLREEEAERRERIEEERQKKL 339
PTZ00121 PTZ00121
MAEBL; Provisional
 442-553 1.58e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  442 KAYKRSKRQSLREARITEKLEKQQKIEQERKRrqkhQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHAntEREQK 521
Cdd:PTZ00121  1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKA----EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA--EEAKK 1614

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1977155862  522 KENERIEKERMRRlmaedEEGYRKLIDQKKDK 553
Cdd:PTZ00121  1615 AEEAKIKAEELKK-----AEEEKKKVEQLKKK 1641
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1795-1832 2.17e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 37.62  E-value: 2.17e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1977155862 1795 NECLYNNG-GCSHTCNDLKVGFECLCPSGFQLadkKRCQ 1832
Cdd:cd00054      3 DECASGNPcQNGGTCVNTVGSYRCSCPPGYTG---RNCE 38
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 362-552 6.59e-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 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 6.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  362 KPRGLDPVEILQEREY-------RLQARIAHRIQELENLPGSLPGDLRTKANIELKALRLLNFQRQLRQEVVVCMRRDTA 434
Cdd:TIGR02169  669 SRSEPAELQRLRERLEglkrelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  435 LETALNAK-----------AYKRSKRQSLREA-----------RITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFK 492
Cdd:TIGR02169  749 LEQEIENVkselkeleariEELEEDLHKLEEAlndlearlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1977155862  493 EYHRSvtgKIQKLTKAVATYHAN-TEREQKKENERIEKERMRRLMAEDEEGYRKLIDQKKD 552
Cdd:TIGR02169  829 EYLEK---EIQELQEQRIDLKEQiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
 
Name Accession Description Interval E-value
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
 714-964 1.06e-172

DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4, also known as transcription activator BRG1) is a component of the CREST-BRG1 complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. Mutation of SMARCA4 (BRG1), the ATPase of BAF (mSWI/SNF) and PBAF complexes, contributes to a range of malignancies and neurologic disorders. SMARCA4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350820 [Multi-domain]  Cd Length: 251  Bit Score: 524.61  E-value: 1.06e-172
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  714 YYSVAHAVTEKVEKQSSLLVNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIV 793
Cdd:cd18062      1 YYAVAHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  794 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHH 873
Cdd:cd18062     81 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  874 CKLTQVLNTHYLAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 953
Cdd:cd18062    161 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 240

                          250
                   ....*....|.
gi 1977155862  954 VLRPFLLRRLK 964
Cdd:cd18062    241 VLRPFLLRRLK 251
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
 734-964 2.51e-167

DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, members 2 and 4 (SMARCA2 and SMARCA4) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350754 [Multi-domain]  Cd Length: 233  Bit Score: 509.22  E-value: 2.51e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  734 NGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIVPLSTLSNWVYEFDKWAPSVV 813
Cdd:cd17996      1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  814 KVSYKGSPAARRAFVPQLRSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYLAPRRILLT 893
Cdd:cd17996     81 KIVYKGTPDVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHARYRLLLT 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1977155862  894 GTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKV--DLNEEETILIIRRLHKVLRPFLLRRLK 964
Cdd:cd17996    161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVkiELNEEETLLIIRRLHKVLRPFLLRRLK 233
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
 714-964 3.09e-162

DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2, also known as brahma homolog) is a component of the BAF complex. SMARCA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350821 [Multi-domain]  Cd Length: 251  Bit Score: 496.12  E-value: 3.09e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  714 YYSVAHAVTEKVEKQSSLLVNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIV 793
Cdd:cd18063      1 YYTVAHAITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  794 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHH 873
Cdd:cd18063     81 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  874 CKLTQVLNTHYLAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 953
Cdd:cd18063    161 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHK 240

                          250
                   ....*....|.
gi 1977155862  954 VLRPFLLRRLK 964
Cdd:cd18063    241 VLRPFLLRRLK 251
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 733-1179 8.73e-154

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 502.41  E-value: 8.73e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  733 VNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIVPLSTLSNWVYEFDKWAPSV 812
Cdd:PLN03142   166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  813 VKVSYKGSPAARRAFVPQ-LRSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYlapr 888
Cdd:PLN03142   246 RAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  889 RILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGEkvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 968
Cdd:PLN03142   322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  969 AQLPEK-----------------------------GKGGTKTLMNTIMQLRKICNHPYMFQHIEESfsehlgftGGIVQG 1019
Cdd:PLN03142   392 KGLPPKketilkvgmsqmqkqyykallqkdldvvnAGGERKRLLNIAMQLRKCCNHPYLFQGAEPG--------PPYTTG 463

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1020 PDLYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRNFKYLRLDGTTKAEDRGMLLKAFNDPASQYFVF 1099
Cdd:PLN03142   464 EHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVF 543

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1100 LLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAG 1179
Cdd:PLN03142   544 LLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQG 623
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 733-1163 1.65e-116

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 386.12  E-value: 1.65e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  733 VNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEyKRINGPFLIIVPLSTLSNWVYEFDKWAPSV 812
Cdd:COG0553    238 LKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQRELAKFAPGL 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  813 VKVSYKGSPAARRAFVPqlrSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLNThyL-APRRIL 891
Cdd:COG0553    317 RVLVLDGTRERAKGANP---FEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRA--LkARHRLA 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  892 LTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPfamtGEKVDLNEEEtiliirRLHKVLRPFLLRRLKKEVEAQL 971
Cdd:COG0553    392 LTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP----IEKGDEEALE------RLRRLLRPFLLRRTKEDVLKDL 461

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  972 PEK-----------------------------GKGGTKTLMN---TIMQLRKICNHPYMFQHIEESFSEHlgftggivqg 1019
Cdd:COG0553    462 PEKteetlyveltpeqralyeavleylrreleGAEGIRRRGLilaALTRLRQICSHPALLLEEGAELSGR---------- 531

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1020 pdlyraSGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRNFKYLRLDGTTKAEDRGMLLKAFNDPASqYFVF 1099
Cdd:COG0553    532 ------SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPE-APVF 604

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1977155862 1100 LLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILA 1163
Cdd:COG0553    605 LISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 740-999 4.38e-101

SNF2-related 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). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 326.56  E-value: 4.38e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  740 YQIKGLEWLVSLYNN-NLNGILADEMGLGKTIQTIALITYLMEYKRI-NGPFLIIVPLSTLSNWVYEFDKWA--PSVVKV 815
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNwGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  816 SYKGSPAAR-RAFVPQLRSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYLAPRRILLTG 894
Cdd:pfam00176   81 VLHGNKRPQeRWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK-SLKTRNRWILTG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  895 TPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetiLIIRRLHKVLRPFLLRRLKKEVEAQLP-- 972
Cdd:pfam00176  160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK---------KGVSRLHKLLKPFLLRRTKKDVEKSLPpk 230

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1977155862  973 --------------------------------EKGKGGTKTLMNTIMQLRKICNHPYMF 999
Cdd:pfam00176  231 veyilfcrlsklqrklyqtfllkkdlnaiktgEGGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
 734-964 3.18e-93

DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 and 5 (SMARCA1 and SMARCA5) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350755 [Multi-domain]  Cd Length: 222  Bit Score: 301.16  E-value: 3.18e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  734 NGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIVPLSTLSNWVYEFDKWAPSVV 813
Cdd:cd17997      1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  814 KVSYKGSPAARRAFV-PQLRSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYlaprR 889
Cdd:cd17997     81 VVVLIGDKEERADIIrDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVrlfNSRN----R 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1977155862  890 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNApfamtgEKVDLNEEEtilIIRRLHKVLRPFLLRRLK 964
Cdd:cd17997    157 LLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNV------NNCDDDNQE---VVQRLHKVLRPFLLRRIK 222
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
 734-964 1.13e-91

DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or SMARCA6) is a major epigenetic regulator crucial for normal heterochromatin structure and function. HELLS is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350767 [Multi-domain]  Cd Length: 236  Bit Score: 297.38  E-value: 1.13e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  734 NGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEyKRINGPFLIIVPLSTLSNWVYEFDKWAPSVV 813
Cdd:cd18009      1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRE-RGVWGPFLVIAPLSTLPNWVNEFARFTPSVP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  814 KVSYKGSPAARRAFVPQLRS-----GKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYLAPR 888
Cdd:cd18009     80 VLLYHGTKEERERLRKKIMKregtlQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELK-TFNSDN 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1977155862  889 RILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFN--APFAMTGEKVDLNEEETILIIRRLHKVLRPFLLRRLK 964
Cdd:cd18009    159 RLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDfsSLSDNAADISNLSEEREQNIVHMLHAILKPFLLRRLK 236
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
 737-962 4.69e-82

DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or DOMO1) is the core catalytic component of the multiprotein chromatin-remodeling SRCAP complex, that is necessary for the incorporation of the histone variant H2A.Z into nucleosomes. SRCAP is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350761 [Multi-domain]  Cd Length: 223  Bit Score: 269.22  E-value: 4.69e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 816
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  817 YKGSPAARRAfvpqLRSG-----KFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYLAPRRIL 891
Cdd:cd18003     81 YYGSAKERKL----KRQGwmkpnSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLN-FNTQRRLL 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1977155862  892 LTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPF-AMTGEKVDLNEEetilIIRRLHKVLRPFLLRR 962
Cdd:cd18003    156 LTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLtAMSEGSQEENEE----LVRRLHKVLRPFLLRR 223
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
 736-962 7.69e-81

DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and similar proteins; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as the substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but is also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. Both are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350751 [Multi-domain]  Cd Length: 218  Bit Score: 265.37  E-value: 7.69e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  736 QLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKV 815
Cdd:cd17993      1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  816 SYKGSPAARRA------FVPQLRSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYLAPRR 889
Cdd:cd17993     81 VYLGDIKSRDTireyefYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKE-FKTNNR 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1977155862  890 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEqwfnapfamtgekVDLNEEETILiIRRLHKVLRPFLLRR 962
Cdd:cd17993    160 LLITGTPLQNSLKELWALLHFLMPGKFDIWEEFE-------------EEHDEEQEKG-IADLHKELEPFILRR 218
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
 737-913 4.58e-80

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins 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: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 261.73  E-value: 4.58e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 816
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  817 YKGSPAARRAFVPQLRSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYlAPRRILLTGTP 896
Cdd:cd17919     81 YHGSQRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR-AKRRLLLTGTP 159

                          170
                   ....*....|....*..
gi 1977155862  897 LQNKLPELWALLNFLLP 913
Cdd:cd17919    160 LQNNLEELWALLDFLDP 176
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
 737-962 1.55e-76

DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; Chromodomain-helicase-DNA-binding protein 6-9 (CHD6, CHD7, CHD8, and CHD9) are members of the 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: 350753 [Multi-domain]  Cd Length: 223  Bit Score: 253.32  E-value: 1.55e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVkVS 816
Cdd:cd17995      1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTDMNV-VV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  817 YKGSPAARR------AFVPQL------RSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHY 884
Cdd:cd17995     80 YHGSGESRQiiqqyeMYFKDAqgrkkkGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLK-KL 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1977155862  885 LAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 962
Cdd:cd17995    159 TLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFG----------DLKTAEQ---VEKLQALLKPYMLRR 223
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
 724-974 5.27e-74

DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 (SMARCA5, also called SNF2H) is the catalytic subunit of the four known chromatin-remodeling complexes: CHRAC, RSF, ACF/WCRF, and WICH. SMARCA5 plays a major role organising arrays of nucleosomes adjacent to the binding sites for the architectural transcription factor CTCF sites and acts to promote CTCF binding SMARCA5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350822 [Multi-domain]  Cd Length: 244  Bit Score: 246.89  E-value: 5.27e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  724 KVEKQSSLLVNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIVPLSTLSNWVY 803
Cdd:cd18064      3 RFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  804 EFDKWAPSVVKVSYKGSPAARRAFVPQ-LRSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLNt 882
Cdd:cd18064     83 EFKRWVPTLRAVCLIGDKDQRAAFVRDvLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR- 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  883 HYLAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetilIIRRLHKVLRPFLLRR 962
Cdd:cd18064    162 EFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQK----------LVERLHMVLRPFLLRR 231

