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Conserved domains on  [gi|1709636372|gb|TSK62620|]
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Transcription activator BRG1 [Bagarius yarrelli]

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 ...
720-970 5.60e-171

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: 525.76  E-value: 5.60e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  720 YYAVAHAVTEKVDKQSALLINGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIV 799
Cdd:cd18062      1 YYAVAHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  800 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 879
Cdd:cd18062     81 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  880 CKLTQVLNTHYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 959
Cdd:cd18062    161 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 240
                          250
                   ....*....|.
gi 1709636372  960 VLRPFLLRRLK 970
Cdd:cd18062    241 VLRPFLLRRLK 251
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
739-1216 2.35e-158

Probable chromatin-remodeling complex ATPase chain; Provisional


The actual alignment was detected with superfamily member PLN03142:

Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 520.90  E-value: 2.35e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  739 INGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWAPSV 818
Cdd:PLN03142   166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  819 VKVSYKGSPAARRAFVPQ-LRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYlapr 894
Cdd:PLN03142   246 RAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  895 RVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGEkvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 974
Cdd:PLN03142   322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  975 AQLPEKVEYVIKCDMSALQRVLYRHMQAKGV-LLTDGSEKDKkgkggtktLMNTIMQLRKICNHPYMFQQIEESfsehlg 1053
Cdd:PLN03142   392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLNIAMQLRKCCNHPYLFQGAEPG------ 457
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1054 fsGGIVQGADLYRASGKFEVLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRNFKYLRLD-----EDRGMLLKMFND 1128
Cdd:PLN03142   458 --PPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDgntggEDRDASIDAFNK 535
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1129 PESQYFIFLLSTRAGGLGLNLQSADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNV 1208
Cdd:PLN03142   536 PGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615

                   ....*...
gi 1709636372 1209 DQKVIQAG 1216
Cdd:PLN03142   616 DALVIQQG 623
AP_MHD_Cterm super family cl10970
C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD); ...
2527-2741 5.80e-142

C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD); This family corresponds to the C-terminal domain of heterotetrameric AP complexes medium mu subunits and its homologs existing in monomeric stonins, delta-subunit of the heteroheptameric coat protein I (delta-COPI), a protein encoded by a pro-death gene referred as MuD (also known as MUDENG, mu-2 related death-inducing gene), an endocytic adaptor syp1, the mammalian FCH domain only proteins (FCHo1/2), SH3-containing GRB2-like protein 3-interacting protein 1 (SGIP1), and related proteins. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. Stonins have been characterized as clathrin-dependent AP-2 mu chain related factors and may act as cargo-specific sorting adaptors in endocytosis. Coat protein complex I (COPI)-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER, and intra-Golgi transport. MuD is distantly related to the C-terminal domain of mu2 subunit of AP-2. It is able to induce cell death by itself and plays an important role in cell death in various tissues. Syp1 represents a novel type of endocytic adaptor protein that participates in endocytosis, promotes vesicle tabulation, and contributes to cell polarity and stress responses. It shares the same domain architecture with its two ubiquitously expressed mammalian counterparts, FCHo1/2, which represent key initial proteins ultimately controlling cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. They bind specifically to the plasma membrane and recruit the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. Another mammalian neuronal-specific protein SGIP1 does have a C-terminal MHD and has been classified into this family as well. It is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis. It is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15.


The actual alignment was detected with superfamily member cd09259:

Pssm-ID: 472082  Cd Length: 268  Bit Score: 443.31  E-value: 5.80e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2527 TNAVSWRSEGIKYKKNEVFIDVIESINVLVNANGSVMSSDIVGSIKLKTMLSGMPELRLGLNDRVLFALTGRDKGKTVAM 2606
Cdd:cd09259      1 TNAVSWRSEGIKYKKNEVFIDVIESVNVLVNANGSVLSSEIVGCIKLKVFLSGMPELRLGLNDRVLFELTGRDKNKTVEL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2607 EDVKFHQCVRLSRFESDRTISFIPPDGESELMSYRINTHVKPLIWIESVIEKFSHSRVEIMVKAKGQFKKQSVANNVEVR 2686
Cdd:cd09259     81 EDVKFHQCVRLSRFENDRTISFIPPDGDFELMSYRLNTQVKPLIWIESVIEKFSHSRVEIMVKAKGQFKKQSVANNVEIR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2687 VPVPSDADSPKFKTSTGHAKYVPEKNVVVWTIKSFP------------------------------------------VR 2724
Cdd:cd09259    161 VPVPSDADSPKFKTSVGSAKYVPEKNVVVWSIKSFPggkeylmrahfglpsveneelegkppitvkfeipyftvsgiqVR 240
                          250
                   ....*....|....*..
gi 1709636372 2725 YMKIIEKSGYQALPWVR 2741
Cdd:cd09259    241 YMKIIEKSGYQALPWVR 257
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1410-1516 8.13e-62

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: 206.89  E-value: 8.13e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1410 LTKKMKKIVDAVIKYKESSnGRQLSEVFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQ 1489
Cdd:cd05516      2 LTKKMNKIVDVVIKYKDSD-GRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQ 80
                           90       100
                   ....*....|....*....|....*..
gi 1709636372 1490 TFNLEGSLIYEDSIVLQSVFTSLRQKI 1516
Cdd:cd05516     81 TFNLEGSLIYEDSIVLQSVFKSARQKI 107
longin-like super family cl38905
Longin-like domains; Longin-like domains are small protein domains present in a variety of ...
2429-2515 2.80e-47

Longin-like domains; Longin-like domains are small protein domains present in a variety of proteins and members of protein complexes involved in or required for different steps during the transport of proteins from the ribosome to the ER to the plasma membrane, via the Golgi apparatus. Examples are mu and sigma subunits of the heterotetrameric adaptor protein (AP) complex, zeta and delta subunits of the heterotetrameric F-COPI complex, a subgroup of R-SNARE proteins, a subfamily of the transport protein particle (TRAPP), and the signal recognition particle receptor subunit alpha (SR-alpha).


The actual alignment was detected with superfamily member cd14835:

Pssm-ID: 365781  Cd Length: 139  Bit Score: 166.57  E-value: 2.80e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2429 VLICRNYKGDVDMSEIDHFLPLLLQQEEEGLMCP-----------------------------------------VFTEY 2467
Cdd:cd14835     12 VLISRNYRGDVPMSVIEKFMPLLMEKEEEGNLTPiltdggvtyiyikhnnlyllavtkknanaamvlsflyklveVFKEY 91
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1709636372 2468 FKELEEESIQDNFVVVYELLDELMDFGFPQTTDSKILQEYITQEGNKL 2515
Cdd:cd14835     92 FKELEEESIRDNFVIIYELLDEMMDFGYPQTTESKILQEYITQESHKL 139
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2763-2919 7.92e-32

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.76  E-value: 7.92e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2763 DAGKSLTSAAVRGDAAEVRRLLEERRVHPDTRNEFGKTALQV-MMMGNTNVACLLLENGADPNIQDRFGITPAHDAARTG 2841
Cdd:COG0666     85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLaAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2842 FLDTLCVLVDYGASVNIPDQSGALPIHIAIREGYRDVVEFL----AprsNLGHQDTRGDTALDIAEASCTPDMVELLKRQ 2917
Cdd:COG0666    165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLleagA---DVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                   ..
gi 1709636372 2918 LE 2919
Cdd:COG0666    242 GA 243
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
1273-1340 4.10e-28

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: 109.27  E-value: 4.10e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709636372 1273 DRRREEARNPK-RRPRLMEEDELPTWIMKDDAEVERLTCEEEAEKMFGRGSRQRKEVDYSDSLTEKQWL 1340
Cdd:pfam14619    1 ERRREEAEQLPpLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
HSA smart00573
domain in helicases and associated with SANT domains;
453-525 3.92e-26

domain in helicases and associated with SANT domains;


:

Pssm-ID: 214727 [Multi-domain]  Cd Length: 73  Bit Score: 103.63  E-value: 3.92e-26
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709636372   453 QKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKMQKLTKAVATYHANTEREQKKENERIEKERMRRLMA 525
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
605-648 1.89e-15

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: 72.16  E-value: 1.89e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1709636372  605 QMSDLPVKVIHVDSGKILSGVDAPKAGQLDTWLEMNPGYEVAPR 648
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 ...
175-209 5.80e-15

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: 70.44  E-value: 5.80e-15
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1709636372  175 PFNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQ 209
Cdd:pfam08880    1 PFTPAQLQELRAQILAYKYLSRNQPVPPELQQAIF 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
1679-1713 4.63e-14

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: 68.00  E-value: 4.63e-14
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1709636372 1679 CTADEFRCADGQCISSSFVCDEDADCSDGSDEASC 1713
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
1596-1628 1.50e-13

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: 66.50  E-value: 1.50e-13
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1709636372  1596 TCTEQQFMCGNKKCITKQWVCDGMDDCGDGADE 1628
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
1763-1797 2.02e-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: 2.02e-13
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1709636372 1763 CSGQEFQCSNGQCIHTIWRCDGGFDCADHSDESNC 1797
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
1717-1749 4.83e-13

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: 65.35  E-value: 4.83e-13
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1709636372  1717 TCTSGSFQCNNSVCVPELWACDGDPDCPDGSDE 1749
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_b pfam00058
Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif ...
2096-2136 8.04e-12

Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif after the most conserved region of the repeat. The YWTD repeat is found in multiple tandem repeats and has been predicted to form a beta-propeller structure.


:

Pssm-ID: 459654  Cd Length: 42  Bit Score: 61.79  E-value: 8.04e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1709636372 2096 NFMYWTDWGSPAKIEKSGLNGADRTALVTDNIFWPTGITLD 2136
Cdd:pfam00058    1 GRLYWTDSSLRASISSADLNGSDRKTLFTDDLQHPNAIAVD 41
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1801-1836 1.47e-11

Low-density lipoprotein receptor domain class A;


:

Pssm-ID: 395011  Cd Length: 37  Bit Score: 61.11  E-value: 1.47e-11
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1709636372 1801 TCRLDEFRCGDGSCIPGVRQCDGEFHCKDLSDEKDC 1836
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LY smart00135
Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) ...
2034-2075 1.96e-11

Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. Also present in a variety of molecules similar to gp300/megalin.


:

Pssm-ID: 214531 [Multi-domain]  Cd Length: 43  Bit Score: 60.69  E-value: 1.96e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1709636372  2034 TLIGNQMSSPNGLAVDWIHGNIYWTDTFLESISVATKDGSKR 2075
Cdd:smart00135    2 TLLSSGLGHPNGLAVDWIEGRLYWTDWGLDVIEVANLDGTNR 43
EGF_CA smart00179
Calcium-binding EGF-like domain;
1920-1950 5.65e-10

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 56.49  E-value: 5.65e-10
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1709636372  1920 DIDECADPDTCSQ--VCVNLVGSFKCDCQAGYE 1950
Cdd:smart00179    1 DIDECASGNPCQNggTCVNTVGSYRCECPPGYT 33
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
19-351 6.25e-10

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


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 65.03  E-value: 6.25e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   19 GPMMGPGPSPGSSHGMMGPSPG--------PSTTSGHSVSQQGAAGYTQQDSMHPMHKSLE-SLHEKNVGEESRFGQMKG 89
Cdd:pfam09606  122 NLLASLGRPQMPMGGAGFPSQMsrvgrmqpGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQgQAGGMNGGQQGPMGGQMP 201
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   90 VSMRAGGHAGMGPPPSPMDQHSQGYPSPLGSSDHVSSPLPA--GAPSTSGPllsssctSSSPLEGTDSQPSRsgAPSNTP 167
Cdd:pfam09606  202 PQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAmqQQQPQQQG-------QQSQLGMGINQMQQ--MPQGVG 272
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  168 GSSANPTPFNQNQLHQLRAQIMAYKMLARGQPLPDHLQ-MAVQGKR--PMPGMQQGQAMPSLPPGGAGGPVTGPGPLGPN 244
Cdd:pfam09606  273 GGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQtRQQQQQQggNHPAAHQQQMNQSVGQGGQVVALGGLNHLETW 352
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  245 Y--NRGHVLSGPSVPP-----SGPNAVPSANGPPKTWPEGPMVNAA--TPSNAPQKLIPPQ--------PTGRPSPVPPS 307
Cdd:pfam09606  353 NpgNFGGLGANPMQRGqpgmmSSPSPVPGQQVRQVTPNQFMRQSPQpsVPSPQGPGSQPPQshpggmipSPALIPSPSPQ 432
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1709636372  308 VPPAASPVMPPQTQSPGH----PGHSAQPTPTIP-----LHQKHNRITPMQKP 351
Cdd:pfam09606  433 MSQQPAQQRTIGQDSPGGslntPGQSAVNSPLNPqeeqlYREKYRQLTKYIEP 485
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
1884-1918 9.57e-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: 55.71  E-value: 9.57e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1709636372 1884 CLENNGGCSHICNDLKIGYECLCPSGYRLV-DHKRC 1918
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQdDGRTC 36
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
1638-1674 3.14e-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: 3.14e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1709636372 1638 CLSSEFTCSQSpvQCVSTRWRCDGKADCENGADELGC 1674
Cdd:cd00112      1 CPPNEFRCANG--RCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1840-1874 1.21e-08

Low-density lipoprotein receptor domain class A;


:

Pssm-ID: 395011  Cd Length: 37  Bit Score: 52.64  E-value: 1.21e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1709636372 1840 SKCEGKDtFQCRSGECISIDKVCDKQRDCRDLSDE 1874
Cdd:pfam00057    1 STCSPNE-FQCGSGECIPRSWVCDGDPDCGDGSDE 34
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
357-570 2.95e-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: 56.48  E-value: 2.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  357 VEILQEREYRLEARITHRIQELENLpGSLAGDLRTKATIELKALRLLNFQRQLRQEVVVcmRRDAALETALDAKAYKRSK 436
Cdd:COG1196    283 LEEAQAEEYELLAELARLEQDIARL-EERRRELEERLEELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAE 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  437 RQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKMQKLTKAVATYHANTEREQKKENERIE 516
Cdd:COG1196    360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1709636372  517 KERMRRLMAEDEEGYRKLIDQKKDKRLAyLLQQTDEYVANLTELVRAHKAVQAL 570
Cdd:COG1196    440 EEEALEEAAEEEAELEEEEEALLELLAE-LLEEAALLEAALAELLEELAEAAAR 492
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
2241-2278 3.82e-06

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: 45.70  E-value: 3.82e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1709636372 2241 NGGCEYLCLPAPKvnqlspKYTCACPDDKVLGPDMRKC 2278
Cdd:pfam14670    5 NGGCSHLCLNTPG------GYTCSCPEGYELQDDGRTC 36
LY smart00135
Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) ...
2122-2160 6.17e-06

Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. Also present in a variety of molecules similar to gp300/megalin.


:

Pssm-ID: 214531 [Multi-domain]  Cd Length: 43  Bit Score: 45.29  E-value: 6.17e-06
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1709636372  2122 LVTDNIFWPTGITLDLVNQRLYWLDAKLHMLSSIGVDGG 2160
Cdd:smart00135    3 LLSSGLGHPNGLAVDWIEGRLYWTDWGLDVIEVANLDGT 41
Ldl_recept_b super family cl44468
Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif ...
2140-2182 6.20e-06

Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif after the most conserved region of the repeat. The YWTD repeat is found in multiple tandem repeats and has been predicted to form a beta-propeller structure.


The actual alignment was detected with superfamily member pfam00058:

Pssm-ID: 459654  Cd Length: 42  Bit Score: 45.23  E-value: 6.20e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1709636372 2140 QRLYWLDAKLH-MLSSIGVDGGLRHTLIVDErhLANPFSLAVFE 2182
Cdd:pfam00058    1 GRLYWTDSSLRaSISSADLNGSDRKTLFTDD--LQHPNAIAVDP 42
Ldl_recept_b super family cl44468
Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif ...
2183-2223 3.42e-05

Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif after the most conserved region of the repeat. The YWTD repeat is found in multiple tandem repeats and has been predicted to form a beta-propeller structure.


The actual alignment was detected with superfamily member pfam00058:

Pssm-ID: 459654  Cd Length: 42  Bit Score: 43.30  E-value: 3.42e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1709636372 2183 EKVYWTDSFSQSILTANRLTGKNI-TKVVENLASPKDIVLYH 2223
Cdd:pfam00058    1 GRLYWTDSSLRASISSADLNGSDRkTLFTDDLQHPNAIAVDP 42
NHL super family cl18310
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
2002-2102 7.89e-05

NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.


The actual alignment was detected with superfamily member cd14962:

Pssm-ID: 302697 [Multi-domain]  Cd Length: 271  Bit Score: 47.20  E-value: 7.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2002 DVSSGTIFWSDLFHKKIysSPIDKAAysanhvtliGNQMSSPNGLAVDwIHGNIYWTDTFLESISVATKDGsKRMTLIKE 2081
Cdd:cd14962     29 DTGRGAVFVFDLPNGKV--FVIGNAG---------PNRFVSPIGVAID-ANGNLYVSDAELGKVFVFDRDG-KFLRAIGA 95
                           90       100
                   ....*....|....*....|...
gi 1709636372 2082 GL--SKPHAIVVDPERNFMYWTD 2102
Cdd:cd14962     96 GAlfKRPTGIAVDPAGKRLYVVD 118
 
Name Accession Description Interval E-value
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
720-970 5.60e-171

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: 525.76  E-value: 5.60e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  720 YYAVAHAVTEKVDKQSALLINGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIV 799
Cdd:cd18062      1 YYAVAHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  800 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 879
Cdd:cd18062     81 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  880 CKLTQVLNTHYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 959
Cdd:cd18062    161 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 240
                          250
                   ....*....|.
gi 1709636372  960 VLRPFLLRRLK 970
Cdd:cd18062    241 VLRPFLLRRLK 251
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
739-1216 2.35e-158

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 520.90  E-value: 2.35e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  739 INGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWAPSV 818
Cdd:PLN03142   166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  819 VKVSYKGSPAARRAFVPQ-LRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYlapr 894
Cdd:PLN03142   246 RAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  895 RVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGEkvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 974
Cdd:PLN03142   322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  975 AQLPEKVEYVIKCDMSALQRVLYRHMQAKGV-LLTDGSEKDKkgkggtktLMNTIMQLRKICNHPYMFQQIEESfsehlg 1053
Cdd:PLN03142   392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLNIAMQLRKCCNHPYLFQGAEPG------ 457
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1054 fsGGIVQGADLYRASGKFEVLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRNFKYLRLD-----EDRGMLLKMFND 1128
Cdd:PLN03142   458 --PPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDgntggEDRDASIDAFNK 535
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1129 PESQYFIFLLSTRAGGLGLNLQSADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNV 1208
Cdd:PLN03142   536 PGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615

                   ....*...
gi 1709636372 1209 DQKVIQAG 1216
Cdd:PLN03142   616 DALVIQQG 623
AP-1_Mu1B_Cterm cd09259
C-terminal domain of medium Mu1B subunit in epithelial cell-specific clathrin-associated ...
2527-2741 5.80e-142

C-terminal domain of medium Mu1B subunit in epithelial cell-specific clathrin-associated adaptor protein (AP) complex AP-1; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from different AP complexes exhibits similarity with each other. This subfamily corresponds to the C-terminal domain of heterotetrameric clathrin-associated adaptor protein complex 1 (AP-1) medium mu1B subunit encoded by ap1m2 gene exclusively expressed in polarized epithelial cells. Epithelial cell-specific AP-1 is used to sort proteins to the basolateral plasma membrane, which involves the formation of clathrin-coated vesicles (CCVs) from the trans-Golgi network (TGN). Recruitment of AP-1 to the TGN membrane is regulated by a small GTPase, ADP-ribosylation factor 1 (ARF1). The phosphorylation/dephosphorylation events can also regulate the function of AP-1. The membrane-anchored cargo molecules can be linked to the outer lattice of CCVs by AP-1. Those cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-1 mu1B subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic reside-binding. Besides, AP-1 mu1B subunit mediates the basolateral recycling of low-density lipoprotein receptor (LDLR) and transferrin receptor (TfR) from the sorting endosomes, where the basolateral sorting signal does not belong to the tyrosine-based signals. Thus, the binding site in mu1B subunit of AP-1 for the signals of LDLR and TfR might be distinct from that for YXXPhi signals.


Pssm-ID: 271167  Cd Length: 268  Bit Score: 443.31  E-value: 5.80e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2527 TNAVSWRSEGIKYKKNEVFIDVIESINVLVNANGSVMSSDIVGSIKLKTMLSGMPELRLGLNDRVLFALTGRDKGKTVAM 2606
Cdd:cd09259      1 TNAVSWRSEGIKYKKNEVFIDVIESVNVLVNANGSVLSSEIVGCIKLKVFLSGMPELRLGLNDRVLFELTGRDKNKTVEL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2607 EDVKFHQCVRLSRFESDRTISFIPPDGESELMSYRINTHVKPLIWIESVIEKFSHSRVEIMVKAKGQFKKQSVANNVEVR 2686
Cdd:cd09259     81 EDVKFHQCVRLSRFENDRTISFIPPDGDFELMSYRLNTQVKPLIWIESVIEKFSHSRVEIMVKAKGQFKKQSVANNVEIR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2687 VPVPSDADSPKFKTSTGHAKYVPEKNVVVWTIKSFP------------------------------------------VR 2724
Cdd:cd09259    161 VPVPSDADSPKFKTSVGSAKYVPEKNVVVWSIKSFPggkeylmrahfglpsveneelegkppitvkfeipyftvsgiqVR 240
                          250
                   ....*....|....*..
gi 1709636372 2725 YMKIIEKSGYQALPWVR 2741
Cdd:cd09259    241 YMKIIEKSGYQALPWVR 257
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
739-1200 2.54e-121

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 401.14  E-value: 2.54e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  739 INGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEyKRLNGPYLIIVPLSTLSNWVYEFDKWAPSV 818
Cdd:COG0553    238 LKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQRELAKFAPGL 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  819 VKVSYKGSPAARRAFVPqlrSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThyL-APRRVL 897
Cdd:COG0553    317 RVLVLDGTRERAKGANP---FEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRA--LkARHRLA 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  898 LTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPfamtGEKVDLNEEEtiliirRLHKVLRPFLLRRLKKEVEAQL 977
Cdd:COG0553    392 LTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP----IEKGDEEALE------RLRRLLRPFLLRRTKEDVLKDL 461
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  978 PEKVEYVIKCDMSALQRVLYRHMqakgVLLTDGSEKDKKGKGGTKTLMNTIMQLRKICNHPYMFQQIEESFSEHlgfsgg 1057
Cdd:COG0553    462 PEKTEETLYVELTPEQRALYEAV----LEYLRRELEGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSGR------ 531
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1058 ivqgadlyraSGKFEVLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRNFKYLRLD-----EDRGMLLKMFNDPESq 1132
Cdd:COG0553    532 ----------SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHggtsaEERDELVDRFQEGPE- 600
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709636372 1133 YFIFLLSTRAGGLGLNLQSADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILA 1200
Cdd:COG0553    601 APVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
746-1041 4.89e-115

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: 367.01  E-value: 4.89e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  746 YQIKGLEWLVSLYNN-NLNGILADEMGLGKTIQTIALITYLMEYKRL-NGPYLIIVPLSTLSNWVYEFDKWA--PSVVKV 821
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNwGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  822 SYKGSPAAR-RAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYLAPRRVLLTG 900
Cdd:pfam00176   81 VLHGNKRPQeRWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK-SLKTRNRWILTG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  901 TPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetiLIIRRLHKVLRPFLLRRLKKEVEAQLPEK 980
Cdd:pfam00176  160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK---------KGVSRLHKLLKPFLLRRTKKDVEKSLPPK 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709636372  981 VEYVIKCDMSALQRVLY-RHMQAKGVLLTDGSEkdkKGKGGTKTLMNTIMQLRKICNHPYMF 1041
Cdd:pfam00176  231 VEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGE---GGREIKASLLNILMRLRKICNHPGLI 289
Adap_comp_sub pfam00928
Adaptor complexes medium subunit family; This family also contains members which are coatomer ...
2530-2741 8.84e-79

Adaptor complexes medium subunit family; This family also contains members which are coatomer subunits.


Pssm-ID: 395742  Cd Length: 259  Bit Score: 261.85  E-value: 8.84e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2530 VSWRSEGIKYKKNEVFIDVIESINVLVNANGSVMSSDIVGSIKLKTMLSGMPELRLGLNDRVLFaltgrdkgktVAMEDV 2609
Cdd:pfam00928    1 VPWRPPGIKYKKNEVFLDVIERVSVIVDKDGGLLNSEVQGTIDLKCFLSGMPELRLGLNDKLLL----------IELDDV 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2610 KFHQCVRLSRFESDRTISFIPPDGESELMSYRI-NTHVKPLIWIES-VIEKFSHSRVEIMVKAKGQFKKQSVANNVEVRV 2687
Cdd:pfam00928   71 SFHQCVNLDKFESERVISFIPPDGEFELMRYRLsTNEVKLPFTVKPiVSVSGDEGRVEIEVKLRSDFPKKLTAENVVISI 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2688 PVPSDADSPKFKTSTGHAKYVPEKNVVVWTIKSFP--------------------------------------------V 2723
Cdd:pfam00928  151 PVPKEASSPVLRVSDGKAKYDPEENALEWSIKKIPggnesslsgelelsvesssddefpsdppisvefsipmftasglkV 230
                          250
                   ....*....|....*...
gi 1709636372 2724 RYMKIIEKSgYQALPWVR 2741
Cdd:pfam00928  231 RYLKVEEEN-YKPYKWVR 247
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1410-1516 8.13e-62

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: 206.89  E-value: 8.13e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1410 LTKKMKKIVDAVIKYKESSnGRQLSEVFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQ 1489
Cdd:cd05516      2 LTKKMNKIVDVVIKYKDSD-GRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQ 80
                           90       100
                   ....*....|....*....|....*..
gi 1709636372 1490 TFNLEGSLIYEDSIVLQSVFTSLRQKI 1516
Cdd:cd05516     81 TFNLEGSLIYEDSIVLQSVFKSARQKI 107
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1068-1189 2.08e-52

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: 181.14  E-value: 2.08e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1068 SGKFEVLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRNFKYLRLD-----EDRGMLLKMFNDPESqYFIFLLSTRA 1142
Cdd:cd18793     10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDgstssKERQKLVDRFNEDPD-IRVFLLSTKA 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1709636372 1143 GGLGLNLQSADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLC 1189
Cdd:cd18793     89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
AP1_Mu_N cd14835
AP-1 complex subunit mu N-terminal domain; AP-1 complex mu subunit is part of the ...
2429-2515 2.80e-47

AP-1 complex subunit mu N-terminal domain; AP-1 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large gamma-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In the case of AP-1 the coat protein is clathrin. AP-1 binds the phospholipid PI(4)P which plays a role in its localisation to the trans-Golgi network (TGN)/endosome. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341439  Cd Length: 139  Bit Score: 166.57  E-value: 2.80e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2429 VLICRNYKGDVDMSEIDHFLPLLLQQEEEGLMCP-----------------------------------------VFTEY 2467
Cdd:cd14835     12 VLISRNYRGDVPMSVIEKFMPLLMEKEEEGNLTPiltdggvtyiyikhnnlyllavtkknanaamvlsflyklveVFKEY 91
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1709636372 2468 FKELEEESIQDNFVVVYELLDELMDFGFPQTTDSKILQEYITQEGNKL 2515
Cdd:cd14835     92 FKELEEESIRDNFVIIYELLDEMMDFGYPQTTESKILQEYITQESHKL 139
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2763-2919 7.92e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.76  E-value: 7.92e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2763 DAGKSLTSAAVRGDAAEVRRLLEERRVHPDTRNEFGKTALQV-MMMGNTNVACLLLENGADPNIQDRFGITPAHDAARTG 2841
Cdd:COG0666     85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLaAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2842 FLDTLCVLVDYGASVNIPDQSGALPIHIAIREGYRDVVEFL----AprsNLGHQDTRGDTALDIAEASCTPDMVELLKRQ 2917
Cdd:COG0666    165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLleagA---DVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                   ..
gi 1709636372 2918 LE 2919
Cdd:COG0666    242 GA 243
BROMO smart00297
bromo domain;
1408-1516 1.20e-31

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 120.46  E-value: 1.20e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  1408 PSLTKKMKKIVDAVIKYKESsngRQLSEVFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQN 1487
Cdd:smart00297    2 PKLQKKLQELLKAVLDKLDS---HPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                            90       100
                    ....*....|....*....|....*....
gi 1709636372  1488 AQTFNLEGSLIYEDSIVLQSVFTSLRQKI 1516
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
DEXDc smart00487
DEAD-like helicases superfamily;
742-931 3.85e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 122.60  E-value: 3.85e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   742 QLKQYQIKGLEWLvslYNNNLNGILADEMGLGKTIQ-TIALITYLMEYKrlNGPYLIIVPLSTL-SNWVYEFDKWAPS-V 818
Cdd:smart00487    8 PLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGK--GGRVLVLVPTRELaEQWAEELKKLGPSlG 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   819 VKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKD--KQILAKIRWKYMIVDEGHRMKN--HHCKLTQVLNTHYLAPR 894
Cdd:smart00487   83 LKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKNVQ 162
                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 1709636372   895 RVLLTGTPLQNKLPELWALLN--FLLPTIFKSCSTFEQW 931
Cdd:smart00487  163 LLLLSATPPEEIENLLELFLNdpVFIDVGFTPLEPIEQF 201
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
1273-1340 4.10e-28

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: 109.27  E-value: 4.10e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709636372 1273 DRRREEARNPK-RRPRLMEEDELPTWIMKDDAEVERLTCEEEAEKMFGRGSRQRKEVDYSDSLTEKQWL 1340
Cdd:pfam14619    1 ERRREEAEQLPpLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
HSA smart00573
domain in helicases and associated with SANT domains;
453-525 3.92e-26

domain in helicases and associated with SANT domains;


Pssm-ID: 214727 [Multi-domain]  Cd Length: 73  Bit Score: 103.63  E-value: 3.92e-26
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709636372   453 QKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKMQKLTKAVATYHANTEREQKKENERIEKERMRRLMA 525
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1069-1178 2.18e-24

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: 99.98  E-value: 2.18e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1069 GKFEVLDRILPKLRatNHKVLLFCQMTSlmTIMEDYFAYR-NFKYLRLD-----EDRGMLLKMFNDPESQyfiFLLSTRA 1142
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKK--TLEAELLLEKeGIKVARLHgdlsqEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1709636372 1143 GGLGLNLQSADTVVIFDSDWNPHQDLQAQDRAHRIG 1178
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HSA pfam07529
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ...
454-520 5.52e-23

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: 94.56  E-value: 5.52e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709636372  454 KIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKMQKLTKAVATYHANTEREQKKENERIEKERM 520
Cdd:pfam07529    1 RDEPERREKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQKRIEREEKQRL 67
HELICc smart00490
helicase superfamily c-terminal domain;
1100-1178 1.32e-18

