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Conserved domains on  [gi|297265931|ref|XP_001112947.2|]
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PREDICTED: endothelial PAS domain-containing protein 1 isoform 3 [Macaca mulatta]

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List of domain hits

Name Accession Description Interval E-value
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
204-303 4.99e-17

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


:

Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 78.06  E-value: 4.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265931 204 SKTFLSRHSMDMKFTYCDDRITELIGYHPEELLGRSAYEFYHALDSENMTKSHQNLCTKGQVVSGQYRMLAKHGGYVWLE 283
Cdd:cd00130    1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                         90       100
                 ....*....|....*....|
gi 297265931 284 TQGTVIYNPRNLQPQCIMCV 303
Cdd:cd00130   81 VSLTPIRDEGGEVIGLLGVV 100
HLH cd00083
Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription ...
12-68 7.52e-10

Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription factors; 60-100 amino acids long. A DNA-binding basic region is followed by two alpha-helices separated by a variable loop region; HLH forms homo- and heterodimers, dimerization creates a parallel, left-handed, four helix bundle; the basic region N-terminal to the first amphipathic helix mediates high-affinity DNA-binding; there are several groups of HLH proteins: those (E12/E47) which bind specific hexanucleotide sequences such as E-box (5-CANNTG-3) or StRE 5-ATCACCCCAC-3), those lacking the basic domain (Emc, Id) function as negative regulators since they fail to bind DNA, those (hairy, E(spl), deadpan) which repress transcription although they can bind specific hexanucleotide sequences such as N-box (5-CACGc/aG-3), those which have a COE domain (Collier/Olf-1/EBF) which is involved in both in dimerization and in DNA binding, and those which bind pentanucleotides ACGTG or GCGTG and have a PAS domain which allows the dimerization between PAS proteins, the binding of small molecules (e.g., dioxin), and interactions with non-PAS proteins.


:

Pssm-ID: 238036  Cd Length: 60  Bit Score: 56.45  E-value: 7.52e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 297265931  12 SERRKEKSRDAARCRRSKETEVFYELAHELPLPHSvSSHLDKASIMRLAISFLRTHK 68
Cdd:cd00083    1 RKSRREAHNLRERRRRERINDAFDELRSLLPTLPP-SKKLSKAEILRKAVDYIKSLQ 56
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
95-145 1.44e-08

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


:

Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 53.41  E-value: 1.44e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 297265931  95 GFIAVVTQDGDMIFLSENISKFMGLTQVELTGHSIFDFTHPCDHEEIRENL 145
Cdd:cd00130    3 DGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERL 53
HIF-1a_CTAD pfam08778
HIF-1 alpha C terminal transactivation domain; Hypoxia inducible factor-1 alpha (HIF-1 alpha) ...
793-832 7.39e-18

HIF-1 alpha C terminal transactivation domain; Hypoxia inducible factor-1 alpha (HIF-1 alpha) is the regulatory subunit of the heterodimeric transcription factor HIF-1. It plays a key role in cellular response to low oxygen tension. This region corresponds to the C terminal transactivation domain.


:

Pssm-ID: 149743  Cd Length: 40  Bit Score: 78.87  E-value: 7.39e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 297265931  793 FESYLLPELTRYDCEVNVPVLGSSTLLQGGDLLRALDQAT 832
Cdd:pfam08778   1 FSSSTLPQLTRYDCEVNAPLQGRQYLLQGEELLRALDQVN 40
HIF-1 pfam11413
Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic ...
478-512 4.35e-12

Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic homeostatic responses to oxygen availability. In the presence of oxygen HIF-1 alpha is targeted for proteasomal degradation by pHVL, a ubiquitination complex.


:

Pssm-ID: 204647  Cd Length: 34  Bit Score: 62.32  E-value: 4.35e-12
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 297265931  478 STQTDFNELDLETLAPYIPMDgEDFQLSPICPEER 512
Cdd:pfam11413   1 FTSQDMEDLDLEMLAPYIPMD-DDFQLTPIDQLEP 34
DAG1 super family cl12309
Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the ...
541-763 6.25e-04

Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the dystrophin-associated glycoproteins, which is encoded by a 5.5 kb transcript in human. The protein product is cleaved into two non-covalently associated subunits, [alpha] (N-terminal) and [beta] (C-terminal). In skeletal muscle the dystroglycan complex works as a transmembrane linkage between the extracellular matrix and the cytoskeleton. [alpha]-dystroglycan is extracellular and binds to merosin ([alpha]-2 laminin) in the basement membrane, while [beta]-dystroglycan is a transmembrane protein and binds to dystrophin, which is a large rod-like cytoskeletal protein, absent in Duchenne muscular dystrophy patients. Dystrophin binds to intracellular actin cables. In this way, the dystroglycan complex, which links the extracellular matrix to the intracellular actin cables, is thought to provide structural integrity in muscle tissues. The dystroglycan complex is also known to serve as an agrin receptor in muscle, where it may regulate agrin-induced acetylcholine receptor clustering at the neuromuscular junction. There is also evidence which suggests the function of dystroglycan as a part of the signal transduction pathway because it is shown that Grb2, a mediator of the Ras-related signal pathway, can interact with the cytoplasmic domain of dystroglycan. In general, aberrant expression of dystrophin-associated protein complex underlies the pathogenesis of Duchenne muscular dystrophy, Becker muscular dystrophy and severe childhood autosomal recessive muscular dystrophy. Interestingly, no genetic disease has been described for either [alpha]- or [beta]-dystroglycan. Dystroglycan is widely distributed in non-muscle tissues as well as in muscle tissues. During epithelial morphogenesis of kidney, the dystroglycan complex is shown to act as a receptor for the basement membrane. Dystroglycan expression in mouse brain and neural retina has also been reported. However, the physiological role of dystroglycan in non-muscle tissues has remained unclear.


The actual alignment was detected with superfamily member pfam05454:

Pssm-ID: 147567  Cd Length: 290  Bit Score: 41.14  E-value: 6.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265931  541 PHSPFLLDKFQQqLESKKTEPEHRPmSSIFfdagsKASLPPCCGQASTPLSSMGGRSNTQWPPDPPLHFGPTKwavgdqr 620
Cdd:pfam05454  60 PHEPCPKEQVAM-LSKKILDSDGSP-REAF-----KNALEPEFKLTNISVVGTGSCRHTEFIPTNPLDYIPSR------- 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265931  621 teflgAAPLGPPVSPPHISTFKTRSAKGFGArgPDVLSPAM------VALSNKLKLKRQLEYEEQA----------FQD- 683
Cdd:pfam05454 126 -----TPPTGTPDRPPEKSSEDDVYLHTVIP--AVVVAAILliagiiAMICYRKKRKGKLTLEDQAtfikkgvpiiFADe 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265931  684 LSGGDPPGGSTSHLMWKRMKnlrggsCPLMPDKPLSANVPNGKFTQNPVRGLGHPLRHL-----PLPQPPSAVSPGENSK 758
Cdd:pfam05454 199 LDDSKPPPSSSMPLILKEEK------PPLPPPEYPNQNVPETTPLNQDLLGEYTPLRDEdpnapPYQPPPPFTTPMEGKG 272

                  ....*
gi 297265931  759 SRFPA 763
Cdd:pfam05454 273 SRPKN 277
PAS_11 pfam14598
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
207-309 2.88e-23

PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), which binds to an LXXLL motif in the C-terminal region of STAT6 (Signal transducer and activator of transcription 6).


:

Pssm-ID: 258736 [Multi-domain]  Cd Length: 110  Bit Score: 96.17  E-value: 2.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265931  207 FLSRHSMDMKFTYCDDRITELI-GYHPEELLGRSAYEFYHALDSENMTKSHQNLCTKGQVVSGQYRMLAKHGGYVWLETQ 285
Cdd:pfam14598   4 FTTRHDMDGKIIHIDTSGLRAVlGYLTEELVGRSIYDLCHPDDLRTLKKHLREVYDNGQARSSIYRLRLRDGDFVYVHTK 83
                          90       100
                  ....*....|....*....|....
gi 297265931  286 GTVIYNPRNLQPQCIMCVNYVLSE 309
Cdd:pfam14598  84 SKLFRNQKTNEQDFIMCTHTLLSE 107
 
Name Accession Description Interval E-value
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
204-303 4.99e-17

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 78.06  E-value: 4.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265931 204 SKTFLSRHSMDMKFTYCDDRITELIGYHPEELLGRSAYEFYHALDSENMTKSHQNLCTKGQVVSGQYRMLAKHGGYVWLE 283
Cdd:cd00130    1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                         90       100
                 ....*....|....*....|
gi 297265931 284 TQGTVIYNPRNLQPQCIMCV 303
Cdd:cd00130   81 VSLTPIRDEGGEVIGLLGVV 100
HLH cd00083
Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription ...
12-68 7.52e-10

Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription factors; 60-100 amino acids long. A DNA-binding basic region is followed by two alpha-helices separated by a variable loop region; HLH forms homo- and heterodimers, dimerization creates a parallel, left-handed, four helix bundle; the basic region N-terminal to the first amphipathic helix mediates high-affinity DNA-binding; there are several groups of HLH proteins: those (E12/E47) which bind specific hexanucleotide sequences such as E-box (5-CANNTG-3) or StRE 5-ATCACCCCAC-3), those lacking the basic domain (Emc, Id) function as negative regulators since they fail to bind DNA, those (hairy, E(spl), deadpan) which repress transcription although they can bind specific hexanucleotide sequences such as N-box (5-CACGc/aG-3), those which have a COE domain (Collier/Olf-1/EBF) which is involved in both in dimerization and in DNA binding, and those which bind pentanucleotides ACGTG or GCGTG and have a PAS domain which allows the dimerization between PAS proteins, the binding of small molecules (e.g., dioxin), and interactions with non-PAS proteins.


Pssm-ID: 238036  Cd Length: 60  Bit Score: 56.45  E-value: 7.52e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 297265931  12 SERRKEKSRDAARCRRSKETEVFYELAHELPLPHSvSSHLDKASIMRLAISFLRTHK 68
Cdd:cd00083    1 RKSRREAHNLRERRRRERINDAFDELRSLLPTLPP-SKKLSKAEILRKAVDYIKSLQ 56
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
95-145 1.44e-08

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 53.41  E-value: 1.44e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 297265931  95 GFIAVVTQDGDMIFLSENISKFMGLTQVELTGHSIFDFTHPCDHEEIRENL 145
Cdd:cd00130    3 DGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERL 53
HIF-1a_CTAD pfam08778
HIF-1 alpha C terminal transactivation domain; Hypoxia inducible factor-1 alpha (HIF-1 alpha) ...
793-832 7.39e-18

HIF-1 alpha C terminal transactivation domain; Hypoxia inducible factor-1 alpha (HIF-1 alpha) is the regulatory subunit of the heterodimeric transcription factor HIF-1. It plays a key role in cellular response to low oxygen tension. This region corresponds to the C terminal transactivation domain.


Pssm-ID: 149743  Cd Length: 40  Bit Score: 78.87  E-value: 7.39e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 297265931  793 FESYLLPELTRYDCEVNVPVLGSSTLLQGGDLLRALDQAT 832
Cdd:pfam08778   1 FSSSTLPQLTRYDCEVNAPLQGRQYLLQGEELLRALDQVN 40
HIF-1 pfam11413
Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic ...
478-512 4.35e-12

Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic homeostatic responses to oxygen availability. In the presence of oxygen HIF-1 alpha is targeted for proteasomal degradation by pHVL, a ubiquitination complex.


Pssm-ID: 204647  Cd Length: 34  Bit Score: 62.32  E-value: 4.35e-12
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 297265931  478 STQTDFNELDLETLAPYIPMDgEDFQLSPICPEER 512
Cdd:pfam11413   1 FTSQDMEDLDLEMLAPYIPMD-DDFQLTPIDQLEP 34
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
84-145 2.59e-09

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 54.71  E-value: 2.59e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297265931    84 QMDNLYLKALEGFIAVVTQDGDMIFLSENISKFMGLTQVELTGHSIFDFTHPCDHEEIRENL 145
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEAL 62
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
204-259 8.97e-09

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 53.17  E-value: 8.97e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 297265931   204 SKTFLSRHSMDMKFTYCDDRITELIGYHPEELLGRSAYEFYHALDSENMTKSHQNL 259
Cdd:smart00091  10 LPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRL 65
HLH smart00353
helix loop helix domain;
20-65 7.57e-08

helix loop helix domain;


Pssm-ID: 197674  Cd Length: 53  Bit Score: 50.29  E-value: 7.57e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 297265931    20 RDAARCRRSKETEVFYELAHELPlPHSVSSHLDKASIMRLAISFLR 65
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLP-TLPKNKKLSKAEILRLAIEYIK 45
DAG1 pfam05454
Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the ...
541-763 6.25e-04

Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the dystrophin-associated glycoproteins, which is encoded by a 5.5 kb transcript in human. The protein product is cleaved into two non-covalently associated subunits, [alpha] (N-terminal) and [beta] (C-terminal). In skeletal muscle the dystroglycan complex works as a transmembrane linkage between the extracellular matrix and the cytoskeleton. [alpha]-dystroglycan is extracellular and binds to merosin ([alpha]-2 laminin) in the basement membrane, while [beta]-dystroglycan is a transmembrane protein and binds to dystrophin, which is a large rod-like cytoskeletal protein, absent in Duchenne muscular dystrophy patients. Dystrophin binds to intracellular actin cables. In this way, the dystroglycan complex, which links the extracellular matrix to the intracellular actin cables, is thought to provide structural integrity in muscle tissues. The dystroglycan complex is also known to serve as an agrin receptor in muscle, where it may regulate agrin-induced acetylcholine receptor clustering at the neuromuscular junction. There is also evidence which suggests the function of dystroglycan as a part of the signal transduction pathway because it is shown that Grb2, a mediator of the Ras-related signal pathway, can interact with the cytoplasmic domain of dystroglycan. In general, aberrant expression of dystrophin-associated protein complex underlies the pathogenesis of Duchenne muscular dystrophy, Becker muscular dystrophy and severe childhood autosomal recessive muscular dystrophy. Interestingly, no genetic disease has been described for either [alpha]- or [beta]-dystroglycan. Dystroglycan is widely distributed in non-muscle tissues as well as in muscle tissues. During epithelial morphogenesis of kidney, the dystroglycan complex is shown to act as a receptor for the basement membrane. Dystroglycan expression in mouse brain and neural retina has also been reported. However, the physiological role of dystroglycan in non-muscle tissues has remained unclear.


Pssm-ID: 147567  Cd Length: 290  Bit Score: 41.14  E-value: 6.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265931  541 PHSPFLLDKFQQqLESKKTEPEHRPmSSIFfdagsKASLPPCCGQASTPLSSMGGRSNTQWPPDPPLHFGPTKwavgdqr 620
Cdd:pfam05454  60 PHEPCPKEQVAM-LSKKILDSDGSP-REAF-----KNALEPEFKLTNISVVGTGSCRHTEFIPTNPLDYIPSR------- 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265931  621 teflgAAPLGPPVSPPHISTFKTRSAKGFGArgPDVLSPAM------VALSNKLKLKRQLEYEEQA----------FQD- 683
Cdd:pfam05454 126 -----TPPTGTPDRPPEKSSEDDVYLHTVIP--AVVVAAILliagiiAMICYRKKRKGKLTLEDQAtfikkgvpiiFADe 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265931  684 LSGGDPPGGSTSHLMWKRMKnlrggsCPLMPDKPLSANVPNGKFTQNPVRGLGHPLRHL-----PLPQPPSAVSPGENSK 758
Cdd:pfam05454 199 LDDSKPPPSSSMPLILKEEK------PPLPPPEYPNQNVPETTPLNQDLLGEYTPLRDEdpnapPYQPPPPFTTPMEGKG 272

                  ....*
gi 297265931  759 SRFPA 763
Cdd:pfam05454 273 SRPKN 277
PAS_11 pfam14598
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
207-309 2.88e-23

PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), which binds to an LXXLL motif in the C-terminal region of STAT6 (Signal transducer and activator of transcription 6).


Pssm-ID: 258736 [Multi-domain]  Cd Length: 110  Bit Score: 96.17  E-value: 2.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265931  207 FLSRHSMDMKFTYCDDRITELI-GYHPEELLGRSAYEFYHALDSENMTKSHQNLCTKGQVVSGQYRMLAKHGGYVWLETQ 285
Cdd:pfam14598   4 FTTRHDMDGKIIHIDTSGLRAVlGYLTEELVGRSIYDLCHPDDLRTLKKHLREVYDNGQARSSIYRLRLRDGDFVYVHTK 83
                          90       100
                  ....*....|....*....|....
gi 297265931  286 GTVIYNPRNLQPQCIMCVNYVLSE 309
Cdd:pfam14598  84 SKLFRNQKTNEQDFIMCTHTLLSE 107
PAS COG2202
PAS domain [Signal transduction mechanisms];
96-291 9.91e-06

PAS domain [Signal transduction mechanisms];


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 46.38  E-value: 9.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265931  96 FIAVVTQDGDMIFLSENISKFMGLTQVELTGhsIFDFTHPCDHEEIRENLSLK---NGILNCVLHCTGQVKVYNNCPPHN 172
Cdd:COG2202    1 LILVLDRDGRIIYANEAAEELLGYSAEELLG--LLLALHPEDRDRLRELLRRLlagEELLSEELRLVRKDGEERWVELSA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265931 173 SLCGYKEPLLSCLIIMCEP----------IQHPSHMDIPLD-SKTFLSRHSMDMKFTYCDDRITELIGYHPEELLGRSAY 241
Cdd:COG2202   79 APLRDGEGRVLGLLGLRDIterkraeealRESEERLRALLEaSPDGIWVLDEDGRILYANPAAEELLGYSPEEELGRGLS 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 297265931 242 EFYHALDSEN--MTKSHQNLCTKGQVVSGQYRMLAKHGGYV-WLETQGTVIYN 291
Cdd:COG2202  159 DLIHPEDEERreLELARALAEGRGGPLEIEYRVRRKDGERVrWILSRISPVRD 211
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
97-147 1.30e-03