                          250
                   ....*....|..
gi 1977155862  963 LKKEVEAQLPEK 974
Cdd:cd18064    232 IKADVEKSLPPK 243
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
 724-964 1.87e-72

DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 (SMARCA1, also called SNF2L) is a component of NURF (nucleosome-remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes which promote the perturbation of chromatin structure in an ATP-dependent manner. SMARCA1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350823 [Multi-domain]  Cd Length: 233  Bit Score: 242.23  E-value: 1.87e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  724 KVEKQSSLLVNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIVPLSTLSNWVY 803
Cdd:cd18065      3 RFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMN 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  804 EFDKWAPSVVKVSYKGSPAARRAFV-PQLRSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLNt 882
Cdd:cd18065     83 EFKRWVPSLRAVCLIGDKDARAAFIrDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR- 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  883 HYLAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetilIIRRLHKVLRPFLLRR 962
Cdd:cd18065    162 EFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQK----------LVERLHAVLKPFLLRR 231


                   ..
gi 1977155862  963 LK 964
Cdd:cd18065    232 IK 233
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
 737-962 1.07e-65

DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 chromatin remodeling complex. INO80 removes histone H3-containing nucleosomes from associated chromatin, promotes CENP-ACnp1 chromatin assembly at the centromere in a redundant manner with another chromatin-remodeling factor Chd1Hrp1. INO80 mutants have severe defects in oxygen consumption and promiscuous cell division that is no longer coupled with metabolic status. INO80 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350760 [Multi-domain]  Cd Length: 229  Bit Score: 222.38  E-value: 1.07e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 816
Cdd:cd18002      1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  817 YKGSPAAR---RAFVPQ----LRSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYLAPRR 889
Cdd:cd18002     81 YWGNPKDRkvlRKFWDRknlyTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTL-LSFHCRNR 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1977155862  890 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGE-KVDLNEEEtiliIRRLHKVLRPFLLRR 962
Cdd:cd18002    160 LLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAEnKTGLNEHQ----LKRLHMILKPFMLRR 229
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
 725-962 3.07e-63

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. CHD2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350812 [Multi-domain]  Cd Length: 237  Bit Score: 215.64  E-value: 3.07e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  725 VEKQSSLL--VNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIVPLSTLSNWV 802
Cdd:cd18054      7 LKKQPSYIggENLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQ 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  803 YEFDKWAPSVVKVSYKGSPAARRAFV------PQLRSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKL 876
Cdd:cd18054     87 REFEIWAPEINVVVYIGDLMSRNTIReyewihSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  877 TQVLnTHYLAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQwfnapfaMTGEKVDLNEEEtiliirrLHKVLR 956
Cdd:cd18054    167 YKTL-IDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEE-------DHGKGRENGYQS-------LHKVLE 231


                   ....*.
gi 1977155862  957 PFLLRR 962
Cdd:cd18054    232 PFLLRR 237
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
 733-964 2.09e-62

DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350770 [Multi-domain]  Cd Length: 218  Bit Score: 212.43  E-value: 2.09e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  733 VNGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRiNGPFLIIVPLSTLSNWVYEFDKWAPSV 812
Cdd:cd18012      1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGR-KGPSLVVAPTSLIYNWEEEAAKFAPEL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  813 VKVSYKGSPAARRAfvpQLRSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQV---LNTHYlaprR 889
Cdd:cd18012     80 KVLVIHGTKRKREK---LRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAvkaLKADH----R 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1977155862  890 ILLTGTPLQNKLPELWALLNFLLPTIFKScstfEQWFNAPFAMTGEKvDLNEEEtiliIRRLHKVLRPFLLRRLK 964
Cdd:cd18012    153 LALTGTPIENHLGELWSIFDFLNPGLLGS----YKRFKKRFAKPIEK-DGDEEA----LEELKKLISPFILRRLK 218
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
 1373-1479 1.19e-61

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: 205.74  E-value: 1.19e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1373 LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1452
Cdd:cd05516      2 LTKKMNKIVDVVIKYKDSD-GRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQ 80

                           90       100
                   ....*....|....*....|....*..
gi 1977155862 1453 TFNLEGSLIYEDSIVLQSVFTSVRQKI 1479
Cdd:cd05516     81 TFNLEGSLIYEDSIVLQSVFKSARQKI 107
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 737-962 4.23e-59

DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, also known as ALC1) is involved in DNA repair by regulating chromatin relaxation following DNA damage. CHD1L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350764 [Multi-domain]  Cd Length: 216  Bit Score: 203.05  E-value: 4.23e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 816
Cdd:cd18006      1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  817 YKGSPAARRAFVPQLRS-GKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYLaPRRILLTGT 895
Cdd:cd18006     81 YMGDKEKRLDLQQDIKStNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSV-DFRLLLTGT 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1977155862  896 PLQNKLPELWALLNFLLPTIFkSCSTFEQWFNApFAMTGEKVDLNEEetiliirrLHKVLRPFLLRR 962
Cdd:cd18006    160 PIQNSLQELYALLSFIEPNVF-PKDKLDDFIKA-YSETDDESETVEE--------LHLLLQPFLLRR 216
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 1026-1152 1.77e-57

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 195.00  E-value: 1.77e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1026 SGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRNFKYLRLDGTTKAEDRGMLLKAFNDPaSQYFVFLLSTRA 1105
Cdd:cd18793     10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDIRVFLLSTKA 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1977155862 1106 GGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLC 1152
Cdd:cd18793     89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
 737-962 1.14e-56

DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD3, CHD4, and CHD5 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350752 [Multi-domain]  Cd Length: 196  Bit Score: 195.35  E-value: 1.14e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 816
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  817 YKGSpaarrafvpqlrsgkfNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYLApRRILLTGTP 896
Cdd:cd17994     81 YVGD----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIG-YKLLLTGTP 143

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1977155862  897 LQNKLPELWALLNFLLPTIFKSCSTFeqwfnapfamTGEKVDLNEEETiliIRRLHKVLRPFLLRR 962
Cdd:cd17994    144 LQNNLEELFHLLNFLTPERFNNLQGF----------LEEFADISKEDQ---IKKLHDLLGPHMLRR 196
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
 737-916 1.35e-53

DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 (SMARCAD1, also known as ATP-dependent helicase 1 or Hel1) possesses intrinsic ATP-dependent nucleosome-remodeling activity and is required for both DNA repair and heterochromatin organization. SMARCAD1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350756 [Multi-domain]  Cd Length: 187  Bit Score: 186.05  E-value: 1.35e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEyKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 816
Cdd:cd17998      1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKE-IGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  817 YKGSPAARRafvpQLR------SGKFNALLTTYEYII---KDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYLAP 887
Cdd:cd17998     80 YYGSQEERK----HLRydilkgLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMT-INAN 154

                          170       180
                   ....*....|....*....|....*....
gi 1977155862  888 RRILLTGTPLQNKLPELWALLNFLLPTIF 916
Cdd:cd17998    155 FRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
 736-962 1.21e-50

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350811 [Multi-domain]  Cd Length: 237  Bit Score: 179.48  E-value: 1.21e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  736 QLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKV 815
Cdd:cd18053     20 ELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  816 SYKGSPAARRAFV------PQLRSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYLAPRR 889
Cdd:cd18053    100 VYLGDINSRNMIRthewmhPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTL-IDFKSNHR 178

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1977155862  890 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQwfnapfaMTGEKVDLNEEEtiliirrLHKVLRPFLLRR 962
Cdd:cd18053    179 LLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEE-------EHGKGREYGYAS-------LHKELEPFLLRR 237
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
 737-962 1.95e-50

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; Chromodomain-helicase-DNA-binding protein 6 (CHD6) is a DNA-dependent ATPase that plays a role in chromatin remodeling. It regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. It activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2.2 and acts as a transcriptional repressor of different viruses including influenza virus or papillomavirus. During influenza virus infection, the viral polymerase complex localizes CHD6 to inactive chromatin where it gets degraded in a proteasome independent-manner. CHD6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350816 [Multi-domain]  Cd Length: 222  Bit Score: 178.31  E-value: 1.95e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIaliTYLME--YKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVK 814
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSI---TFLSEifLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  815 VsYKGSPAARRAFV------------PQLRSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLNT 882
Cdd:cd18058     78 V-YHGSQISRQMIQqyemyyrdeqgnPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  883 HYLApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 962
Cdd:cd18058    157 MALE-HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFG----------DLKTEEQ---VKKLQSILKPMMLRR 222
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
 737-913 2.38e-49

DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, also known Cockayne syndrome group B (CSB), Rad26 in Saccharomyces cerevisiae, and Rhp26 in Schizosaccharomyces pombe) is a DNA-binding protein that is important in transcription-coupled excision repair. ERCC6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350758 [Multi-domain]  Cd Length: 193  Bit Score: 174.05  E-value: 2.38e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIVPLSTLSNWVYEFDKWAP------ 810
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPpfrvvv 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  811 ------SVVKVSYKGSPAARRAFVPQLRsGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQV---LN 881
Cdd:cd18000     81 lhssgsGTGSEEKLGSIERKSQLIRKVV-GDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLAckqLR 159

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1977155862  882 ThylaPRRILLTGTPLQNKLPELWALLNFLLP 913
Cdd:cd18000    160 T----PHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
 737-962 3.31e-49

DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in eukaryotes) regulates transcription in association with TATA binding protein (TBP). Mot1, Ino80C, and NC2 function coordinately to regulate pervasive transcription in yeast and mammals. Mot1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350757 [Multi-domain]  Cd Length: 232  Bit Score: 175.23  E-value: 3.31e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALItYLMEYKR------INGPFLIIVPLSTLSNWVYEFDKWAP 810
Cdd:cd17999      1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCIL-ASDHHKRansfnsENLPSLVVCPPTLVGHWVAEIKKYFP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  811 SVVK--VSYKGSPAARRAFVPQLrsGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYLAPR 888
Cdd:cd17999     80 NAFLkpLAYVGPPQERRRLREQG--EKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAV-KQLKANH 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1977155862  889 RILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVD--LNEEETILIIRRLHKVLRPFLLRR 962
Cdd:cd17999    157 RLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKAsaKEQEAGALALEALHKQVLPFLLRR 232
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
 737-962 5.87e-49

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; Chromodomain-helicase-DNA-binding protein 7 (CHD7) is a probable transcription regulator. It may be involved in the 45S precursor rRNA production. CHD7 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350817 [Multi-domain]  Cd Length: 222  Bit Score: 174.06  E-value: 5.87e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALItYLMEYKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVkVS 816
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNV-VV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  817 YKGSPAARRAFV--------PQLR----SGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHY 884
Cdd:cd18059     79 YHGSQASRRTIQlyemyfkdPQGRvikgSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1977155862  885 LApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 962
Cdd:cd18059    159 LE-HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
 737-962 5.88e-49

DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint helicase (ERCC6L, also known as RAD26L) is an essential component of the mitotic spindle assembly checkpoint, by acting as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. ERCC6L is proposed to stimulate cancer cell proliferation by promoting cell cycle through a way of RAB31-MAPK-CDK2. ERCC6L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350759 [Multi-domain]  Cd Length: 232  Bit Score: 174.48  E-value: 5.88e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPfLIIVPLSTLSNWVYEFDKWAPSV-VKV 815
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSV-LVVMPTSLIPHWVKEFAKWTPGLrVKV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  816 SYKGSPAARRAfvpQLRS--GKFNALLTTYEYIIKDKQVLA-----KIRWKYMIVDEGHRMKNHHCKLTQVLntHYL-AP 887
Cdd:cd18001     80 FHGTSKKERER---NLERiqRGGGVLLTTYGMVLSNTEQLSaddhdEFKWDYVILDEGHKIKNSKTKSAKSL--REIpAK 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1977155862  888 RRILLTGTPLQNKLPELWALLNFLLP-TIFKSCSTFEQWFNAPFAMTGEKVDLNEEETI--LIIRRLHKVLRPFLLRR 962
Cdd:cd18001    155 NRIILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENPITRGRDKDATQGEKALgsEVAENLRQIIKPYFLRR 232
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
 737-962 2.03e-48