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 82.64  E-value: 1.32e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  1100 IMEDYFAYRNFKYLRLD-----EDRGMLLKMFNDPESQyfiFLLSTRAGGLGLNLQSADTVVIFDSDWNPHQDLQAQDRA 1174
Cdd:smart00490    2 ELAELLKELGIKVARLHgglsqEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 1709636372  1175 HRIG 1178
Cdd:smart00490   79 GRAG 82
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1366-1518 2.32e-18

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 89.86  E-value: 2.32e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1366 RDRDLDSGPSTSGTRGARDKDEDSKRQKKRGRP-------PAEKITPNPPS---LTKKMKKIVDAVIKYkESSNGRQLSE 1435
Cdd:COG5076     89 SPFEKNRPESLRFDEIVFLAIESVTPESGLGSLlmahlktSVKKRKTPKIEdelLYADNKAIAKFKKQL-FLRDGRFLSS 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1436 VFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSLRQK 1515
Cdd:COG5076    168 IFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEE 247

                   ...
gi 1709636372 1516 IEK 1518
Cdd:COG5076    248 IPE 250
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1414-1502 2.76e-18

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: 81.59  E-value: 2.76e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1414 MKKIVDAVIKykessngRQLSEVFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFNL 1493
Cdd:pfam00439    1 CLEILDKLME-------HPIAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNG 73

                   ....*....
gi 1709636372 1494 EGSLIYEDS 1502
Cdd:pfam00439   74 PGSVIYKAA 82
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
605-648 1.89e-15

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: 72.16  E-value: 1.89e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1709636372  605 QMSDLPVKVIHVDSGKILSGVDAPKAGQLDTWLEMNPGYEVAPR 648
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 ...
175-209 5.80e-15

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: 70.44  E-value: 5.80e-15
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1709636372  175 PFNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQ 209
Cdd:pfam08880    1 PFTPAQLQELRAQILAYKYLSRNQPVPPELQQAIF 35
BRK smart00592
domain in transcription and CHROMO domain helicases;
606-650 2.48e-14

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 69.30  E-value: 2.48e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 1709636372   606 MSDLPVKVIHVDSGKILSGVDAPKAGQLDTWLEMNPGYEVAPRSD 650
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
1679-1713 4.63e-14

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: 68.00  E-value: 4.63e-14
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1709636372 1679 CTADEFRCADGQCISSSFVCDEDADCSDGSDEASC 1713
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
1596-1628 1.50e-13

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: 66.50  E-value: 1.50e-13
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1709636372  1596 TCTEQQFMCGNKKCITKQWVCDGMDDCGDGADE 1628
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
1763-1797 2.02e-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: 2.02e-13
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1709636372 1763 CSGQEFQCSNGQCIHTIWRCDGGFDCADHSDESNC 1797
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1677-1713 3.49e-13

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 65.73  E-value: 3.49e-13
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1709636372 1677 RNCTADEFRCADGQCISSSFVCDEDADCSDGSDEASC 1713
Cdd:pfam00057    1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
Ank_2 pfam12796
Ankyrin repeats (3 copies);
2808-2882 4.04e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 4.04e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709636372 2808 GNTNVACLLLENGADPNIQDRFGITPAHDAARTGFLDTLCVLVDYgASVNIPDQsGALPIHIAIREGYRDVVEFL 2882
Cdd:pfam12796    8 GNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLL 80
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
1717-1749 4.83e-13

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: 65.35  E-value: 4.83e-13
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1709636372  1717 TCTSGSFQCNNSVCVPELWACDGDPDCPDGSDE 1749
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
1679-1710 7.21e-13

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: 64.58  E-value: 7.21e-13
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1709636372  1679 CTADEFRCADGQCISSSFVCDEDADCSDGSDE 1710
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1717-1754 7.92e-13

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 64.58  E-value: 7.92e-13
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1709636372 1717 TCTSGSFQCNNSVCVPELWACDGDPDCPDGSDEwsEHC 1754
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDE--ENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
1718-1754 2.39e-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: 2.39e-12
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1709636372 1718 CTSGSFQCNNSVCVPELWACDGDPDCPDGSDEwsEHC 1754
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDE--ENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
1763-1794 3.21e-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: 62.65  E-value: 3.21e-12
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1709636372  1763 CSGQEFQCSNGQCIHTIWRCDGGFDCADHSDE 1794
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
QLQ smart00951
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ...
175-208 3.50e-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: 62.94  E-value: 3.50e-12
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1709636372   175 PFNQNQLHQLRAQIMAYK-MLARGQPLPDHLQMAV 208
Cdd:smart00951    2 PFTPAQLELLRAQILAYKyLLARNQPVPPELLQAI 36
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
1597-1629 3.85e-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: 62.61  E-value: 3.85e-12
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1709636372 1597 CTEQQFMCGNKKCITKQWVCDGMDDCGDGADEL 1629
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEE 33
Ldl_recept_b pfam00058
Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif ...
2096-2136 8.04e-12

Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif after the most conserved region of the repeat. The YWTD repeat is found in multiple tandem repeats and has been predicted to form a beta-propeller structure.


Pssm-ID: 459654  Cd Length: 42  Bit Score: 61.79  E-value: 8.04e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1709636372 2096 NFMYWTDWGSPAKIEKSGLNGADRTALVTDNIFWPTGITLD 2136
Cdd:pfam00058    1 GRLYWTDSSLRASISSADLNGSDRKTLFTDDLQHPNAIAVD 41
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1801-1836 1.47e-11

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 61.11  E-value: 1.47e-11
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1709636372 1801 TCRLDEFRCGDGSCIPGVRQCDGEFHCKDLSDEKDC 1836
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LY smart00135
Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) ...
2034-2075 1.96e-11

Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. Also present in a variety of molecules similar to gp300/megalin.


Pssm-ID: 214531 [Multi-domain]  Cd Length: 43  Bit Score: 60.69  E-value: 1.96e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1709636372  2034 TLIGNQMSSPNGLAVDWIHGNIYWTDTFLESISVATKDGSKR 2075
Cdd:smart00135    2 TLLSSGLGHPNGLAVDWIEGRLYWTDWGLDVIEVANLDGTNR 43
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
1802-1836 2.94e-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: 60.30  E-value: 2.94e-11
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1709636372 1802 CRLDEFRCGDGSCIPGVRQCDGEFHCKDLSDEKDC 1836
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1762-1797 8.04e-11

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 58.80  E-value: 8.04e-11
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1709636372 1762 PCSGQEFQCSNGQCIHTIWRCDGGFDCADHSDESNC 1797
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
EGF_CA smart00179
Calcium-binding EGF-like domain;
1920-1950 5.65e-10

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 56.49  E-value: 5.65e-10
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1709636372  1920 DIDECADPDTCSQ--VCVNLVGSFKCDCQAGYE 1950
Cdd:smart00179    1 DIDECASGNPCQNggTCVNTVGSYRCECPPGYT 33
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
19-351 6.25e-10

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: 65.03  E-value: 6.25e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   19 GPMMGPGPSPGSSHGMMGPSPG--------PSTTSGHSVSQQGAAGYTQQDSMHPMHKSLE-SLHEKNVGEESRFGQMKG 89
Cdd:pfam09606  122 NLLASLGRPQMPMGGAGFPSQMsrvgrmqpGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQgQAGGMNGGQQGPMGGQMP 201
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   90 VSMRAGGHAGMGPPPSPMDQHSQGYPSPLGSSDHVSSPLPA--GAPSTSGPllsssctSSSPLEGTDSQPSRsgAPSNTP 167
Cdd:pfam09606  202 PQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAmqQQQPQQQG-------QQSQLGMGINQMQQ--MPQGVG 272
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  168 GSSANPTPFNQNQLHQLRAQIMAYKMLARGQPLPDHLQ-MAVQGKR--PMPGMQQGQAMPSLPPGGAGGPVTGPGPLGPN 244
Cdd:pfam09606  273 GGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQtRQQQQQQggNHPAAHQQQMNQSVGQGGQVVALGGLNHLETW 352
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  245 Y--NRGHVLSGPSVPP-----SGPNAVPSANGPPKTWPEGPMVNAA--TPSNAPQKLIPPQ--------PTGRPSPVPPS 307
Cdd:pfam09606  353 NpgNFGGLGANPMQRGqpgmmSSPSPVPGQQVRQVTPNQFMRQSPQpsVPSPQGPGSQPPQshpggmipSPALIPSPSPQ 432
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1709636372  308 VPPAASPVMPPQTQSPGH----PGHSAQPTPTIP-----LHQKHNRITPMQKP 351
Cdd:pfam09606  433 MSQQPAQQRTIGQDSPGGslntPGQSAVNSPLNPqeeqlYREKYRQLTKYIEP 485
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
1801-1833 7.26e-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: 56.10  E-value: 7.26e-10
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1709636372  1801 TCRLDEFRCGDGSCIPGVRQCDGEFHCKDLSDE 1833
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
1884-1918 9.57e-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: 55.71  E-value: 9.57e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1709636372 1884 CLENNGGCSHICNDLKIGYECLCPSGYRLV-DHKRC 1918
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQdDGRTC 36
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
2803-2921 1.17e-09

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.15  E-value: 1.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2803 QVMMMGNTNVACLLLENGADPNIQDRFGITPAHDAARTGFLDTLCVLVDYGASVNIPDQSGALPIHIAIREGYRDVVEFL 2882
Cdd:PTZ00322    88 QLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1709636372 2883 APRSNLGHQdtrgdtaldiAEASCTPDMVELLKRQLESS 2921
Cdd:PTZ00322   168 SRHSQCHFE----------LGANAKPDSFTGKPPSLEDS 196
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
1638-1674 3.14e-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: 3.14e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1709636372 1638 CLSSEFTCSQSpvQCVSTRWRCDGKADCENGADELGC 1674
Cdd:cd00112      1 CPPNEFRCANG--RCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1596-1629 3.21e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 54.56  E-value: 3.21e-09
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1709636372 1596 TCTEQQFMCGNKKCITKQWVCDGMDDCGDGADEL 1629
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEE 35
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1920-1950 4.21e-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: 54.18  E-value: 4.21e-09
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1709636372 1920 DIDECADPDTCS--QVCVNLVGSFKCDCQAGYE 1950
Cdd:cd00054      1 DIDECASGNPCQngGTCVNTVGSYRCSCPPGYT 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1840-1874 1.21e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 52.64  E-value: 1.21e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1709636372 1840 SKCEGKDtFQCRSGECISIDKVCDKQRDCRDLSDE 1874
Cdd:pfam00057    1 STCSPNE-FQCGSGECIPRSWVCDGDPDCGDGSDE 34
LY smart00135
Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) ...
2077-2119 1.38e-08

Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. Also present in a variety of molecules similar to gp300/megalin.


Pssm-ID: 214531 [Multi-domain]  Cd Length: 43  Bit Score: 52.60  E-value: 1.38e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1709636372  2077 TLIKEGLSKPHAIVVDPERNFMYWTDWGSPaKIEKSGLNGADR 2119
Cdd:smart00135    2 TLLSSGLGHPNGLAVDWIEGRLYWTDWGLD-VIEVANLDGTNR 43
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
1844-1874 1.67e-08

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: 52.21  E-value: 1.67e-08
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1709636372 1844 GKDTFQCRSGECISIDKVCDKQRDCRDLSDE 1874
Cdd:cd00112      2 PPNEFRCANGRCIPSSWVCDGEDDCGDGSDE 32
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1636-1674 2.65e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 51.87  E-value: 2.65e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1709636372 1636 KKCLSSEFTCSQSpvQCVSTRWRCDGKADCENGADELGC 1674
Cdd:pfam00057    1 STCSPNEFQCGSG--ECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
1846-1874 2.73e-08

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: 51.87  E-value: 2.73e-08
                            10        20
                    ....*....|....*....|....*....
gi 1709636372  1846 DTFQCRSGECISIDKVCDKQRDCRDLSDE 1874
Cdd:smart00192    5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
PHA03247 PHA03247
large tegument protein UL36; Provisional
102-351 2.82e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.95  E-value: 2.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  102 PPPSPMDQHSQGYPSPLGSSDHVSSPLPAGAPSTSGPllsssCTSSSPLEGTDSQPSRSGAPSNTPGSSANPTPFNQnql 181
Cdd:PHA03247  2614 PSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE-----RPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRR--- 2685
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  182 HQLRAQIMAYKMLAR-----------------GQPLPDHLQMAVQGKRPMPGMQQGQAMPSLP--PGGAGGPVTGPGPLG 242
Cdd:PHA03247  2686 RAARPTVGSLTSLADpppppptpepaphalvsATPLPPGPAAARQASPALPAAPAPPAVPAGPatPGGPARPARPPTTAG 2765
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  243 PNYNrghvlSGPSVPPSGP----------------NAVPSANGP-PKTWPEGPMVNAATPSNAPQKLIPPQPTGRPSPVP 305
Cdd:PHA03247  2766 PPAP-----APPAAPAAGPprrltrpavaslsesrESLPSPWDPaDPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPP 2840
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1709636372  306 PSVPPAASPVMPPQTQSPGHPGH---SAQPTPTIPLHQKHNRITPMQKP 351
Cdd:PHA03247  2841 PPPGPPPPSLPLGGSVAPGGDVRrrpPSRSPAAKPAAPARPPVRRLARP 2889
Ldl_recept_b pfam00058
Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif ...
2053-2093 1.49e-07

Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif after the most conserved region of the repeat. The YWTD repeat is found in multiple tandem repeats and has been predicted to form a beta-propeller structure.


Pssm-ID: 459654  Cd Length: 42  Bit Score: 49.85  E-value: 1.49e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1709636372 2053 GNIYWTDTFLE-SISVATKDGSKRMTLIKEGLSKPHAIVVDP 2093
Cdd:pfam00058    1 GRLYWTDSSLRaSISSADLNGSDRKTLFTDDLQHPNAIAVDP 42
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
357-570 2.95e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 2.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  357 VEILQEREYRLEARITHRIQELENLpGSLAGDLRTKATIELKALRLLNFQRQLRQEVVVcmRRDAALETALDAKAYKRSK 436
Cdd:COG1196    283 LEEAQAEEYELLAELARLEQDIARL-EERRRELEERLEELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAE 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  437 RQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKMQKLTKAVATYHANTEREQKKENERIE 516
Cdd:COG1196    360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1709636372  517 KERMRRLMAEDEEGYRKLIDQKKDKRLAyLLQQTDEYVANLTELVRAHKAVQAL 570
Cdd:COG1196    440 EEEALEEAAEEEAELEEEEEALLELLAE-LLEEAALLEAALAELLEELAEAAAR 492
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
1637-1671 5.58e-07

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: 48.01  E-value: 5.58e-07
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1709636372  1637 KCLSSEFTCSQSpvQCVSTRWRCDGKADCENGADE 1671
Cdd:smart00192    1 TCPPGEFQCDNG--RCIPSSWVCDGVDDCGDGSDE 33
EGF_CA pfam07645
Calcium-binding EGF domain;
1920-1948 1.82e-06

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 46.46  E-value: 1.82e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1709636372 1920 DIDECADP-DTCSQ--VCVNLVGSFKCDCQAG 1948
Cdd:pfam07645    1 DVDECATGtHNCPAntVCVNTIGSFECRCPDG 32
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
2241-2278 3.82e-06

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: 45.70  E-value: 3.82e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1709636372 2241 NGGCEYLCLPAPKvnqlspKYTCACPDDKVLGPDMRKC 2278
Cdd:pfam14670    5 NGGCSHLCLNTPG------GYTCSCPEGYELQDDGRTC 36
LY smart00135
Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) ...
2122-2160 6.17e-06

Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. Also present in a variety of molecules similar to gp300/megalin.


Pssm-ID: 214531 [Multi-domain]  Cd Length: 43  Bit Score: 45.29  E-value: 6.17e-06
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1709636372  2122 LVTDNIFWPTGITLDLVNQRLYWLDAKLHMLSSIGVDGG 2160
Cdd:smart00135    3 LLSSGLGHPNGLAVDWIEGRLYWTDWGLDVIEVANLDGT 41
Ldl_recept_b pfam00058
Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif ...
2140-2182 6.20e-06

Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif after the most conserved region of the repeat. The YWTD repeat is found in multiple tandem repeats and has been predicted to form a beta-propeller structure.


Pssm-ID: 459654  Cd Length: 42  Bit Score: 45.23  E-value: 6.20e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1709636372 2140 QRLYWLDAKLH-MLSSIGVDGGLRHTLIVDErhLANPFSLAVFE 2182
Cdd:pfam00058    1 GRLYWTDSSLRaSISSADLNGSDRKTLFTDD--LQHPNAIAVDP 42
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
358-543 8.40e-06

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: 50.69  E-value: 8.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  358 EILQEREyRLEARITHRIQELEnlpgslagdlRTKATIElkALRLlnfqrQLRQEVVVCMRRDAALETALDakayKRSKR 437
Cdd:pfam13868  177 EIEEEKE-REIARLRAQQEKAQ----------DEKAERD--ELRA-----KLYQEEQERKERQKEREEAEK----KARQR 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  438 QSLREARITEKLEKQQKIEQERKRRQkhQEYLNSILQHAKDFKEYHRSVTGKMQKLTK-AVATYHANTEREQKKENERIE 516
Cdd:pfam13868  235 QELQQAREEQIELKERRLAEEAEREE--EEFERMLRKQAEDEEIEQEEAEKRRMKRLEhRRELEKQIEEREEQRAAEREE 312
                          170       180
                   ....*....|....*....|....*..
gi 1709636372  517 KERMRRLMAEDEEGYRKLIDQKKDKRL 543
Cdd:pfam13868  313 ELEEGERLREEEAERRERIEEERQKKL 339
EGF_CA smart00179
Calcium-binding EGF-like domain;
1880-1919 1.00e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 44.55  E-value: 1.00e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1709636372  1880 NVNECLENNGgCSH--ICNDLKIGYECLCPSGYRlvDHKRCE 1919
Cdd:smart00179    1 DIDECASGNP-CQNggTCVNTVGSYRCECPPGYT--DGRNCE 39
Ldl_recept_b pfam00058
Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif ...
2183-2223 3.42e-05

Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif after the most conserved region of the repeat. The YWTD repeat is found in multiple tandem repeats and has been predicted to form a beta-propeller structure.


Pssm-ID: 459654  Cd Length: 42  Bit Score: 43.30  E-value: 3.42e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1709636372 2183 EKVYWTDSFSQSILTANRLTGKNI-TKVVENLASPKDIVLYH 2223
Cdd:pfam00058    1 GRLYWTDSSLRASISSADLNGSDRkTLFTDDLQHPNAIAVDP 42
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1880-1919 4.10e-05

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: 43.01  E-value: 4.10e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1709636372 1880 NVNECLENNG-GCSHICNDLKIGYECLCPSGYRLvdhKRCE 1919
Cdd:cd00054      1 DIDECASGNPcQNGGTCVNTVGSYRCSCPPGYTG---RNCE 38
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
2002-2102 7.89e-05

Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271332 [Multi-domain]  Cd Length: 271  Bit Score: 47.20  E-value: 7.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2002 DVSSGTIFWSDLFHKKIysSPIDKAAysanhvtliGNQMSSPNGLAVDwIHGNIYWTDTFLESISVATKDGsKRMTLIKE 2081
Cdd:cd14962     29 DTGRGAVFVFDLPNGKV--FVIGNAG---------PNRFVSPIGVAID-ANGNLYVSDAELGKVFVFDRDG-KFLRAIGA 95
                           90       100
                   ....*....|....*....|...
gi 1709636372 2082 GL--SKPHAIVVDPERNFMYWTD 2102
Cdd:cd14962     96 GAlfKRPTGIAVDPAGKRLYVVD 118
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
363-569 8.14e-05

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: 48.53  E-value: 8.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  363 REYRLEARITHRIQELENLPGSLAGDLRtkatielkalRLLNFQRQLRQEVVVCMRRDAALETALDAKAYKRSKRQslre 442
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELR----------RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK---- 736
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  443 ARITEKLEKQQKIEQER----------------KRRQKH--QEYLNSIlqHAKDFKEYHRSVTGKMQKLTKAVATYHANT 504
Cdd:TIGR02169  737 ERLEELEEDLSSLEQEIenvkselkelearieeLEEDLHklEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARL 814
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709636372  505 EREQKKENER-IEKERMRRLMAEDEEGYRKLIDQKKD---------KRLAYLLQQTDEYVANLTELVRAHKAVQA 569
Cdd:TIGR02169  815 REIEQKLNRLtLEKEYLEKEIQELQEQRIDLKEQIKSiekeienlnGKKEELEEELEELEAALRDLESRLGDLKK 889
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
1996-2147 1.61e-04

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 45.84  E-value: 1.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1996 VVALDMDVSSGTIFWSDLFHKKIysSPIDKAAYSANHVTLIGnqmSSPNGLAVDWIHGNIYWTDTFLESISVATKDGSKR 2075
Cdd:COG3391     70 ADGADAGADGRRLYVANSGSGRV--SVIDLATGKVVATIPVG---GGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKV 144
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709636372 2076 MTLIKEGlSKPHAIVVDPERNFMYWTDWGSP--AKIEkSGLNGADRTalVTDNI---FWPTGITLDLVNQRLYWLDA 2147
Cdd:COG3391    145 VATIPVG-AGPHGIAVDPDGKRLYVANSGSNtvSVIV-SVIDTATGK--VVATIpvgGGPVGVAVSPDGRRLYVANR 217
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
178-424 4.44e-04

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


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 45.95  E-value: 4.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  178 QNQLHQLRAQimaykmlARGQPLPdhlqmavqgkRPMPGMQQGQAMpslpPGGAGGPVTGPGPLGPNYNRghvlsgPSVP 257
Cdd:TIGR01628  372 QDQFMQLQPR-------MRQLPMG----------SPMGGAMGQPPY----YGQGPQQQFNGQPLGWPRMS------MMPT 424
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  258 PSGPNAVPSANGPPktwpegPMVNAATPSNAPQKLIPPQPTGrpspvppsvppaaspVMPPQTQSPGHPGHSAQPTPTIP 337
Cdd:TIGR01628  425 PMGPGGPLRPNGLA------PMNAVRAPSRNAQNAAQKPPMQ---------------PVMYPPNYQSLPLSQDLPQPQST 483
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  338 LHQKHNRITPMQKPCGLDPveilQEREYRLEARITHRIQELE-NLPGSLAGDLrtkatIELK---ALRLLNFQRQLRQEV 413
Cdd:TIGR01628  484 ASQGGQNKKLAQVLASATP----QMQKQVLGERLFPLVEAIEpALAAKITGML-----LEMDnseLLHLLESPELLKSKV 554
                          250
                   ....*....|.
gi 1709636372  414 vvcmrrDAALE 424
Cdd:TIGR01628  555 ------DEALE 559
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
2771-2901 5.25e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.39  E-value: 5.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2771 AAVRGDAAEVRRLLEERRVHPDTRNEFGKTALQV-MMMGNTNVACLLLENGAD----PNIQDRF-GITPAHDAARTGFLD 2844
Cdd:cd22192     24 AAKENDVQAIKKLLKCPSCDLFQRGALGETALHVaALYDNLEAAVVLMEAAPElvnePMTSDLYqGETALHIAVVNQNLN 103
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709636372 2845 TLCVLVDYGASVNIPDQSGAL--------------PIHIAIREGYRDVVEFLAPR-SNLGHQDTRGDTALDI 2901
Cdd:cd22192    104 LVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHgADIRAQDSLGNTVLHI 175
LY smart00135
Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) ...
2163-2205 5.83e-04

Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. Also present in a variety of molecules similar to gp300/megalin.


Pssm-ID: 214531 [Multi-domain]  Cd Length: 43  Bit Score: 39.89  E-value: 5.83e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1709636372  2163 HTLIVDERHLANPFSLAVFEEKVYWTDSFSQSILTANrLTGKN 2205
Cdd:smart00135    1 RTLLSSGLGHPNGLAVDWIEGRLYWTDWGLDVIEVAN-LDGTN 42
PTZ00121 PTZ00121
MAEBL; Provisional
430-541 7.35e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 7.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  430 KAYKRSKRQSLREARITEKLEKQQKIEQERKRrqkhQEYLNSILQHAKDFKEYHRSVTGKMQKLTKAVATYHAntEREQK 509
Cdd:PTZ00121  1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKA----EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA--EEAKK 1614
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1709636372  510 KENERIEKERMRRlmaedEEGYRKLIDQKKDK 541
Cdd:PTZ00121  1615 AEEAKIKAEELKK-----AEEEKKKVEQLKKK 1641
 
Name Accession Description Interval E-value
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
720-970 5.60e-171

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: 525.76  E-value: 5.60e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  720 YYAVAHAVTEKVDKQSALLINGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIV 799
Cdd:cd18062      1 YYAVAHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  800 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 879
Cdd:cd18062     81 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  880 CKLTQVLNTHYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 959
Cdd:cd18062    161 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 240
                          250
                   ....*....|.
gi 1709636372  960 VLRPFLLRRLK 970
Cdd:cd18062    241 VLRPFLLRRLK 251
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
740-970 2.79e-166

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: 511.53  E-value: 2.79e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  740 NGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWAPSVV 819
Cdd:cd17996      1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  820 KVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYLAPRRVLLT 899
Cdd:cd17996     81 KIVYKGTPDVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHARYRLLLT 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709636372  900 GTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKV--DLNEEETILIIRRLHKVLRPFLLRRLK 970
Cdd:cd17996    161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVkiELNEEETLLIIRRLHKVLRPFLLRRLK 233
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
720-970 6.26e-163

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: 502.67  E-value: 6.26e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  720 YYAVAHAVTEKVDKQSALLINGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIV 799
Cdd:cd18063      1 YYTVAHAITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  800 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 879
Cdd:cd18063     81 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  880 CKLTQVLNTHYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 959
Cdd:cd18063    161 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHK 240
                          250
                   ....*....|.
gi 1709636372  960 VLRPFLLRRLK 970
Cdd:cd18063    241 VLRPFLLRRLK 251
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
739-1216 2.35e-158

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 520.90  E-value: 2.35e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  739 INGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWAPSV 818
Cdd:PLN03142   166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  819 VKVSYKGSPAARRAFVPQ-LRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYlapr 894
Cdd:PLN03142   246 RAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  895 RVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGEkvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 974
Cdd:PLN03142   322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  975 AQLPEKVEYVIKCDMSALQRVLYRHMQAKGV-LLTDGSEKDKkgkggtktLMNTIMQLRKICNHPYMFQQIEESfsehlg 1053
Cdd:PLN03142   392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLNIAMQLRKCCNHPYLFQGAEPG------ 457
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1054 fsGGIVQGADLYRASGKFEVLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRNFKYLRLD-----EDRGMLLKMFND 1128
Cdd:PLN03142   458 --PPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDgntggEDRDASIDAFNK 535
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1129 PESQYFIFLLSTRAGGLGLNLQSADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNV 1208
Cdd:PLN03142   536 PGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL 615

                   ....*...
gi 1709636372 1209 DQKVIQAG 1216
Cdd:PLN03142   616 DALVIQQG 623
AP-1_Mu1B_Cterm cd09259
C-terminal domain of medium Mu1B subunit in epithelial cell-specific clathrin-associated ...
2527-2741 5.80e-142

C-terminal domain of medium Mu1B subunit in epithelial cell-specific clathrin-associated adaptor protein (AP) complex AP-1; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from different AP complexes exhibits similarity with each other. This subfamily corresponds to the C-terminal domain of heterotetrameric clathrin-associated adaptor protein complex 1 (AP-1) medium mu1B subunit encoded by ap1m2 gene exclusively expressed in polarized epithelial cells. Epithelial cell-specific AP-1 is used to sort proteins to the basolateral plasma membrane, which involves the formation of clathrin-coated vesicles (CCVs) from the trans-Golgi network (TGN). Recruitment of AP-1 to the TGN membrane is regulated by a small GTPase, ADP-ribosylation factor 1 (ARF1). The phosphorylation/dephosphorylation events can also regulate the function of AP-1. The membrane-anchored cargo molecules can be linked to the outer lattice of CCVs by AP-1. Those cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-1 mu1B subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic reside-binding. Besides, AP-1 mu1B subunit mediates the basolateral recycling of low-density lipoprotein receptor (LDLR) and transferrin receptor (TfR) from the sorting endosomes, where the basolateral sorting signal does not belong to the tyrosine-based signals. Thus, the binding site in mu1B subunit of AP-1 for the signals of LDLR and TfR might be distinct from that for YXXPhi signals.


Pssm-ID: 271167  Cd Length: 268  Bit Score: 443.31  E-value: 5.80e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2527 TNAVSWRSEGIKYKKNEVFIDVIESINVLVNANGSVMSSDIVGSIKLKTMLSGMPELRLGLNDRVLFALTGRDKGKTVAM 2606
Cdd:cd09259      1 TNAVSWRSEGIKYKKNEVFIDVIESVNVLVNANGSVLSSEIVGCIKLKVFLSGMPELRLGLNDRVLFELTGRDKNKTVEL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2607 EDVKFHQCVRLSRFESDRTISFIPPDGESELMSYRINTHVKPLIWIESVIEKFSHSRVEIMVKAKGQFKKQSVANNVEVR 2686
Cdd:cd09259     81 EDVKFHQCVRLSRFENDRTISFIPPDGDFELMSYRLNTQVKPLIWIESVIEKFSHSRVEIMVKAKGQFKKQSVANNVEIR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2687 VPVPSDADSPKFKTSTGHAKYVPEKNVVVWTIKSFP------------------------------------------VR 2724
Cdd:cd09259    161 VPVPSDADSPKFKTSVGSAKYVPEKNVVVWSIKSFPggkeylmrahfglpsveneelegkppitvkfeipyftvsgiqVR 240
                          250
                   ....*....|....*..
gi 1709636372 2725 YMKIIEKSGYQALPWVR 2741
Cdd:cd09259    241 YMKIIEKSGYQALPWVR 257
AP-1_Mu1_Cterm cd09250
C-terminal domain of medium Mu1 subunit in clathrin-associated adaptor protein (AP) complex ...
2527-2741 8.25e-130

C-terminal domain of medium Mu1 subunit in clathrin-associated adaptor protein (AP) complex AP-1; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric clathrin-associated adaptor protein complex 1 (AP-1) medium mu1 subunit, which includes two closely related homologs, mu1A (encoded by ap1m1) and mu1B (encoded by ap1m2). Mu1A is ubiquitously expressed, but mu1B is expressed exclusively in polarized epithelial cells. AP-1 has been implicated in bi-directional transport between the trans-Golgi network (TGN) and endosomes. It plays an essential role in the formation of clathrin-coated vesicles (CCVs) from the trans-Golgi network (TGN). Epithelial cell-specific AP-1 is also involved in sorting to the basolateral surface of polarized epithelial cells. Recruitment of AP-1 to the TGN membrane is regulated by a small GTPase, ADP-ribosylation factor 1 (ARF1). Phosphorylation/dephosphorylation events can also regulate the function of AP-1. The membrane-anchored cargo molecules can be linked to the outer lattice of CCVs by AP-1. Those cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-1 mu1 subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


Pssm-ID: 271158  Cd Length: 272  Bit Score: 408.91  E-value: 8.25e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2527 TNAVSWRSEGIKYKKNEVFIDVIESINVLVNANGSVMSSDIVGSIKLKTMLSGMPELRLGLNDRVLFALTGRD-KGKTVA 2605
Cdd:cd09250      1 TNAVSWRPEGIKYKKNEVFLDVIESVNLLVDLNGQVLRSEIVGAIKMRSYLSGMPELKLGLNDKVLFEATGRSsKGKAVE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2606 MEDVKFHQCVRLSRFESDRTISFIPPDGESELMSYRINTHVKPLIWIESVIEKFSHSRVEIMVKAKGQFKKQSVANNVEV 2685
Cdd:cd09250     81 LEDVKFHQCVRLSRFENDRTISFIPPDGEFELMSYRLSTQVKPLIWVEPTVERHSRSRVEIMVKAKTQFKRRSTANNVEI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2686 RVPVPSDADSPKFKTSTGHAKYVPEKNVVVWTIKSFP------------------------------------------- 2722
Cdd:cd09250    161 RIPVPPDADSPRFKCSAGSVVYAPEKDALLWKIKSFPggkefsmraefglpsieseeeqgtekkapiqvkfeipyftvsg 240
                          250       260
                   ....*....|....*....|.
gi 1709636372 2723 --VRYMKIIEKSGYQALPWVR 2741
Cdd:cd09250    241 lqVRYLKIIEKSGYQALPWVR 261
AP-1_Mu1A_Cterm cd09258
C-terminal domain of medium Mu1A subunit in ubiquitously expressed clathrin-associated adaptor ...
2526-2741 1.03e-125

C-terminal domain of medium Mu1A subunit in ubiquitously expressed clathrin-associated adaptor protein (AP) complex AP-1; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This subfamily corresponds to the C-terminal domain of heterotetrameric clathrin-associated adaptor protein complex 1 (AP-1) medium mu1A subunit encoded by ap1m1 gene, which is ubiquitously expressed in all mammalian tissues and cells. AP-1 has been implicated in bidirectional transport between the trans-Golgi network (TGN) and endosomes. It is involved in the formation of clathrin-coated vesicles (CCVs) from the trans-Golgi network (TGN). The ubiquitous AP-1 is recruited to the TGN membrane, as well as to immature secretory granules. Recruitment of AP-1 to the TGN membrane is regulated by a small GTPase, ADP-ribosylation factor 1 (ARF1). Phosphorylation/dephosphorylation events can also regulate the function of AP-1. The membrane-anchored cargo molecules can be linked to the outer lattice of CCVs by AP-1. Those cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-1 mu1A subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


Pssm-ID: 271166  Cd Length: 270  Bit Score: 396.95  E-value: 1.03e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2526 VTNAVSWRSEGIKYKKNEVFIDVIESINVLVNANGSVMSSDIVGSIKLKTMLSGMPELRLGLNDRVLFALTGRDKGKTVA 2605
Cdd:cd09258      1 VTNAVSWRSEGIKYRKNEVFLDVIESVNLLVSANGNVLRSEIVGSIKMRVYLSGMPELRLGLNDKVLFENTGRGKSKSVE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2606 MEDVKFHQCVRLSRFESDRTISFIPPDGESELMSYRINTHVKPLIWIESVIEKFSHSRVEIMVKAKGQFKKQSVANNVEV 2685
Cdd:cd09258     81 LEDVKFHQCVRLSRFENDRTISFIPPDGEFELMSYRLNTHVKPLIWIESVIERHSHSRVEYMIKAKSQFKRRSTANNVEI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2686 RVPVPSDADSPKFKTSTGHAKYVPEKNVVVWTIKSFP------------------------------------------V 2723
Cdd:cd09258    161 HIPVPNDADSPKFKTTVGSVKYVPENSEIVWSIKSFPggkeylmrahfglpsveseekegrppisvkfeipyfttsgiqV 240
                          250
                   ....*....|....*...
gi 1709636372 2724 RYMKIIEKSGYQALPWVR 2741
Cdd:cd09258    241 RYLKIIEKSGYQALPWVR 258
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
739-1200 2.54e-121

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 401.14  E-value: 2.54e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  739 INGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEyKRLNGPYLIIVPLSTLSNWVYEFDKWAPSV 818
Cdd:COG0553    238 LKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIVAPTSLVGNWQRELAKFAPGL 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  819 VKVSYKGSPAARRAFVPqlrSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThyL-APRRVL 897
Cdd:COG0553    317 RVLVLDGTRERAKGANP---FEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRA--LkARHRLA 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  898 LTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPfamtGEKVDLNEEEtiliirRLHKVLRPFLLRRLKKEVEAQL 977
Cdd:COG0553    392 LTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP----IEKGDEEALE------RLRRLLRPFLLRRTKEDVLKDL 461
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  978 PEKVEYVIKCDMSALQRVLYRHMqakgVLLTDGSEKDKKGKGGTKTLMNTIMQLRKICNHPYMFQQIEESFSEHlgfsgg 1057
Cdd:COG0553    462 PEKTEETLYVELTPEQRALYEAV----LEYLRRELEGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSGR------ 531
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1058 ivqgadlyraSGKFEVLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRNFKYLRLD-----EDRGMLLKMFNDPESq 1132
Cdd:COG0553    532 ----------SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHggtsaEERDELVDRFQEGPE- 600
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709636372 1133 YFIFLLSTRAGGLGLNLQSADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILA 1200
Cdd:COG0553    601 APVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
746-1041 4.89e-115

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: 367.01  E-value: 4.89e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  746 YQIKGLEWLVSLYNN-NLNGILADEMGLGKTIQTIALITYLMEYKRL-NGPYLIIVPLSTLSNWVYEFDKWA--PSVVKV 821
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNwGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  822 SYKGSPAAR-RAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYLAPRRVLLTG 900
Cdd:pfam00176   81 VLHGNKRPQeRWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK-SLKTRNRWILTG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  901 TPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetiLIIRRLHKVLRPFLLRRLKKEVEAQLPEK 980
Cdd:pfam00176  160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK---------KGVSRLHKLLKPFLLRRTKKDVEKSLPPK 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709636372  981 VEYVIKCDMSALQRVLY-RHMQAKGVLLTDGSEkdkKGKGGTKTLMNTIMQLRKICNHPYMF 1041
Cdd:pfam00176  231 VEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGE---GGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
740-970 1.81e-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: 302.32  E-value: 1.81e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  740 NGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWAPSVV 819
Cdd:cd17997      1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  820 KVSYKGSPAARRAFV-PQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYlaprR 895
Cdd:cd17997     81 VVVLIGDKEERADIIrDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVrlfNSRN----R 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709636372  896 VLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNApfamtgEKVDLNEEEtilIIRRLHKVLRPFLLRRLK 970
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 ...
740-970 1.16e-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: 297.76  E-value: 1.16e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  740 NGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEyKRLNGPYLIIVPLSTLSNWVYEFDKWAPSVV 819
Cdd:cd18009      1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRE-RGVWGPFLVIAPLSTLPNWVNEFARFTPSVP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  820 KVSYKGSPAARRAFVPQLRS-----GKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYLAPR 894
Cdd:cd18009     80 VLLYHGTKEERERLRKKIMKregtlQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELK-TFNSDN 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709636372  895 RVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFN--APFAMTGEKVDLNEEETILIIRRLHKVLRPFLLRRLK 970
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 ...
743-968 1.94e-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: 270.76  E-value: 1.94e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWAPSVVKVS 822
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  823 YKGSPAARRAfvpqLRSG-----KFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYLAPRRVL 897
Cdd:cd18003     81 YYGSAKERKL----KRQGwmkpnSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLN-FNTQRRLL 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709636372  898 LTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPF-AMTGEKVDLNEEetilIIRRLHKVLRPFLLRR 968
Cdd:cd18003    156 LTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLtAMSEGSQEENEE----LVRRLHKVLRPFLLRR 223
AP-2_Mu2_Cterm cd09251
C-terminal domain of medium Mu2 subunit in ubiquitously expressed clathrin-associated adaptor ...
2539-2741 1.31e-80

C-terminal domain of medium Mu2 subunit in ubiquitously expressed clathrin-associated adaptor protein (AP) complex AP-2; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, -2, -3, and -4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric clathrin-associated adaptor protein complex 2 (AP-2) medium mu2 subunit. Mu2 is ubiquitously expressed in mammals. In higher eukaryotes, AP-2 plays a critical role in clathrin-mediated endocytosis from the plasma membrane in different cells. The membrane-anchored cargo molecules can be linked to the outer lattice of CCVs by AP-2. Those cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-2 mu2 subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding. Since the Y-X-X-Phi binding site is buried in the core structure of AP-2, a phosphorylation induced conformational change is required when the cargo molecules binds to AP-2. In addition, the C-terminal domain of mu2 subunit has been shown to bind other molecules. For instance, it can bind phosphoinositides, in particular PI[4,5]P2, which might be involved in the recognition process of the tyrosine-based signals. It can also interact with synaptotagmins, a family of important modulators of calcium-dependent neurosecretion within the synaptic vesicle (SV) membrane. Since many of the other endocytic adaptors responsible for biogenesis of synaptic vesicles exist, in the absence of AP-2, clathrin-mediated endocytosis can still occur. However, the cells may not survive in the complete absence of clathrin as well as AP-2.


Pssm-ID: 271159  Cd Length: 263  Bit Score: 267.15  E-value: 1.31e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2539 YKKNEVFIDVIESINVLVNANGSVMSSDIVGSIKLKTMLSGMPELRLGLNDRVLFALTGRDK------GKTVAMEDVKFH 2612
Cdd:cd09251      1 YRKNEVFLDVVESVNLLMSPQGQVLRADVDGVIVMKTYLSGMPECKFGLNDKLVLESEGKEKsgsksgKGSVELDDCTFH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2613 QCVRLSRFESDRTISFIPPDGESELMSYRINTHVKPLIWIESVIEKFSHSRVEIMVKAKGQFKKQSVANNVEVRVPVPSD 2692
Cdd:cd09251     81 QCVRLSKFDSERSISFIPPDGEFELMRYRVTENINLPFRVIPLVKEVGRTKLEYKVKIKSNFPPKLLATNVVVRIPVPKN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2693 ADSPKFKTSTGHAKYVPEKNVVVWTIKSFP-------------------------------------------VRYMKII 2729
Cdd:cd09251    161 TAKVTINVSKGKAKYDPEENAIVWKIKKFAgmtestlsaevellsttskkkkwsrppismdfevpmftasglrVRYLKVF 240
                          250
                   ....*....|..
gi 1709636372 2730 EKSGYQALPWVR 2741
Cdd:cd09251    241 EKSNYKTVKWVR 252
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
743-919 2.09e-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: 263.27  E-value: 2.09e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWAPSVVKVS 822
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  823 YKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYlAPRRVLLTGTP 902
Cdd:cd17919     81 YHGSQRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR-AKRRLLLTGTP 159
                          170
                   ....*....|....*..
gi 1709636372  903 LQNKLPELWALLNFLLP 919
Cdd:cd17919    160 LQNNLEELWALLDFLDP 176
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
742-968 6.63e-80

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: 263.45  E-value: 6.63e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  742 QLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWAPSVVKV 821
Cdd:cd17993      1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  822 SYKGSPAARRA------FVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYLAPRR 895
Cdd:cd17993     81 VYLGDIKSRDTireyefYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKE-FKTNNR 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709636372  896 VLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEqwfnapfamtgekVDLNEEETILiIRRLHKVLRPFLLRR 968
Cdd:cd17993    160 LLITGTPLQNSLKELWALLHFLMPGKFDIWEEFE-------------EEHDEEQEKG-IADLHKELEPFILRR 218
Adap_comp_sub pfam00928
Adaptor complexes medium subunit family; This family also contains members which are coatomer ...
2530-2741 8.84e-79

Adaptor complexes medium subunit family; This family also contains members which are coatomer subunits.


Pssm-ID: 395742  Cd Length: 259  Bit Score: 261.85  E-value: 8.84e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2530 VSWRSEGIKYKKNEVFIDVIESINVLVNANGSVMSSDIVGSIKLKTMLSGMPELRLGLNDRVLFaltgrdkgktVAMEDV 2609
Cdd:pfam00928    1 VPWRPPGIKYKKNEVFLDVIERVSVIVDKDGGLLNSEVQGTIDLKCFLSGMPELRLGLNDKLLL----------IELDDV 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2610 KFHQCVRLSRFESDRTISFIPPDGESELMSYRI-NTHVKPLIWIES-VIEKFSHSRVEIMVKAKGQFKKQSVANNVEVRV 2687
Cdd:pfam00928   71 SFHQCVNLDKFESERVISFIPPDGEFELMRYRLsTNEVKLPFTVKPiVSVSGDEGRVEIEVKLRSDFPKKLTAENVVISI 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2688 PVPSDADSPKFKTSTGHAKYVPEKNVVVWTIKSFP--------------------------------------------V 2723
Cdd:pfam00928  151 PVPKEASSPVLRVSDGKAKYDPEENALEWSIKKIPggnesslsgelelsvesssddefpsdppisvefsipmftasglkV 230
                          250
                   ....*....|....*...
gi 1709636372 2724 RYMKIIEKSgYQALPWVR 2741
Cdd:pfam00928  231 RYLKVEEEN-YKPYKWVR 247
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
743-968 5.72e-77

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: 255.25  E-value: 5.72e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWAPSVVkVS 822
Cdd:cd17995      1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTDMNV-VV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  823 YKGSPAARR------AFVPQL------RSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHY 890
Cdd:cd17995     80 YHGSGESRQiiqqyeMYFKDAqgrkkkGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLK-KL 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709636372  891 LAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 968
Cdd:cd17995    159 TLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFG----------DLKTAEQ---VEKLQALLKPYMLRR 223
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
741-980 1.74e-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: 248.81  E-value: 1.74e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  741 GQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWAPSVVK 820
Cdd:cd18064     14 GKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRA 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  821 VSYKGSPAARRAFVPQ-LRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYLAPRRVLLT 899
Cdd:cd18064     94 VCLIGDKDQRAAFVRDvLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR-EFKTTNRLLLT 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  900 GTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetilIIRRLHKVLRPFLLRRLKKEVEAQLPE 979
Cdd:cd18064    173 GTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQK----------LVERLHMVLRPFLLRRIKADVEKSLPP 242

                   .
gi 1709636372  980 K 980
Cdd:cd18064    243 K 243
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
741-970 3.07e-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: 241.85  E-value: 3.07e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  741 GQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWAPSVVK 820
Cdd:cd18065     14 GTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRA 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  821 VSYKGSPAARRAFV-PQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYLAPRRVLLT 899
Cdd:cd18065     94 VCLIGDKDARAAFIrDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR-EFKTTNRLLLT 172
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709636372  900 GTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetilIIRRLHKVLRPFLLRRLK 970
Cdd:cd18065    173 GTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQK----------LVERLHAVLKPFLLRRIK 233
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
743-968 8.40e-66

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: 223.54  E-value: 8.40e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWAPSVVKVS 822
Cdd:cd18002      1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  823 YKGSPAAR---RAFVPQ----LRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYLAPRR 895
Cdd:cd18002     81 YWGNPKDRkvlRKFWDRknlyTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTL-LSFHCRNR 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709636372  896 VLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGE-KVDLNEEEtiliIRRLHKVLRPFLLRR 968
Cdd:cd18002    160 LLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAEnKTGLNEHQ----LKRLHMILKPFMLRR 229
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
739-970 1.46e-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: 213.58  E-value: 1.46e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  739 INGQLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEyKRLNGPYLIIVPLSTLSNWVYEFDKWAPSV 818
Cdd:cd18012      1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKE-EGRKGPSLVVAPTSLIYNWEEEAAKFAPEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  819 VKVSYKGSPAARRAfvpQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQV---LNTHYlaprR 895
Cdd:cd18012     80 KVLVIHGTKRKREK---LRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAvkaLKADH----R 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709636372  896 VLLTGTPLQNKLPELWALLNFLLPTIFKScstfEQWFNAPFAMTGEKvDLNEEEtiliIRRLHKVLRPFLLRRLK 970
Cdd:cd18012    153 LALTGTPIENHLGELWSIFDFLNPGLLGS----YKRFKKRFAKPIEK-DGDEEA----LEELKKLISPFILRRLK 218
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
742-968 3.25e-62

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: 213.33  E-value: 3.25e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  742 QLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWAPSVVKV 821
Cdd:cd18054     20 ELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  822 SYKGSPAARRAFV------PQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYLAPRR 895
Cdd:cd18054    100 VYIGDLMSRNTIReyewihSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTL-IDFKSNHR 178
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709636372  896 VLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQwfnapfaMTGEKVDLNEEEtiliirrLHKVLRPFLLRR 968
Cdd:cd18054    179 LLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEE-------DHGKGRENGYQS-------LHKVLEPFLLRR 237
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1410-1516 8.13e-62

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: 206.89  E-value: 8.13e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1410 LTKKMKKIVDAVIKYKESSnGRQLSEVFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQ 1489
Cdd:cd05516      2 LTKKMNKIVDVVIKYKDSD-GRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQ 80
                           90       100
                   ....*....|....*....|....*..
gi 1709636372 1490 TFNLEGSLIYEDSIVLQSVFTSLRQKI 1516
Cdd:cd05516     81 TFNLEGSLIYEDSIVLQSVFKSARQKI 107
AP_MHD_Cterm cd07954
C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD); ...
2543-2723 7.18e-61

C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD); This family corresponds to the C-terminal domain of heterotetrameric AP complexes medium mu subunits and its homologs existing in monomeric stonins, delta-subunit of the heteroheptameric coat protein I (delta-COPI), a protein encoded by a pro-death gene referred as MuD (also known as MUDENG, mu-2 related death-inducing gene), an endocytic adaptor syp1, the mammalian FCH domain only proteins (FCHo1/2), SH3-containing GRB2-like protein 3-interacting protein 1 (SGIP1), and related proteins. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. Stonins have been characterized as clathrin-dependent AP-2 mu chain related factors and may act as cargo-specific sorting adaptors in endocytosis. Coat protein complex I (COPI)-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER, and intra-Golgi transport. MuD is distantly related to the C-terminal domain of mu2 subunit of AP-2. It is able to induce cell death by itself and plays an important role in cell death in various tissues. Syp1 represents a novel type of endocytic adaptor protein that participates in endocytosis, promotes vesicle tabulation, and contributes to cell polarity and stress responses. It shares the same domain architecture with its two ubiquitously expressed mammalian counterparts, FCHo1/2, which represent key initial proteins ultimately controlling cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. They bind specifically to the plasma membrane and recruit the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. Another mammalian neuronal-specific protein SGIP1 does have a C-terminal MHD and has been classified into this family as well. It is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis. It is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15.


Pssm-ID: 271157  Cd Length: 245  Bit Score: 209.95  E-value: 7.18e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2543 EVFIDVIESINVLVNANGSVMSSDIVGSIKLKTMLSGMPELRLGLNDRVLfaltgrdkgkTVAMEDVKFHQCVRLSRFES 2622
Cdd:cd07954      1 EVFLDVVEKVNLLISKDGSLLNSEVQGEIALKSFLSGMPEIRLGLNNPDV----------GIKLDDVSFHPCVRLKRFES 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2623 DRTISFIPPDGESELMSYRINTH-VKPLIWIESVIeKFSHSRVEIMVKAKGQFKKQSVANNVEVRVPVPSDADSPKFKTS 2701
Cdd:cd07954     71 ERVISFIPPDGEFELMSYRTVEPwSILPITIFPVV-SEEGSQLEVVITLKLSESLQLTAENVEVHIPLPSGVTSLKSKPS 149
                          170       180
                   ....*....|....*....|..
gi 1709636372 2702 TGHAKYVPEKNVVVWTIKSFPV 2723
Cdd:cd07954    150 DGQAKFDPEKNALVWRIKRIPV 171
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
743-968 4.11e-60

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: 206.52  E-value: 4.11e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWAPSVVKVS 822
Cdd:cd18006      1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  823 YKGSPAARRAFVPQLRS-GKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYLaPRRVLLTGT 901
Cdd:cd18006     81 YMGDKEKRLDLQQDIKStNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSV-DFRLLLTGT 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709636372  902 PLQNKLPELWALLNFLLPTIFkSCSTFEQWFNApFAMTGEKVDLNEEetiliirrLHKVLRPFLLRR 968
Cdd:cd18006    160 PIQNSLQELYALLSFIEPNVF-PKDKLDDFIKA-YSETDDESETVEE--------LHLLLQPFLLRR 216
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
743-968 5.75e-57

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: 196.51  E-value: 5.75e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWAPSVVKVS 822
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  823 YKGSpaarrafvpqlrsgkfNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYLApRRVLLTGTP 902
Cdd:cd17994     81 YVGD----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIG-YKLLLTGTP 143
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709636372  903 LQNKLPELWALLNFLLPTIFKSCSTFeqwfnapfamTGEKVDLNEEETiliIRRLHKVLRPFLLRR 968
Cdd:cd17994    144 LQNNLEELFHLLNFLTPERFNNLQGF----------LEEFADISKEDQ---IKKLHDLLGPHMLRR 196
AP-4_Mu4_Cterm cd09253
C-terminal domain of medium Mu4 subunit in adaptor protein (AP) complex AP-4; AP complexes ...
2533-2722 1.22e-54

C-terminal domain of medium Mu4 subunit in adaptor protein (AP) complex AP-4; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 4 (AP-4) medium mu4 subunit. AP-4 plays a role in signal-mediated trafficking of integral membrane proteins in mammalian cells. Unlike other AP complexes, AP-4 is found only in mammals and plants. It is believed to be part of a nonclathrin coat, since it might function independently of clathrin, a scaffolding protein participating in the formation of coated vesicles. Recruitment of AP-4 to the trans-Golgi network (TGN) membrane is regulated by a small GTPase, ADP-ribosylation factor 1 (ARF1) or a related protein. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. One of the most important sorting signals binding to mu subunits of AP complexes are tyrosine-based endocytotic signals, which are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. However, AP-4 does not bind most canonical tyrosine-based signals except for two naturally occurring ones from the lysosomal membrane proteins CD63 and LAMP-2a. It binds YX [FYL][FL]E motif, where X can be any residue, from the cytosolic tails of amyloid precursor protein (APP) family members in a distinct way.


Pssm-ID: 271161  Cd Length: 271  Bit Score: 192.79  E-value: 1.22e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2533 RSEGIKYKKNEVFIDVIESINVLVNANGSVMSSDIVGSIKLKTMLSGMPELRLGLNDRVLFALTGRDKGKT-VAMEDVKF 2611
Cdd:cd09253      2 SSRGSQDKRNEIFVDVLERLSVVFNANGQVLNSEIDGSIQMKSYLPGNPELRLALNEDLVIGKRENRAYYSaVVLDDCNF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2612 HQCVRLSRFESDRTISFIPPDGESELMSYRINTHVKPLIWIESVIEKFSHSRVEIMVKAKGQFKKQSVANNVEVRVPVPS 2691
Cdd:cd09253     82 HESVDLEEFESDRTLSLTPPDGEFTLMNYRISGEFKPPFRVFPSVEETSPYKLELVLKLRADFPPKSTATNVVVRIPLPK 161
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1709636372 2692 DADSPKFKTSTG----HAKYVPEKNVVVWTIKSFP 2722
Cdd:cd09253    162 GTTSVSCELGSGasgqSAEYKEKEKLVLWNIKKFP 196
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
743-922 5.18e-54

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: 187.98  E-value: 5.18e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRlNGPYLIIVPLSTLSNWVYEFDKWAPSVVKVS 822
Cdd:cd17998      1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGI-PGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  823 YKGSPAARRafvpQLR------SGKFNVLLTTYEYII---KDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYLAP 893
Cdd:cd17998     80 YYGSQEERK----HLRydilkgLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMT-INAN 154
                          170       180
                   ....*....|....*....|....*....
gi 1709636372  894 RRVLLTGTPLQNKLPELWALLNFLLPTIF 922
Cdd:cd17998    155 FRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1068-1189 2.08e-52

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: 181.14  E-value: 2.08e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1068 SGKFEVLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRNFKYLRLD-----EDRGMLLKMFNDPESqYFIFLLSTRA 1142
Cdd:cd18793     10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDgstssKERQKLVDRFNEDPD-IRVFLLSTKA 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1709636372 1143 GGLGLNLQSADTVVIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLC 1189
Cdd:cd18793     89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
742-968 3.11e-51

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: 181.79  E-value: 3.11e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  742 QLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWAPSVVKV 821
Cdd:cd18053     20 ELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  822 SYKGSPAARRAFV------PQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYLAPRR 895
Cdd:cd18053    100 VYLGDINSRNMIRthewmhPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTL-IDFKSNHR 178
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709636372  896 VLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQwfnapfaMTGEKVDLNEEEtiliirrLHKVLRPFLLRR 968
Cdd:cd18053    179 LLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEE-------EHGKGREYGYAS-------LHKELEPFLLRR 237
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
743-968 6.49e-51

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: 180.24  E-value: 6.49e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIaliTYLME--YKRLNGPYLIIVPLSTLSNWVYEFDKWAPSVVK 820
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSI---TFLSEifLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  821 VsYKGSPAARRAFV------------PQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNT 888
Cdd:cd18058     78 V-YHGSQISRQMIQqyemyyrdeqgnPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  889 HYLApRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 968
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, ...
743-919 2.64e-50

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: 177.52  E-value: 2.64e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWAP------ 816
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPpfrvvv 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  817 ------SVVKVSYKGSPAARRAFVPQLRsGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQV---LN 887
Cdd:cd18000     81 lhssgsGTGSEEKLGSIERKSQLIRKVV-GDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLAckqLR 159
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1709636372  888 ThylaPRRVLLTGTPLQNKLPELWALLNFLLP 919
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 ...
743-968 3.95e-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: 175.62  E-value: 3.95e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALItYLMEYKR------LNGPYLIIVPLSTLSNWVYEFDKWAP 816
Cdd:cd17999      1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCIL-ASDHHKRansfnsENLPSLVVCPPTLVGHWVAEIKKYFP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  817 SVVK--VSYKGSPAARRAFVPQLrsGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYLAPR 894
Cdd:cd17999     80 NAFLkpLAYVGPPQERRRLREQG--EKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAV-KQLKANH 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709636372  895 RVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVD--LNEEETILIIRRLHKVLRPFLLRR 968
Cdd:cd17999    157 RLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKAsaKEQEAGALALEALHKQVLPFLLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
743-968 5.42e-49

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: 175.25  E-value: 5.42e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWAPSVVKVS 822
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  823 YKGSPAARRAFVPQ--------LRSG------------KFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKL 882
Cdd:cd18057     81 YTGDKESRSVIRENefsfednaIRSGkkvfrmkkeaqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  883 TQVLNThYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgekVDLNEEETiliIRRLHKVLR 962
Cdd:cd18057    161 FRVLNS-YKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF----------ADISKEDQ---IKKLHDLLG 226

                   ....*.
gi 1709636372  963 PFLLRR 968
Cdd:cd18057    227 PHMLRR 232
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
743-968 1.90e-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: 173.66  E-value: 1.90e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWAPSVVKVS 822
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  823 YKGSPAAR-------------------RAFVPQLRSG-KFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKL 882
Cdd:cd18055     81 YTGDKDSRaiirenefsfddnavkggkKAFKMKREAQvKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  883 TQVLNThYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgekVDLNEEETiliIRRLHKVLR 962
Cdd:cd18055    161 FRVLNG-YKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF----------ADISKEDQ---IKKLHDLLG 226

                   ....*.
gi 1709636372  963 PFLLRR 968
Cdd:cd18055    227 PHMLRR 232
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
743-968 2.78e-48

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: 172.91  E-value: 2.78e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALItYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWAPSVVkVS 822
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNV-VV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  823 YKGSPAARRAFV--------PQLR----SGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHY 890
Cdd:cd18059     79 YHGSQASRRTIQlyemyfkdPQGRvikgSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709636372  891 LApRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 968
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 ...
743-968 2.92e-48

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: 172.94  E-value: 2.92e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPyLIIVPLSTLSNWVYEFDKWAPSV-VKV 821
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSV-LVVMPTSLIPHWVKEFAKWTPGLrVKV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  822 SYKGSPAARRAfvpQLRS--GKFNVLLTTYEYIIKDKQILA-----KIRWKYMIVDEGHRMKNHHCKLTQVLntHYL-AP 893
Cdd:cd18001     80 FHGTSKKERER---NLERiqRGGGVLLTTYGMVLSNTEQLSaddhdEFKWDYVILDEGHKIKNSKTKSAKSL--REIpAK 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709636372  894 RRVLLTGTPLQNKLPELWALLNFLLP-TIFKSCSTFEQWFNAPFAMTGEKVDLNEEETI--LIIRRLHKVLRPFLLRR 968
Cdd:cd18001    155 NRIILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENPITRGRDKDATQGEKALgsEVAENLRQIIKPYFLRR 232
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
743-968 8.38e-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: 171.39  E-value: 8.38e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKrLNGPYLIIVPLSTLSNWVYEFDKWApSVVKVS 822
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVG-IHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  823 YKGSPAARRA--------------FVPQlrSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNt 888
Cdd:cd18060     79 YHGSLASRQMiqqyemyckdsrgrLIPG--AYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLK- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  889 HYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 968
Cdd:cd18060    156 HMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
AP-3_Mu3_Cterm cd09252
C-terminal domain of medium Mu3 subunit in adaptor protein (AP) complex AP-3; AP complexes ...
2530-2722 1.31e-47

C-terminal domain of medium Mu3 subunit in adaptor protein (AP) complex AP-3; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This family corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 3 (AP-3) medium mu3 subunit, which includes two closely related homologs, mu3A (P47A, encoded by ap3m1) and mu1B (P47B, encoded by ap3m2). Mu3A is ubiquitously expressed, but mu3B is specifically expressed in neurons and neuroendocrine cells. AP-3 is particularly important for targeting integral membrane proteins to lysosomes and lysome-related organelles at trans-Golgi network (TGN) and/or endosomes, such as the yeast vacuole, fly pigment granules and mammalian melanosomes, platelet dense bodies and the secretory lysosomes of cytotoxic T lymphocytes. Unlike AP-1 and AP-2, which function in conjunction with clathrin which is a scaffolding protein participating in the formation of coated vesicles, the nature of the outer shell of AP-3 containing coats remains to be elucidated. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-3 mu3 subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