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; Chromodomain-helicase-DNA-binding protein 8 (CHD8) is a DNA helicase that acts as a chromatin remodeling factor and regulates transcription. It also acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. It suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity and of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. It also acts as a negative regulator of Wnt signaling pathway and CTNNB1-targeted gene expression. CHD8 is also involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. It also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. CHD8 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350818 [Multi-domain]  Cd Length: 222  Bit Score: 172.55  E-value: 2.03e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKrINGPFLIIVPLSTLSNWVYEFDKWApSVVKVS 816
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVG-IHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  817 YKGSPAARRA--------------FVPQlrSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLNt 882
Cdd:cd18060     79 YHGSLASRQMiqqyemyckdsrgrLIPG--AYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLK- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  883 HYLAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 962
Cdd:cd18060    156 HMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
 737-962 2.21e-48

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. CHD3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350813 [Multi-domain]  Cd Length: 232  Bit Score: 172.89  E-value: 2.21e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 816
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  817 YKGSPAAR-------------------RAFVPQLRSG-KFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKL 876
Cdd:cd18055     81 YTGDKDSRaiirenefsfddnavkggkKAFKMKREAQvKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  877 TQVLNThYLAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgekVDLNEEETiliIRRLHKVLR 956
Cdd:cd18055    161 FRVLNG-YKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF----------ADISKEDQ---IKKLHDLLG 226


                   ....*.
gi 1977155862  957 PFLLRR 962
Cdd:cd18055    227 PHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
 737-962 6.03e-48

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350815 [Multi-domain]  Cd Length: 232  Bit Score: 171.79  E-value: 6.03e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 816
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  817 YKGSPAARRAFVPQ--------LRSG------------KFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKL 876
Cdd:cd18057     81 YTGDKESRSVIRENefsfednaIRSGkkvfrmkkeaqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  877 TQVLNThYLAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgekVDLNEEETiliIRRLHKVLR 956
Cdd:cd18057    161 FRVLNS-YKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF----------ADISKEDQ---IKKLHDLLG 226


                   ....*.
gi 1977155862  957 PFLLRR 962
Cdd:cd18057    227 PHMLRR 232
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
 737-962 2.07e-47

DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350763 [Multi-domain]  Cd Length: 245  Bit Score: 170.64  E-value: 2.07e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALIT-----------------YLMEYKRIN---GPFLIIVPLS 796
Cdd:cd18005      1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAavlgktgtrrdrennrpRFKKKPPASsakKPVLIVAPLS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  797 TLSNWVYEFDKWAPSVVKVsYKGSpaaRRAFVPQLR--SGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHC 874
Cdd:cd18005     81 VLYNWKDELDTWGHFEVGV-YHGS---RKDDELEGRlkAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  875 KLTQVLNThYLAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPF----AMTGEKVDLNEEETilIIRR 950
Cdd:cd18005    157 KLTQAMKE-LKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIkrgqRHTATARELRLGRK--RKQE 233

                          250
                   ....*....|..
gi 1977155862  951 LHKVLRPFLLRR 962
Cdd:cd18005    234 LAVKLSKFFLRR 245
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
 737-962 1.62e-45

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. CHD4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350814 [Multi-domain]  Cd Length: 232  Bit Score: 164.85  E-value: 1.62e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 816
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  817 YKGSPAArRAFVPQ---------LRSG------------KFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCK 875
Cdd:cd18056     81 YVGDKDS-RAIIREnefsfednaIRGGkkasrmkkeasvKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  876 LTQVLNTHYLApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgekVDLNEEETiliIRRLHKVL 955
Cdd:cd18056    160 FFRVLNGYSLQ-HKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEF----------ADIAKEDQ---IKKLHDML 225


                   ....*..
gi 1977155862  956 RPFLLRR 962
Cdd:cd18056    226 GPHMLRR 232
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
 737-962 3.68e-44

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; Chromodomain-helicase-DNA-binding protein 9 (CHD9) acts as a transcriptional coactivator for PPARA and possibly other nuclear receptors. It is proposed to be a ATP-dependent chromatin remodeling protein. CHD9 has DNA-dependent ATPase activity and binds to A/T-rich DNA. It also associates with A/T-rich regulatory regions in promoters of genes that participate in the differentiation of progenitors during osteogenesis. CHD9 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350819 [Multi-domain]  Cd Length: 222  Bit Score: 160.56  E-value: 3.68e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTialITYLMEYKR--INGPFLIIVPLSTLSNWVYEFDKWAPSVVk 814
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQS---ITFLYEILLtgIRGPFLIIAPLSTIANWEREFRTWTDLNV- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  815 VSYKGSPAARRAFV--------PQLR----SGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLNT 882
Cdd:cd18061     77 VVYHGSLISRQMIQqyemyfrdSQGRiirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  883 HYLApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 962
Cdd:cd18061    157 MNLE-HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
 737-962 2.49e-41

DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350762 [Multi-domain]  Cd Length: 240  Bit Score: 152.83  E-value: 2.49e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVS--LYNNNLNG---ILADEMGLGKTIQTIALITYLMEYKRINGP----FLIIVPLSTLSNWVYEFDK 807
Cdd:cd18004      1 LRPHQREGVQFLYDclTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  808 WAPSVVK--VSYKGSPAARRAFVPQLRSGK-FNALLTTYE-YIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLNTh 883
Cdd:cd18004     81 WLGLRRIkvVTADGNAKDVKASLDFFSSAStYPVLIISYEtLRRHAEKLSKKISIDLLICDEGHRLKNSESKTTKALNS- 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  884 YLAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvDLNEEETILIIRRLH---KVLRPFLL 960
Cdd:cd18004    160 LPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDP-DASEEDKELGAERSQelsELTSRFIL 238


                   ..
gi 1977155862  961 RR 962
Cdd:cd18004    239 RR 240
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
 737-962 2.98e-40

DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350766 [Multi-domain]  Cd Length: 241  Bit Score: 149.75  E-value: 2.98e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSLynnnlNGILADEMGLGKTIQTIALI-----------------TYLMEYKRINGPFLIIVPLSTLS 799
Cdd:cd18008      1 LLPYQKQGLAWMLPR-----GGILADEMGLGKTIQALALIlatrpqdpkipeeleenSSDPKKLYLSKTTLIVVPLSLLS 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  800 NWVYEFDK-WAPSVVKVS-YKGSPAARRAFVPQlrsgKFNALLTTY-----EY-----------IIKDKQVLAKIRWKYM 861
Cdd:cd18008     76 QWKDEIEKhTKPGSLKVYvYHGSKRIKSIEELS----DYDIVITTYgtlasEFpknkkgggrdsKEKEASPLHRIRWYRV 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  862 IVDEGHRMKNHHCKLTQV---LNTHylapRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvd 938
Cdd:cd18008    152 ILDEAHNIKNRSTKTSRAvcaLKAE----RRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRK-- 225

                          250       260
                   ....*....|....*....|....
gi 1977155862  939 lneeetilIIRRLHKVLRPFLLRR 962
Cdd:cd18008    226 --------ALERLQALLKPILLRR 241
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
 737-950 2.27e-37

DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) which is involved in transcriptional regulation and chromatin remodeling, and ARIP4 (also called androgen receptor-interacting protein 4, RAD54 like 2 or RAD54L2) which modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350765 [Multi-domain]  Cd Length: 239  Bit Score: 141.66  E-value: 2.27e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLE--W--LVSLYNNNLNG---ILADEMGLGKTIQTIALI-TYLMEYKRINGPfLIIVPLSTLSNWVYEFDKW 808
Cdd:cd18007      1 LKPHQVEGVRflWsnLVGTDVGSDEGggcILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDEFKKW 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  809 APSVVkVSYKGSPAARRAFVPQLRSGKFNA-------LLTTYEY---IIKDKQVLAKIRWKYM-----------IVDEGH 867
Cdd:cd18007     80 LPPDL-RPLLVLVSLSASKRADARLRKINKwhkeggvLLIGYELfrnLASNATTDPRLKQEFIaalldpgpdllVLDEGH 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  868 RMKNHHCKLTQVLNTHYlAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAmTGEKVDLNEEETILI 947
Cdd:cd18007    159 RLKNEKSQLSKALSKVK-TKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIE-AGQCVDSTEEDVRLM 236


                   ...
gi 1977155862  948 IRR 950
Cdd:cd18007    237 LKR 239
BROMO smart00297
bromo domain;
1371-1479 2.22e-31

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 119.31  E-value: 2.22e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  1371 PNLTKKMKKIVDAVIKYKDSssgRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQN 1450
Cdd:smart00297    2 PKLQKKLQELLKAVLDKLDS---HPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78

                            90       100
                    ....*....|....*....|....*....
gi 1977155862  1451 AQTFNLEGSLIYEDSIVLQSVFTSVRQKI 1479
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
DEXDc smart00487
DEAD-like helicases superfamily;
736-925 3.12e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 122.60  E-value: 3.12e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862   736 QLKQYQIKGLEWLvslYNNNLNGILADEMGLGKTIQ-TIALITYLMEYKriNGPFLIIVPLSTL-SNWVYEFDKWAPS-V 812
Cdd:smart00487    8 PLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGK--GGRVLVLVPTRELaEQWAEELKKLGPSlG 82

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862   813 VKVSYKGSPAARRAFVPQLRSGKFNALLTTYEYIIKD--KQVLAKIRWKYMIVDEGHRMKN--HHCKLTQVLNTHYLAPR 888
Cdd:smart00487   83 LKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKNVQ 162

                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 1977155862   889 RILLTGTPLQNKLPELWALLN--FLLPTIFKSCSTFEQW 925
Cdd:smart00487  163 LLLLSATPPEEIENLLELFLNdpVFIDVGFTPLEPIEQF 201
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
 737-962 1.19e-30

DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as HIP116 or SMARCA3) has both helicase and E3 ubiquitin ligase activities and ATP-dependent nucleosome-remodeling activity. HLTF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350829 [Multi-domain]  Cd Length: 239  Bit Score: 122.19  E-value: 1.19e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSLYNNNL-----------------------------NGILADEMGLGKTIQTIALItylmeykrING 787
Cdd:cd18071      1 LLPHQKQALAWMVSRENSQDlppfweeavglflntitnfsqkkrpelvrGGILADDMGLGKTLTTISLI--------LAN 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  788 PFLIIVPLSTLSNWVYEF-DKWAPSVVKV-SYKGspAARRAFVPQLrsGKFNALLTTY-----EYIIKDKQVLAKIRWKY 860
Cdd:cd18071     73 FTLIVCPLSVLSNWETQFeEHVKPGQLKVyTYHG--GERNRDPKLL--SKYDIVLTTYntlasDFGAKGDSPLHTINWLR 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  861 MIVDEGHRMKNHHCKLTQ-VLNTHylAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMtGEKVDL 939
Cdd:cd18071    149 VVLDEGHQIRNPNAQQTKaVLNLS--SERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTM-GDPTGL 225

                          250       260
                   ....*....|....*....|...
gi 1977155862  940 neeetiliiRRLHKVLRPFLLRR 962
Cdd:cd18071    226 ---------KRLQVLMKQITLRR 239
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
 1373-1477 4.95e-30

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: 115.48  E-value: 4.95e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1373 LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1452
Cdd:cd05515      1 MQQKLWELYNAVKNYTDGR-GRRLSLIFMRLPSKSEYPDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNAC 79

                           90       100
                   ....*....|....*....|....*
gi 1977155862 1453 TFNLEGSLIYEDSIVLQSVFTSVRQ 1477
Cdd:cd05515     80 KYNEPDSQIYKDALTLQKVLLETKR 104
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
 737-962 1.76e-29

DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as RDH54, binds to double-stranded DNA, displays ATPase activity in the presence of DNA, and may have a role in meiotic and mitotic recombination. RAD54B is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350824 [Multi-domain]  Cd Length: 235  Bit Score: 118.79  E-value: 1.76e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSL-----YNNNLNGILADEMGLGKTIQTIALITYLMEykriNGPF---------LIIVPLSTLSNWV 802
Cdd:cd18066      1 LRPHQREGIEFLYECvmgmrVNERFGAILADEMGLGKTLQCISLIWTLLR----QGPYggkpvikraLIVTPGSLVKNWK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  803 YEFDKWAPSV-VKVSYKGSPAARRAFVpqlRSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVLn 881
Cdd:cd18066     77 KEFQKWLGSErIKVFTVDQDHKVEEFI---ASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTAL- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  882 THYLAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIR--RLHKVLRPFL 959
Cdd:cd18066    153 TSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARaaELTRLTGLFI 232


                   ...
gi 1977155862  960 LRR 962
Cdd:cd18066    233 LRR 235
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 1027-1141 1.37e-28

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: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 111.53  E-value: 1.37e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1027 GKFELLDRILPKLRatNHKVLLFCQMTSlmTIMEDYFAYR-NFKYLRLDGTTKAEDRGMLLKAFNDPASQyfvFLLSTRA 1105
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKK--TLEAELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1977155862 1106 GGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIG 1141
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
 1373-1475 7.02e-28

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: 109.35  E-value: 7.02e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1373 LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1452
Cdd:cd05519      1 LKAAMLEIYDAVLNCEDET-GRKLSELFLEKPSKKLYPDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANAR 79

                           90       100
                   ....*....|....*....|...
gi 1977155862 1453 TFNLEGSLIYEDSIVLQSVFTSV 1475
Cdd:cd05519     80 TYNQEGSIVYEDAVEMEKAFKKK 102
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
 1373-1472 9.41e-28

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


Pssm-ID: 99922 [Multi-domain]  Cd Length: 99  Bit Score: 108.61  E-value: 9.41e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1373 LTKKMKKIVDAVIKYKdsssgRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1452
Cdd:cd04369      1 LKKKLRSLLDALKKLK-----RDLSEPFLEPVDPKEAPDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAK 75

                           90       100
                   ....*....|....*....|
gi 1977155862 1453 TFNLEGSLIYEDSIVLQSVF 1472
Cdd:cd04369     76 TYNGPGSPIYKDAKKLEKLF 95
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 737-950 4.77e-27

DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a like 1, also known as HARP) is recruited to stalled replication forks to promote repair and helps restart replication. It plays a role in DNA repair, telomere maintenance and replication fork stability in response to DNA replication stress. Mutations cause Schimke Immunoosseous Dysplasia. SMARCAL1 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350768 [Multi-domain]  Cd Length: 213  Bit Score: 110.76  E-value: 4.77e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSlynNNLNGILADEMGLGKTIQTIALITYLmeykRINGPFLIIVPLSTLSNWVYEFDKWAPSV---- 812
Cdd:cd18010      1 LLPFQREGVCFALR---RGGRVLIADEMGLGKTVQAIAIAAYY----REEWPLLIVCPSSLRLTWADEIERWLPSLppdd 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  813 VKVSYKGSPAARRafvpqlRSGKFNalLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQV---LNTHylAPRR 889
Cdd:cd18010     74 IQVIVKSKDGLRD------GDAKVV--IVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAalpLLKR--AKRV 143

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  890 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTF-EQWFNA----PFAMTGEKVDLNEEETILI----IRR 950
Cdd:cd18010    144 ILLSGTPALSRPIELFTQLDALDPKLFGRFHDFgRRYCAAkqggFGWDYSGSSNLEELHLLLLatimIRR 213
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
 737-962 2.56e-26

DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as RAD54L or RAD54, plays a role in homologous recombination related repair of DNA double-strand breaks. RAD54A is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350825 [Multi-domain]  Cd Length: 243  Bit Score: 109.87  E-value: 2.56e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWL----VSLYNNNLNG-ILADEMGLGKTIQTIALITYLM----EYKRINGPFLIIVPLSTLSNWVYEFDK 807
Cdd:cd18067      1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLrqspQCKPEIDKAIVVSPSSLVKNWANELGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  808 W-----APSVV--KVSYKGSPAARRAFVPQLRSGKFNALLTTYEYIIKDKQVLAKIRWKYMIVDEGHRMKNHHCKLTQVL 880
Cdd:cd18067     81 WlggrlQPLAIdgGSKKEIDRKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  881 NThYLAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETILIIRRLHK---VLRP 957
Cdd:cd18067    161 DS-LNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPI-LKGRDADASEKERQLGEEKLQElisIVNR 238


                   ....*
gi 1977155862  958 FLLRR 962
Cdd:cd18067    239 CIIRR 243
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
 737-950 8.98e-25

DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called RAD54 like 2 or RAD54L2 ) modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. ARIP4 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350827 [Multi-domain]  Cd Length: 227  Bit Score: 104.90  E-value: 8.98e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLvslYNN------------NLNGILADEMGLGKTIQTIALITYLMEYKRINgPFLIIVPLSTLSNWVYE 804
Cdd:cd18069      1 LKPHQIGGIRFL---YDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDVLLRHTGAK-TVLAIVPVNTLQNWLSE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  805 FDKWAPSVVKVSyKGSPAARRAFVPQLRSGKFNALLTTYEYIIKDKQVL----AKIRWK----YMIVDEGHRMKNHHCKL 876
Cdd:cd18069     77 FNKWLPPPEALP-NVRPRPFKVFILNDEHKTTAARAKVIEDWVKDGGVLlmgyEMFRLRpgpdVVICDEGHRIKNCHAST 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1977155862  877 TQVLNtHYLAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETILIIRR 950
Cdd:cd18069    156 SQALK-NIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPI-LNGQCVDSTPQDVKLMRYR 227
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
 1375-1471 2.26e-24

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 [Multi-domain]  Cd Length: 103  Bit Score: 99.44  E-value: 2.26e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1375 KKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTF 1454
Cdd:cd05518      3 KRMLALFLYVLEYREGS-GRRLCDLFMEKPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHY 81

                           90
                   ....*....|....*..
gi 1977155862 1455 NLEGSLIYEDSIVLQSV 1471
Cdd:cd05518     82 NEEGSQVYEDANILEKV 98
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
 1236-1303 4.13e-24

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: 464219 [Multi-domain]  Cd Length: 69  Bit Score: 97.33  E-value: 4.13e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1977155862 1236 DRRREEARNPK-RKPRLMEEDELPTWIMKDDAEVERLTCEEEEEKMFGRGSRQRKEVDYSDSLTEKQWL 1303
Cdd:pfam14619    1 ERRREEAEQLPpLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
HSA smart00573
domain in helicases and associated with SANT domains;
465-537 1.25e-23

domain in helicases and associated with SANT domains;


Pssm-ID: 214727 [Multi-domain]  Cd Length: 73  Bit Score: 95.93  E-value: 1.25e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1977155862   465 QKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERMRRLMA 537
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
 1380-1473 1.48e-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: 96.74  E-value: 1.48e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1380 IVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGS 1459
Cdd:cd05517      8 LLEAVMTATDPS-GRLISELFQKLPSKVLYPDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFNEPGS 86

                           90
                   ....*....|....
gi 1977155862 1460 LIYEDSIVLQSVFT 1473
Cdd:cd05517     87 QVYKDANAIKKIFT 100
HELICc smart00490
helicase superfamily c-terminal domain;
1058-1141 2.56e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 92.66  E-value: 2.56e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  1058 IMEDYFAYRNFKYLRLDGTTKAEDRGMLLKAFNDPASQyfvFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRA 1137
Cdd:smart00490    2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78


                    ....
gi 1977155862  1138 HRIG 1141
Cdd:smart00490   79 GRAG 82
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
 1380-1479 2.08e-21

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 [Multi-domain]  Cd Length: 113  Bit Score: 91.24  E-value: 2.08e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1380 IVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGS 1459
Cdd:cd05524     10 LYDTIRNYKSED-GRILCESFIRVPKRRNEPEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDS 88

                           90       100
                   ....*....|....*....|
gi 1977155862 1460 LIYEDSIVLQSVFTSVRQKI 1479
Cdd:cd05524     89 PEHKDACKLWELFLSARNEV 108
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
 1392-1474 6.08e-21

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: 89.32  E-value: 6.08e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1392 SGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSV 1471
Cdd:cd05520     19 QGQLLAEPFLKLPSKRKYPDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIYKDAEKLQKL 98


                   ...
gi 1977155862 1472 FTS 1474
Cdd:cd05520     99 MQA 101
HSA pfam07529
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ...
 466-532 6.96e-21

HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. This region does not form a compact domain in the known structures.


Pssm-ID: 462194 [Multi-domain]  Cd Length: 67  Bit Score: 88.01  E-value: 6.96e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1977155862  466 KIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERM 532
Cdd:pfam07529    1 RDEPERREKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQKRIEREEKQRL 67
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
 737-962 3.97e-20

DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called Forkhead-box E1/FOXE1 ) is a transcription termination factor that couples ATP hydrolysis with the removal of RNA polymerase II from the DNA template. Single nucleotide polymorphism (SNP) within the 5'-UTR of TTF2 is associated with thyroid cancer risk.TTF2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 91.77  E-value: 3.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSLYNNNLNG-ILADEMGLGKTIQTIALITYLMEYKR----------------------INGPFLIIV 793
Cdd:cd18072      1 LLLHQKQALAWLLWRERQKPRGgILADDMGLGKTLTMIALILAQKNTQNrkeeekekalteweskkdstlvPSAGTLVVC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  794 PLSTLSNWVYEFD-KWAPSVVKV-SYKGSPAARRAFVpqLRSgkFNALLTTYEYIIK----DKQ-----VLAKIRWKYMI 862
Cdd:cd18072     81 PASLVHQWKNEVEsRVASNKLRVcLYHGPNRERIGEV--LRD--YDIVITTYSLVAKeiptYKEesrssPLFRIAWARII 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  863 VDEGHRMKNHH-------CKLtqvlNTHYlaprRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGE 935
Cdd:cd18072    157 LDEAHNIKNPKvqasiavCKL----RAHA----RWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGGE 228

                          250       260
                   ....*....|....*....|....*..
gi 1977155862  936 kvdlneeetiliirRLHKVLRPFLLRR 962
Cdd:cd18072    229 --------------RLNILTKSLLLRR 241
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
 759-916 6.16e-20

DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 90.04  E-value: 6.16e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  759 ILADEMGLGKTIQTIALITYLM---EYKRIngpfLIIVPLSTLSNW-VYEFDK-WAPSVVKVSYKGSPAARRAFVPQLRs 833
Cdd:cd18011     21 LLADEVGLGKTIEAGLIIKELLlrgDAKRV----LILCPASLVEQWqDELQDKfGLPFLILDRETAAQLRRLIGNPFEE- 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  834 gkFNALLTTYEYI---IKDKQVLAKIRWKYMIVDEGHRMKNHHC-------KLTQVLNTHylAPRRILLTGTPLQNKLPE 903
Cdd:cd18011     96 --FPIVIVSLDLLkrsEERRGLLLSEEWDLVVVDEAHKLRNSGGgketkryKLGRLLAKR--ARHVLLLTATPHNGKEED 171

                          170
                   ....*....|...
gi 1977155862  904 LWALLNFLLPTIF 916
Cdd:cd18011    172 FRALLSLLDPGRF 184
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
 758-950 7.58e-20

DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) is involved in transcriptional regulation and chromatin remodeling. Mutations in humans cause mental retardation, X-linked, syndromic, with hypotonic facies 1 (MRXSHF1) and alpha-thalassemia myelodysplasia syndrome (ATMDS). ATRX is part of the a DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350826 [Multi-domain]  Cd Length: 246  Bit Score: 91.10  E-value: 7.58e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  758 GILADEMGLGKTIQTIALI-TYLMEYKRIN-GPFLIIVPLSTLSNWVYEFDKWA-----PSVVKV----SYKGSPaaRRA 826
Cdd:cd18068     31 CILAHCMGLGKTLQVVTFLhTVLLCEKLENfSRVLVVCPLNTVLNWLNEFEKWQeglkdEEKIEVnelaTYKRPQ--ERS 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  827 FVPQLRSGKFNALLTTYEYI--------IKDKQVLAKIRWKYM--------IVDEGHRMKNHHCKLTQVLNThYLAPRRI 890
Cdd:cd18068    109 YKLQRWQEEGGVMIIGYDMYrilaqernVKSREKLKEIFNKALvdpgpdfvVCDEGHILKNEASAVSKAMNS-IRTKRRI 187

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  891 LLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAmTGEKVDLNEEETILIIRR 950
Cdd:cd18068    188 VLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQ-NGQCADSTLVDVRVMKKR 246
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
 1377-1465 2.77e-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: 425683 [Multi-domain]  Cd Length: 84  Bit Score: 83.90  E-value: 2.77e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1377 MKKIVDAVIKykdsssgRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNL 1456
Cdd:pfam00439    1 CLEILDKLME-------HPIAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNG 73


                   ....*....
gi 1977155862 1457 EGSLIYEDS 1465
Cdd:pfam00439   74 PGSVIYKAA 82
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
 1345-1479 2.50e-17

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 86.01  E-value: 2.50e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1345 SREKDDENKKQKKRGRPPAEKLSPNPPN--LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDF 1422
Cdd:COG5076    113 TPESGLGSLLMAHLKTSVKKRKTPKIEDelLYADNKAIAKFKKQLFLRD-GRFLSSIFLGLPSKREYPDYYEIIKSPMDL 191

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1977155862 1423 KKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKI 1479
Cdd:COG5076    192 LTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEI 248
Bromo_Rsc1_2_I cd05521
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
 1373-1470 3.42e-17

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: 78.90  E-value: 3.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1373 LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNhkYRSLNDLEKDVMLLCQNAQ 1452
Cdd:cd05521      2 LSKKLKPLYDGIYTLKEEN-GIEIHPIFNVLPLRKDYPDYYKIIKNPLSLNTVKKRLPH--YTNAQEFVNDLAQIPWNAR 78

                           90
                   ....*....|....*...
gi 1977155862 1453 TFNLEGSLIYEDSIVLQS 1470
Cdd:cd05521     79 LYNTKGSVIYKYALILEK 96
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
 599-642 1.19e-16

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


Pssm-ID: 462196  Cd Length: 44  Bit Score: 75.24  E-value: 1.19e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1977155862  599 QMSDLPVKVIHVDSGKILTGADAPKAGQLDAWLEMNPGYEVAPR 642
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
BRK smart00592
domain in transcription and CHROMO domain helicases;
600-644 2.85e-16

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 74.31  E-value: 2.85e-16
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 1977155862   600 MSDLPVKVIHVDSGKILTGADAPKAGQLDAWLEMNPGYEVAPRSD 644
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
 1376-1475 3.46e-16

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 [Multi-domain]  Cd Length: 104  Bit Score: 75.74  E-value: 3.46e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1376 KMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFN 1455
Cdd:cd05522      5 RIKNILKGLRKERDEN-GRLLTLHFEKLPDKAREPEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYN 83

                           90       100
                   ....*....|....*....|
gi 1977155862 1456 LEGSLIYEDSIVLQSVFTSV 1475
Cdd:cd05522     84 ENDSQEYKDAVLLEKEARLL 103
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
 737-927 8.74e-15

DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 75.46  E-value: 8.74e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVSlynNNLNGILADeMGLGKTIQTIALITYLMEYKRInGPFLIIVPLSTLSN-WVYEFDKW-APSVVK 814
Cdd:cd18013      1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTVTTLTALSDLQLDDFT-RRVLVIAPLRVARStWPDEVEKWnHLRNLT 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  815 VSYK-GSPAARRafvpqlRSGKFNALLTTYEY-IIKDKQVLAKIRWKY--MIVDEGHRMKNHHCKLTQVLNTH-YLAPRR 889
Cdd:cd18013     76 VSVAvGTERQRS------KAANTPADLYVINReNLKWLVNKSGDPWPFdmVVIDELSSFKSPRSKRFKALRKVrPVIKRL 149

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1977155862  890 ILLTGTPLQNKLPELWALLNFL--LPTIFKSCSTF-EQWFN 927
Cdd:cd18013    150 IGLTGTPSPNGLMDLWAQIALLdqGERLGRSITAYrERWFD 190
QLQ pfam08880
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ...
 165-199 2.05e-14

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: 462622  Cd Length: 35  Bit Score: 68.52  E-value: 2.05e-14
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1977155862  165 PFNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQ 199
Cdd:pfam08880    1 PFTPAQLQELRAQILAYKYLSRNQPVPPELQQAIF 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1676-1710 4.30e-14

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 67.66  E-value: 4.30e-14
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1977155862 1676 CSSLEFQCGSGECVHQKWLCDGTNDCRDHSDETNC 1710
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
 737-911 5.86e-14

DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously expressed protein that contains motifs characteristic of several DNA repair proteins, transcription factors, and helicases. SHPRH is a functional homolog of S. cerevisiae RAD5 and is involved in DNA repair. SHPRH is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 73.92  E-value: 5.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLEWLVslynnNLNGILADEMGLGKTIQTIALI------------TYLMEYKRIN-------------GPFLI 791
Cdd:cd18070      1 LLPYQRRAVNWML-----VPGGILADEMGLGKTVEVLALIllhprpdndldaADDDSDEMVCcpdclvaetpvssKATLI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  792 IVPLSTLSNWVYEFDKWAPSVVKVS-YKGspaARRAFVPQLRSGKFNA----LLTTYEYIIKD----------------- 849
Cdd:cd18070     76 VCPSAILAQWLDEINRHVPSSLKVLtYQG---VKKDGALASPAPEILAeydiVVTTYDVLRTElhyaeanrsnrrrrrqk 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1977155862  850 -----KQVLAKIRWKYMIVDEghrMKNHHCKLTQVLNTHYLAPR--RILLTGTPLQNKLPELWALLNFL 911
Cdd:cd18070    153 ryeapPSPLVLVEWWRVCLDE---AQMVESSTSKAAEMARRLPRvnRWCVSGTPIQRGLDDLFGLLSFL 218
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1676-1710 1.00e-13

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 66.46  E-value: 1.00e-13
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1977155862 1676 CSSLEFQCGSGECVHQKWLCDGTNDCRDHSDETNC 1710
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1714-1749 1.70e-13

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 66.12  E-value: 1.70e-13
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1977155862 1714 TCRPDEFQCNDGTCIHGSRQCDREYDCKDLSDELGC 1749
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
 1376-1472 7.41e-13

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 [Multi-domain]  Cd Length: 101  Bit Score: 66.42  E-value: 7.41e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1376 KMKKIVDAVIKYKDSSSgrqlsevFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFN 1455
Cdd:cd05509      5 QLKKVLDSLKNHKSAWP-------FLEPVDKEEAPDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYN 77

                           90
                   ....*....|....*..
gi 1977155862 1456 LEGSLIYEDSIVLQSVF 1472
Cdd:cd05509     78 GPDTEYYKCANKLEKFF 94
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
 1380-1472 1.28e-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: 66.26  E-value: 1.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1380 IVDAVIKYKDSSSgrqlsevFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGS 1459
Cdd:cd05504     20 LLVEIVKHKDSWP-------FLRPVSKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVFSNCFLYNPEHT 92

                           90
                   ....*....|...
gi 1977155862 1460 LIYEDSIVLQSVF 1472
Cdd:cd05504     93 SVYKAGTRLQRFF 105
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1628-1665 1.39e-12

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 63.42  E-value: 1.39e-12
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1977155862 1628 TCGPNMFQCNNSACIPLLWACDGDPECLDQSDEwpQNC 1665
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDE--ENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1590-1624 1.58e-12

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 63.38  E-value: 1.58e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1977155862 1590 CTDDEFRCRSGKCISVQFVCDEEKDCDDGSDEDSC 1624
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1715-1749 6.12e-12

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 61.45  E-value: 6.12e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1977155862 1715 CRPDEFQCNDGTCIHGSRQCDREYDCKDLSDELGC 1749
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
QLQ smart00951
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ...
 165-198 7.98e-12

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: 61.39  E-value: 7.98e-12
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1977155862   165 PFNQNQLHQLRAQIMAYK-MLARGQPLPDHLQMAV 198
Cdd:smart00951    2 PFTPAQLELLRAQILAYKyLLARNQPVPPELLQAI 36
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1676-1707 9.81e-12

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 61.11  E-value: 9.81e-12
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1977155862  1676 CSSLEFQCGSGECVHQKWLCDGTNDCRDHSDE 1707
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
 1373-1477 1.61e-11

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 [Multi-domain]  Cd Length: 106  Bit Score: 62.79  E-value: 1.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1373 LTKKMKKIVDAVIKYKDSSSGrQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1452
Cdd:cd05525      3 LAQVLKEICDAIITYKDSNGQ-SLAIPFINLPSKKKNPDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAE 81

                           90       100
                   ....*....|....*....|....*
gi 1977155862 1453 TFNLEGSLIYEDSIVLQSVFTSVRQ 1477
Cdd:cd05525     82 KYYGRKSPIGRDVCRLRKAYYQAKH 106
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1552-1581 2.29e-11

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 59.91  E-value: 2.29e-11
                           10        20        30
                   ....*....|....*....|....*....|
gi 1977155862 1552 NYFQCANERCVPYRWICDGTDDCGDGSDEL 1581
Cdd:cd00112      4 NEFRCANGRCIPSSWVCDGEDDCGDGSDEE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1628-1660 2.71e-11

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 59.57  E-value: 2.71e-11
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1977155862  1628 TCGPNMFQCNNSACIPLLWACDGDPECLDQSDE 1660
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1588-1624 3.01e-11

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 59.57  E-value: 3.01e-11
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1977155862 1588 KNCTDDEFRCRSGKCISVQFVCDEEKDCDDGSDEDSC 1624
Cdd:pfam00057    1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1590-1621 3.89e-11

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 59.18  E-value: 3.89e-11
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1977155862  1590 CTDDEFRCRSGKCISVQFVCDEEKDCDDGSDE 1621
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1552-1580 4.68e-11

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 59.18  E-value: 4.68e-11
                            10        20
                    ....*....|....*....|....*....
gi 1977155862  1552 NYFQCANERCVPYRWICDGTDDCGDGSDE 1580
Cdd:smart00192    5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1629-1665 7.68e-11

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 58.37  E-value: 7.68e-11
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1977155862 1629 CGPNMFQCNNSACIPLLWACDGDPECLDQSDEWpqNC 1665
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEE--NC 35
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
 1404-1472 8.61e-11

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: 60.38  E-value: 8.61e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1977155862 1404 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVF 1472
Cdd:cd05499     30 PVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVF 98
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
 1408-1455 1.27e-10

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: 60.45  E-value: 1.27e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1977155862 1408 ELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFN 1455
Cdd:cd05528     32 EVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYN 79
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1714-1746 1.39e-10

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 57.64  E-value: 1.39e-10
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1977155862  1714 TCRPDEFQCNDGTCIHGSRQCDREYDCKDLSDE 1746
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 1797-1831 5.24e-10

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 56.10  E-value: 5.24e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1977155862 1797 CLYNNGGCSHTCNDLKVGFECLCPSGFQLA-DKKRC 1831
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQdDGRTC 36
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
 1371-1474 8.50e-10

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: 58.50  E-value: 8.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1371 PNLTKKMKKIVDavikykdsSSGRQLSEVFIQ-LPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQ 1449
Cdd:cd05529     27 ERLISGLDKLLL--------SLQLEIAEYFEYpVDLRAWYPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILS 98