Pssm-ID: 271160  Cd Length: 251  Bit Score: 172.00  E-value: 1.31e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2530 VSWRSEGIKYKKNEVFIDVIESINVLVNANGSVMSSDIVGSIKLKTMLSGMPELRLGLNDRVLFaltgrdkgktvamEDV 2609
Cdd:cd09252      1 VPWRRAGVKYTNNEIYFDVVEEIDAIVDKSGKPVSGEVRGEIDCNSRLSGMPDLLLSFNNPRLL-------------DDP 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2610 KFHQCVRLSRFESDRTISFIPPDGESELMSYRI--NTHVKPLIWiesVIEKFSHS----RVEIMVKAKGqfKKQSVANNV 2683
Cdd:cd09252     68 SFHPCVRYSRWESERVLSFIPPDGKFTLMSYRVdlNSLVSLPVY---VKPQISFSgssgRFEITVGSRQ--NLGKSIENV 142
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1709636372 2684 EVRVPVPSDADSPKFKTSTGHAKYVPEKNVVVWTIKSFP 2722
Cdd:cd09252    143 VVEIPLPKGVKSLRLTASHGSFSFDSSTKTLVWNIGKLT 181
AP1_Mu_N cd14835
AP-1 complex subunit mu N-terminal domain; AP-1 complex mu subunit is part of the ...
2429-2515 2.80e-47

AP-1 complex subunit mu N-terminal domain; AP-1 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large gamma-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In the case of AP-1 the coat protein is clathrin. AP-1 binds the phospholipid PI(4)P which plays a role in its localisation to the trans-Golgi network (TGN)/endosome. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341439  Cd Length: 139  Bit Score: 166.57  E-value: 2.80e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2429 VLICRNYKGDVDMSEIDHFLPLLLQQEEEGLMCP-----------------------------------------VFTEY 2467
Cdd:cd14835     12 VLISRNYRGDVPMSVIEKFMPLLMEKEEEGNLTPiltdggvtyiyikhnnlyllavtkknanaamvlsflyklveVFKEY 91
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1709636372 2468 FKELEEESIQDNFVVVYELLDELMDFGFPQTTDSKILQEYITQEGNKL 2515
Cdd:cd14835     92 FKELEEESIRDNFVIIYELLDEMMDFGYPQTTESKILQEYITQESHKL 139
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
743-968 1.31e-46

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: 168.71  E-value: 1.31e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALIT-----------------YLMEYKRLN---GPYLIIVPLS 802
Cdd:cd18005      1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAavlgktgtrrdrennrpRFKKKPPASsakKPVLIVAPLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  803 TLSNWVYEFDKWAPSVVKVsYKGSpaaRRAFVPQLR--SGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHC 880
Cdd:cd18005     81 VLYNWKDELDTWGHFEVGV-YHGS---RKDDELEGRlkAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  881 KLTQVLNThYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPF----AMTGEKVDLNEEETilIIRR 956
Cdd:cd18005    157 KLTQAMKE-LKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIkrgqRHTATARELRLGRK--RKQE 233
                          250
                   ....*....|..
gi 1709636372  957 LHKVLRPFLLRR 968
Cdd:cd18005    234 LAVKLSKFFLRR 245
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
743-968 9.74e-46

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: 166.01  E-value: 9.74e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWAPSVVKVS 822
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  823 YKGSPAArRAFVPQ---------LRSG------------KFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCK 881
Cdd:cd18056     81 YVGDKDS-RAIIREnefsfednaIRGGkkasrmkkeasvKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  882 LTQVLNTHYLApRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgekVDLNEEETiliIRRLHKVL 961
Cdd:cd18056    160 FFRVLNGYSLQ-HKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEF----------ADIAKEDQ---IKKLHDML 225

                   ....*..
gi 1709636372  962 RPFLLRR 968
Cdd:cd18056    226 GPHMLRR 232
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
743-968 1.44e-43

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: 159.40  E-value: 1.44e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTialITYLMEYKR--LNGPYLIIVPLSTLSNWVYEFDKWAPSVVk 820
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQS---ITFLYEILLtgIRGPFLIIAPLSTIANWEREFRTWTDLNV- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  821 VSYKGSPAARRAFV--------PQLR----SGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNT 888
Cdd:cd18061     77 VVYHGSLISRQMIQqyemyfrdSQGRiirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  889 HYLApRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 968
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 ...
743-968 1.91e-42

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: 156.68  E-value: 1.91e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVS--LYNNNLNG---ILADEMGLGKTIQTIALITYLMEYKRLNGP----YLIIVPLSTLSNWVYEFDK 813
Cdd:cd18004      1 LRPHQREGVQFLYDclTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  814 WAPSVVK--VSYKGSPAARRAFVPQLRSGK-FNVLLTTYE-YIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTh 889
Cdd:cd18004     81 WLGLRRIkvVTADGNAKDVKASLDFFSSAStYPVLIISYEtLRRHAEKLSKKISIDLLICDEGHRLKNSESKTTKALNS- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  890 YLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvDLNEEETILIIRRLH---KVLRPFLL 966
Cdd:cd18004    160 LPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDP-DASEEDKELGAERSQelsELTSRFIL 238

                   ..
gi 1709636372  967 RR 968
Cdd:cd18004    239 RR 240
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
743-968 3.18e-41

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: 153.21  E-value: 3.18e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSLynnnlNGILADEMGLGKTIQTIALI-----------------TYLMEYKRLNGPYLIIVPLSTLS 805
Cdd:cd18008      1 LLPYQKQGLAWMLPR-----GGILADEMGLGKTIQALALIlatrpqdpkipeeleenSSDPKKLYLSKTTLIVVPLSLLS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  806 NWVYEFDK-WAPSVVKVS-YKGSPAARRAFVPQlrsgKFNVLLTTY-----EY-----------IIKDKQILAKIRWKYM 867
Cdd:cd18008     76 QWKDEIEKhTKPGSLKVYvYHGSKRIKSIEELS----DYDIVITTYgtlasEFpknkkgggrdsKEKEASPLHRIRWYRV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  868 IVDEGHRMKNHHCKLTQV---LNTHylapRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvd 944
Cdd:cd18008    152 ILDEAHNIKNRSTKTSRAvcaLKAE----RRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRK-- 225
                          250       260
                   ....*....|....*....|....
gi 1709636372  945 lneeetilIIRRLHKVLRPFLLRR 968
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 ...
743-956 2.77e-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: 2.77e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLE--W--LVSLYNNNLNG---ILADEMGLGKTIQTIALITYLMEYKRLNGPYLIIVPLSTLSNWVYEFDKWA 815
Cdd:cd18007      1 LKPHQVEGVRflWsnLVGTDVGSDEGggcILAHTMGLGKTLQVITFLHTYLAAAPRRSRPLVLCPASTLYNWEDEFKKWL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  816 PSVVkVSYKGSPAARRAFVPQLRSGKFN-------VLLTTYEY---IIKDKQILAKIRWKYM-----------IVDEGHR 874
Cdd:cd18007     81 PPDL-RPLLVLVSLSASKRADARLRKINkwhkeggVLLIGYELfrnLASNATTDPRLKQEFIaalldpgpdllVLDEGHR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  875 MKNHHCKLTQVLNTHYlAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAmTGEKVDLNEEETILII 954
Cdd:cd18007    160 LKNEKSQLSKALSKVK-TKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIE-AGQCVDSTEEDVRLML 237

                   ..
gi 1709636372  955 RR 956
Cdd:cd18007    238 KR 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2763-2919 7.92e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.76  E-value: 7.92e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2763 DAGKSLTSAAVRGDAAEVRRLLEERRVHPDTRNEFGKTALQV-MMMGNTNVACLLLENGADPNIQDRFGITPAHDAARTG 2841
Cdd:COG0666     85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLaAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2842 FLDTLCVLVDYGASVNIPDQSGALPIHIAIREGYRDVVEFL----AprsNLGHQDTRGDTALDIAEASCTPDMVELLKRQ 2917
Cdd:COG0666    165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLleagA---DVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                   ..
gi 1709636372 2918 LE 2919
Cdd:COG0666    242 GA 243
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
743-968 1.10e-31

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: 125.66  E-value: 1.10e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSLYNNNL-----------------------------NGILADEMGLGKTIQTIALItylmeykrLNG 793
Cdd:cd18071      1 LLPHQKQALAWMVSRENSQDlppfweeavglflntitnfsqkkrpelvrGGILADDMGLGKTLTTISLI--------LAN 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  794 PYLIIVPLSTLSNWVYEF-DKWAPSVVKV-SYKGspAARRAFVPQLrsGKFNVLLTTY-----EYIIKDKQILAKIRWKY 866
Cdd:cd18071     73 FTLIVCPLSVLSNWETQFeEHVKPGQLKVyTYHG--GERNRDPKLL--SKYDIVLTTYntlasDFGAKGDSPLHTINWLR 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  867 MIVDEGHRMKNHHCKLTQ-VLNTHylAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMtGEKVDL 945
Cdd:cd18071    149 VVLDEGHQIRNPNAQQTKaVLNLS--SERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTM-GDPTGL 225
                          250       260
                   ....*....|....*....|...
gi 1709636372  946 neeetiliiRRLHKVLRPFLLRR 968
Cdd:cd18071    226 ---------KRLQVLMKQITLRR 239
BROMO smart00297
bromo domain;
1408-1516 1.20e-31

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 120.46  E-value: 1.20e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  1408 PSLTKKMKKIVDAVIKYKESsngRQLSEVFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQN 1487
Cdd:smart00297    2 PKLQKKLQELLKAVLDKLDS---HPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                            90       100
                    ....*....|....*....|....*....
gi 1709636372  1488 AQTFNLEGSLIYEDSIVLQSVFTSLRQKI 1516
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
DEXDc smart00487
DEAD-like helicases superfamily;
742-931 3.85e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 122.60  E-value: 3.85e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   742 QLKQYQIKGLEWLvslYNNNLNGILADEMGLGKTIQ-TIALITYLMEYKrlNGPYLIIVPLSTL-SNWVYEFDKWAPS-V 818
Cdd:smart00487    8 PLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGK--GGRVLVLVPTRELaEQWAEELKKLGPSlG 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   819 VKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKD--KQILAKIRWKYMIVDEGHRMKN--HHCKLTQVLNTHYLAPR 894
Cdd:smart00487   83 LKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKNVQ 162
                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 1709636372   895 RVLLTGTPLQNKLPELWALLN--FLLPTIFKSCSTFEQW 931
Cdd:smart00487  163 LLLLSATPPEEIENLLELFLNdpVFIDVGFTPLEPIEQF 201
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
743-968 1.68e-30

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: 122.26  E-value: 1.68e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSL-----YNNNLNGILADEMGLGKTIQTIALITYLMEykrlNGPY---------LIIVPLSTLSNWV 808
Cdd:cd18066      1 LRPHQREGIEFLYECvmgmrVNERFGAILADEMGLGKTLQCISLIWTLLR----QGPYggkpvikraLIVTPGSLVKNWK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  809 YEFDKWAPSV-VKVSYKGSPAARRAFVpqlRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLn 887
Cdd:cd18066     77 KEFQKWLGSErIKVFTVDQDHKVEEFI---ASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTAL- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  888 THYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIR--RLHKVLRPFL 965
Cdd:cd18066    153 TSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARaaELTRLTGLFI 232

                   ...
gi 1709636372  966 LRR 968
Cdd:cd18066    233 LRR 235
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
1410-1514 9.10e-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: 115.09  E-value: 9.10e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1410 LTKKMKKIVDAVIKYKESSnGRQLSEVFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQ 1489
Cdd:cd05515      1 MQQKLWELYNAVKNYTDGR-GRRLSLIFMRLPSKSEYPDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNAC 79
                           90       100
                   ....*....|....*....|....*
gi 1709636372 1490 TFNLEGSLIYEDSIVLQSVFTSLRQ 1514
Cdd:cd05515     80 KYNEPDSQIYKDALTLQKVLLETKR 104
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
1410-1510 9.38e-29

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: 112.43  E-value: 9.38e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1410 LTKKMKKIVDAVIKYkESSNGRQLSEVFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQ 1489
Cdd:cd05519      1 LKAAMLEIYDAVLNC-EDETGRKLSELFLEKPSKKLYPDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANAR 79
                           90       100
                   ....*....|....*....|.
gi 1709636372 1490 TFNLEGSLIYEDSIVLQSVFT 1510
Cdd:cd05519     80 TYNQEGSIVYEDAVEMEKAFK 100
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
743-968 3.97e-28

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: 115.64  E-value: 3.97e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWL----VSLYNNNLNG-ILADEMGLGKTIQTIALITYLM----EYKRLNGPYLIIVPLSTLSNWVYEFDK 813
Cdd:cd18067      1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLrqspQCKPEIDKAIVVSPSSLVKNWANELGK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  814 W-----APSVV--KVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVL 886
Cdd:cd18067     81 WlggrlQPLAIdgGSKKEIDRKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  887 NThYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETILIIRRLHK---VLRP 963
Cdd:cd18067    161 DS-LNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPI-LKGRDADASEKERQLGEEKLQElisIVNR 238

                   ....*
gi 1709636372  964 FLLRR 968
Cdd:cd18067    239 CIIRR 243
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
1273-1340 4.10e-28

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: 109.27  E-value: 4.10e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709636372 1273 DRRREEARNPK-RRPRLMEEDELPTWIMKDDAEVERLTCEEEAEKMFGRGSRQRKEVDYSDSLTEKQWL 1340
Cdd:pfam14619    1 ERRREEAEQLPpLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
1410-1512 8.68e-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: 109.38  E-value: 8.68e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1410 LTKKMKKIVDAVIKYKessngRQLSEVFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQ 1489
Cdd:cd04369      1 LKKKLRSLLDALKKLK-----RDLSEPFLEPVDPKEAPDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAK 75
                           90       100
                   ....*....|....*....|...
gi 1709636372 1490 TFNLEGSLIYEDSIVLQSVFTSL 1512
Cdd:cd04369     76 TYNGPGSPIYKDAKKLEKLFEKL 98
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
743-956 1.59e-26

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: 109.99  E-value: 1.59e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSlynNNLNGILADEMGLGKTIQTIALITYLmeykRLNGPYLIIVPLSTLSNWVYEFDKWAPSV---- 818
Cdd:cd18010      1 LLPFQREGVCFALR---RGGRVLIADEMGLGKTVQAIAIAAYY----REEWPLLIVCPSSLRLTWADEIERWLPSLppdd 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  819 VKVSYKGSPAARRafvpqlRSGKFNVllTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQV---LNTHylAPRR 895
Cdd:cd18010     74 IQVIVKSKDGLRD------GDAKVVI--VSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAalpLLKR--AKRV 143
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  896 VLLTGTPLQNKLPELWALLNFLLPTIFKSCSTF-EQWFNA----PFAMTGEKVDLNEEETILI----IRR 956
Cdd:cd18010    144 ILLSGTPALSRPIELFTQLDALDPKLFGRFHDFgRRYCAAkqggFGWDYSGSSNLEELHLLLLatimIRR 213
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2749-2914 2.31e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.97  E-value: 2.31e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2749 LLKTNKQTMVLSEGDAGKSLTSAAVRGDAAEVRRLLEERRVHPDTRNEFGKTAL-QVMMMGNTNVACLLLENGADPNIQD 2827
Cdd:COG0666     38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLhAAARNGDLEIVKLLLEAGADVNARD 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2828 RFGITPAHDAARTGFLDTLCVLVDYGASVNIPDQSGALPIHIAIREGYRDVVEFL----AprsNLGHQDTRGDTALDIAE 2903
Cdd:COG0666    118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLleagA---DVNARDNDGETPLHLAA 194
                          170
                   ....*....|.
gi 1709636372 2904 ASCTPDMVELL 2914
Cdd:COG0666    195 ENGHLEIVKLL 205
HSA smart00573
domain in helicases and associated with SANT domains;
453-525 3.92e-26

domain in helicases and associated with SANT domains;


Pssm-ID: 214727 [Multi-domain]  Cd Length: 73  Bit Score: 103.63  E-value: 3.92e-26
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709636372   453 QKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKMQKLTKAVATYHANTEREQKKENERIEKERMRRLMA 525
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
AP-3_Mu3A_Cterm cd09260
C-terminal domain of medium Mu3A subunit in ubiquitously expressed adaptor protein (AP) ...
2530-2718 1.36e-25

C-terminal domain of medium Mu3A subunit in ubiquitously expressed adaptor protein (AP) complex AP-3; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This subfamily corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 3 (AP-3) medium mu3A subunit encoded by ap3m1gene. Mu3A is ubiquitously expressed in all mammalian tissues and cells. It appears to be localized to the trans-Golgi network (TGN) and/or endosomes and participates in trafficking to the vacuole/lysosome in yeast, flies, and mammals. Unlike AP-1 and AP-2, which function in conjunction with clathrin which is a scaffolding protein participating in the formation of coated vesicles, the nature of the outer shell of ubiquitous AP-3 containing coats remains to be elucidated. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-3 mu3A subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


Pssm-ID: 211371  Cd Length: 254  Bit Score: 108.65  E-value: 1.36e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2530 VSWRSEGIKYKKNEVFIDVIESINVLVNANGSVMSSDIVGSIKLKTMLSGMPELRLG-LNDRVLfaltgrdkgktvamED 2608
Cdd:cd09260      1 IPWRRAGVKYTNNEAYFDVVEEIDAIIDKSGSTVFAEIQGVIDACIKLSGMPDLSLSfMNPRLL--------------DD 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2609 VKFHQCVRLSRFESDRTISFIPPDGESELMSYRINTH--VKPLIWIE---SVIEKFSHSRVEIMVKAKGQFKKqsVANNV 2683
Cdd:cd09260     67 VSFHPCIRFKRWESERVLSFIPPDGNFRLISYRVSSQnlVAIPVYVKhniSFKENSSCGRFDITIGPKQNMGK--TIEGI 144
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1709636372 2684 EVRVPVPSDADSPKFKTSTGHAKYVPEKNVVVWTI 2718
Cdd:cd09260    145 TVTVHMPKVVLNMNLTPTQGSYTFDPVTKVLAWDV 179
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
743-956 2.10e-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: 107.21  E-value: 2.10e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLvslYNN------------NLNGILADEMGLGKTIQTIALITYLMEYKRLNgPYLIIVPLSTLSNWVYE 810
Cdd:cd18069      1 LKPHQIGGIRFL---YDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDVLLRHTGAK-TVLAIVPVNTLQNWLSE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  811 FDKWAPSVV----------KVSYKGSPAARRAFVPQLRS---GKFNVLLTTYE-YIIKDKQILakirwkyMIVDEGHRMK 876
Cdd:cd18069     77 FNKWLPPPEalpnvrprpfKVFILNDEHKTTAARAKVIEdwvKDGGVLLMGYEmFRLRPGPDV-------VICDEGHRIK 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  877 NHHCKLTQVLNtHYLAPRRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETILIIRR 956
Cdd:cd18069    150 NCHASTSQALK-NIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPI-LNGQCVDSTPQDVKLMRYR 227
AP-3_Mu3B_Cterm cd09261
C-terminal domain of medium Mu3B subunit in neuron-specific adaptor protein (AP) complex AP-3; ...
2530-2718 4.10e-25

C-terminal domain of medium Mu3B subunit in neuron-specific adaptor protein (AP) complex AP-3; AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. There are four AP complexes, AP-1, AP-2, AP-3, and AP-4, described in various eukaryotic organisms. Each AP complex consists of four subunits: two large chains (one each of gamma/alpha/delta/epsilon and beta1-4, respectively), a medium mu chain (mu1-4), and a small sigma chain (sigma1-4). Each of the four subunits from the different AP complexes exhibits similarity with each other. This subfamily corresponds to the C-terminal domain of heterotetrameric adaptor protein complex 3 (AP-3) medium mu3B subunit encoded by ap3m2 gene. Mu3B is specifically expressed in neurons and neuroendocrine cells. Neuron-specific AP-3 appears to be involved in synaptic vesicle biogenesis from endosomes in neurons and plays an important role in synaptic transmission in the central nervous system. Unlike AP-1 and AP-2, which function in conjunction with clathrin which is a scaffolding protein participating in the formation of coated vesicles, the nature of the outer shell of neuron-specific AP-3 containing coats remains to be elucidated. Membrane-anchored cargo molecules interact with adaptors through short sorting signals in their cytosolic segments. Tyrosine-based endocytotic signals are one of the most important sorting signals. They are of the form Y-X-X-Phi, where Y is tyrosine, X is any amino acid and Phi is a bulky hydrophobic residue that can be Leu, Ile, Met, Phe, or Val. These kinds of sorting signals can be recognized by the C-terminal domain of AP-3 mu3B subunit, also known as Y-X-X-Phi signal-binding domain that contains two hydrophobic pockets, one for the tyrosine-binding and one for the bulky hydrophobic residue-binding.


Pssm-ID: 211372  Cd Length: 254  Bit Score: 107.05  E-value: 4.10e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2530 VSWRSEGIKYKKNEVFIDVIESINVLVNANGSVMSSDIVGSIKLKTMLSGMPELRLG-LNDRVLfaltgrdkgktvamED 2608
Cdd:cd09261      1 VPWRRTGVKYTNNEAYFDVIEEIDAIIDKSGSTITAEIQGVIDACVKLTGMPDLTLSfMNPRLL--------------DD 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2609 VKFHQCVRLSRFESDRTISFIPPDGESELMSYRINTH--VKPLIWIESVI---EKFSHSRVEIMVKAKGQFKKqsVANNV 2683
Cdd:cd09261     67 VSFHPCVRFKRWESERILSFIPPDGNFRLLSYHVSAQnlVAIPVYVKHNIsfrEGSSLGRFEITLGPKQTMGK--TVEGV 144
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1709636372 2684 EVRVPVPSDADSPKFKTSTGHAKYVPEKNVVVWTI 2718
Cdd:cd09261    145 TVTSQMPKGVLNMSLTPSQGTYTFDPVTKLLSWDV 179
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
1412-1515 1.35e-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: 100.21  E-value: 1.35e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1412 KKMKKIVDAVIKYKESsNGRQLSEVFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTF 1491
Cdd:cd05518      3 KRMLALFLYVLEYREG-SGRRLCDLFMEKPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHY 81
                           90       100
                   ....*....|....*....|....
gi 1709636372 1492 NLEGSLIYEDSIVLQSVftsLRQK 1515
Cdd:cd05518     82 NEEGSQVYEDANILEKV---LKEK 102
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1069-1178 2.18e-24

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: 99.98  E-value: 2.18e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1069 GKFEVLDRILPKLRatNHKVLLFCQMTSlmTIMEDYFAYR-NFKYLRLD-----EDRGMLLKMFNDPESQyfiFLLSTRA 1142
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKK--TLEAELLLEKeGIKVARLHgdlsqEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1709636372 1143 GGLGLNLQSADTVVIFDSDWNPHQDLQAQDRAHRIG 1178
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
AP-like_stonins_MHD cd09255
Mu homology domain (MHD) of adaptor-like proteins (AP-like), stonins; A small family of ...
2533-2722 1.79e-23

Mu homology domain (MHD) of adaptor-like proteins (AP-like), stonins; A small family of proteins named stonins has been characterized as clathrin-dependent AP-2 mu2 chain related factors, which may act as cargo-specific sorting adaptors in endocytosis. Stonins include stonin 1 and stonin 2, which are only mammalian homologs of Drosophila stoned B, a presynaptic protein implicated in neurotransmission and synaptic vesicle (SV) recycling. They are conserved from C. elegans to humans, but are not found in prokaryotes or yeasts. This family corresponds to the mu homology domain of stonins, which is distantly related to the C-terminal domain of mu chains among AP complexes. Due to the low degree of sequence conservation of the corresponding binding site, the mu homology domain of stonins is unable to recognize tyrosine-based endocytic sorting signals. To data, little is known about the localization and function of stonin 1. Stonin 2, also known as stoned B, acts as an AP-2-dependent synaptotagmin-specific sorting adaptors for SV endocytosis. Stoned A is not a stonin. It is structurally unrelated to the adaptins and does not appear to have mammalian homologs. It is not included in this family.


Pssm-ID: 271163 [Multi-domain]  Cd Length: 315  Bit Score: 104.03  E-value: 1.79e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2533 RSEGIKYKKNEVFIDVIESINVLVNANGSVMSSDIVGSIKLKTMLSGMPELRLGLNDRVlfaLTGRD-----------KG 2601
Cdd:cd09255      2 RDRGITYREDEITVDVTDEFHGKVTKTGEIKKLGVTVQIHILSFVTGDPECVLGLNDLE---VEGREvvrrqdimpssTD 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2602 KTVAMEDVKFHQCVRLSRFESDRTISFIPPDG-ESELMSYRINTHVKPL-IWIESVIE-KFSHSRVEIMVKAKGQFKKQS 2678
Cdd:cd09255     79 QWIKLHNCEFHSCVDVEEFEQSRSIKFHPLDAcRFELMRFRTRYNKKNLpLTLKSVVSvKGAHVELRADVRMSGYHSRNP 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2679 VA----NNVEVRVPVPSD--------------------------------ADSPKFKTSTGHAKYVPEKNVVVWTIKSFP 2722
Cdd:cd09255    159 LAqvpcENIMIRFPVPESwvpafrtekrfrekslkskknkkasggstaesLSEPVIEVSVGSAKYEHAYRAVVWRIDRLP 238
HSA pfam07529
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ...
454-520 5.52e-23

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: 94.56  E-value: 5.52e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709636372  454 KIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKMQKLTKAVATYHANTEREQKKENERIEKERM 520
Cdd:pfam07529    1 RDEPERREKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQKRIEREEKQRL 67
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
1428-1510 1.05e-22

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: 94.81  E-value: 1.05e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1428 SNGRQLSEVFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFNLEGSLIYEDSIVLQS 1507
Cdd:cd05517     18 PSGRLISELFQKLPSKVLYPDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFNEPGSQVYKDANAIKK 97

                   ...
gi 1709636372 1508 VFT 1510
Cdd:cd05517     98 IFT 100
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
1417-1516 8.04e-22

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: 92.78  E-value: 8.04e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1417 IVDAVIKYKeSSNGRQLSEVFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFNLEGS 1496
Cdd:cd05524     10 LYDTIRNYK-SEDGRILCESFIRVPKRRNEPEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDS 88
                           90       100
                   ....*....|....*....|
gi 1709636372 1497 LIYEDSIVLQSVFTSLRQKI 1516
Cdd:cd05524     89 PEHKDACKLWELFLSARNEV 108
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
764-956 7.98e-21

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: 94.57  E-value: 7.98e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  764 GILADEMGLGKTIQTIALI-TYLMEYKRLN-GPYLIIVPLSTLSNWVYEFDKWA-----PSVVKV----SYKGSPaaRRA 832
Cdd:cd18068     31 CILAHCMGLGKTLQVVTFLhTVLLCEKLENfSRVLVVCPLNTVLNWLNEFEKWQeglkdEEKIEVnelaTYKRPQ--ERS 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  833 FVPQLRSGKFNVLLTTYE-YII----KDKQILAKIRWKYM-----------IVDEGHRMKNHHCKLTQVLNThYLAPRRV 896
Cdd:cd18068    109 YKLQRWQEEGGVMIIGYDmYRIlaqeRNVKSREKLKEIFNkalvdpgpdfvVCDEGHILKNEASAVSKAMNS-IRTKRRI 187
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  897 LLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAmTGEKVDLNEEETILIIRR 956
Cdd:cd18068    188 VLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQ-NGQCADSTLVDVRVMKKR 246
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
743-968 8.26e-21

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: 94.08  E-value: 8.26e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSLYNNNLNG-ILADEMGLGKTIQTIALITY----------------LMEYKRLN------GPYLIIV 799
Cdd:cd18072      1 LLLHQKQALAWLLWRERQKPRGgILADDMGLGKTLTMIALILAqkntqnrkeeekekalTEWESKKDstlvpsAGTLVVC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  800 PLSTLSNWVYEFD-KWAPSVVKV-SYKGSPAARRAFVpqLRSgkFNVLLTTYEYIIK----DKQ-----ILAKIRWKYMI 868
Cdd:cd18072     81 PASLVHQWKNEVEsRVASNKLRVcLYHGPNRERIGEV--LRD--YDIVITTYSLVAKeiptYKEesrssPLFRIAWARII 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  869 VDEGHRMKNHH-------CKLtqvlNTHYlaprRVLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGE 941
Cdd:cd18072    157 LDEAHNIKNPKvqasiavCKL----RAHA----RWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGGE 228
                          250       260
                   ....*....|....*....|....*..
gi 1709636372  942 kvdlneeetiliirRLHKVLRPFLLRR 968
Cdd:cd18072    229 --------------RLNILTKSLLLRR 241
AP_Mu_N cd14828
AP complex subunit mu N-terminal domain; AP complex mu subunits are part of the ...
2429-2510 5.80e-20

AP complex subunit mu N-terminal domain; AP complex mu subunits are part of the heterotetrameric adaptor protein (AP) complex which consists of one large subunit (alpha-, gamma-, delta- or epsilon), one beta-, one mu-, and one sigma-subunit. In general, AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In most cases the coat protein is clathrin (AP1 and AP2 complex), but some of the other members of the AP complex family are associated with nonclathrin coats. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341432  Cd Length: 136  Bit Score: 88.41  E-value: 5.80e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2429 VLICRNYKGDV-DMSEIDHFLPLLLQQEEE-------------------GL---------------------MCPVFTEY 2467
Cdd:cd14828     12 PLISRNYRADInLQSVVQDFFKAYKKLNPEerppiissngwnfiyikrdDLyfvsvtqtnvnlmsvlvfldqFYDLLKDY 91
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1709636372 2468 FKE--LEEESIQDNFVVVYELLDELMDFGFPQTTDSKILQEYITQ 2510
Cdd:cd14828     92 FGVkkLDKNSIIDNFVLIYELIDESIDFGIIQLTDYNILKDYIKV 136
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
1430-1508 8.79e-20

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


Pssm-ID: 99951  Cd Length: 103  Bit Score: 86.62  E-value: 8.79e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709636372 1430 GRQLSEVFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFNLEGSLIYEDSIVLQSV 1508
Cdd:cd05520     20 GQLLAEPFLKLPSKRKYPDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIYKDAEKLQKL 98
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
765-922 1.53e-19

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: 89.66  E-value: 1.53e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  765 ILADEMGLGKTIQTIALITYLM---EYKRLngpyLIIVPLSTLSNW-VYEFDK-WAPSVVKVSYKGSPAARRAFVPQLRs 839
Cdd:cd18011     21 LLADEVGLGKTIEAGLIIKELLlrgDAKRV----LILCPASLVEQWqDELQDKfGLPFLILDRETAAQLRRLIGNPFEE- 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  840 gkFNVLLTTYEYI---IKDKQILAKIRWKYMIVDEGHRMKNHHC-------KLTQVLNTHylAPRRVLLTGTPLQNKLPE 909
Cdd:cd18011     96 --FPIVIVSLDLLkrsEERRGLLLSEEWDLVVVDEAHKLRNSGGgketkryKLGRLLAKR--ARHVLLLTATPHNGKEED 171
                          170
                   ....*....|...
gi 1709636372  910 LWALLNFLLPTIF 922
Cdd:cd18011    172 FRALLSLLDPGRF 184
AP2_Mu_N cd14836
AP-2 complex subunit mu N-terminal domain; AP-2 complex mu subunit is part of the ...
2463-2514 4.65e-19

AP-2 complex subunit mu N-terminal domain; AP-2 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-2 complex which consists of one large alpha-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In the case of AP-2 the coat protein is clathrin. AP-2 binds the phospholipid PI(4,5)P2 which is important for its localisation to the plasma membrane. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341440  Cd Length: 140  Bit Score: 86.04  E-value: 4.65e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1709636372 2463 VFTEYFKELEEESIQDNFVVVYELLDELMDFGFPQTTDSKILQEYITQEGNK 2514
Cdd:cd14836     88 LFKSYFGKFNEDSIKNNFVLIYELLDEILDFGYPQNTEPEALKTYITQEGVK 139
HELICc smart00490
helicase superfamily c-terminal domain;
1100-1178 1.32e-18

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 82.64  E-value: 1.32e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  1100 IMEDYFAYRNFKYLRLD-----EDRGMLLKMFNDPESQyfiFLLSTRAGGLGLNLQSADTVVIFDSDWNPHQDLQAQDRA 1174
Cdd:smart00490    2 ELAELLKELGIKVARLHgglsqEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 1709636372  1175 HRIG 1178
Cdd:smart00490   79 GRAG 82
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1366-1518 2.32e-18

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 89.86  E-value: 2.32e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1366 RDRDLDSGPSTSGTRGARDKDEDSKRQKKRGRP-------PAEKITPNPPS---LTKKMKKIVDAVIKYkESSNGRQLSE 1435
Cdd:COG5076     89 SPFEKNRPESLRFDEIVFLAIESVTPESGLGSLlmahlktSVKKRKTPKIEdelLYADNKAIAKFKKQL-FLRDGRFLSS 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1436 VFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSLRQK 1515
Cdd:COG5076    168 IFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEE 247

                   ...
gi 1709636372 1516 IEK 1518
Cdd:COG5076    248 IPE 250
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1414-1502 2.76e-18

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: 81.59  E-value: 2.76e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1414 MKKIVDAVIKykessngRQLSEVFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFNL 1493
Cdd:pfam00439    1 CLEILDKLME-------HPIAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNG 73

                   ....*....
gi 1709636372 1494 EGSLIYEDS 1502
Cdd:pfam00439   74 PGSVIYKAA 82
Bromo_Rsc1_2_I cd05521
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1410-1507 2.16e-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: 80.06  E-value: 2.16e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1410 LTKKMKKIVDAVIKYKESsNGRQLSEVFIQLPSRKELPEYYELIRRPVDFRKIKERIRshRYRSLNDLERDVMLLCQNAQ 1489
Cdd:cd05521      2 LSKKLKPLYDGIYTLKEE-NGIEIHPIFNVLPLRKDYPDYYKIIKNPLSLNTVKKRLP--HYTNAQEFVNDLAQIPWNAR 78
                           90
                   ....*....|....*...
gi 1709636372 1490 TFNLEGSLIYEDSIVLQS 1507
Cdd:cd05521     79 LYNTKGSVIYKYALILEK 96
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2768-2900 2.51e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 82.31  E-value: 2.51e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2768 LTSAAVRGDAAEVRRLLEeRRVHPDTRNEFGKTALQV-MMMGNTNVACLLLENGADPNIQDRFGITPAHDAARTGFLDTL 2846
Cdd:COG0666    157 LHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLHLaAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1709636372 2847 CVLVDYGASVNIPDQSGALPIHIAIREGYRDVVEFLAPRSNLGHQDTRGDTALD 2900
Cdd:COG0666    236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1413-1512 3.28e-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: 76.51  E-value: 3.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1413 KMKKIVDAVIKYKeSSNGRQLSEVFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFN 1492
Cdd:cd05522      5 RIKNILKGLRKER-DENGRLLTLHFEKLPDKAREPEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYN 83
                           90       100
                   ....*....|....*....|
gi 1709636372 1493 LEGSLIYEDSIVLQSVFTSL 1512
Cdd:cd05522     84 ENDSQEYKDAVLLEKEARLL 103
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2748-2914 5.59e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.15  E-value: 5.59e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2748 FLLKTNKQTMVLSEGDAGKSLTSAAVRGDAAEVRRLLEERRVHPDTRNEFGKTALQVMMMGNTNVACLLLENGADPNIQD 2827
Cdd:COG0666      5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2828 RFGITPAHDAARTGFLDTLCVLVDYGASVNIPDQSGALPIHIAIREGYRDVVEFL-APRSNLGHQDTRGDTALDIAEASC 2906
Cdd:COG0666     85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLlEAGADVNAQDNDGNTPLHLAAANG 164

                   ....*...
gi 1709636372 2907 TPDMVELL 2914
Cdd:COG0666    165 NLEIVKLL 172
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
605-648 1.89e-15

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: 72.16  E-value: 1.89e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1709636372  605 QMSDLPVKVIHVDSGKILSGVDAPKAGQLDTWLEMNPGYEVAPR 648
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
AP_longin-like cd14823
Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the ...
2429-2507 4.62e-15

Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the heterotetrameric adaptor protein (AP) complex which consists of one large subunit (alpha-, gamma-, delta- or epsilon), one beta-, one mu-, and one sigma-subunit. In general, AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In most cases the coat protein is clathrin (AP1 and AP2 complex), but some of the other members of the AP complex family are associated with nonclathrin coats. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.


Pssm-ID: 341427  Cd Length: 131  Bit Score: 74.09  E-value: 4.62e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2429 VLICRNYKGDV--DMSEIDHFLPLLLQQEE--------EGL-----------MC--------------------PVFTEY 2467
Cdd:cd14823     12 RLFAKYYDDTYpsVKEQKAFEKNIFNKKHRtdseivllEGLrvvykssidlyFVvigsknenellllevlnclvDVLSEY 91
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1709636372 2468 FKELEEESIQDNFVVVYELLDELMDFGFPQTTDSKILQEY 2507
Cdd:cd14823     92 FRKVEERAILENFEGLYFALDEIVDGGYIQETDPKQVVHF 131
QLQ pfam08880
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ...
175-209 5.80e-15

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: 70.44  E-value: 5.80e-15
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1709636372  175 PFNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQ 209
Cdd:pfam08880    1 PFTPAQLQELRAQILAYKYLSRNQPVPPELQQAIF 35
AP3_Mu_N cd14837
AP-3 complex subunit mu N-terminal domain; AP-3 complex mu subunit is part of the ...
2463-2508 1.22e-14

AP-3 complex subunit mu N-terminal domain; AP-3 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large delta-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. AP-3 binds the coat protein clathrin and the phospholipid PI(3)P and it is localized in the endosome. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341441  Cd Length: 139  Bit Score: 73.32  E-value: 1.22e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1709636372 2463 VFTEYFKELEEESIQDNFVVVYELLDELMDFGFPQTTDSKILQEYI 2508
Cdd:cd14837     87 VLEDYFGSLSESTIKENFVVVYQLLEEMLDNGFPLTTEPNALKELV 132
BRK smart00592
domain in transcription and CHROMO domain helicases;
606-650 2.48e-14

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 69.30  E-value: 2.48e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 1709636372   606 MSDLPVKVIHVDSGKILSGVDAPKAGQLDTWLEMNPGYEVAPRSD 650
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
743-917 4.33e-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: 75.07  E-value: 4.33e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVslynnNLNGILADEMGLGKTIQTIALI------------TYLMEYKRLN-------------GPYLI 797
Cdd:cd18070      1 LLPYQRRAVNWML-----VPGGILADEMGLGKTVEVLALIllhprpdndldaADDDSDEMVCcpdclvaetpvssKATLI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  798 IVPLSTLSNWVYEFDKWAPSVVKVS-YKGspaARRAFVPQLRSGKF----NVLLTTYEYIIKD----------------- 855
Cdd:cd18070     76 VCPSAILAQWLDEINRHVPSSLKVLtYQG---VKKDGALASPAPEIlaeyDIVVTTYDVLRTElhyaeanrsnrrrrrqk 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709636372  856 -----KQILAKIRWKYMIVDEghrMKNHHCKLTQVLNTHYLAPR--RVLLTGTPLQNKLPELWALLNFL 917
Cdd:cd18070    153 ryeapPSPLVLVEWWRVCLDE---AQMVESSTSKAAEMARRLPRvnRWCVSGTPIQRGLDDLFGLLSFL 218
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
1679-1713 4.63e-14

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: 68.00  E-value: 4.63e-14
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1709636372 1679 CTADEFRCADGQCISSSFVCDEDADCSDGSDEASC 1713
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
1596-1628 1.50e-13

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: 66.50  E-value: 1.50e-13
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1709636372  1596 TCTEQQFMCGNKKCITKQWVCDGMDDCGDGADE 1628
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
1763-1797 2.02e-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: 2.02e-13
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1709636372 1763 CSGQEFQCSNGQCIHTIWRCDGGFDCADHSDESNC 1797
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
743-933 2.17e-13

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: 72.00  E-value: 2.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLEWLVSlynNNLNGILADeMGLGKTIQTIALITYLMEyKRLNGPYLIIVPLSTLSN-WVYEFDKW-APSVVK 820
Cdd:cd18013      1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTVTTLTALSDLQL-DDFTRRVLVIAPLRVARStWPDEVEKWnHLRNLT 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  821 VSYK-GSPAARRAfvpqLRSGKFNVLLTTYEYIIK-DKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTH-YLAPRRVL 897
Cdd:cd18013     76 VSVAvGTERQRSK----AANTPADLYVINRENLKWlVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALRKVrPVIKRLIG 151
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1709636372  898 LTGTPLQNKLPELWALLNFL--LPTIFKSCSTF-EQWFN 933
Cdd:cd18013    152 LTGTPSPNGLMDLWAQIALLdqGERLGRSITAYrERWFD 190
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1677-1713 3.49e-13

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 65.73  E-value: 3.49e-13
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1709636372 1677 RNCTADEFRCADGQCISSSFVCDEDADCSDGSDEASC 1713
Cdd:pfam00057    1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
Ank_2 pfam12796
Ankyrin repeats (3 copies);
2808-2882 4.04e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 4.04e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709636372 2808 GNTNVACLLLENGADPNIQDRFGITPAHDAARTGFLDTLCVLVDYgASVNIPDQsGALPIHIAIREGYRDVVEFL 2882
Cdd:pfam12796    8 GNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLL 80
AP4_Mu_N cd14838
AP-4 complex subunit mu N-terminal domain; AP-4 complex mu subunit is part of the ...
2460-2511 4.41e-13

AP-4 complex subunit mu N-terminal domain; AP-4 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large epsilon-, one beta-, one mu-, and one sigma-subunit. AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. AP-4 does not bind the coat protein clathrin, it is associated with nonclathrin coats. Its phospholipid binding partner is unknown and it is localized in the trans-Golgi network (TGN). The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341442  Cd Length: 137  Bit Score: 68.73  E-value: 4.41e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1709636372 2460 MCPVFTEYFKELEEESIQDNFVVVYELLDELMDFGFPQTTDSKILQEYITQE 2511
Cdd:cd14838     82 IAKLIKDYCGVLNEESIRKNFVLIYELLDEILDFGYPQTTSTEQLKSFVYNE 133
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
1717-1749 4.83e-13

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: 65.35  E-value: 4.83e-13
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1709636372  1717 TCTSGSFQCNNSVCVPELWACDGDPDCPDGSDE 1749
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
1679-1710 7.21e-13

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: 64.58  E-value: 7.21e-13
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1709636372  1679 CTADEFRCADGQCISSSFVCDEDADCSDGSDE 1710
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1717-1754 7.92e-13

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 64.58  E-value: 7.92e-13
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1709636372 1717 TCTSGSFQCNNSVCVPELWACDGDPDCPDGSDEwsEHC 1754
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDE--ENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
1718-1754 2.39e-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: 2.39e-12
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1709636372 1718 CTSGSFQCNNSVCVPELWACDGDPDCPDGSDEwsEHC 1754
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDE--ENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
1763-1794 3.21e-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: 62.65  E-value: 3.21e-12
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1709636372  1763 CSGQEFQCSNGQCIHTIWRCDGGFDCADHSDE 1794
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
QLQ smart00951
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ...
175-208 3.50e-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: 62.94  E-value: 3.50e-12
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1709636372   175 PFNQNQLHQLRAQIMAYK-MLARGQPLPDHLQMAV 208
Cdd:smart00951    2 PFTPAQLELLRAQILAYKyLLARNQPVPPELLQAI 36
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
1597-1629 3.85e-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: 62.61  E-value: 3.85e-12
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1709636372 1597 CTEQQFMCGNKKCITKQWVCDGMDDCGDGADEL 1629
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEE 33
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
1437-1518 7.42e-12

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


Pssm-ID: 99941 [Multi-domain]  Cd Length: 101  Bit Score: 64.11  E-value: 7.42e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1437 FIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFtslRQKI 1516
Cdd:cd05509     22 FLEPVDKEEAPDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYNGPDTEYYKCANKLEKFF---WKKL 98

                   ..
gi 1709636372 1517 EK 1518
Cdd:cd05509     99 KE 100
Ldl_recept_b pfam00058
Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif ...
2096-2136 8.04e-12

Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif after the most conserved region of the repeat. The YWTD repeat is found in multiple tandem repeats and has been predicted to form a beta-propeller structure.


Pssm-ID: 459654  Cd Length: 42  Bit Score: 61.79  E-value: 8.04e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1709636372 2096 NFMYWTDWGSPAKIEKSGLNGADRTALVTDNIFWPTGITLD 2136
Cdd:pfam00058    1 GRLYWTDSSLRASISSADLNGSDRKTLFTDDLQHPNAIAVD 41
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
1410-1514 9.23e-12

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: 63.95  E-value: 9.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1410 LTKKMKKIVDAVIKYKESsNGRQLSEVFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQ 1489
Cdd:cd05525      3 LAQVLKEICDAIITYKDS-NGQSLAIPFINLPSKKKNPDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAE 81
                           90       100
                   ....*....|....*....|....*
gi 1709636372 1490 TFNLEGSLIYEDSIVLQSVFTSLRQ 1514
Cdd:cd05525     82 KYYGRKSPIGRDVCRLRKAYYQAKH 106
Ank_2 pfam12796
Ankyrin repeats (3 copies);
2835-2914 1.22e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 1.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2835 HDAARTGFLDTLCVLVDYGASVNIPDQSGALPIHIAIREGYRDVVEFLAPRSNLGHQDtRGDTALDIAEASCTPDMVELL 2914
Cdd:pfam12796    2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD-NGRTALHYAARSGHLEIVKLL 80
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1801-1836 1.47e-11

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 61.11  E-value: 1.47e-11
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1709636372 1801 TCRLDEFRCGDGSCIPGVRQCDGEFHCKDLSDEKDC 1836
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LY smart00135
Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) ...
2034-2075 1.96e-11

Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. Also present in a variety of molecules similar to gp300/megalin.


Pssm-ID: 214531 [Multi-domain]  Cd Length: 43  Bit Score: 60.69  E-value: 1.96e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1709636372  2034 TLIGNQMSSPNGLAVDWIHGNIYWTDTFLESISVATKDGSKR 2075
Cdd:smart00135    2 TLLSSGLGHPNGLAVDWIEGRLYWTDWGLDVIEVANLDGTNR 43
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
1802-1836 2.94e-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: 60.30  E-value: 2.94e-11
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1709636372 1802 CRLDEFRCGDGSCIPGVRQCDGEFHCKDLSDEKDC 1836
Cdd:cd00112      1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
1437-1509 5.13e-11

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: 62.03  E-value: 5.13e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709636372 1437 FIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFNLEGSLIYEDSIVLQSVF 1509
Cdd:cd05504     33 FLRPVSKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVFSNCFLYNPEHTSVYKAGTRLQRFF 105
Ank_2 pfam12796
Ankyrin repeats (3 copies);
2771-2860 6.80e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.90  E-value: 6.80e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2771 AAVRGDAAEVRRLLEERrVHPDTRNEFGKTALQV-MMMGNTNVACLLLENgADPNIQDRfGITPAHDAARTGFLDTLCVL 2849
Cdd:pfam12796    4 AAKNGNLELVKLLLENG-ADANLQDKNGRTALHLaAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLL 80
                           90
                   ....*....|.
gi 1709636372 2850 VDYGASVNIPD 2860
Cdd:pfam12796   81 LEKGADINVKD 91
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1762-1797 8.04e-11

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 58.80  E-value: 8.04e-11
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1709636372 1762 PCSGQEFQCSNGQCIHTIWRCDGGFDCADHSDESNC 1797
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
AP_stonin-1_MHD cd09262
Mu homology domain (MHD) of adaptor-like protein (AP-like), stonin-1 (also called Stoned ...
2539-2722 1.35e-10

Mu homology domain (MHD) of adaptor-like protein (AP-like), stonin-1 (also called Stoned B-like factor); A small family of proteins named stonins has been characterized as clathrin-dependent AP-2 mu2 chain related factors, which may act as cargo-specific sorting adaptors in endocytosis. Stonins include stonin 1 and stonin 2, which are the only mammalian homologs of Drosophila stoned B, a presynaptic protein implicated in neurotransmission and synaptic vesicle (SV) recycling. They are conserved from C. elegans to humans, but are not found in prokaryotes or yeasts. This family corresponds to the mu homology domain of stonin 1, which is distantly related to the C-terminal domain of mu chains among AP complexes. Due to the low degree of sequence conservation of the corresponding binding site, the mu homology domain of stonin-1 is unable to recognize tyrosine-based endocytic sorting signals. To data, little is known about the localization and function of stonin-1.


Pssm-ID: 271168  Cd Length: 314  Bit Score: 65.35  E-value: 1.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2539 YKKNEVFIDVIESINVLVNANGSVMSSDIVGSIKLKTMLSGMPELRLGLNDRVLFALTGR----DKGKT-VAMEDVKFHQ 2613
Cdd:cd09262      8 YEEQELSLEIVDNFWGKVTKEGKVVESAVITQIYCLCFVNGPGECFLTLNDLELLKRDESygekEAGKKwIEILDCHFHK 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2614 CVRLSRFESDRTISFIPPDG-ESELMSYR--INTHVKPLIWIESVIEKFSHSRVEIMVKAKGQFKKQSVA------NNVE 2684
Cdd:cd09262     88 CVNEQEFEQSRIIKFSPLDAcRAELMRFKtaYNGTQLPFSVKATVVVQGAYVELQAFLNMASTALSFGVSdshplcENVV 167
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2685 VRVPVPS-------------------------------DADS-PKFKTSTGHAKYVPEKNVVVWTIKSFP 2722
Cdd:cd09262    168 IRFPVPAqwikalwtmnlqrqkslkakmnrraclgalrETESrPVIQVSVGTAKYESAYSAVVWKIDRLP 237
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
1441-1512 2.10e-10

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


Pssm-ID: 99931  Cd Length: 102  Bit Score: 59.99  E-value: 2.10e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709636372 1441 PSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSL 1512
Cdd:cd05499     30 PVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVFNDK 101
AP_stonin-2_MHD cd09263
Mu homology domain (MHD) of adaptor-like protein (AP-like), stonin-2; A small family of ...
2536-2722 5.44e-10

Mu homology domain (MHD) of adaptor-like protein (AP-like), stonin-2; A small family of proteins named stonins has been characterized as clathrin-dependent AP-2 mu2 chain related factors, which may act as cargo-specific sorting adaptors in endocytosis. Stonins include stonin 1 and stonin 2, which are the only mammalian homologs of Drosophila stoned B, a presynaptic protein implicated in neurotransmission and synaptic vesicle (SV) recycling. They are conserved from C. elegans to humans, but are not found in prokaryotes or yeasts. This family corresponds to the mu homology domain of stonin 2, which is distantly related to the C-terminal domain of mu chains among AP complexes. Due to the low degree of sequence conservation of the corresponding binding site, the mu homology domain of stonin-2 is unable to recognize tyrosine-based endocytic sorting signals. It acts as an AP-2-dependent synaptotagmin-specific sorting adaptor for SV endocytosis.


Pssm-ID: 271169  Cd Length: 318  Bit Score: 63.50  E-value: 5.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2536 GIKYKKNEVFIDVIESIN-VLVNANGSVMSSDIVGSIKLKTMLSGMPELRLGLNDrvlFALTGRD-----------KGKT 2603
Cdd:cd09263      5 GLNYTEEEITVDVRDEFYgILSKGDSRILQHLVLTRINMLSFLSGLAECRLGLND---ILIKGNEivsrqdimpttTTKW 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2604 VAMEDVKFHQCVRLSRFESDRTISFIPPDG-ESELMSYRINTHVKPLIWIESVIEKFSHSRVEI---MVKAKGqFKK--- 2676
Cdd:cd09263     82 IKLRDCRFHECVDEDEFNNSRAILFNPLDAcRFELMRFRTVFAEKTLPFTLRTAASVNGAEVEVqswLVMSTG-FSSnrd 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2677 ---QSVANNVEVRVPVPSD--------------------------------ADSPKFKTSTGHAKYVPEKNVVVWTIKSF 2721
Cdd:cd09263    161 pltQVPCENVMIRYPVPEEwvknfrresvlgekslkakvnkgasfgststsGSEPVMRVTLGTAKYEHAFNSIVWRINRL 240

                   .
gi 1709636372 2722 P 2722
Cdd:cd09263    241 P 241
EGF_CA smart00179
Calcium-binding EGF-like domain;
1920-1950 5.65e-10

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 56.49  E-value: 5.65e-10
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1709636372  1920 DIDECADPDTCSQ--VCVNLVGSFKCDCQAGYE 1950
Cdd:smart00179    1 DIDECASGNPCQNggTCVNTVGSYRCECPPGYT 33
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
1445-1492 5.69e-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: 58.91  E-value: 5.69e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1709636372 1445 ELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFN 1492
Cdd:cd05528     32 EVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYN 79
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
19-351 6.25e-10

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: 65.03  E-value: 6.25e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   19 GPMMGPGPSPGSSHGMMGPSPG--------PSTTSGHSVSQQGAAGYTQQDSMHPMHKSLE-SLHEKNVGEESRFGQMKG 89
Cdd:pfam09606  122 NLLASLGRPQMPMGGAGFPSQMsrvgrmqpGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQgQAGGMNGGQQGPMGGQMP 201
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   90 VSMRAGGHAGMGPPPSPMDQHSQGYPSPLGSSDHVSSPLPA--GAPSTSGPllsssctSSSPLEGTDSQPSRsgAPSNTP 167
Cdd:pfam09606  202 PQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAmqQQQPQQQG-------QQSQLGMGINQMQQ--MPQGVG 272
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  168 GSSANPTPFNQNQLHQLRAQIMAYKMLARGQPLPDHLQ-MAVQGKR--PMPGMQQGQAMPSLPPGGAGGPVTGPGPLGPN 244
Cdd:pfam09606  273 GGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQtRQQQQQQggNHPAAHQQQMNQSVGQGGQVVALGGLNHLETW 352
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  245 Y--NRGHVLSGPSVPP-----SGPNAVPSANGPPKTWPEGPMVNAA--TPSNAPQKLIPPQ--------PTGRPSPVPPS 307
Cdd:pfam09606  353 NpgNFGGLGANPMQRGqpgmmSSPSPVPGQQVRQVTPNQFMRQSPQpsVPSPQGPGSQPPQshpggmipSPALIPSPSPQ 432
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1709636372  308 VPPAASPVMPPQTQSPGH----PGHSAQPTPTIP-----LHQKHNRITPMQKP 351
Cdd:pfam09606  433 MSQQPAQQRTIGQDSPGGslntPGQSAVNSPLNPqeeqlYREKYRQLTKYIEP 485
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
1801-1833 7.26e-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: 56.10  E-value: 7.26e-10
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1709636372  1801 TCRLDEFRCGDGSCIPGVRQCDGEFHCKDLSDE 1833
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
1884-1918 9.57e-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: 55.71  E-value: 9.57e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1709636372 1884 CLENNGGCSHICNDLKIGYECLCPSGYRLV-DHKRC 1918
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQdDGRTC 36
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
2803-2921 1.17e-09

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.15  E-value: 1.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2803 QVMMMGNTNVACLLLENGADPNIQDRFGITPAHDAARTGFLDTLCVLVDYGASVNIPDQSGALPIHIAIREGYRDVVEFL 2882
Cdd:PTZ00322    88 QLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1709636372 2883 APRSNLGHQdtrgdtaldiAEASCTPDMVELLKRQLESS 2921
Cdd:PTZ00322   168 SRHSQCHFE----------LGANAKPDSFTGKPPSLEDS 196
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1408-1512 1.63e-09

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


Pssm-ID: 99958  Cd Length: 128  Bit Score: 58.12  E-value: 1.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1408 PSLTKKMKKIVDavikykesSNGRQLSEVFIQ-LPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQ 1486
Cdd:cd05529     27 ERLISGLDKLLL--------SLQLEIAEYFEYpVDLRAWYPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILS 98
                           90       100
                   ....*....|....*....|....*.
gi 1709636372 1487 NAQTFNLEGSLIYEDSIVLQSVFTSL 1512
Cdd:cd05529     99 NAETFNEPNSEIAKKAKRLSDWLLRI 124
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
102-320 2.26e-09

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


Pssm-ID: 464609 [Multi-domain]  Cd Length: 325  Bit Score: 61.75  E-value: 2.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  102 PPPSPMDQHSQgypSPLGSSdHVSSPLPAGAPSTSGPLlssSCTSSSPLEGTDSQPSRSGAPSNTPGSSANP-TPFNQNQ 180
Cdd:pfam15279  103 PSSSPTSSNSS---KPLISV-ASSSKLLAPKPHEPPSL---PPPPLPPKKGRRHRPGLHPPLGRPPGSPPMSmTPRGLLG 175
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  181 LHQLRAQIMAYKMLARGQ--PLPDHLQMAvqgkrPMPGMQQGQAMPSLPPggAGGPVTGPGPLGPNYNRGHvlsGPSVPP 258
Cdd:pfam15279  176 KPQQHPPPSPLPAFMEPSsmPPPFLRPPP-----SIPQPNSPLSNPMLPG--IGPPPKPPRNLGPPSNPMH---RPPFSP 245
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709636372  259 SGPNAVPSANGPPKTwPEGPMVNAATPSNAPQklIPPQPTGRPSPVPPSVPPAASPVMPPQT 320
Cdd:pfam15279  246 HHPPPPPTPPGPPPG-LPPPPPRGFTPPFGPP--FPPVNMMPNPPEMNFGLPSLAPLVPPVT 304
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
1638-1674 3.14e-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: 3.14e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1709636372 1638 CLSSEFTCSQSpvQCVSTRWRCDGKADCENGADELGC 1674
Cdd:cd00112      1 CPPNEFRCANG--RCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1596-1629 3.21e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 54.56  E-value: 3.21e-09
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1709636372 1596 TCTEQQFMCGNKKCITKQWVCDGMDDCGDGADEL 1629
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEE 35
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1920-1950 4.21e-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: 54.18  E-value: 4.21e-09
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1709636372 1920 DIDECADPDTCS--QVCVNLVGSFKCDCQAGYE 1950
Cdd:cd00054      1 DIDECASGNPCQngGTCVNTVGSYRCSCPPGYT 33
PHA02874 PHA02874
ankyrin repeat protein; Provisional
2766-2914 4.22e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.52  E-value: 4.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2766 KSLTSAAVRGDAAEVRRLLEERRVHPDTRNEFGKTALQVMMMGNT-NVACLLLENGADPNIQDRFGITPAHDAARTGFLD 2844
Cdd:PHA02874   125 KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFfDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA 204
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709636372 2845 TLCVLVDYGASVNIPDQSGALPIHIAIREGyRDVVEFLAPRSNLGHQDTRGDTALDIA-EASCTPDMVELL 2914
Cdd:PHA02874   205 CIKLLIDHGNHIMNKCKNGFTPLHNAIIHN-RSAIELLINNASINDQDIDGSTPLHHAiNPPCDIDIIDIL 274
PHA03095 PHA03095
ankyrin-like protein; Provisional
2776-2914 4.73e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.58  E-value: 4.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2776 DAAEVRRLLEErrvHPDT--RNEFGKTALQVMMMGN----TNVACLLLENGADPNIQDRFGITPAHDAARTGF-LDTLCV 2848
Cdd:PHA03095    26 TVEEVRRLLAA---GADVnfRGEYGKTPLHLYLHYSsekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKL 102
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709636372 2849 LVDYGASVNIPDQSGALPIHI-----AIREgyrDVVEFLAPR-SNLGHQDTRGDTALDIAEAS--CTPDMVELL 2914
Cdd:PHA03095   103 LIKAGADVNAKDKVGRTPLHVylsgfNINP---KVIRLLLRKgADVNALDLYGMTPLAVLLKSrnANVELLRLL 173
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
1447-1499 7.80e-09

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: 55.49  E-value: 7.80e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1709636372 1447 PEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFNLEGSLIY 1499
Cdd:cd05513     32 PGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYNKPDTIYY 84
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1840-1874 1.21e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 52.64  E-value: 1.21e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1709636372 1840 SKCEGKDtFQCRSGECISIDKVCDKQRDCRDLSDE 1874
Cdd:pfam00057    1 STCSPNE-FQCGSGECIPRSWVCDGDPDCGDGSDE 34
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
1435-1506 1.24e-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: 54.71  E-value: 1.24e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709636372 1435 EVFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFNLEGSLIYEDSIVLQ 1506
Cdd:cd05512     20 EIFSEPVDLSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYNAKDTIFYRAAVRLR 91
LY smart00135
Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) ...
2077-2119 1.38e-08

Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. Also present in a variety of molecules similar to gp300/megalin.