                           90       100
                   ....*....|....*....|....*
gi 1977155862 1450 NAQTFNLEGSLIYEDSIVLQSVFTS 1474
Cdd:cd05529     99 NAETFNEPNSEIAKKAKRLSDWLLR 123
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 1757-1787 1.74e-09

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 54.56  E-value: 1.74e-09
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1977155862  1757 GPDKFQCKSGECIKMAQVCDKQRDCRDWSDE 1787
Cdd:smart00192    3 PPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 1757-1787 1.84e-09

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 54.52  E-value: 1.84e-09
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1977155862 1757 GPDKFQCKSGECIKMAQVCDKQRDCRDWSDE 1787
Cdd:cd00112      2 PPNEFRCANGRCIPSSWVCDGEDDCGDGSDE 32
EGF_CA smart00179
Calcium-binding EGF-like domain;
1833-1863 2.17e-09

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 54.56  E-value: 2.17e-09
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1977155862  1833 DIDECQNPDACSQ--ICINLEGGYKCECREGYH 1863
Cdd:smart00179    1 DIDECASGNPCQNggTCVNTVGSYRCECPPGYT 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1757-1787 2.29e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 54.18  E-value: 2.29e-09
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1977155862 1757 GPDKFQCKSGECIKMAQVCDKQRDCRDWSDE 1787
Cdd:pfam00057    4 SPNEFQCGSGECIPRSWVCDGDPDCGDGSDE 34
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
 1404-1473 5.01e-09

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: 55.36  E-value: 5.01e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1404 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFT 1473
Cdd:cd05498     30 PEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHPVHAMARKLQDVFE 99
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
 1407-1474 5.34e-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: 55.07  E-value: 5.34e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1977155862 1407 KELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTS 1474
Cdd:cd05503     28 KLVPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEVGRAGHNMRKFFEK 95
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1833-1865 5.96e-09

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 53.02  E-value: 5.96e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1977155862 1833 DIDECQNPDACS--QICINLEGGYKCECREGYHLD 1865
Cdd:cd00054      1 DIDECASGNPCQngGTCVNTVGSYRCSCPPGYTGR 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1552-1581 5.97e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 53.02  E-value: 5.97e-09
                           10        20        30
                   ....*....|....*....|....*....|
gi 1977155862 1552 NYFQCANERCVPYRWICDGTDDCGDGSDEL 1581
Cdd:pfam00057    6 NEFQCGSGECIPRSWVCDGDPDCGDGSDEE 35
ResIII pfam04851
Type III restriction enzyme, res subunit;
736-896 6.02e-09

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 56.91  E-value: 6.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  736 QLKQYQIKGLE-WLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEyKRINGPFLIIVP-LSTLSNWVYEFDKWAPSVV 813
Cdd:pfam04851    3 ELRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFK-KGPIKKVLFLVPrKDLLEQALEEFKKFLPNYV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  814 KVSYKGSPaarRAFVPQLRSGKFnaLLTTYEYIIKD----KQVLAKIRWKYMIVDEGHRM--KNHhcklTQVLNthYLAP 887
Cdd:pfam04851   82 EIGEIISG---DKKDESVDDNKI--VVTTIQSLYKAlelaSLELLPDFFDVIIIDEAHRSgaSSY----RNILE--YFKP 150

                          170
                   ....*....|
gi 1977155862  888 RRIL-LTGTP 896
Cdd:pfam04851  151 AFLLgLTATP 160
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
 1373-1469 1.36e-08

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: 53.94  E-value: 1.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1373 LTKKMKKIVDAViKYKDSSsgrqlsEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1452
Cdd:cd05512      2 LEVLLRKTLDQL-QEKDTA------EIFSEPVDLSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCL 74

                           90
                   ....*....|....*..
gi 1977155862 1453 TFNLEGSLIYEDSIVLQ 1469
Cdd:cd05512     75 AYNAKDTIFYRAAVRLR 91
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
 1410-1462 1.38e-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: 53.95  E-value: 1.38e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1977155862 1410 PEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIY 1462
Cdd:cd05513     32 PGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYNKPDTIYY 84
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 757-895 1.94e-08

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 55.10  E-value: 1.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  757 NGILADEMGLGKTIQTIALITYLMEYKRinGPFLIIVPLSTLSNWVYE-FDKWAPSVVKVSYKGSpaaRRAFVPQLRSGK 835
Cdd:cd00046      3 NVLITAPTGSGKTLAALLAALLLLLKKG--KKVLVLVPTKALALQTAErLRELFGPGIRVAVLVG---GSSAEEREKNKL 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1977155862  836 FNA--LLTTYEYIIKDKQVLAKI---RWKYMIVDEGHRM----KNHHCKLTQVLNTHYLAPRRILLTGT 895
Cdd:cd00046     78 GDAdiIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALlidsRGALILDLAVRKAGLKNAQVILLSAT 146
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
734-1290 2.84e-08

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 58.88  E-value: 2.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  734 NGQLKQYQIKGLE-WLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRIngpfLIIVPLSTLSN-WVYEFDKWAPS 811
Cdd:COG1061     78 SFELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV----LVLVPRRELLEqWAEELRRFLGD 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  812 VVKVSYKgspaarrafvpqlRSGKFNALLTTYEYIIKDKQvLAKI--RWKYMIVDEGhrmknHHC---KLTQVLNtHYLA 886
Cdd:COG1061    154 PLAGGGK-------------KDSDAPITVATYQSLARRAH-LDELgdRFGLVIIDEA-----HHAgapSYRRILE-AFPA 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  887 PRRILLTGTPlqNKLPELWALLNFLLPTIFkscstfeqwfnapfamtgeKVDLNEeetilIIRRlhKVLRPFLLRRLKKE 966
Cdd:COG1061    214 AYRLGLTATP--FRSDGREILLFLFDGIVY-------------------EYSLKE-----AIED--GYLAPPEYYGIRVD 265

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  967 VEAQLPEkgkggtktlmntimqlrkicnhpymFQHIEESFSEHLgftggivqgpdLYRASGKFELLDRILPKlRATNHKV 1046
Cdd:COG1061    266 LTDERAE-------------------------YDALSERLREAL-----------AADAERKDKILRELLRE-HPDDRKT 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1047 LLFCQMTSLMTIMEDYFAYRNFKYLRLDGTTKAEDRGMLLKAFNDPASQYfvfLLSTRAGGLGLNLQSADTVIIFDsdwn 1126
Cdd:COG1061    309 LVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRI---LVTVDVLNEGVDVPRLDVAILLR---- 381

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1127 PHQDLQ--AQdrahRIGqqnevRVLRL------CTV-----NSVEEKILAAAKYKLNVDQKVIQAGMFDQKSSSHERRAF 1193
Cdd:COG1061    382 PTGSPRefIQ----RLG-----RGLRPapgkedALVydfvgNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVK 452

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1194 LQAILEHEEQDEEEDEVPDDETVNQMIARSEEEFDHFMRMDLDRRREEARNPKRKPRLMEEDELPTWIMKDDAEVERLTC 1273
Cdd:COG1061    453 PALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLL 532

                          570
                   ....*....|....*..
gi 1977155862 1274 EEEEEKMFGRGSRQRKE 1290
Cdd:COG1061    533 LLLLELLELLAALLRLE 549
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
 1394-1479 4.01e-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 [Multi-domain]  Cd Length: 109  Bit Score: 53.06  E-value: 4.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1394 RQLSEVFIQLPSR-------KELPEYYELIRKPVDFKKIKERIR----NHkYRSLNDLEKDVMLLCQNAQTFNLEGSLIY 1462
Cdd:cd05502     11 RLLLELYCHELSLpfhepvsPSVPNYYKIIKTPMDLSLIRKKLQpkspQH-YSSPEEFVADVRLMFKNCYKFNEEDSEVA 89

                           90
                   ....*....|....*..
gi 1977155862 1463 EDSIVLQSVFTSVRQKI 1479
Cdd:cd05502     90 QAGKELELFFEEQLKEI 106
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 1838-1871 7.85e-08

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 49.93  E-value: 7.85e-08
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1977155862 1838 QNPDACSQICINLEGGYKCECREGYHLDPVNKSC 1871
Cdd:pfam14670    3 VNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
Bromo_WDR9_II cd05496
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
 1375-1479 8.51e-08

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: 52.46  E-value: 8.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1375 KKMKKIVDAVIKYKDSSSGRQLSEVFiqlpsrkELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTF 1454
Cdd:cd05496      8 KQCKELVNLMWDCEDSEPFRQPVDLL-------KYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSY 80

                           90       100
                   ....*....|....*....|....*.
gi 1977155862 1455 NL-EGSLIYEDSIVLQSVFTSVRQKI 1479
Cdd:cd05496     81 TPnKRSRIYSMTLRLSALFEEHIKKI 106
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
 1407-1479 1.91e-07

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 [Multi-domain]  Cd Length: 112  Bit Score: 51.11  E-value: 1.91e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1977155862 1407 KELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNleGSliyedsivlQSVFTSVRQKI 1479
Cdd:cd05511     28 KKVPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYN--GP---------DSVYTKKAKEM 89
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
 1404-1472 2.35e-07

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: 50.77  E-value: 2.35e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1977155862 1404 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVF 1472
Cdd:cd05500     31 PVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQMGKRLQAAF 99
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 369-582 3.19e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 3.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  369 VEILQEREYRLQARIA-------HRIQELENLpgslpgdLRTKANIELKALRLLNFQRQLRQEVVvcmRRDTALETALNA 441
Cdd:COG1196    283 LEEAQAEEYELLAELArleqdiaRLEERRREL-------EERLEELEEELAELEEELEELEEELE---ELEEELEEAEEE 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  442 KAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQK 521
Cdd:COG1196    353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1977155862  522 KENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAyLLQQTDEYVANLTELVRAHKAAQAL 582
Cdd:COG1196    433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE-LLEEAALLEAALAELLEELAEAAAR 492
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 737-896 3.88e-07

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 51.54  E-value: 3.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  737 LKQYQIKGLE-WLvsLYNNNLNGILADEMGLGKTIQTIALITYLMEykrinGPFLIIVP-LSTLSNWVYEFDKWAPSVVk 814
Cdd:cd17926      1 LRPYQEEALEaWL--AHKNNRRGILVLPTGSGKTLTALALIAYLKE-----LRTLIVVPtDALLDQWKERFEDFLGDSS- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  815 vsykgspaarrafVPQLRSGK------FNALLTTYEYIIKDKQVLAKI--RWKYMIVDEGHrmknHHC--KLTQVLnTHY 884
Cdd:cd17926     73 -------------IGLIGGGKkkdfddANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAH----HLPakTFSEIL-KEL 134

                          170
                   ....*....|..
gi 1977155862  885 LAPRRILLTGTP 896
Cdd:cd17926    135 NAKYRLGLTATP 146
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
 1408-1479 1.97e-06

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: 48.19  E-value: 1.97e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1977155862 1408 ELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGsliyeDSIVL--QSVFTSVRQKI 1479
Cdd:cd05497     36 NLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKPG-----DDVVLmaQTLEKLFLQKL 104
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
 1404-1472 2.28e-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: 47.71  E-value: 2.28e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1977155862 1404 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVF 1472
Cdd:cd05506     27 VVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTMAKELLKIF 95
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
 1377-1455 2.98e-06

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: 47.74  E-value: 2.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1377 MKKIVDAVikYKDSSSGRQlSEVFIQ-LPSRKElPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFN 1455
Cdd:cd05507      4 WKKAILLV--YRTLASHRY-ASVFLKpVTEDIA-PGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYN 79
EGF_CA pfam07645
Calcium-binding EGF domain;
1833-1861 5.66e-06

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 44.54  E-value: 5.66e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1977155862 1833 DIDECQNP-DACSQ--ICINLEGGYKCECREG 1861
Cdd:pfam07645    1 DVDECATGtHNCPAntVCVNTIGSFECRCPDG 32
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
 1375-1461 6.74e-06

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: 46.38  E-value: 6.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1375 KKMKKIVDAVIKYKDSSSGRQLsevfiqlPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTF 1454
Cdd:cd05505      3 QKCEEILSKILKYRFSWPFREP-------VTADEAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAEKY 75


                   ....*..
gi 1977155862 1455 NLEGSLI 1461
Cdd:cd05505     76 YENGSYV 82
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
 1397-1455 1.15e-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 [Multi-domain]  Cd Length: 112  Bit Score: 46.28  E-value: 1.15e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1977155862 1397 SEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFN 1455
Cdd:cd05510     26 STPFLTKVSKREAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLYN 84
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 1836-1871 1.42e-05

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 43.62  E-value: 1.42e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1977155862 1836 ECQNPDACS--QICINLEGGYKCECREGYHLDpvnKSC 1871
Cdd:cd00053      1 ECAASNPCSngGTCVNTPGSYRCVCPPGYTGD---RSC 35
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 1094-1142 1.86e-05

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 44.62  E-value: 1.86e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1977155862 1094 SQYFVFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQ 1142
Cdd:cd18785     20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK 68
EGF smart00181
Epidermal growth factor-like domain;
1836-1866 2.83e-05

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 42.89  E-value: 2.83e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1977155862  1836 ECQNPDACSQ-ICINLEGGYKCECREGYHLDP 1866
Cdd:smart00181    1 ECASGGPCSNgTCINTPGSYTCSCPPGYTGDK 32
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
 1404-1474 7.03e-05

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: 43.97  E-value: 7.03e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1977155862 1404 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTS 1474
Cdd:cd05495     31 PKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWLYNRKTSRVYKYCTKLAEVFEQ 101
TYA pfam01021
Ty transposon capsid protein; Ty are yeast transposons. A 5.7kb transcript codes for p3 a ...
 42-130 1.18e-04

Ty transposon capsid protein; Ty are yeast transposons. A 5.7kb transcript codes for p3 a fusion protein of TYA and TYB. The TYA protein is analogous to the gag protein of retroviruses. TYA a is cleaved to form 46kd protein which can form mature virion like particles. This entry corresponds to the capsid protein from Ty1 and Ty2 transposons.


Pssm-ID: 425992  Cd Length: 384  Bit Score: 46.87  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862   42 PPAAGHPLPPQGPsgYPQenmHQMHKPmdamhEKAMPDD-PRYGQMKGMGMRPAGHSGMGPPPSPMDQHSQgYPSPLGGS 120
Cdd:pfam01021   56 PQPASVPPPQNGP--YSQ---QCMMTP-----NQANPSGwPFYGHPSMMPYTPYQMSPMYFPPGPQSQFPQ-YPSSVGTP 124

                           90
                   ....*....|
gi 1977155862  121 EHAPSPVPAN 130
Cdd:pfam01021  125 LSTPSPESGN 134
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 35-208 1.25e-04

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 46.93  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862   35 MMGPSPGPPAAGHPLPPQGPSGYPQENMHQMHKPMDAMHEKAMPDDPRY-----GQMK-----------------GMGMR 92
Cdd:pfam09606  284 MGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQsvgqgGQVValgglnhletwnpgnfgGLGAN 363

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862   93 PA--GHSGMGPPPSP---------------MDQHSQGYPSPLGGSEHAPSPVPANGPPSGPLMPPGPGGVPQDNADPQTL 155
Cdd:pfam09606  364 PMqrGQPGMMSSPSPvpgqqvrqvtpnqfmRQSPQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQQRTI 443

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1977155862  156 GQQNRGGP----------TPFNQNQLHQLRAQimaYKMLargQPLPDHLqmavqgKRPMAGMQ 208
Cdd:pfam09606  444 GQDSPGGSlntpgqsavnSPLNPQEEQLYREK---YRQL---TKYIEPL------KRMIAKME 494
Bromo_polybromo_VI cd05526
Bromodomain, polybromo repeat VI. Polybromo is a nuclear protein of unknown function, which ...
 1391-1479 1.95e-04

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: 42.74  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862 1391 SSGRQLSEVFIQLPSRKELPEyyELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQS 1470
Cdd:cd05526     21 EEGRCYSDSLAELPELAVDGV--GPKKIPLTLDIIKRNVDKGRYRRLDKFQEDMFEVLERARRLSRTDSEIYEDAVELQQ 98


                   ....*....
gi 1977155862 1471 VFTSVRQKI 1479
Cdd:cd05526     99 FFIKIRDEL 107
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 42-211 1.97e-04

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 46.54  E-value: 1.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862   42 PPAAGHPLPPQGPSGYPQENMHQMHKPMDAMHEKAMPddprygqMKGMGMRPAGHS--GMGPP--PSPMDQHSQGYPSPL 117
Cdd:pfam09606   97 QMMGPMGPGPGGPMGQQMGGPGTASNLLASLGRPQMP-------MGGAGFPSQMSRvgRMQPGgqAGGMMQPSSGQPGSG 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  118 GGSEHAPSPVPANGPPSGPLMPPGPGGVPQdnaDPQTLGQQNRGGPTPfNQNQLHQLRAqimaykmlARGQPLPDHLQMA 197
Cdd:pfam09606  170 TPNQMGPNGGPGQGQAGGMNGGQQGPMGGQ---MPPQMGVPGMPGPAD-AGAQMGQQAQ--------ANGGMNPQQMGGA 237

                          170
                   ....*....|....
gi 1977155862  198 vQGKRPMAGMQQQM 211
Cdd:pfam09606  238 -PNQVAMQQQQPQQ 250
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 1837-1865 2.42e-04

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 40.27  E-value: 2.42e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1977155862 1837 CQ-NPDACSQ--ICINLEGGYKCECREGYHLD 1865
Cdd:pfam12947    1 CSdNNGGCHPnaTCTNTGGSFTCTCNDGYTGD 32
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
 765-864 2.81e-04

DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 43.86  E-value: 2.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  765 GLGKTiqTIALITYLMEYKRiNGPFLIIVPLSTLSNWVYE----FDKWAPSVVK--VSYKGSPA-ARRAFVPQLRSGKFN 837
Cdd:cd17924     42 GVGKT--TFGLATSLYLASK-GKRSYLIFPTKSLVKQAYErlskYAEKAGVEVKilVYHSRLKKkEKEELLEKIEKGDFD 118

                           90       100
                   ....*....|....*....|....*..
gi 1977155862  838 ALLTTYEYIIKDKQVLAKIRWKYMIVD 864
Cdd:cd17924    119 ILVTTNQFLSKNFDLLSNKKFDFVFVD 145
PHA03378 PHA03378
EBNA-3B; Provisional
 38-209 3.07e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.83  E-value: 3.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862   38 PSPGPPAAGHPLPPQGPSGYPQENMHQMHKPMDAMHEKAMPDDPRYGQ-MKGMGMRPAGHSGMGPPPspmdQHSQGYPSP 116
Cdd:PHA03378   701 PTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAaAPGRARPPAAAPGRARPP----AAAPGAPTP 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  117 LGGSEHAPSPVpangppsgplmppgpggvpqdnadpqtlgQQNRGGPTPFNQNQLHQLRAQIMAYKMLARGQPLPDHLQM 196
Cdd:PHA03378   777 QPPPQAPPAPQ-----------------------------QRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQ 827

                          170       180
                   ....*....|....*....|..
gi 1977155862  197 AVQG---------KRPMAGMQQ 209
Cdd:PHA03378   828 LLTGgvkrgrpslKKPAALERQ 849
EGF_CA smart00179
Calcium-binding EGF-like domain;
1795-1832 5.08e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.15  E-value: 5.08e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1977155862  1795 NECLYNNGgCSH--TCNDLKVGFECLCPSGFQlaDKKRCQ 1832
Cdd:smart00179    3 DECASGNP-CQNggTCVNTVGSYRCECPPGYT--DGRNCE 39
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 405-581 7.13e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.37  E-value: 7.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  405 ANIELKALRLLNFQRQLRQEVVVCMRRDTALETALNAKaykrskRQSLREARiTEKLEKQQKIEQERKRRQKHQEYLNSI 484
Cdd:COG1579     13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAA------KTELEDLE-KEIKRLELEIEEVEARIKKYEEQLGNV 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  485 lqhaKDFKEYhrsvtgkiQKLTKAVATyhantereQKKENERIEKErMRRLMAEDEEgYRKLIDQKKDK------RLAYL 558
Cdd:COG1579     86 ----RNNKEY--------EALQKEIES--------LKRRISDLEDE-ILELMERIEE-LEEELAELEAElaeleaELEEK 143

                          170       180
                   ....*....|....*....|...
gi 1977155862  559 LQQTDEYVANLTELVRAHKAAQA 581
Cdd:COG1579    144 KAELDEELAELEAELEELEAERE 166
PHA03418 PHA03418
hypothetical E4 protein; Provisional
 38-126 1.06e-03

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 42.80  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862   38 PSPGPPAA--GHPLPP--QGPSGYPQENMHQMHKPMDAmhekamPDDPRYGQM-KGMGMRPAGHSGM------------- 99
Cdd:PHA03418    60 LTPRPPAQpnGHNKPPvtKQPGGEGTEEDHQAPLAADA------DDDPRPGKRsKADEHGPAPGRAAlapfkldldqdpl 133

                           90       100
                   ....*....|....*....|....*....
gi 1977155862  100 --GPPPSPMDQHSQGYPSPLGGSEHAPSP 126
Cdd:PHA03418   134 hgDPDPPPGATGGQGEEPPEGGEESQPPL 162
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 370-555 1.31e-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: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 43.37  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  370 EILQEREyRLQARIAHRIQELEnlpgslpgdlRTKANIElkALRLlnfqrQLRQEVVVCMRRDTALETALNakayKRSKR 449
Cdd:pfam13868  177 EIEEEKE-REIARLRAQQEKAQ----------DEKAERD--ELRA-----KLYQEEQERKERQKEREEAEK----KARQR 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  450 QSLREARITEKLEKQQKIEQERKRRQkhQEYLNSILQHAKDFKEYHRSVTGKIQKLTK-AVATYHANTEREQKKENERIE 528
Cdd:pfam13868  235 QELQQAREEQIELKERRLAEEAEREE--EEFERMLRKQAEDEEIEQEEAEKRRMKRLEhRRELEKQIEEREEQRAAEREE 312

                          170       180
                   ....*....|....*....|....*..
gi 1977155862  529 KERMRRLMAEDEEGYRKLIDQKKDKRL 555
Cdd:pfam13868  313 ELEEGERLREEEAERRERIEEERQKKL 339
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 38-130 1.31e-03

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 41.56  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862   38 PSPGPPAAGHPLPPQ--GPSGYPQENMHQMHkpmdamHEKAMPDDPRYGQMKGMGMRPAGHSGMGPPPSPMDQHS----Q 111
Cdd:pfam15240   55 PPQPPASDDPPGPPPpgGPQQPPPQGGKQKP------QGPPPQGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGpppqG 128

                           90
                   ....*....|....*....
gi 1977155862  112 GYPSPLGGSEHAPSPVPAN 130
Cdd:pfam15240  129 GGPPPQGGNQQGPPPPPPG 147
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
 1817-1836 1.46e-03

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteriztic pattern 'ababcc'. They are found in blood coagulation proteins such as fibrillin, Clr and Cls, thrombomodulin, and the LDL receptor. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal cysteine residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In cEGFs the C-terminal thiol resides on the C-terminal beta-sheet, resulting in long loop-lengths between the cysteine residues of disulfide 'c', typically C[10+]XC. These longer loop-lengths may have arisen by selective cysteine loss from a four-disulfide EGF template such as laminin or integrin. Tandem cEGF domains have five linking residues between terminal cysteines of adjacent domains. cEGF domains may or may not bind calcium in the linker region. cEGF domains with the consensus motif CXN4X[F,Y]XCXC are hydroxylated exclusively on the asparagine residue.