Pssm-ID: 214531 [Multi-domain]  Cd Length: 43  Bit Score: 52.60  E-value: 1.38e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1709636372  2077 TLIKEGLSKPHAIVVDPERNFMYWTDWGSPaKIEKSGLNGADR 2119
Cdd:smart00135    2 TLLSSGLGHPNGLAVDWIEGRLYWTDWGLD-VIEVANLDGTNR 43
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
1431-1516 1.65e-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: 54.60  E-value: 1.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1431 RQLSEVFIQLPSR-------KELPEYYELIRRPVDFRKIKERIR---SHRYRSLNDLERDVMLLCQNAQTFNLEGSLIYE 1500
Cdd:cd05502     11 RLLLELYCHELSLpfhepvsPSVPNYYKIIKTPMDLSLIRKKLQpksPQHYSSPEEFVADVRLMFKNCYKFNEEDSEVAQ 90
                           90
                   ....*....|....*.
gi 1709636372 1501 DSIVLQSVFTSLRQKI 1516
Cdd:cd05502     91 AGKELELFFEEQLKEI 106
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
1844-1874 1.67e-08

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: 52.21  E-value: 1.67e-08
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1709636372 1844 GKDTFQCRSGECISIDKVCDKQRDCRDLSDE 1874
Cdd:cd00112      2 PPNEFRCANGRCIPSSWVCDGEDDCGDGSDE 32
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
1414-1492 2.24e-08

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: 54.29  E-value: 2.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1414 MKKIVDAVIKYKESSngrQLSEVFIQ-LPSRKElPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFN 1492
Cdd:cd05507      4 WKKAILLVYRTLASH---RYASVFLKpVTEDIA-PGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYN 79
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
1636-1674 2.65e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 51.87  E-value: 2.65e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1709636372 1636 KKCLSSEFTCSQSpvQCVSTRWRCDGKADCENGADELGC 1674
Cdd:pfam00057    1 STCSPNEFQCGSG--ECIPRSWVCDGDPDCGDGSDEENC 37
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2777-2914 2.72e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.04  E-value: 2.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2777 AAEVRRLLEERRVHPDTRNEFGKTALQVMMMGNTNVACLLLENGADPNIQDRFGITPAHDAARTGFLDTLCVLVDYGASV 2856
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1709636372 2857 NIPDQSGALPIHIAIREGYRDVVEFL-APRSNLGHQDTRGDTALDIAEASCTPDMVELL 2914
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLlEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
1846-1874 2.73e-08

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: 51.87  E-value: 2.73e-08
                            10        20
                    ....*....|....*....|....*....
gi 1709636372  1846 DTFQCRSGECISIDKVCDKQRDCRDLSDE 1874
Cdd:smart00192    5 GEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
PHA03247 PHA03247
large tegument protein UL36; Provisional
102-351 2.82e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.95  E-value: 2.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  102 PPPSPMDQHSQGYPSPLGSSDHVSSPLPAGAPSTSGPllsssCTSSSPLEGTDSQPSRSGAPSNTPGSSANPTPFNQnql 181
Cdd:PHA03247  2614 PSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE-----RPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRR--- 2685
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  182 HQLRAQIMAYKMLAR-----------------GQPLPDHLQMAVQGKRPMPGMQQGQAMPSLP--PGGAGGPVTGPGPLG 242
Cdd:PHA03247  2686 RAARPTVGSLTSLADpppppptpepaphalvsATPLPPGPAAARQASPALPAAPAPPAVPAGPatPGGPARPARPPTTAG 2765
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  243 PNYNrghvlSGPSVPPSGP----------------NAVPSANGP-PKTWPEGPMVNAATPSNAPQKLIPPQPTGRPSPVP 305
Cdd:PHA03247  2766 PPAP-----APPAAPAAGPprrltrpavaslsesrESLPSPWDPaDPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPP 2840
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1709636372  306 PSVPPAASPVMPPQTQSPGHPGH---SAQPTPTIPLHQKHNRITPMQKP 351
Cdd:PHA03247  2841 PPPGPPPPSLPLGGSVAPGGDVRrrpPSRSPAAKPAAPARPPVRRLARP 2889
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
98-334 3.07e-08

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 59.78  E-value: 3.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   98 AGMGPPPSPMDQHSQGYPSplgssdhvSSPLPAGAPSTSGPL-LSSSCTSSSPLEGTDSQPSRSGAPSNTPGSSANPTPF 176
Cdd:pfam03154  195 ATAGPTPSAPSVPPQGSPA--------TSQPPNQTQSTAAPHtLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPL 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  177 NQNQLHqlraqimaykmlARGQPLPDHLQmavQGKRPMPGMQQGQAMPSLPPGGAGGPVTGPGPLGPnynrGHVLSGPSV 256
Cdd:pfam03154  267 PQPSLH------------GQMPPMPHSLQ---TGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAP----GQSQQRIHT 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  257 PPSGPNavPSANGPPKTWPegpmvnaatpsnapqklIPPQPtgrpspvppsvppaasPVMP-------------PQTQSP 323
Cdd:pfam03154  328 PPSQSQ--LQSQQPPREQP-----------------LPPAP----------------LSMPhikpppttpipqlPNPQSH 372
                          250
                   ....*....|.
gi 1709636372  324 GHPGHSAQPTP 334
Cdd:pfam03154  373 KHPPHLSGPSP 383
PHA02874 PHA02874
ankyrin repeat protein; Provisional
2816-2882 4.63e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.44  E-value: 4.63e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709636372 2816 LLENGADPNIQDRFGITPAHDAARTGFLDTLCVLVDYGASVNIPDQSGALPIHIAIREGYRDVVEFL 2882
Cdd:PHA02874   110 ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLL 176
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
763-901 5.01e-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: 54.33  E-value: 5.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  763 NGILADEMGLGKTIQTIALITYLMEYKRlnGPYLIIVPLSTLSNWVYE-FDKWAPSVVKVSY--KGSPAARRAfvpQLRS 839
Cdd:cd00046      3 NVLITAPTGSGKTLAALLAALLLLLKKG--KKVLVLVPTKALALQTAErLRELFGPGIRVAVlvGGSSAEERE---KNKL 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709636372  840 GKFNVLLTTYEYIIKDKQILAKI---RWKYMIVDEGHRM----KNHHCKLTQVLNTHYLAPRRVLLTGT 901
Cdd:cd00046     78 GDADIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALlidsRGALILDLAVRKAGLKNAQVILLSAT 146
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
1441-1510 5.81e-08

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


Pssm-ID: 99930  Cd Length: 102  Bit Score: 53.05  E-value: 5.81e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1441 PSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFT 1510
Cdd:cd05498     30 PEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHPVHAMARKLQDVFE 99
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
1444-1496 7.01e-08

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


Pssm-ID: 99943 [Multi-domain]  Cd Length: 112  Bit Score: 53.04  E-value: 7.01e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1709636372 1444 KELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFNLEGS 1496
Cdd:cd05511     28 KKVPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDS 80
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
27-464 7.71e-08

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 58.24  E-value: 7.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   27 SPGSSHGMMGPSPGPS--------TTSGHSVSQQGAAGYTQQ-DSMH-PMHKSLESLHEKNVGEESRFGQMKGVSMRAGG 96
Cdd:pfam03154  200 TPSAPSVPPQGSPATSqppnqtqsTAAPHTLIQQTPTLHPQRlPSPHpPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMP 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   97 HA-GMGPPPSPMDQHSQGYPSPLGSSDHVSSPLPagAPSTSGPLLSSSCTSSSPLEGTDSQPSRSG----APSNTPGSSA 171
Cdd:pfam03154  280 HSlQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGP--SPAAPGQSQQRIHTPPSQSQLQSQQPPREQplppAPLSMPHIKP 357
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  172 NP-TPFNQ---NQLHQLRAQIMA---YKMLARGQP---------LPDH---------LQMavqgkrpMPGMQQGQAMPSL 226
Cdd:pfam03154  358 PPtTPIPQlpnPQSHKHPPHLSGpspFQMNSNLPPppalkplssLSTHhppsahpppLQL-------MPQSQQLPPPPAQ 430
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  227 PPGGAGGPvTGPGPLGPNYNRGHVLSGPSVPP--------SGPNAVPSANGPPKTWPEGpMVNAATPSNAPQKLIPPQPT 298
Cdd:pfam03154  431 PPVLTQSQ-SLPPPAASHPPTSGLHQVPSQSPfpqhpfvpGGPPPITPPSGPPTSTSSA-MPGIQPPSSASVSSSGPVPA 508
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  299 GRPSPVPPSVPPAASPVMPPQTQSPGHPGHSAQPTPTI---PLHQ-------KHnritpmqkpcgLDpveilqeREYRLE 368
Cdd:pfam03154  509 AVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEPTVvntPSHAsqsarfyKH-----------LD-------RGYNSC 570
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  369 ARithriQELENLPgsLAGDLRTKatielkalrllnfqrqlrqevvvcmRRDAALETAldakayKRSKRQSLREARITEK 448
Cdd:pfam03154  571 AR-----TDLYFMP--LAGSKLAK-------------------------KREEALEKA------KREAEQKAREEKEREK 612
                          490
                   ....*....|....*.
gi 1709636372  449 lEKQQKIEQERKRRQK 464
Cdd:pfam03154  613 -EKEKERERERERERE 627
PHA02874 PHA02874
ankyrin repeat protein; Provisional
2792-2902 7.85e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.67  E-value: 7.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2792 DTRNEFGKTALQ-VMMMGNTNVACLLLENGADPNIQDRFGITPAHDAARTGFLDTLCVLVDYGASVNIPDQSGALPIHIA 2870
Cdd:PHA02874   118 NIKDAELKTFLHyAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNA 197
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1709636372 2871 IREG-YRDVVEFLAPRSNLGHQDTRGDTALDIA 2902
Cdd:PHA02874   198 AEYGdYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA02875 PHA02875
ankyrin repeat protein; Provisional
2768-2924 8.92e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.31  E-value: 8.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2768 LTSAAVRGDAAEVRRLLEERRVHPDTRNEFGKTALQV-MMMGNTNVACLLLENGADPNIQDRFGITPAHDAARTGFLDTL 2846
Cdd:PHA02875    72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLaTILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2847 CVLVDYGASVNIPDQSGALPIHIAIREGYRDVVEFLAPR-SNLGHQDTRGD-TALDIAEASCTPDMVEL-LKRQLESSMT 2923
Cdd:PHA02875   152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSgANIDYFGKNGCvAALCYAIENNKIDIVRLfIKRGADCNIM 231

                   .
gi 1709636372 2924 F 2924
Cdd:PHA02875   232 F 232
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
1444-1511 1.14e-07

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: 51.99  E-value: 1.14e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709636372 1444 KELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTS 1511
Cdd:cd05503     28 KLVPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEVGRAGHNMRKFFEK 95
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
102-297 1.45e-07

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


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 53.34  E-value: 1.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  102 PPPSPMDQHSQGYPSPLGSSDHVSSPLPAGAPSTSGPllsssctsssPLEGTDSQPSrsgaPSNTPGSSANPTPfnqnql 181
Cdd:pfam06346    1 PPPPPLPGDSSTIPLPPGACIPTPPPLPGGGGPPPPP----------PLPGSAAIPP----PPPLPGGTSIPPP------ 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  182 hqlraqimaykmlargQPLPDhlQMAVQGKRPMPGMQQGQAMPSLpPGGAGGPvTGPGPLgPnynrghvlSGPSVPPSgP 261
Cdd:pfam06346   61 ----------------PPLPG--AASIPPPPPLPGSTGIPPPPPL-PGGAGIP-PPPPPL-P--------GGAGVPPP-P 110
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1709636372  262 NAVPSANG--PPKTWPEGPMVnaatPSNAPQKLIPPQP 297
Cdd:pfam06346  111 PPLPGGPGipPPPPFPGGPGI----PPPPPGMGMPPPP 144
Ldl_recept_b pfam00058
Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif ...
2053-2093 1.49e-07

Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif after the most conserved region of the repeat. The YWTD repeat is found in multiple tandem repeats and has been predicted to form a beta-propeller structure.


Pssm-ID: 459654  Cd Length: 42  Bit Score: 49.85  E-value: 1.49e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1709636372 2053 GNIYWTDTFLE-SISVATKDGSKRMTLIKEGLSKPHAIVVDP 2093
Cdd:pfam00058    1 GRLYWTDSSLRaSISSADLNGSDRKTLFTDDLQHPNAIAVDP 42
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
2802-2914 1.63e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.19  E-value: 1.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2802 LQVMMMGNTNVACLLLENGADPNIQDRFGITPAHDAARTGFLDTLCVLVDYGASVNIPDQSGALPIHIAIREGYR----- 2876
Cdd:PLN03192   530 LTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHkifri 609
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709636372 2877 --------------DVVEFLAPRSNLG-------------HQDTRGDTALDIAEASCTPDMVELL 2914
Cdd:PLN03192   610 lyhfasisdphaagDLLCTAAKRNDLTamkellkqglnvdSEDHQGATALQVAMAEDHVDMVRLL 674
Ank_5 pfam13857
Ankyrin repeats (many copies);
2849-2902 1.81e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.04  E-value: 1.81e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1709636372 2849 LVDYG-ASVNIPDQSGALPIHIAIREGYRDVVEFL-APRSNLGHQDTRGDTALDIA 2902
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLlAYGVDLNLKDEEGLTALDLA 56
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
1441-1509 2.58e-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: 51.16  E-value: 2.58e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709636372 1441 PSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFNLEGSLIYEDSIVLQSVF 1509
Cdd:cd05500     31 PVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQMGKRLQAAF 99
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
357-570 2.95e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 2.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  357 VEILQEREYRLEARITHRIQELENLpGSLAGDLRTKATIELKALRLLNFQRQLRQEVVVcmRRDAALETALDAKAYKRSK 436
Cdd:COG1196    283 LEEAQAEEYELLAELARLEQDIARL-EERRRELEERLEELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAE 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  437 RQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKMQKLTKAVATYHANTEREQKKENERIE 516
Cdd:COG1196    360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1709636372  517 KERMRRLMAEDEEGYRKLIDQKKDKRLAyLLQQTDEYVANLTELVRAHKAVQAL 570
Cdd:COG1196    440 EEEALEEAAEEEAELEEEEEALLELLAE-LLEEAALLEAALAELLEELAEAAAR 492
ResIII pfam04851
Type III restriction enzyme, res subunit;
742-902 3.82e-07

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 52.29  E-value: 3.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  742 QLKQYQIKGLE-WLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEyKRLNGPYLIIVP-LSTLSNWVYEFDKWAPSVV 819
Cdd:pfam04851    3 ELRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFK-KGPIKKVLFLVPrKDLLEQALEEFKKFLPNYV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  820 KVSYKGSPaarRAFVPQLRSGKfnVLLTTYEYIIKD----KQILAKIRWKYMIVDEGHRM--KNHhcklTQVLNthYLAP 893
Cdd:pfam04851   82 EIGEIISG---DKKDESVDDNK--IVVTTIQSLYKAlelaSLELLPDFFDVIIIDEAHRSgaSSY----RNILE--YFKP 150
                          170
                   ....*....|
gi 1709636372  894 RRVL-LTGTP 902
Cdd:pfam04851  151 AFLLgLTATP 160
PHA03247 PHA03247
large tegument protein UL36; Provisional
102-356 4.57e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.10  E-value: 4.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  102 PPPSPMdqhSQGYPSPLG-SSDHVSSPLPAGAPSTSGPllssscTSSSPLEGTDSQPSRSGAPSNTPGSSANPTPFNQNQ 180
Cdd:PHA03247  2710 PAPHAL---VSATPLPPGpAAARQASPALPAAPAPPAV------PAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPP 2780
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  181 LHQLRAQIMAYKMLARGQPLP----DHlQMAVQGKRPMPGMQQGQAMPSLPPGGA--GGPVTGPGPLGPNynrghVLSGP 254
Cdd:PHA03247  2781 RRLTRPAVASLSESRESLPSPwdpaDP-PAAVLAPAAALPPAASPAGPLPPPTSAqpTAPPPPPGPPPPS-----LPLGG 2854
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  255 SVPPSGPnavPSANGPPKTWPEGPmvnaATPSNAPQKLIPPQPTGRPSPVPPSVppaaspvmPPQTQSPGHPGHSAQPTP 334
Cdd:PHA03247  2855 SVAPGGD---VRRRPPSRSPAAKP----AAPARPPVRRLARPAVSRSTESFALP--------PDQPERPPQPQAPPPPQP 2919
                          250       260
                   ....*....|....*....|..
gi 1709636372  335 TIPLHQKHNRITPMQKPCGLDP 356
Cdd:PHA03247  2920 QPQPPPPPQPQPPPPPPPRPQP 2941
Ank_5 pfam13857
Ankyrin repeats (many copies);
2816-2870 5.32e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 5.32e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1709636372 2816 LLENG-ADPNIQDRFGITPAHDAARTGFLDTLCVLVDYGASVNIPDQSGALPIHIA 2870
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
1637-1671 5.58e-07

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: 48.01  E-value: 5.58e-07
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1709636372  1637 KCLSSEFTCSQSpvQCVSTRWRCDGKADCENGADE 1671
Cdd:smart00192    1 TCPPGEFQCDNG--RCIPSSWVCDGVDDCGDGSDE 33
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
743-902 7.89e-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: 51.15  E-value: 7.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  743 LKQYQIKGLE-WLvsLYNNNLNGILADEMGLGKTIQTIALITYLMEykrlnGPYLIIVP-LSTLSNWVYEFDKWAPSVVk 820
Cdd:cd17926      1 LRPYQEEALEaWL--AHKNNRRGILVLPTGSGKTLTALALIAYLKE-----LRTLIVVPtDALLDQWKERFEDFLGDSS- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  821 vsykgspaarrafVPQLRSGK------FNVLLTTYEYIIKDKQILAKI--RWKYMIVDEGHrmknHHC--KLTQVLnTHY 890
Cdd:cd17926     73 -------------IGLIGGGKkkdfddANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAH----HLPakTFSEIL-KEL 134
                          170
                   ....*....|..
gi 1709636372  891 LAPRRVLLTGTP 902
Cdd:cd17926    135 NAKYRLGLTATP 146
Bromo_WDR9_II cd05496
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1434-1516 9.16e-07

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: 50.15  E-value: 9.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1434 SEVFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFNL-EGSLIYEDSIVLQSVFTSL 1512
Cdd:cd05496     23 SEPFRQPVDLLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYTPnKRSRIYSMTLRLSALFEEH 102

                   ....
gi 1709636372 1513 RQKI 1516
Cdd:cd05496    103 IKKI 106
PHA03247 PHA03247
large tegument protein UL36; Provisional
87-356 1.06e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.94  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   87 MKGVSMRAGGHAGMGPPPSPmdqhsqgyPSPLGSSDHVSSPLPAGAPSTSGPLLSSSCTSssplEGTDSQPSRSGAPSNT 166
Cdd:PHA03247  2537 IRGLEELASDDAGDPPPPLP--------PAAPPAAPDRSVPPPRPAPRPSEPAVTSRARR----PDAPPQSARPRAPVDD 2604
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  167 PGSSANPTPFNqnqlhqlraqimaykmlargqPLP--DHlqmavqgkRPMPGMQQGQAMPSLPPGgaGGPVTGPGPLGPN 244
Cdd:PHA03247  2605 RGDPRGPAPPS---------------------PLPpdTH--------APDPPPPSPSPAANEPDP--HPPPTVPPPERPR 2653
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  245 YNRGHVLSGPSVPPSGPNAVPSANGPPKTW-------PEGPMVNAA-------TPSNAPQKLIP--PQPTGRPSPVPPSV 308
Cdd:PHA03247  2654 DDPAPGRVSRPRRARRLGRAAQASSPPQRPrrraarpTVGSLTSLAdppppppTPEPAPHALVSatPLPPGPAAARQASP 2733
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1709636372  309 PPAASPVMPPQTQSPGHPGHSAQPtPTIPLHQKHNRITPMQKPCGLDP 356
Cdd:PHA03247  2734 ALPAAPAPPAVPAGPATPGGPARP-ARPPTTAGPPAPAPPAAPAAGPP 2780
PHA03095 PHA03095
ankyrin-like protein; Provisional
2773-2888 1.19e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.88  E-value: 1.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2773 VRGDAAEVRRLLEeRRVHPDTRNEFGKTALQVMMMGNTNVACL---LLENGADPNIQDRFGITPAHDAA---RTGFLDTL 2846
Cdd:PHA03095   198 FKPRARIVRELIR-AGCDPAATDMLGNTPLHSMATGSSCKRSLvlpLLIAGISINARNRYGQTPLHYAAvfnNPRACRRL 276
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1709636372 2847 CVLvdyGASVNIPDQSGALPIHIAIREGYRDVVE-FLAPRSNL 2888
Cdd:PHA03095   277 IAL---GADINAVSSDGNTPLSLMVRNNNGRAVRaALAKNPSA 316
PHA03378 PHA03378
EBNA-3B; Provisional
97-349 1.25e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 54.30  E-value: 1.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   97 HAGMGPPPSPMDQHSQGYPSPLGSsdHVSSPLPAGApSTSGPLLSSSCTSSSPleGTDSQPSRSGAPSNTPgssanpTPF 176
Cdd:PHA03378   560 HDQLLPAPGLGPLQIQPLTSPTTS--QLASSAPSYA-QTPWPVPHPSQTPEPP--TTQSHIPETSAPRQWP------MPL 628
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  177 NQNQLHQLRAQIMAYKMLARGQP-----------LPDHLQMAVQGKRPMPGMQQGQAMPSLPPGGAGGPVTGPGPLGPNy 245
Cdd:PHA03378   629 RPIPMRPLRMQPITFNVLVFPTPhqppqveitpyKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPP- 707
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  246 nrgHVLSGPSVPPSG-------PNAVPSANGPPKTWPeGPMvnaATPSNAPQKLIPPQPTGRPSPVPPSVPPAASPVMPP 318
Cdd:PHA03378   708 ---AAPPGRAQRPAAatgrarpPAAAPGRARPPAAAP-GRA---RPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPP 780
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1709636372  319 qtQSPGHPGHSAQPTPTiPLHQKHNRITPMQ 349
Cdd:PHA03378   781 --QAPPAPQQRPRGAPT-PQPPPQAGPTSMQ 808
EGF_CA pfam07645
Calcium-binding EGF domain;
1920-1948 1.82e-06

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 46.46  E-value: 1.82e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1709636372 1920 DIDECADP-DTCSQ--VCVNLVGSFKCDCQAG 1948
Cdd:pfam07645    1 DVDECATGtHNCPAntVCVNTIGSFECRCPDG 32
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
37-467 2.28e-06

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 53.62  E-value: 2.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   37 PSPGPsTTSGHSVSQQGAAGYT----QQDSMHPMHKSLES---LHEKNVGEESRFGQmkgvsmragghaGMGPPPSPMDQ 109
Cdd:pfam03154  195 ATAGP-TPSAPSVPPQGSPATSqppnQTQSTAAPHTLIQQtptLHPQRLPSPHPPLQ------------PMTQPPPPSQV 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  110 HSQGYPSPlgsSDHVSSPlPAGAPSTSGPLLSSSCTSSSPLeGTDSQPSRSGAP------SNTPGSSANPTPFNQNQLHQ 183
Cdd:pfam03154  262 SPQPLPQP---SLHGQMP-PMPHSLQTGPSHMQHPVPPQPF-PLTPQSSQSQVPpgpspaAPGQSQQRIHTPPSQSQLQS 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  184 LRAqimaykmlARGQPLPD------HLQMAvqGKRPMPGMQQGQA--------------MPS-LPPGGAGGPVTG----- 237
Cdd:pfam03154  337 QQP--------PREQPLPPaplsmpHIKPP--PTTPIPQLPNPQShkhpphlsgpspfqMNSnLPPPPALKPLSSlsthh 406
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  238 -----PGPLGPNYNRGHVLSGPSVPP----SGPNAVPSANGPPktwpegPMVNAATPSNAPQKLIPPQPTGRPSPVPPSV 308
Cdd:pfam03154  407 ppsahPPPLQLMPQSQQLPPPPAQPPvltqSQSLPPPAASHPP------TSGLHQVPSQSPFPQHPFVPGGPPPITPPSG 480
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  309 PPAASPVMPPQTQSPGhpghSAQPTPTIPLhqkhnritPMQKPCGLDPVEILQEreyrlearithRIQELENlPGSLAGD 388
Cdd:pfam03154  481 PPTSTSSAMPGIQPPS----SASVSSSGPV--------PAAVSCPLPPVQIKEE-----------ALDEAEE-PESPPPP 536
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  389 LR------TKATIELKALRLLNFQRQLRQEVVVCMRRD---AALETALDAK----AYKRSKRQSLREARITEKLEKQQKI 455
Cdd:pfam03154  537 PRspspepTVVNTPSHASQSARFYKHLDRGYNSCARTDlyfMPLAGSKLAKkreeALEKAKREAEQKAREEKEREKEKEK 616
                          490
                   ....*....|...
gi 1709636372  456 EQERKR-RQKHQE 467
Cdd:pfam03154  617 EREREReREREAE 629
PHA03100 PHA03100
ankyrin repeat protein; Provisional
2815-2882 3.58e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.36  E-value: 3.58e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709636372 2815 LLLENGADPNIQDRFGITPAHDAARTGFLDTLCVLVDYGASVNIPDQSGALPIHIAIREGYRDVVEFL 2882
Cdd:PHA03100   177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
2241-2278 3.82e-06

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: 45.70  E-value: 3.82e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1709636372 2241 NGGCEYLCLPAPKvnqlspKYTCACPDDKVLGPDMRKC 2278
Cdd:pfam14670    5 NGGCSHLCLNTPG------GYTCSCPEGYELQDDGRTC 36
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
101-353 4.39e-06

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


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 50.76  E-value: 4.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  101 GPPPSPMdqhsqgYPSplgssdhvsSPLPAGAPSTSGPLLsssctsssplegtdsqPSrsgAPSNTPGSSANPTPfnqnq 180
Cdd:pfam15822   61 GPAPTGM------YPS---------IPLTGPSPGPPAPFP----------------PS---GPSCPPPGGPYPAP----- 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  181 lhqlraqimaykmLARGqPLPdhlqmavQGKRPMPGMQqgqaMPSLP-PGGAGGPVTGPGPLGPnynRGHVLSGPSVPPS 259
Cdd:pfam15822  102 -------------TVPG-PGP-------IGPYPTPNMP----FPELPrPYGAPTDPAAAAPSGP---WGSMSSGPWAPGM 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  260 G-----PNAVPSANGPPKTWPEGPMVNAATPsnAPQKLIPPQPTGrpspvppsvppaASPVMPPQTQSPGHPGhsaqPTP 334
Cdd:pfam15822  154 GgqypaPNMPYPSPGPYPAVPPPQSPGAAPP--VPWGTVPPGPWG------------PPAPYPDPTGSYPMPG----LYP 215
                          250
                   ....*....|....*....
gi 1709636372  335 TIPlhqkhnriTPMQKPCG 353
Cdd:pfam15822  216 TPN--------NPFQVPSG 226
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
358-570 5.58e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 5.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  358 EILQEREYRLEARITHRIQELENLPGSLAGDLRTKATIELKALRLLNFQRQLRQEVVVCMRRDAALETALDAKAYKRSKR 437
Cdd:COG1196    305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  438 QSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKMQKLTKAVATYHANTER--EQKKENERI 515
Cdd:COG1196    385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEleEEEEALLEL 464
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1709636372  516 EKERMRRLMAEDEEGYRKLIDQKKDKRLAYLLQQTDEYVANLTELVRAHKAVQAL 570
Cdd:COG1196    465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
LY smart00135
Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) ...
2122-2160 6.17e-06

Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. Also present in a variety of molecules similar to gp300/megalin.


Pssm-ID: 214531 [Multi-domain]  Cd Length: 43  Bit Score: 45.29  E-value: 6.17e-06
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1709636372  2122 LVTDNIFWPTGITLDLVNQRLYWLDAKLHMLSSIGVDGG 2160
Cdd:smart00135    3 LLSSGLGHPNGLAVDWIEGRLYWTDWGLDVIEVANLDGT 41
Ldl_recept_b pfam00058
Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif ...
2140-2182 6.20e-06

Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif after the most conserved region of the repeat. The YWTD repeat is found in multiple tandem repeats and has been predicted to form a beta-propeller structure.


Pssm-ID: 459654  Cd Length: 42  Bit Score: 45.23  E-value: 6.20e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1709636372 2140 QRLYWLDAKLH-MLSSIGVDGGLRHTLIVDErhLANPFSLAVFE 2182
Cdd:pfam00058    1 GRLYWTDSSLRaSISSADLNGSDRKTLFTDD--LQHPNAIAVDP 42
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
1445-1517 7.02e-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: 47.03  E-value: 7.02e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709636372 1445 ELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFNLEGsliyeDSIVL--QSVFTSLRQKIE 1517
Cdd:cd05497     36 NLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKPG-----DDVVLmaQTLEKLFLQKLA 105
PHA03100 PHA03100
ankyrin repeat protein; Provisional
2809-2882 7.26e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.20  E-value: 7.26e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709636372 2809 NTNVACLLLENGADPNIQDRFGITPAHDAART--GFLDTLCVLVDYGASVNIPDQSGALPIHIAIREGYRD--VVEFL 2882
Cdd:PHA03100    85 VKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLL 162
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
1441-1509 8.14e-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: 46.55  E-value: 8.14e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709636372 1441 PSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFNLEGSLIYEDSIVLQSVF 1509
Cdd:cd05506     27 VVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTMAKELLKIF 95
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
358-543 8.40e-06

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: 50.69  E-value: 8.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  358 EILQEREyRLEARITHRIQELEnlpgslagdlRTKATIElkALRLlnfqrQLRQEVVVCMRRDAALETALDakayKRSKR 437
Cdd:pfam13868  177 EIEEEKE-REIARLRAQQEKAQ----------DEKAERD--ELRA-----KLYQEEQERKERQKEREEAEK----KARQR 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  438 QSLREARITEKLEKQQKIEQERKRRQkhQEYLNSILQHAKDFKEYHRSVTGKMQKLTK-AVATYHANTEREQKKENERIE 516
Cdd:pfam13868  235 QELQQAREEQIELKERRLAEEAEREE--EEFERMLRKQAEDEEIEQEEAEKRRMKRLEhRRELEKQIEEREEQRAAEREE 312
                          170       180
                   ....*....|....*....|....*..
gi 1709636372  517 KERMRRLMAEDEEGYRKLIDQKKDKRL 543
Cdd:pfam13868  313 ELEEGERLREEEAERRERIEEERQKKL 339
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
149-272 9.46e-06

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 48.50  E-value: 9.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  149 PLEGTDSQPSRSGAPSNTP--GSSANPTPFNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQGKRPMPGMQQGQAMPSL 226
Cdd:pfam15240   50 PPGGFPPQPPASDDPPGPPppGGPQQPPPQGGKQKPQGPPPQGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQGG 129
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1709636372  227 PPGGAGGPVTGPGPLGPNYNRGHvlsgPSVPPSGPNavPSanGPPK 272
Cdd:pfam15240  130 GPPPQGGNQQGPPPPPPGNPQGP----PQRPPQPGN--PQ--GPPQ 167
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
740-902 9.64e-06

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 51.18  E-value: 9.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  740 NGQLKQYQIKGLE-WLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEYKRLngpyLIIVPLSTLSN-WVYEFDKWAPS 817
Cdd:COG1061     78 SFELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV----LVLVPRRELLEqWAEELRRFLGD 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  818 VVKVSYKgspaarrafvpqlRSGKFNVLLTTYEYIIKDKQiLAKI--RWKYMIVDEGhrmknHHC---KLTQVLNtHYLA 892
Cdd:COG1061    154 PLAGGGK-------------KDSDAPITVATYQSLARRAH-LDELgdRFGLVIIDEA-----HHAgapSYRRILE-AFPA 213
                          170
                   ....*....|
gi 1709636372  893 PRRVLLTGTP 902
Cdd:COG1061    214 AYRLGLTATP 223
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
209-356 9.83e-06

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 48.50  E-value: 9.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  209 QGKRPMPGMQ-QGQAMPSLPP-GGAGGPVTGPGPLGPNYNRGHvlSGPSVPPSGPNAvPSANGPPKTWPEGPmvnaaTPS 286
Cdd:pfam15240   36 EGQSQQGGQGpQGPPPGGFPPqPPASDDPPGPPPPGGPQQPPP--QGGKQKPQGPPP-QGGPRPPPGKPQGP-----PPQ 107
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709636372  287 NAPQKLIPPQPTGRPSPvppsvppaaspvmPPQTQS-PGHPGHSAQPTPTIPLHQKHnriTPMQKPCGLDP 356
Cdd:pfam15240  108 GGNQQQGPPPPGKPQGP-------------PPQGGGpPPQGGNQQGPPPPPPGNPQG---PPQRPPQPGNP 162
EGF_CA smart00179
Calcium-binding EGF-like domain;
1880-1919 1.00e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 44.55  E-value: 1.00e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1709636372  1880 NVNECLENNGgCSH--ICNDLKIGYECLCPSGYRlvDHKRCE 1919
Cdd:smart00179    1 DIDECASGNP-CQNggTCVNTVGSYRCECPPGYT--DGRNCE 39
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
358-552 1.05e-05

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: 50.30  E-value: 1.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  358 EILQEREYRLEARITHRIQELENlpgslagDLRTKATIELKALRLLNFQRQLRQEvvvcmRRDAALETA-LDAKAYKRSK 436
Cdd:pfam13868  131 EIDEFNEEQAEWKELEKEEEREE-------DERILEYLKEKAEREEEREAEREEI-----EEEKEREIArLRAQQEKAQD 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  437 RQSLREARITEKLEKqqkiEQERKRRQKHQEYLNSILQHAKDFKEYHRsvtgKMQKLTKAvatyhantEREQKKENERIE 516
Cdd:pfam13868  199 EKAERDELRAKLYQE----EQERKERQKEREEAEKKARQRQELQQARE----EQIELKER--------RLAEEAEREEEE 262
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1709636372  517 KERMRRLMAEDEEGYRKLIDQKKDKRLAY---LLQQTDE 552
Cdd:pfam13868  263 FERMLRKQAEDEEIEQEEAEKRRMKRLEHrreLEKQIEE 301
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
1997-2221 1.13e-05

NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.