Pssm-ID: 463661  Cd Length: 22  Bit Score: 37.77  E-value: 1.46e-03
                           10        20
                   ....*....|....*....|.
gi 1977155862 1817 CLCPSGFQL-ADKKRCQDIDE 1836
Cdd:pfam12662    2 CSCPPGYQLdPDGRTCVDIDE 22
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 19-211 1.52e-03

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 43.46  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862   19 GMMGPSPGPSPGSTHSMMGPSPGPPAAGHPLPPQG-PSGYPQENMHQMHKPMDAMHEKAMPDDPRYGQMKGMGMRPAGHS 97
Cdd:pfam09606  111 GQQMGGPGTASNLLASLGRPQMPMGGAGFPSQMSRvGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNG 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862   98 GMGPPPS---PMDQHSQGYPSPLGGSEHAPSPVPANgppsgplmpPGPGGVPQDNADPQTLGQQNRGGPTPfNQNQLHQL 174
Cdd:pfam09606  191 GQQGPMGgqmPPQMGVPGMPGPADAGAQMGQQAQAN---------GGMNPQQMGGAPNQVAMQQQQPQQQG-QQSQLGMG 260

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1977155862  175 RAQIMAYkmlARGQPLPDHLQMAVQGKRPMAGMQQQM 211
Cdd:pfam09606  261 INQMQQM---PQGVGGGAGQGGPGQPMGPPGQQPGAM 294
PTZ00121 PTZ00121
MAEBL; Provisional
 442-553 1.58e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  442 KAYKRSKRQSLREARITEKLEKQQKIEQERKRrqkhQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHAntEREQK 521
Cdd:PTZ00121  1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKA----EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA--EEAKK 1614

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1977155862  522 KENERIEKERMRRlmaedEEGYRKLIDQKKDK 553
Cdd:PTZ00121  1615 AEEAKIKAEELKK-----AEEEKKKVEQLKKK 1641
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 371-582 1.64e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  371 ILQEREYRL-----QARIAHRIQELENlpgslpgDLRTKAnIELKALRLLNFQRQLRQ----------EVVVCMRRDTAL 435
Cdd:COG1196    194 ILGELERQLeplerQAEKAERYRELKE-------ELKELE-AELLLLKLRELEAELEEleaeleeleaELEELEAELAEL 265

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  436 ETALNAKAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHAN 515
Cdd:COG1196    266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1977155862  516 ----TEREQKKENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAyLLQQTDEYVANLTELVRAHKAAQAL 582
Cdd:COG1196    346 leeaEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE-ALRAAAELAAQLEELEEAEEALLER 415
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1795-1832 2.17e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 37.62  E-value: 2.17e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1977155862 1795 NECLYNNG-GCSHTCNDLKVGFECLCPSGFQLadkKRCQ 1832
Cdd:cd00054      3 DECASGNPcQNGGTCVNTVGSYRCSCPPGYTG---RNCE 38
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
434-581 2.34e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  434 ALETALNAKAYKRSKRQSLREARitEKLEKQQK-IEQERKRRQKHQEYLNSILQHAKDFKEYHR------SVTGKIQKLT 506
Cdd:COG4717     75 ELEEELKEAEEKEEEYAELQEEL--EELEEELEeLEAELEELREELEKLEKLLQLLPLYQELEAleaelaELPERLEELE 152

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1977155862  507 KAVATYHANTEREQKKENERIEKER-MRRLMAEDEEGYRKLIdQKKDKRLAYLLQQTDEYVANLTELVRAHKAAQA 581
Cdd:COG4717    153 ERLEELRELEEELEELEAELAELQEeLEELLEQLSLATEEEL-QDLAEELEELQQRLAELEEELEEAQEELEELEE 227
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 381-581 2.42e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 2.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  381 ARIAHRIQELE-NLpgslpGDLRTKANielKALRLLNFQRQLRQ-EVVVCMRRDTALETALNAKAYKRSKRQSLREARIT 458
Cdd:COG1196    189 ERLEDILGELErQL-----EPLERQAE---KAERYRELKEELKElEAELLLLKLRELEAELEELEAELEELEAELEELEA 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  459 EKLEKQQKIEQERkrrQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERMRRLMAE 538
Cdd:COG1196    261 ELAELEAELEELR---LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1977155862  539 DEEGYRKLIDQKKDKRLAyLLQQTDEYVANLTELVRAHKAAQA 581
Cdd:COG1196    338 ELEELEEELEEAEEELEE-AEAELAEAEEALLEAEAELAEAEE 379
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
349-580 2.59e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 2.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  349 QLHQKQNRITPIQKPRGLDPVEILQE--REY-RLQARIAHRIQELENLPGSLpGDLRTKANIELKALRLLNFQRQLRQE- 424
Cdd:COG4717    171 ELAELQEELEELLEQLSLATEEELQDlaEELeELQQRLAELEEELEEAQEEL-EELEEELEQLENELEAAALEERLKEAr 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  425 ---------VVVCMRRDTALETALNAKAY---------------KRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEY 480
Cdd:COG4717    250 lllliaaalLALLGLGGSLLSLILTIAGVlflvlgllallflllAREKASLGKEAEELQALPALEELEEEELEELLAALG 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  481 LNSILQHAKDFKEYHRsvtgkIQKLTKAVATYHANTEREQKKENERIEKERMRRLMAEDEEGYRKLIDQKKD-----KRL 555
Cdd:COG4717    330 LPPDLSPEELLELLDR-----IEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEyqelkEEL 404

                          250       260
                   ....*....|....*....|....*
gi 1977155862  556 AYLLQQTDEYVANLTELVRAHKAAQ 580
Cdd:COG4717    405 EELEEQLEELLGELEELLEALDEEE 429
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 418-564 2.81e-03

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: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 42.63  E-value: 2.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  418 QRQLRQEVvvcMRRDTALETALNAKAYKRSKRQSLREARITEklEKQQKIEQERKRRQKHQEYLNSILQHAKdfkEYHRS 497
Cdd:pfam15709  360 QRRLQQEQ---LERAEKMREELELEQQRRFEEIRLRKQRLEE--ERQRQEEEERKQRLQLQAAQERARQQQE---EFRRK 431

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1977155862  498 VTgKIQKLTKAVATYHANTEREQKKENERIEKERMRRLMAEDEEgyrklidqkkdKRLAYLLQQTDE 564
Cdd:pfam15709  432 LQ-ELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEE-----------ERLEYQRQKQEA 486
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 765-896 3.02e-03

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: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 40.30  E-value: 3.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  765 GLGKTIqtIALITYL--MEYKRINGPFLIIVPLSTLSNWVYE-FDKWA-PSVVKVSYKGSPAARRAFVPQLRSGKFnaLL 840
Cdd:pfam00270   24 GSGKTL--AFLLPALeaLDKLDNGPQALVLAPTRELAEQIYEeLKKLGkGLGLKVASLLGGDSRKEQLEKLKGPDI--LV 99

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1977155862  841 TTYE---YIIKDKQVLAKIrwKYMIVDEGHRM--KNHHCKLTQVLNTHYLAPRRILLTGTP 896
Cdd:pfam00270  100 GTPGrllDLLQERKLLKNL--KLLVLDEAHRLldMGFGPDLEEILRRLPKKRQILLLSATL 158
EGF smart00181
Epidermal growth factor-like domain;
1796-1832 5.39e-03

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 36.34  E-value: 5.39e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1977155862  1796 ECLyNNGGCSH-TCNDLKVGFECLCPSGFQLAdkKRCQ 1832
Cdd:smart00181    1 ECA-SGGPCSNgTCINTPGSYTCSCPPGYTGD--KRCE 35
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 1796-1832 5.45e-03

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 36.30  E-value: 5.45e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1977155862 1796 ECLYNNGgCSH--TCNDLKVGFECLCPSGFQLadKKRCQ 1832
Cdd:cd00053      1 ECAASNP-CSNggTCVNTPGSYRCVCPPGYTG--DRSCE 36
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
419-581 5.53e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 5.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  419 RQLRQEVVVCMRRDTALETALNA-KAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKdfKEYHRS 497
Cdd:COG4913    258 RELAERYAAARERLAELEYLRAAlRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE--AQIRGN 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  498 VTGKIQKLTKAVAtyHANTEREQKKENERIEKERMRRL---MAEDEEGYRKLIDQKKDkRLAYLLQQTDEYVANLTELVR 574
Cdd:COG4913    336 GGDRLEQLEREIE--RLERELEERERRRARLEALLAALglpLPASAEEFAALRAEAAA-LLEALEEELEALEEALAEAEA 412


                   ....*..
gi 1977155862  575 AHKAAQA 581
Cdd:COG4913    413 ALRDLRR 419
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 400-582 6.13e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 6.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  400 DLRTKANIELKALR-----LLNFQRQLRQEVVVCMRRDTALETALNAKAYKRSKRQSLREARITEKLEKQQKIEQERKRR 474
Cdd:COG4942     20 DAAAEAEAELEQLQqeiaeLEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  475 QKHQEYLNSILQ---------------HAKDFKE------YHRSVTGKIQKLTKAVAtyHANTEREQKKENERIEKERMR 533
Cdd:COG4942    100 EAQKEELAELLRalyrlgrqpplalllSPEDFLDavrrlqYLKYLAPARREQAEELR--ADLAELAALRAELEAERAELE 177

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1977155862  534 RLMAEDEEGYRKLIDQKKDKR--LAYLLQQTDEYVANLTELVRAHKAAQAL 582
Cdd:COG4942    178 ALLAELEEERAALEALKAERQklLARLEKELAELAAELAELQQEAEELEAL 228
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 362-552 6.59e-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 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 6.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  362 KPRGLDPVEILQEREY-------RLQARIAHRIQELENLPGSLPGDLRTKANIELKALRLLNFQRQLRQEVVVCMRRDTA 434
Cdd:TIGR02169  669 SRSEPAELQRLRERLEglkrelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  435 LETALNAK-----------AYKRSKRQSLREA-----------RITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFK 492
Cdd:TIGR02169  749 LEQEIENVkselkeleariEELEEDLHKLEEAlndlearlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1977155862  493 EYHRSvtgKIQKLTKAVATYHAN-TEREQKKENERIEKERMRRLMAEDEEGYRKLIDQKKD 552
Cdd:TIGR02169  829 EYLEK---EIQELQEQRIDLKEQiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 1828-1870 7.12e-03

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 40.06  E-value: 7.12e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1977155862 1828 KKRCQDIDECQN-PDACSQICINLEGGYKCECREGYHLDPVNKS 1870
Cdd:cd01475    181 GKICVVPDLCATlSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 350-581 8.00e-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 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 8.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  350 LHQKQNRITPIQKPRGLDPVEILQEREYRLQARIAHRIQELENLPgslpgDLRTKANIELKAL---RLLNFQRQLRQ--- 423
Cdd:TIGR02169  227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIE-----QLLEELNKKIKDLgeeEQLRVKEKIGElea 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  424 EVVVCMRRDTALETALNAKAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKhqeyLNSILQHAKDFKEYHRSvtgKIQ 503
Cdd:TIGR02169  302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK----LTEEYAELKEELEDLRA---ELE 374

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  504 kltkAVATYHANTEREQKKENERIEKerMRRLMAEDEEGYRKLID--QKKDKRLAYLLQQTDEYVANLTELVRAHKAAQA 581
Cdd:TIGR02169  375 ----EVDKEFAETRDELKDYREKLEK--LKREINELKRELDRLQEelQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
373-541 8.35e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 8.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  373 QEREYR-LQARIA---HRIQELENLPGSLPGDLRtKANIELKALRLLNFQRQLRQEVVVCMRRdtaLETALNAKAYKRSK 448
Cdd:COG4717     86 KEEEYAeLQEELEeleEELEELEAELEELREELE-KLEKLLQLLPLYQELEALEAELAELPER---LEELEERLEELREL 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1977155862  449 RQSLREARiteklekQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATyhanTEREQKKENERIE 528
Cdd:COG4717    162 EEELEELE-------AELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE----AQEELEELEEELE 230

                          170
                   ....*....|...
gi 1977155862  529 KERMRRLMAEDEE 541
Cdd:COG4717    231 QLENELEAAALEE 243
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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