Pssm-ID: 271320 [Multi-domain]  Cd Length: 269  Bit Score: 49.62  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1997 VALDmdvSSGTIFWSDLFHKKIYsspidKAAYSANHVTLIG------NQMSSPNGLAVDwIHGNIYWTDTFLESISVATK 2070
Cdd:cd05819     13 IAVD---SSGNIYVADTGNNRIQ-----VFDPDGNFITSFGsfgsgdGQFNEPAGVAVD-SDGNLYVADTGNHRIQKFDP 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2071 DGSKRMTLIKEGLSK-----PHAIVVDPERNfMYWTDWG-------SPA--KIEKSGLNGADRTALVTdnifwPTGITL- 2135
Cdd:cd05819     84 DGNFLASFGGSGDGDgefngPRGIAVDSSGN-IYVADTGnhriqkfDPDgeFLTTFGSGGSGPGQFNG-----PTGVAVd 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2136 --------DLVNQRLYWLDAKLHMLSSIGVDGglrhtliVDERHLANPFSLAVFEE-KVYWTDSFSQSILTANRLTGKNI 2206
Cdd:cd05819    158 sdgniyvaDTGNHRIQVFDPDGNFLTTFGSTG-------TGPGQFNYPTGIAVDSDgNIYVADSGNNRVQVFDPDGAGFG 230
                          250       260
                   ....*....|....*....|
gi 1709636372 2207 T-----KVVENLASPKDIVL 2221
Cdd:cd05819    231 GngnflGSDGQFNRPSGLAV 250
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
1997-2150 1.15e-05

NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.


Pssm-ID: 271320 [Multi-domain]  Cd Length: 269  Bit Score: 49.62  E-value: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1997 VALDmdvSSGTIFWSDLFHKKI--YSSpidkaaySANHVTLIG------NQMSSPNGLAVDwIHGNIYWTDTFLESISVA 2068
Cdd:cd05819    107 IAVD---SSGNIYVADTGNHRIqkFDP-------DGEFLTTFGsggsgpGQFNGPTGVAVD-SDGNIYVADTGNHRIQVF 175
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2069 TKDGsKRMTLIKEG------LSKPHAIVVDPERNfMYWTDWGSpAKIEKSGLNGADRTA----LVTDNIF-WPTGITLDL 2137
Cdd:cd05819    176 DPDG-NFLTTFGSTgtgpgqFNYPTGIAVDSDGN-IYVADSGN-NRVQVFDPDGAGFGGngnfLGSDGQFnRPSGLAVDS 252
                          170
                   ....*....|...
gi 1709636372 2138 vNQRLYWLDAKLH 2150
Cdd:cd05819    253 -DGNLYVADTGNN 264
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
1412-1498 1.30e-05

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: 45.99  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1412 KKMKKIVDAVIKYKESsngrqlsEVFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTF 1491
Cdd:cd05505      3 QKCEEILSKILKYRFS-------WPFREPVTADEAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAEKY 75

                   ....*..
gi 1709636372 1492 NLEGSLI 1498
Cdd:cd05505     76 YENGSYV 82
PHA03100 PHA03100
ankyrin repeat protein; Provisional
2815-2914 1.41e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.43  E-value: 1.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2815 LLLENGADPNIQDRFGITPAHDAARTGF-----LDTLCVLVDYGASVNIPDQSGALPIHIAIRE--GYRDVVEFLAPR-S 2886
Cdd:PHA03100    53 ILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNgA 132
                           90       100       110
                   ....*....|....*....|....*....|
gi 1709636372 2887 NLGHQDTRGDTALDIAEASCTPD--MVELL 2914
Cdd:PHA03100   133 NVNIKNSDGENLLHLYLESNKIDlkILKLL 162
Ank_4 pfam13637
Ankyrin repeats (many copies);
2832-2882 1.45e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 1.45e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1709636372 2832 TPAHDAARTGFLDTLCVLVDYGASVNIPDQSGALPIHIAIREGYRDVVEFL 2882
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
YvrE COG3386
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
2032-2175 1.54e-05

Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442613 [Multi-domain]  Cd Length: 266  Bit Score: 49.12  E-value: 1.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2032 HVTLIGNQMSSPNGLAVDWiHGNIYWTDTFLE----SISVATKDGSkrMTLIKEGLSKPHAIVVDPERNFMYWTDWGSPA 2107
Cdd:COG3386     84 LADEYGKPLNRPNDGVVDP-DGRLYFTDMGEYlptgALYRVDPDGS--LRVLADGLTFPNGIAFSPDGRTLYVADTGAGR 160
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709636372 2108 ----KIEKSGLNGADRT-ALVTDNIFWPTGITLDlVNQRLY---WLDAKLHMLSSigvDGGLRHTLIVDERHLANP 2175
Cdd:COG3386    161 iyrfDLDADGTLGNRRVfADLPDGPGGPDGLAVD-ADGNLWvalWGGGGVVRFDP---DGELLGRIELPERRPTNV 232
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
771-870 2.13e-05

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: 47.71  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  771 GLGKTiqTIALITYLMEYKRlNGPYLIIVPLSTLSNWVYE----FDKWAPSVVK--VSYKGSPA-ARRAFVPQLRSGKFN 843
Cdd:cd17924     42 GVGKT--TFGLATSLYLASK-GKRSYLIFPTKSLVKQAYErlskYAEKAGVEVKilVYHSRLKKkEKEELLEKIEKGDFD 118
                           90       100
                   ....*....|....*....|....*..
gi 1709636372  844 VLLTTYEYIIKDKQILAKIRWKYMIVD 870
Cdd:cd17924    119 ILVTTNQFLSKNFDLLSNKKFDFVFVD 145
PHA03377 PHA03377
EBNA-3C; Provisional
100-337 2.39e-05

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 50.05  E-value: 2.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  100 MGPPPSPMDQhsqGYP--SPLGSSDHVSSPLPAGAPSTSGPllssscTSSSPLEG-TDSQPSRSGAPSNTPGSSANPTPf 176
Cdd:PHA03377   551 TPPKVSPSDR---GPPkaSPPVMAPPSTGPRVMATPSTGPR------DMAPPSTGpRQQAKCKDGPPASGPHEKQPPSS- 620
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  177 nqnqlhqlRAQIMA---YKMLARGQPLPDHLQMA------VQGKRPMPGMQQgqampslPPGGAGGPVTGPGPLGPNYNR 247
Cdd:PHA03377   621 --------APRDMApsvVRMFLRERLLEQSTGPKpksfweMRAGRDGSGIQQ-------EPSSRRQPATQSTPPRPSWLP 685
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  248 GhVLSGPSVPPSGPNAVPSANGPPKTwPEGPMVNAATPS----NAP-----QKLIPPQPTGRPSPVPPSVppaaspvmPP 318
Cdd:PHA03377   686 S-VFVLPSVDAGRAQPSEESHLSSMS-PTQPISHEEQPRyedpDDPldlslHPDQAPPPSHQAPYSGHEE--------PQ 755
                          250
                   ....*....|....*....
gi 1709636372  319 QTQSPgHPGHSAQPTPTIP 337
Cdd:PHA03377   756 AQQAP-YPGYWEPRPPQAP 773
PHA03247 PHA03247
large tegument protein UL36; Provisional
97-297 2.45e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 2.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   97 HAGMGPPPSPMDQHSQgypSPLGSSDHVSSPLPAGAPSTSGPLLSSSCTSSSPLEGTDSQ---PSRSGAPSNT------- 166
Cdd:PHA03247  2807 PPAAVLAPAAALPPAA---SPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRrrpPSRSPAAKPAaparppv 2883
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  167 -----PGSSANPTPFNQNQLHQLRAQIMAYKMLARGQPLPDhlqmavQGKRPMPGMQ-QGQAMPSLPPGGAGGPVTGPGP 240
Cdd:PHA03247  2884 rrlarPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPP------PPPQPQPPPPpPPRPQPPLAPTTDPAGAGEPSG 2957
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709636372  241 LGPNYNRGHVLSG------PSVPPSGPNA-VPSANGPPKTWPEGPMVNAATPSNAPQKLIPPQP 297
Cdd:PHA03247  2958 AVPQPWLGALVPGrvavprFRVPQPAPSReAPASSTPPLTGHSLSRVSSWASSLALHEETDPPP 3021
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
393-566 3.04e-05

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: 48.00  E-value: 3.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  393 ATIELKALRLLNFQRQLRQEVVVCMRRDAALETALDAKaykrskRQSLREARiTEKLEKQQKIEQERKRRQKHQEYLNSI 472
Cdd:COG1579     13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAA------KTELEDLE-KEIKRLELEIEEVEARIKKYEEQLGNV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  473 lqhaKDFKEYhrsvtgkmQKLTKAVATyhantereQKKENERIEKErMRRLMAEDEEgYRKLIDQKKDK------RLAYL 546
Cdd:COG1579     86 ----RNNKEY--------EALQKEIES--------LKRRISDLEDE-ILELMERIEE-LEEELAELEAElaeleaELEEK 143
                          170       180
                   ....*....|....*....|
gi 1709636372  547 LQQTDEYVANLTELVRAHKA 566
Cdd:COG1579    144 KAELDEELAELEAELEELEA 163
Ldl_recept_b pfam00058
Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif ...
2183-2223 3.42e-05

Low-density lipoprotein receptor repeat class B; This domain is also known as the YWTD motif after the most conserved region of the repeat. The YWTD repeat is found in multiple tandem repeats and has been predicted to form a beta-propeller structure.


Pssm-ID: 459654  Cd Length: 42  Bit Score: 43.30  E-value: 3.42e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1709636372 2183 EKVYWTDSFSQSILTANRLTGKNI-TKVVENLASPKDIVLYH 2223
Cdd:pfam00058    1 GRLYWTDSSLRASISSADLNGSDRkTLFTDDLQHPNAIAVDP 42
PHA02878 PHA02878
ankyrin repeat protein; Provisional
2778-2871 4.03e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.11  E-value: 4.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2778 AEVRRLLEER--RVHPDTRNEfGKTALQVMMMG-NTNVACLLLENGADPNIQDRFGITPAHDAARTGFLDTLCVLVDYGA 2854
Cdd:PHA02878   147 AEITKLLLSYgaDINMKDRHK-GNTALHYATENkDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
                           90
                   ....*....|....*..
gi 1709636372 2855 SVNIPDQSGALPIHIAI 2871
Cdd:PHA02878   226 STDARDKCGNTPLHISV 242
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1880-1919 4.10e-05

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: 43.01  E-value: 4.10e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1709636372 1880 NVNECLENNG-GCSHICNDLKIGYECLCPSGYRLvdhKRCE 1919
Cdd:cd00054      1 DIDECASGNPcQNGGTCVNTVGSYRCSCPPGYTG---RNCE 38
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
1434-1492 4.44e-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: 45.12  E-value: 4.44e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1709636372 1434 SEVFIQLPSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFN 1492
Cdd:cd05510     26 STPFLTKVSKREAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLYN 84
PHA03100 PHA03100
ankyrin repeat protein; Provisional
2779-2914 4.60e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.51  E-value: 4.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2779 EVRRLLEERRVHPDTRNEFGKTALQVMMM---GNTNVACLLLENGADPNIQDRFGITPAHDAARTGF--LDTLCVLVD-- 2851
Cdd:PHA03100    87 EIVKLLLEYGANVNAPDNNGITPLLYAISkksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDkg 166
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709636372 2852 --------------YGASVNIPDQSGALPIHIAIREGYRDVVE-FLAPRSNLGHQDTRGDTALDIAEASCTPDMVELL 2914
Cdd:PHA03100   167 vdinaknrvnyllsYGVPINIKDVYGFTPLHYAVYNNNPEFVKyLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
PHA03378 PHA03378
EBNA-3B; Provisional
94-341 4.88e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 49.30  E-value: 4.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   94 AGGHAGMGPPPSPMDQHSQGyPS----PLGSSDHVSSPLPAgAPSTSGPLLSSSCTSSSPLEGTDSQPSRSGAP------ 163
Cdd:PHA03378   589 APSYAQTPWPVPHPSQTPEP-PTtqshIPETSAPRQWPMPL-RPIPMRPLRMQPITFNVLVFPTPHQPPQVEITpykptw 666
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  164 SNTPGSSANPTPFNQNQLHQLRAQImaykmlARGQPLPdhlqmAVQGKRPMPgmqQGQAMPSLPPGGAGGPVTGPGPLGP 243
Cdd:PHA03378   667 TQIGHIPYQPSPTGANTMLPIQWAP------GTMQPPP-----RAPTPMRPP---AAPPGRAQRPAAATGRARPPAAAPG 732
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  244 NYNRGHVLSGPSVPPSGP--NAVPSANGPPKTWPEGPMVNAATPSNAPQklIPPQPTGRPSPVppsvppaaspvmPPQTQ 321
Cdd:PHA03378   733 RARPPAAAPGRARPPAAApgRARPPAAAPGRARPPAAAPGAPTPQPPPQ--APPAPQQRPRGA------------PTPQP 798
                          250       260
                   ....*....|....*....|
gi 1709636372  322 SPGHPGHSAQPTPTIPLHQK 341
Cdd:PHA03378   799 PPQAGPTSMQLMPRAAPGQQ 818
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
1131-1179 4.97e-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: 43.85  E-value: 4.97e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1709636372 1131 SQYFIFLLSTRAGGLGLNLQSADTVVIFDSDWNPHQDLQAQDRAHRIGQ 1179
Cdd:cd18785     20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK 68
Ank_4 pfam13637
Ankyrin repeats (many copies);
2805-2850 5.95e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 5.95e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1709636372 2805 MMMGNTNVACLLLENGADPNIQDRFGITPAHDAARTGFLDTLCVLV 2850
Cdd:pfam13637    9 AASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
1923-1950 6.94e-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: 42.08  E-value: 6.94e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1709636372 1923 ECADPDTCS--QVCVNLVGSFKCDCQAGYE 1950
Cdd:cd00053      1 ECAASNPCSngGTCVNTPGSYRCVCPPGYT 30
Bromo_polybromo_VI cd05526
Bromodomain, polybromo repeat VI. Polybromo is a nuclear protein of unknown function, which ...
1428-1518 7.60e-05

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


Pssm-ID: 99956  Cd Length: 110  Bit Score: 44.28  E-value: 7.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1428 SNGRQLSEVFIQLPSRKELPEyyELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFNLEGSLIYEDSIVLQS 1507
Cdd:cd05526     21 EEGRCYSDSLAELPELAVDGV--GPKKIPLTLDIIKRNVDKGRYRRLDKFQEDMFEVLERARRLSRTDSEIYEDAVELQQ 98
                           90
                   ....*....|.
gi 1709636372 1508 VFTSLRQKIEK 1518
Cdd:cd05526     99 FFIKIRDELCK 109
NHL_like_6 cd14962
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
2002-2102 7.89e-05

Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271332 [Multi-domain]  Cd Length: 271  Bit Score: 47.20  E-value: 7.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2002 DVSSGTIFWSDLFHKKIysSPIDKAAysanhvtliGNQMSSPNGLAVDwIHGNIYWTDTFLESISVATKDGsKRMTLIKE 2081
Cdd:cd14962     29 DTGRGAVFVFDLPNGKV--FVIGNAG---------PNRFVSPIGVAID-ANGNLYVSDAELGKVFVFDRDG-KFLRAIGA 95
                           90       100
                   ....*....|....*....|...
gi 1709636372 2082 GL--SKPHAIVVDPERNFMYWTD 2102
Cdd:cd14962     96 GAlfKRPTGIAVDPAGKRLYVVD 118
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
363-569 8.14e-05

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: 48.53  E-value: 8.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  363 REYRLEARITHRIQELENLPGSLAGDLRtkatielkalRLLNFQRQLRQEVVVCMRRDAALETALDAKAYKRSKRQslre 442
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELR----------RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK---- 736
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  443 ARITEKLEKQQKIEQER----------------KRRQKH--QEYLNSIlqHAKDFKEYHRSVTGKMQKLTKAVATYHANT 504
Cdd:TIGR02169  737 ERLEELEEDLSSLEQEIenvkselkelearieeLEEDLHklEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARL 814
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709636372  505 EREQKKENER-IEKERMRRLMAEDEEGYRKLIDQKKD---------KRLAYLLQQTDEYVANLTELVRAHKAVQA 569
Cdd:TIGR02169  815 REIEQKLNRLtLEKEYLEKEIQELQEQRIDLKEQIKSiekeienlnGKKEELEEELEELEAALRDLESRLGDLKK 889
PHA03100 PHA03100
ankyrin repeat protein; Provisional
2779-2861 8.35e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 8.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2779 EVRRLLEeRRVHPDTRNEFGKTALQ-VMMMGNTNVACLLLENGADPNIQDRFGITPAHDAARTGFLDTLCVLVDYGASVN 2857
Cdd:PHA03100   174 RVNYLLS-YGVPINIKDVYGFTPLHyAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252

                   ....
gi 1709636372 2858 IPDQ 2861
Cdd:PHA03100   253 TIIE 256
PHA02876 PHA02876
ankyrin repeat protein; Provisional
2796-2892 9.74e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.14  E-value: 9.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2796 EFGKTALQVMMMGNTNVACLLLENGADPNIQDRFGITPAHDAARTGFLDTLCVLVDYGASVNIPDQSGALPIHIAIREGY 2875
Cdd:PHA02876   144 EYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
                           90
                   ....*....|....*...
gi 1709636372 2876 RDVVE-FLAPRSNLGHQD 2892
Cdd:PHA02876   224 IDTIKaIIDNRSNINKND 241
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
1996-2147 1.61e-04

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 45.84  E-value: 1.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1996 VVALDMDVSSGTIFWSDLFHKKIysSPIDKAAYSANHVTLIGnqmSSPNGLAVDWIHGNIYWTDTFLESISVATKDGSKR 2075
Cdd:COG3391     70 ADGADAGADGRRLYVANSGSGRV--SVIDLATGKVVATIPVG---GGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKV 144
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709636372 2076 MTLIKEGlSKPHAIVVDPERNFMYWTDWGSP--AKIEkSGLNGADRTalVTDNI---FWPTGITLDLVNQRLYWLDA 2147
Cdd:COG3391    145 VATIPVG-AGPHGIAVDPDGKRLYVANSGSNtvSVIV-SVIDTATGK--VVATIpvgGGPVGVAVSPDGRRLYVANR 217
EGF smart00181
Epidermal growth factor-like domain;
1923-1953 1.66e-04

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 40.96  E-value: 1.66e-04
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1709636372  1923 ECADPDTCSQ-VCVNLVGSFKCDCQAGYEMDP 1953
Cdd:smart00181    1 ECASGGPCSNgTCINTPGSYTCSCPPGYTGDK 32
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
32-220 1.91e-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: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   32 HGM----MGPSPGPSTTSGHSVSQQGAAGYTQQDSMHPMhKSLESLHEKN--------VGEESRFGQMKGVSMRA----- 94
Cdd:pfam09606  277 QGGpgqpMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQ-QQQGGNHPAAhqqqmnqsVGQGGQVVALGGLNHLEtwnpg 355
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   95 -----------GGHAGMGPPPSPMDQ---HSQGYPSPLGSSDHVSSPLPAGaPSTSGPLLSSSCTSSSP--LEGTDSQPS 158
Cdd:pfam09606  356 nfgglganpmqRGQPGMMSSPSPVPGqqvRQVTPNQFMRQSPQPSVPSPQG-PGSQPPQSHPGGMIPSPalIPSPSPQMS 434
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709636372  159 RS------------GAPSNTPGSSANPTPFNQNQLHQLRAQimaYKMLargQPLPDHLqmavqgKRPMPGMQQG 220
Cdd:pfam09606  435 QQpaqqrtigqdspGGSLNTPGQSAVNSPLNPQEEQLYREK---YRQL---TKYIEPL------KRMIAKMEND 496
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
406-552 1.96e-04

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 46.87  E-value: 1.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  406 QRQLRQEVvvcMRRDAALETALDAKAYKRSKRQSLREARITEklEKQQKIEQERKRRQKHQEYLNSILQHAKdfkEYHRS 485
Cdd:pfam15709  360 QRRLQQEQ---LERAEKMREELELEQQRRFEEIRLRKQRLEE--ERQRQEEEERKQRLQLQAAQERARQQQE---EFRRK 431
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709636372  486 VTgKMQKLTKAVATYHANTEREQKKENERIEKERMRRLMAEDEEgyrklidqkkdKRLAYLLQQTDE 552
Cdd:pfam15709  432 LQ-ELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEE-----------ERLEYQRQKQEA 486
PHA03264 PHA03264
envelope glycoprotein D; Provisional
174-328 2.70e-04

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 46.15  E-value: 2.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  174 TPFNQNQLHQlraQIMAYKMLARGQPLPDHLQmAVQGKRPMPGMQQGQAMP----SLPPGGAGGPVTgPGPLGPNYNRGh 249
Cdd:PHA03264   231 TQYYPQEAHK---AIVDYWFMRHGGVVPPYFE-ESKGYEPPPAPSGGSPAPpgddRPEAKPEPGPVE-DGAPGRETGGE- 304
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709636372  250 vlsGPSVPPSGPNAvpSANGPPKTWPEGPMVNAATPSNAPQKLIPPQPtgrpspvppsvppaaspvmPPQTQSPGHPGH 328
Cdd:PHA03264   305 ---GEGPEPAGRDG--AAGGEPKPGPPRPAPDADRPEGWPSLEAITFP-------------------PPTPATPAVPRA 359
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
36-260 3.23e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.70  E-value: 3.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   36 GPSPGPSTTSGHSVSQQGAAGYTQQDS-----------MHPMHKSLESLHEKNVGEESRFGqmKGVSMRAGGHAGMGPPP 104
Cdd:PHA03307   221 APAPGRSAADDAGASSSDSSSSESSGCgwgpenecplpRPAPITLPTRIWEASGWNGPSSR--PGPASSSSSPRERSPSP 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  105 SPMDQHSQGYPSPLGSSDHV-------------SSPLPAGAPSTSGPLLSSSCTSSSPLEGTDSQPSRSGAPSNTPGSSA 171
Cdd:PHA03307   299 SPSSPGSGPAPSSPRASSSSsssressssstssSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSP 378
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  172 NPTPfnqnqlhqLRAQIMAykmlARGQPLPDHLQMAVQGKRPmpgmqqgQAMPSLPPGGAGGPVTGPGPLGPN-YNRGHV 250
Cdd:PHA03307   379 AASA--------GRPTRRR----ARAAVAGRARRRDATGRFP-------AGRPRPSPLDAGAASGAFYARYPLlTPSGEP 439
                          250
                   ....*....|
gi 1709636372  251 LSGPSVPPSG 260
Cdd:PHA03307   440 WPGSPPPPPG 449
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
381-652 3.92e-04

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: 45.53  E-value: 3.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  381 LPGSLAGDLRTKATIELKALR-----LLNFQRQLRQEVVVCMRRDAALETALDAKAyKRSKRQSLREARITEKLEK-QQK 454
Cdd:COG4942     13 LAAAAQADAAAEAEAELEQLQqeiaeLEKELAALKKEEKALLKQLAALERRIAALA-RRIRALEQELAALEAELAElEKE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  455 IEQERKRRQKHQEYLNSILQ---------------HAKDFKE------YHRSVTGKMQKLTKAVAtyHANTEREQKKENE 513
Cdd:COG4942     92 IAELRAELEAQKEELAELLRalyrlgrqpplalllSPEDFLDavrrlqYLKYLAPARREQAEELR--ADLAELAALRAEL 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  514 RIEKERMRRLMAEDEEGYRKLIDQKKDKR--LAYLLQQTDEYVANLTELVRAHKAVQALkekkkkkkkMKKLENAEGQPL 591
Cdd:COG4942    170 EAERAELEALLAELEEERAALEALKAERQklLARLEKELAELAAELAELQQEAEELEAL---------IARLEAEAAAAA 240
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709636372  592 ALGPDGEPLDETSQMSdLPVKvihvdsGKILSGVDAPKAGQLDtwlemNPGYEVAPRSDSE 652
Cdd:COG4942    241 ERTPAAGFAALKGKLP-WPVS------GRVVRRFGERDGGGGR-----NKGIDIAAPPGAP 289
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
771-902 4.14e-04

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: 43.39  E-value: 4.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  771 GLGKTIqtIALITYL-MEYKRLNGPY-LIIVPLSTLSNWVYE-FDKWA-PSVVKVSYKGSPAARRAFVPQLRSGkfNVLL 846
Cdd:pfam00270   24 GSGKTL--AFLLPALeALDKLDNGPQaLVLAPTRELAEQIYEeLKKLGkGLGLKVASLLGGDSRKEQLEKLKGP--DILV 99
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709636372  847 TTYE---YIIKDKQILAKIrwKYMIVDEGHRM--KNHHCKLTQVLNTHYLAPRRVLLTGTP 902
Cdd:pfam00270  100 GTPGrllDLLQERKLLKNL--KLLVLDEAHRLldMGFGPDLEEILRRLPKKRQILLLSATL 158
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
392-594 4.35e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 4.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  392 KATIeLKALRLLnFQRQLRQEV-----------VVCMRRDAALETALDAKAYKRSKRQSLREARitEKLEKQQK-IEQER 459
Cdd:COG4717     36 KSTL-LAFIRAM-LLERLEKEAdelfkpqgrkpELNLKELKELEEELKEAEEKEEEYAELQEEL--EELEEELEeLEAEL 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  460 KRRQKHQEYLNSILQHAKDFKEYHR------SVTGKMQKLTKAVATYHANTEREQKKENERIEKER-MRRLMAEDEEGYR 532
Cdd:COG4717    112 EELREELEKLEKLLQLLPLYQELEAleaelaELPERLEELEERLEELRELEEELEELEAELAELQEeLEELLEQLSLATE 191
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709636372  533 KLIdQKKDKRLAYLLQQTDEYVANLT----ELVRAHKAVQALKEKKKKKKKMKKLENAEGQPLALG 594
Cdd:COG4717    192 EEL-QDLAEELEELQQRLAELEEELEeaqeELEELEEELEQLENELEAAALEERLKEARLLLLIAA 256
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
1992-2106 4.37e-04

NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.


Pssm-ID: 271320 [Multi-domain]  Cd Length: 269  Bit Score: 45.00  E-value: 4.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1992 QLKNVVALDMDvSSGTIFWSDLFHKKI-YSSPIDKAAYSANHVTLIGNQMSSPNGLAVDwIHGNIYWTDTFLESISVATK 2070
Cdd:cd05819    147 QFNGPTGVAVD-SDGNIYVADTGNHRIqVFDPDGNFLTTFGSTGTGPGQFNYPTGIAVD-SDGNIYVADSGNNRVQVFDP 224
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1709636372 2071 DGSKRMTL-----IKEGLSKPHAIVVDPERNfMYWTDWGSP 2106
Cdd:cd05819    225 DGAGFGGNgnflgSDGQFNRPSGLAVDSDGN-LYVADTGNN 264
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
178-424 4.44e-04

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


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 45.95  E-value: 4.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  178 QNQLHQLRAQimaykmlARGQPLPdhlqmavqgkRPMPGMQQGQAMpslpPGGAGGPVTGPGPLGPNYNRghvlsgPSVP 257
Cdd:TIGR01628  372 QDQFMQLQPR-------MRQLPMG----------SPMGGAMGQPPY----YGQGPQQQFNGQPLGWPRMS------MMPT 424
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  258 PSGPNAVPSANGPPktwpegPMVNAATPSNAPQKLIPPQPTGrpspvppsvppaaspVMPPQTQSPGHPGHSAQPTPTIP 337
Cdd:TIGR01628  425 PMGPGGPLRPNGLA------PMNAVRAPSRNAQNAAQKPPMQ---------------PVMYPPNYQSLPLSQDLPQPQST 483
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  338 LHQKHNRITPMQKPCGLDPveilQEREYRLEARITHRIQELE-NLPGSLAGDLrtkatIELK---ALRLLNFQRQLRQEV 413
Cdd:TIGR01628  484 ASQGGQNKKLAQVLASATP----QMQKQVLGERLFPLVEAIEpALAAKITGML-----LEMDnseLLHLLESPELLKSKV 554
                          250
                   ....*....|.
gi 1709636372  414 vvcmrrDAALE 424
Cdd:TIGR01628  555 ------DEALE 559
PRKCSH-like pfam12999
Glucosidase II beta subunit-like; The sequences found in this family are similar to a region ...
1683-1763 4.80e-04

Glucosidase II beta subunit-like; The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II, which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyzes the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum.


Pssm-ID: 372423 [Multi-domain]  Cd Length: 176  Bit Score: 43.62  E-value: 4.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 1683 EFRCADGQCISSSF--VCDEDADCSDGSDEAScpKPTCTSGSFQCNNSVCVPELW--------ACDGDPdCPDGSDEWSE 1752
Cdd:pfam12999   37 NWKCLNHSEIKLSFdqVNDDYCDCPDGSDEPG--TNACSNGKFYCANEGFIPGYIpsfkvddgVCDYDI-CCDGSDEALG 113
                           90
                   ....*....|.
gi 1709636372 1753 HCshkptPNPC 1763
Cdd:pfam12999  114 KC-----PNKC 119
PHA03247 PHA03247
large tegument protein UL36; Provisional
16-334 5.23e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 5.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   16 PSPGPMMGPGPSPGSSHGMMGPSPGPSTTSGHSVSQQGAAGYT------QQDSMHPMHKSLESL---HEKNVGEESR-FG 85
Cdd:PHA03247  2635 ANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASsppqrpRRRAARPTVGSLTSLadpPPPPPTPEPApHA 2714
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   86 QMKGVSMRAGGHAGMGP-PPSPMDQHSQGYPS----PLGSSDHVSSPLPAGAPSTSGPllsssctsSSPLEGTDSQPSRS 160
Cdd:PHA03247  2715 LVSATPLPPGPAAARQAsPALPAAPAPPAVPAgpatPGGPARPARPPTTAGPPAPAPP--------AAPAAGPPRRLTRP 2786
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  161 GAPSNTPGSSANPTPFNQNQ----LHQLRAQIMAYKMLARGQPLPDHLQMAVQGKRPMPgmqqgqAMPSLPPGGA---GG 233
Cdd:PHA03247  2787 AVASLSESRESLPSPWDPADppaaVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP------PPPSLPLGGSvapGG 2860
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  234 PV--------TGPGPLGPNYNRGHVLSGPSVPPSG-PNAVPSANGPPKTWPEGPmvnaATPSNAPQKLIPPQPTgrpspv 304
Cdd:PHA03247  2861 DVrrrppsrsPAAKPAAPARPPVRRLARPAVSRSTeSFALPPDQPERPPQPQAP----PPPQPQPQPPPPPQPQ------ 2930
                          330       340       350
                   ....*....|....*....|....*....|
gi 1709636372  305 ppsvppaaspvmpPQTQSPGHPGHSAQPTP 334
Cdd:PHA03247  2931 -------------PPPPPPPRPQPPLAPTT 2947
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
2771-2901 5.25e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.39  E-value: 5.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2771 AAVRGDAAEVRRLLEERRVHPDTRNEFGKTALQV-MMMGNTNVACLLLENGAD----PNIQDRF-GITPAHDAARTGFLD 2844
Cdd:cd22192     24 AAKENDVQAIKKLLKCPSCDLFQRGALGETALHVaALYDNLEAAVVLMEAAPElvnePMTSDLYqGETALHIAVVNQNLN 103
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709636372 2845 TLCVLVDYGASVNIPDQSGAL--------------PIHIAIREGYRDVVEFLAPR-SNLGHQDTRGDTALDI 2901
Cdd:cd22192    104 LVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHgADIRAQDSLGNTVLHI 175
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1441-1512 5.39e-04

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: 41.66  E-value: 5.39e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709636372 1441 PSRKELPEYYELIRRPVDFRKIKERIRSHRYRSLNDLERDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSL 1512
Cdd:cd05495     31 PKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWLYNRKTSRVYKYCTKLAEVFEQE 102
LY smart00135
Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) ...
2163-2205 5.83e-04

Low-density lipoprotein-receptor YWTD domain; Type "B" repeats in low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. Also present in a variety of molecules similar to gp300/megalin.


Pssm-ID: 214531 [Multi-domain]  Cd Length: 43  Bit Score: 39.89  E-value: 5.83e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1709636372  2163 HTLIVDERHLANPFSLAVFEEKVYWTDSFSQSILTANrLTGKN 2205
Cdd:smart00135    1 RTLLSSGLGHPNGLAVDWIEGRLYWTDWGLDVIEVAN-LDGTN 42
PHA02876 PHA02876
ankyrin repeat protein; Provisional
2784-2870 5.93e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 5.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2784 LEERRVHPDTRNEFGKTALQVMMMGNTNVACL--LLENGADPNIQDRFGITPAHDAARTG-FLDTLCVLVDYGASVNIPD 2860
Cdd:PHA02876   293 LLERGADVNAKNIKGETPLYLMAKNGYDTENIrtLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARD 372
                           90
                   ....*....|
gi 1709636372 2861 QSGALPIHIA 2870
Cdd:PHA02876   373 YCDKTPIHYA 382
EGF smart00181
Epidermal growth factor-like domain;
1883-1919 6.27e-04

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 39.42  E-value: 6.27e-04
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1709636372  1883 ECLENNGgCSH-ICNDLKIGYECLCPSGYRLVdhKRCE 1919
Cdd:smart00181    1 ECASGGP-CSNgTCINTPGSYTCSCPPGYTGD--KRCE 35
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
357-529 6.49e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 6.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  357 VEILQEREYRLEaRITHRIQELENLPGSLAGDLRtKATIELKALRLLNFQRQLRQEVVVCMRRDAALETALDAkaykrsk 436
Cdd:COG4717     87 EEEYAELQEELE-ELEEELEELEAELEELREELE-KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE------- 157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  437 RQSLREARitEKLEKQQKiEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKMQKLTKAVATyhanTEREQKKENERIE 516
Cdd:COG4717    158 LRELEEEL--EELEAELA-ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE----AQEELEELEEELE 230
                          170
                   ....*....|...
gi 1709636372  517 KERMRRLMAEDEE 529
Cdd:COG4717    231 QLENELEAAALEE 243
NHL_like_5 cd14963
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
2014-2104 7.18e-04

Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271333 [Multi-domain]  Cd Length: 268  Bit Score: 44.20  E-value: 7.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2014 FHKKIYSSPIDKaaysanhvtligNQMSSPNGLAVDwIHGNIYWTDTFLESISVATKDGSKRMTLIKEG-----LSKPHA 2088
Cdd:cd14963    180 FIKELNGSPDGK------------SGFVNPRGIAVD-PDGNLYVVDNLSHRVYVFDEQGKELFTFGGRGkddgqFNLPNG 246
                           90
                   ....*....|....*.
gi 1709636372 2089 IVVDpERNFMYWTDWG 2104
Cdd:cd14963    247 LFID-DDGRLYVTDRE 261
PTZ00121 PTZ00121
MAEBL; Provisional
430-541 7.35e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 7.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  430 KAYKRSKRQSLREARITEKLEKQQKIEQERKRrqkhQEYLNSILQHAKDFKEYHRSVTGKMQKLTKAVATYHAntEREQK 509
Cdd:PTZ00121  1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKA----EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA--EEAKK 1614
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1709636372  510 KENERIEKERMRRlmaedEEGYRKLIDQKKDK 541
Cdd:PTZ00121  1615 AEEAKIKAEELKK-----AEEEKKKVEQLKKK 1641
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
2798-2828 7.78e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 7.78e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1709636372 2798 GKTALQ--VMMMGNTNVACLLLENGADPNIQDR 2828
Cdd:pfam00023    2 GNTPLHlaAGRRGNLEIVKLLLSKGADVNARDK 34
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
328-549 9.01e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.73  E-value: 9.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  328 HSAQPTPTIPLHQKHNRITPMQKPcgldpvEILQEREYRleARITHRIQELENLPGSLAGDLRTKATI------------ 395
Cdd:pfam17380  276 HIVQHQKAVSERQQQEKFEKMEQE------RLRQEKEEK--AREVERRRKLEEAEKARQAEMDRQAAIyaeqermamere 347
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  396 -ELKALRLLNFQRQL----RQEVVVCMRRDAALETALDAKAYKRSK-RQSLREARITEKLEK-------QQKIEQERKRR 462
Cdd:pfam17380  348 rELERIRQEERKRELerirQEEIAMEISRMRELERLQMERQQKNERvRQELEAARKVKILEEerqrkiqQQKVEMEQIRA 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  463 QKH---QEYLNSILQH-AKDFKEYHRSVTGKMQKLTKAvatyhANTEREQKKENERIEKERMRRLMAEDEEgyRKLIDQK 538
Cdd:pfam17380  428 EQEearQREVRRLEEErAREMERVRLEEQERQQQVERL-----RQQEEERKRKKLELEKEKRDRKRAEEQR--RKILEKE 500
                          250
                   ....*....|.
gi 1709636372  539 KDKRLAYLLQQ 549
Cdd:pfam17380  501 LEERKQAMIEE 511
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
84-328 9.75e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 9.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   84 FGQMKGVSMRAGGHAGMGPPPSPMDQHSQGYPSPLGSSDHVSSP------LPAGAPSTSGPLLSSSCTSSSPLEGTDSQP 157
Cdd:PRK07764   578 LGGDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPaapaapAPAGAAAAPAEASAAPAPGVAAPEHHPKHV 657
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  158 SRSGAPSNTPGSSANPTPFnqnqlhqlraqimaykmlargQPLPDHLQMAVQGKRPMPGMQQGQAMPSLPPGGAGGPVTG 237
Cdd:PRK07764   658 AVPDASDGGDGWPAKAGGA---------------------APAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADD 716
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  238 PGPLGPnynrghvlsGPSVPPSGPNAVPSANGPPKTWPEGPMVNAATPSNAPQKLIPPQPTGRPSPVPPSVPPAASPVMP 317
Cdd:PRK07764   717 PAAQPP---------QAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAE 787
                          250
                   ....*....|.
gi 1709636372  318 PQTQSPGHPGH 328
Cdd:PRK07764   788 DDAPSMDDEDR 798
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
364-569 1.05e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  364 EYRLEA------RITHRIQELE-NLpgslaGDLRTKATielKALRLLNFQRQLRQ-EVVVCMRRDAALETALDAKAYKRS 435
Cdd:COG1196    178 ERKLEAteenleRLEDILGELErQL-----EPLERQAE---KAERYRELKEELKElEAELLLLKLRELEAELEELEAELE 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  436 KRQSLREARITEKLEKQQKIEQERkrrQKHQEYLNSILQHAKDFKEYHRSVTGKMQKLTKAVATYHANTEREQKKENERI 515
Cdd:COG1196    250 ELEAELEELEAELAELEAELEELR---LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1709636372  516 EKERMRRLMAEDEEGYRKLIDQKKDKRLAyLLQQTDEYVANLTELVRAHKAVQA 569
Cdd:COG1196    327 ELEEELEELEEELEELEEELEEAEEELEE-AEAELAEAEEALLEAEAELAEAEE 379
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
360-569 1.34e-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: 44.67  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  360 LQEREYRLEaRITHRIQELENLPGSLAGDLRTKATiELKAL---RLLNFQRQLRQ---EVVVCMRRDAALETALDAKAYK 433
Cdd:TIGR02169  246 LASLEEELE-KLTEEISELEKRLEEIEQLLEELNK-KIKDLgeeEQLRVKEKIGEleaEIASLERSIAEKERELEDAEER 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  434 RSKRQSLREARITEKLEKQQKIEQERKRRQKhqeyLNSILQHAKDfkEYHRSVtgkmQKLtKAVATYHANTEREQKKENE 513
Cdd:TIGR02169  324 LAKLEAEIDKLLAEIEELEREIEEERKRRDK----LTEEYAELKE--ELEDLR----AEL-EEVDKEFAETRDELKDYRE 392
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1709636372  514 RIEKerMRRLMAEDEEGYRKLID--QKKDKRLAYLLQQTDEYVANLTELVRAHKAVQA 569
Cdd:TIGR02169  393 KLEK--LKREINELKRELDRLQEelQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
AP_MuD_MHD cd09256
Mu-homology domain (MHD) of a adaptor protein (AP) encoded by mu-2 related death-inducing gene, ...
2566-2722 1.42e-03

Mu-homology domain (MHD) of a adaptor protein (AP) encoded by mu-2 related death-inducing gene, MuD (also known as MUDENG); This family corresponds to the MHD found in a protein encoded by MuD (also known as Adapter-related protein complex 5 subunit mu-1), which is distantly related to the C-terminal domain of the mu2 subunit of AP complexes that participates in clathrin-mediated endocytosis. MuD is evolutionary conserved from mammals to amphibians. It is able to induce cell death by itself and plays an important role in cell death in various tissues.


Pssm-ID: 271164  Cd Length: 276  Bit Score: 43.14  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2566 DIVGSIKLKTMLSGMPElrlglndrVLFALTGRDKGKtvaMEDVKFHQCVR-----LSRFESDRTISFIPPDGESELMSY 2640
Cdd:cd09256     37 SVFGEVRCKAELEGLPE--------VTVSLSVPANSP---LQAIIVHPCVQspesgMLAFSGPYKIRFSPPLGNFVLCRY 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2641 RINTHVKPLI---WIESVIEKfshsRVEIMVKAKGQFKKQSVANNVEVRVPVPSDADSPKF--KTSTGHAKYVPEKNVVV 2715
Cdd:cd09256    106 QSQSVPVPPIlgfYQMKGDEK----HVKFLIQLKLHESVKNSFEYCEVHIPFPNRGLIKHVsaTPSNGQLEVSKEKRRLV 181

                   ....*...
gi 1709636372 2716 WTI-KSFP 2722
Cdd:cd09256    182 WNIgQKFP 189
PHA02878 PHA02878
ankyrin repeat protein; Provisional
2748-2875 1.45e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2748 FLLKTNKQTMVLSEGDagKSLTSAAVRGDAAEVRRLLEERRVHPDTRNEFGKTALQ--VMMMGNTNVACLLLENGADPNI 2825
Cdd:PHA02878   186 LLLSYGANVNIPDKTN--NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHisVGYCKDYDILKLLLEHGVDVNA 263
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1709636372 2826 QDRF-GITPAHDAARTGflDTLCVLVDYGASVNIPDQSGALPIHIAIREGY 2875
Cdd:PHA02878   264 KSYIlGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVKQYL 312
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
1904-1923 1.48e-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: 38.16  E-value: 1.48e-03
                           10        20
                   ....*....|....*....|.
gi 1709636372 1904 CLCPSGYRL-VDHKRCEDIDE 1923
Cdd:pfam12662    2 CSCPPGYQLdPDGRTCVDIDE 22
Ank_5 pfam13857
Ankyrin repeats (many copies);
2783-2835 1.49e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 1.49e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1709636372 2783 LLEERRVHPDTRNEFGKTALqvMMM---GNTNVACLLLENGADPNIQDRFGITPAH 2835
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPL--HVAakyGALEIVRVLLAYGVDLNLKDEEGLTALD 54
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
2038-2195 1.64e-03

NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.


Pssm-ID: 271320 [Multi-domain]  Cd Length: 269  Bit Score: 43.08  E-value: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2038 NQMSSPNGLAVDwIHGNIYWTDTFLESISVATKDGSKRMTLIKEG-----LSKPHAIVVDPERNFmY-----------WT 2101
Cdd:cd05819      5 GELNNPQGIAVD-SSGNIYVADTGNNRIQVFDPDGNFITSFGSFGsgdgqFNEPAGVAVDSDGNL-YvadtgnhriqkFD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2102 DWGSpaKIEKSGLNGADRTALvtdniFWPTGITLD-----LV----NQRLYWLDAKLHMLSSIGVDGGlrhtlivDERHL 2172
Cdd:cd05819     83 PDGN--FLASFGGSGDGDGEF-----NGPRGIAVDssgniYVadtgNHRIQKFDPDGEFLTTFGSGGS-------GPGQF 148
                          170       180
                   ....*....|....*....|....
gi 1709636372 2173 ANPFSLAVF-EEKVYWTDSFSQSI 2195
Cdd:cd05819    149 NGPTGVAVDsDGNIYVADTGNHRI 172
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
2052-2204 1.71e-03

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 42.76  E-value: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2052 HGNIYWTDTFLESISVATKDGSKRMTLIKEGlSKPHAIVVDPERNFMYWTDWGSpAKIekSGLNGADRTalVTDNI---F 2128
Cdd:COG3391     79 GRRLYVANSGSGRVSVIDLATGKVVATIPVG-GGPRGLAVDPDGGRLYVADSGN-GRV--SVIDTATGK--VVATIpvgA 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2129 WPTGITLDLVNQRLYWLDAKLHMLSSI-----GVDGGLRHTLIVDErhlaNPFSLAV--FEEKVYWTDSFSQsilTANRL 2201
Cdd:COG3391    153 GPHGIAVDPDGKRLYVANSGSNTVSVIvsvidTATGKVVATIPVGG----GPVGVAVspDGRRLYVANRGSN---TSNGG 225

                   ...
gi 1709636372 2202 TGK 2204
Cdd:COG3391    226 SNT 228
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
1883-1919 1.73e-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: 38.23  E-value: 1.73e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1709636372 1883 ECLENNGgCSH--ICNDLKIGYECLCPSGYRLVdhKRCE 1919
Cdd:cd00053      1 ECAASNP-CSNggTCVNTPGSYRCVCPPGYTGD--RSCE 36
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
180-351 1.96e-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: 43.84  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  180 QLHQLRAQIMAYKMLARGQPLPDHLQMAV----QGKRPmPGMQQGQAMPSLPPGGA-GGPVTGPGPLGpNYNRGHVLSGP 254
Cdd:pfam09606   59 QQQQPQGGQGNGGMGGGQQGMPDPINALQnlagQGTRP-QMMGPMGPGPGGPMGQQmGGPGTASNLLA-SLGRPQMPMGG 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  255 SVPPSGPNAVPSANGPPKTWPEGPMVNAATPSNAPQKLIPPQP--TGRPSPVPPSVPPAASPVMPPQTQSPGHPGHS--- 329
Cdd:pfam09606  137 AGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGpgQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPAdag 216
                          170       180
                   ....*....|....*....|....*...
gi 1709636372  330 ------AQPTPTIPLHQKHnrITPMQKP 351
Cdd:pfam09606  217 aqmgqqAQANGGMNPQQMG--GAPNQVA 242
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
360-569 2.09e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 2.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  360 LQEREYRLEARITHRIQELEnlpgSLAGDLRTK-ATIELKALRLLNFQRQLRQevvvcMRRDAALETALDAKAYKRSKRQ 438
Cdd:COG1196    237 LEAELEELEAELEELEAELE----ELEAELAELeAELEELRLELEELELELEE-----AQAEEYELLAELARLEQDIARL 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  439 SLREARITEKLEK-QQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKMQKLTKAVATYHAN---TEREQKKENER 514
Cdd:COG1196    308 EERRRELEERLEElEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAElaeAEEELEELAEE 387
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1709636372  515 IEKERMRRLMAEDEEGYRKLIDQKKDKRLAYLLQQTDEYVANLTELVRAHKAVQA 569
Cdd:COG1196    388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
PHA02876 PHA02876
ankyrin repeat protein; Provisional
2809-2914 2.78e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 2.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2809 NTNVACLLLENGADPNIQDRFGITPAHDAARTGFLDTLCVLVDYGASVNIPDQSGALPIHIAI--REGYRDVVEFLAPRS 2886
Cdd:PHA02876   354 NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALcgTNPYMSVKTLIDRGA 433
                           90       100
                   ....*....|....*....|....*....
gi 1709636372 2887 NLGHQDTRGDTALDIA-EASCTPDMVELL 2914
Cdd:PHA02876   434 NVNSKNKDLSTPLHYAcKKNCKLDVIEML 462
PHA03377 PHA03377
EBNA-3C; Provisional
92-339 3.08e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 43.12  E-value: 3.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372   92 MRAGGHA-GMGPPPSpmdqhsqgypSPLGSSDHVSSPLPAGAPSTsgpllssscTSSSPLEGTDSQPSRSGAPSntPGSS 170
Cdd:PHA03377   653 MRAGRDGsGIQQEPS----------SRRQPATQSTPPRPSWLPSV---------FVLPSVDAGRAQPSEESHLS--SMSP 711
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  171 ANPTPFNQN------------QLHQLRAQIMAYKMLARGQPLPDHLQMAVQG---KRPMPGMQQGQAMPSLP-------P 228
Cdd:PHA03377   712 TQPISHEEQpryedpddpldlSLHPDQAPPPSHQAPYSGHEEPQAQQAPYPGywePRPPQAPYLGYQEPQAQgvqvssyP 791
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  229 GGAGgpvtgPGPLGPNYNR-GHVLSGPSV-----PPSGPNAvPSANGPPKTWPEGPMVNAATPSNAPQ---KLIPPQPTG 299
Cdd:PHA03377   792 GYAG-----PWGLRAQHPRyRHSWAYWSQypghgHPQGPWA-PRPPHLPPQWDGSAGHGQDQVSQFPHlqsETGPPRLQL 865
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1709636372  300 RPSPVPPSVPPAASPVMP----PQTQSPGHPGHSAQPTPTIPLH 339
Cdd:PHA03377   866 SQVPQLPYSQTLVSSSAPswssPQPRAPIRPIPTRFPPPPMPLQ 909
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
358-540 3.29e-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: 43.13  E-value: 3.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  358 EILQEREYRLEARI----------THRIQELENLPGSLAGDLRTKATiELKALRllNFQRQLRQEVVVCMRRDAALETAL 427
Cdd:TIGR02169  691 SSLQSELRRIENRLdelsqelsdaSRKIGEIEKEIEQLEQEEEKLKE-RLEELE--EDLSSLEQEIENVKSELKELEARI 767
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  428 DAKAYKRSKRQ--------SLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSvtgKMQKLTKAVAT 499
Cdd:TIGR02169  768 EELEEDLHKLEealndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK---EIQELQEQRID 844
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1709636372  500 YHAN-TEREQKKENERIEKERMRRLMAEDEEGYRKLIDQKKD 540
Cdd:TIGR02169  845 LKEQiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
1930-1958 3.36e-03

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: 37.22  E-value: 3.36e-03
                           10        20
                   ....*....|....*....|....*....
gi 1709636372 1930 CSQVCVNLVGSFKCDCQAGYEMDPMTKEC 1958
Cdd:pfam14670    8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
PHA03095 PHA03095
ankyrin-like protein; Provisional
2794-2907 3.79e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.70  E-value: 3.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2794 RNEFGKTALQVMMMG---NTNVACLLLENGADPNIQDRFGITPAHDAARTG--FLDTLCVLVDYGASVNIPDQSGALPIH 2868
Cdd:PHA03095   113 KDKVGRTPLHVYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGADVYAVDDRFRSLLH 192
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1709636372 2869 I---AIREGYRDVVEFLAPRSNLGHQDTRGDTALDIAEASCT 2907
Cdd:PHA03095   193 HhlqSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSS 234
PHA03379 PHA03379
EBNA-3A; Provisional
102-351 4.70e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 42.74  E-value: 4.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  102 PPPSPMDQHSQGypsPLgSSDHVSSPLPAgAPSTSGPLlsssctssSPLEGTDSQPSRSGAPSNTPGSSANPT-PFN--- 177
Cdd:PHA03379   443 PEPPPVHDLEPG---PL-HDQHSMAPCPV-AQLPPGPL--------QDLEPGDQLPGVVQDGRPACAPVPAPAgPIVrpw 509
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  178 QNQLHQLRAQIMAYKMlargqplPDHlqMAVQgKRPMPGMQQGQAMPSLPPGGAggpVTGPG-PLGPNYNRGHVLSGP-- 254
Cdd:PHA03379   510 EASLSQVPGVAFAPVM-------PQP--MPVE-PVPVPTVALERPVCPAPPLIA---MQGPGeTSGIVRVRERWRPAPwt 576
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  255 SVPPSGPNAVPSANGPPKTWPEgpmvnaATPSNAPQKLIPPQPTGRPSPVPPSVPPAASPVMPPqtQSPGHPGHSAQPTP 334
Cdd:PHA03379   577 PNPPRSPSQMSVRDRLARLRAE------AQPYQASVEVQPPQLTQVSPQQPMEYPLEPEQQMFP--GSPFSQVADVMRAG 648
                          250
                   ....*....|....*..
gi 1709636372  335 TIPLHQKHNRITPMQKP 351
Cdd:PHA03379   649 GVPAMQPQYFDLPLQQP 665
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
366-567 5.39e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.47  E-value: 5.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  366 RLEARITHRIQELenlpgSLAGDLRTKATIELKALRllNFQRQLRQEVVVCMRRDAAlETALDAKAYKR-----SKRQSL 440
Cdd:pfam01576    2 RQEEEMQAKEEEL-----QKVKERQQKAESELKELE--KKHQQLCEEKNALQEQLQA-ETELCAEAEEMrarlaARKQEL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  441 R------EARITEKLEKQQKIEQERKRRQkhqeylnsilQHAKDFKEYHRSVTGKMQKLTKAVATyhanTEREQKKENER 514
Cdd:pfam01576   74 EeilhelESRLEEEEERSQQLQNEKKKMQ----------QHIQDLEEQLDEEEAARQKLQLEKVT----TEAKIKKLEED 139
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1709636372  515 IekermrrLMAEDEEGyrKLIDQKK--DKRLAYL---LQQTDEYVANLTELVRAHKAV 567
Cdd:pfam01576  140 I-------LLLEDQNS--KLSKERKllEERISEFtsnLAEEEEKAKSLSKLKNKHEAM 188
SSDP pfam04503
Single-stranded DNA binding protein, SSDP; This is a family of eukaryotic single-stranded DNA ...
157-344 5.53e-03

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


Pssm-ID: 461334 [Multi-domain]  Cd Length: 293  Bit Score: 41.48  E-value: 5.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  157 PSRSGAPSNTPGSSANPTPFNQNQLHQLRAQIMaykMLAR--GQPLPDhLQMAVQGK--RPMPGMQ---QGQAMPSLPPG 229
Cdd:pfam04503   45 QSPPSHPSSQPSPHAQPPPHNPATMMGPHSQPF---MGPRypGGPRPS-VRMPQQGNdfNGPPGQQpmmPNSMDPTRPGG 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  230 --GAGGP---VTGP-----GPLGP-NYNRGhvLSGPsvPPS---GPNAVPSANGPPKTWPEGPMVNAATP---------- 285
Cdd:pfam04503  121 hpNMGGPmqrMNPPrgpgmGPMGPqSYGPG--MRGP--PPNstdGPGGMPPMNMGPGGRRPWPQPNASNPlpysssspgs 196
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709636372  286 -SNAPQKLIPPQPtgrpspvppsvppaaSPVMPpqtqSPGHPGHSAQPTPTI--PLHQKHNR 344
Cdd:pfam04503  197 yGGPPGGGGPPGP---------------TPIMP----SPQDSTNSGENMYTLmnPVGPGGNR 239
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
433-562 5.89e-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: 42.25  E-value: 5.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  433 KRSKRQSLREaRITEKLEKQQKIEQERKRR-QKHQEYL-NSILQHAKDFKEyhrsvtgkmqkltkavatyhaNTEREQKK 510
Cdd:pfam15709  327 KREQEKASRD-RLRAERAEMRRLEVERKRReQEEQRRLqQEQLERAEKMRE---------------------ELELEQQR 384
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1709636372  511 ENE-------RIEKERMRRlmaEDEEGYRKLIDQKKDKRLAyllQQTDEYVANLTELVR 562
Cdd:pfam15709  385 RFEeirlrkqRLEEERQRQ---EEEERKQRLQLQAAQERAR---QQQEEFRRKLQELQR 437
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
1924-1952 6.00e-03

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: 36.81  E-value: 6.00e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1709636372 1924 CAD-PDTCSQ--VCVNLVGSFKCDCQAGYEMD 1952
Cdd:pfam12947    1 CSDnNGGCHPnaTCTNTGGSFTCTCNDGYTGD 32
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
205-359 7.02e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 7.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  205 QMAVQGKRPMPGMQQGQAMPSLPPGGAGGPVTGPGPlgpnynrghvlsgpsvPPSGPnAVPSANGPPKTWPEGPMVNAAT 284
Cdd:pfam03154  164 QQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGP----------------TPSAP-SVPPQGSPATSQPPNQTQSTAA 226
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709636372  285 PSNAPQKLIPPQPTGRPspvppsvppAASPVMPPQTQSPGHPGHSAQPTPTiPLHqkHNRITPMQKPCGLDPVEI 359
Cdd:pfam03154  227 PHTLIQQTPTLHPQRLP---------SPHPPLQPMTQPPPPSQVSPQPLPQ-PSL--HGQMPPMPHSLQTGPSHM 289
PHA02682 PHA02682
ORF080 virion core protein; Provisional
236-441 7.48e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 41.00  E-value: 7.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  236 TGPGPLGPNynrghvlsgPSVP---PSGPNAVPSANGPPKTWPegpmvnaatpsnAPQKLIPP--QPTGRPSpVPPSVPP 310
Cdd:PHA02682    77 SGQSPLAPS---------PACAapaPACPACAPAAPAPAVTCP------------APAPACPPatAPTCPPP-AVCPAPA 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  311 AASPVMPPQTQS--PGHPGHSAQPTPTIPLHQKHNRITPMQKPCGLDP-VEILQEREYRLEARITHRIqelenlpgsLAG 387
Cdd:PHA02682   135 RPAPACPPSTRQcpPAPPLPTPKPAPAAKPIFLHNQLPPPDYPAASCPtIETAPAASPVLEPRIPDKI---------IDA 205
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1709636372  388 DLRTKATIELKALRLLNFQRQLRQEvVVCMRRDaaLETaldAKAYKRSKRQSLR 441
Cdd:PHA02682   206 DNDDKDLIKKELADIADSVRDLNAE-SLSLTRD--IEN---AKSTTQAAIDDLR 253
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
2764-2822 7.75e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 7.75e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372 2764 AGKSLTSAAVRGDAAEVRRLLEERrVHPDTRNEFGKTALQVMMM-GNTNVACLLLENGAD 2822
Cdd:PLN03192   622 AGDLLCTAAKRNDLTAMKELLKQG-LNVDSEDHQGATALQVAMAeDHVDMVRLLIMNGAD 680
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
400-565 9.15e-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: 41.06  E-value: 9.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  400 LRLLNfqRQLRQEVVVCMRRDAALETALDAKAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDF 479
Cdd:pfam13868    8 LRELN--SKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEER 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709636372  480 KEyhrsvtgkmqkltkavatyhantEREQKKENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAyLLQQTDEYVANLTE 559
Cdd:pfam13868   86 EQ-----------------------KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQ-LREEIDEFNEEQAE 141

                   ....*.
gi 1709636372  560 LVRAHK 565
Cdd:pfam13868  142 WKELEK 147
 
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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