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 38.43  E-value: 1.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 297265931   97 IAVVTQDGDMIFLSENISKFMGLTQVELTGHSIFDFTHPCDHEEIRENLSL 147
Cdd:TIGR00229  16 IIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIER 66
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
216-290 2.33e-03

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 37.66  E-value: 2.33e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297265931  216 KFTYCDDRITELIGYHPEELLGRSAYEFYHALDSENMTKSHQNLCTKGQ-VVSGQYRMLAKHGGYVWLETQGTVIY 290
Cdd:TIGR00229  24 NILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPePVSEERRVRRKDGSEIWVEVSVSPIR 99
 
Name Accession Description Interval E-value
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
204-303 4.99e-17

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 78.06  E-value: 4.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265931 204 SKTFLSRHSMDMKFTYCDDRITELIGYHPEELLGRSAYEFYHALDSENMTKSHQNLCTKGQVVSGQYRMLAKHGGYVWLE 283
Cdd:cd00130    1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                         90       100
                 ....*....|....*....|
gi 297265931 284 TQGTVIYNPRNLQPQCIMCV 303
Cdd:cd00130   81 VSLTPIRDEGGEVIGLLGVV 100
HLH cd00083
Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription ...
12-68 7.52e-10

Helix-loop-helix domain, found in specific DNA- binding proteins that act as transcription factors; 60-100 amino acids long. A DNA-binding basic region is followed by two alpha-helices separated by a variable loop region; HLH forms homo- and heterodimers, dimerization creates a parallel, left-handed, four helix bundle; the basic region N-terminal to the first amphipathic helix mediates high-affinity DNA-binding; there are several groups of HLH proteins: those (E12/E47) which bind specific hexanucleotide sequences such as E-box (5-CANNTG-3) or StRE 5-ATCACCCCAC-3), those lacking the basic domain (Emc, Id) function as negative regulators since they fail to bind DNA, those (hairy, E(spl), deadpan) which repress transcription although they can bind specific hexanucleotide sequences such as N-box (5-CACGc/aG-3), those which have a COE domain (Collier/Olf-1/EBF) which is involved in both in dimerization and in DNA binding, and those which bind pentanucleotides ACGTG or GCGTG and have a PAS domain which allows the dimerization between PAS proteins, the binding of small molecules (e.g., dioxin), and interactions with non-PAS proteins.


Pssm-ID: 238036  Cd Length: 60  Bit Score: 56.45  E-value: 7.52e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 297265931  12 SERRKEKSRDAARCRRSKETEVFYELAHELPLPHSvSSHLDKASIMRLAISFLRTHK 68
Cdd:cd00083    1 RKSRREAHNLRERRRRERINDAFDELRSLLPTLPP-SKKLSKAEILRKAVDYIKSLQ 56
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
95-145 1.44e-08

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 53.41  E-value: 1.44e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 297265931  95 GFIAVVTQDGDMIFLSENISKFMGLTQVELTGHSIFDFTHPCDHEEIRENL 145
Cdd:cd00130    3 DGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERL 53
HIF-1a_CTAD pfam08778
HIF-1 alpha C terminal transactivation domain; Hypoxia inducible factor-1 alpha (HIF-1 alpha) ...
793-832 7.39e-18

HIF-1 alpha C terminal transactivation domain; Hypoxia inducible factor-1 alpha (HIF-1 alpha) is the regulatory subunit of the heterodimeric transcription factor HIF-1. It plays a key role in cellular response to low oxygen tension. This region corresponds to the C terminal transactivation domain.


Pssm-ID: 149743  Cd Length: 40  Bit Score: 78.87  E-value: 7.39e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 297265931  793 FESYLLPELTRYDCEVNVPVLGSSTLLQGGDLLRALDQAT 832
Cdd:pfam08778   1 FSSSTLPQLTRYDCEVNAPLQGRQYLLQGEELLRALDQVN 40
HIF-1 pfam11413
Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic ...
478-512 4.35e-12

Hypoxia-inducible factor-1; HIF-1 is a transcriptional complex and controls cellular systemic homeostatic responses to oxygen availability. In the presence of oxygen HIF-1 alpha is targeted for proteasomal degradation by pHVL, a ubiquitination complex.


Pssm-ID: 204647  Cd Length: 34  Bit Score: 62.32  E-value: 4.35e-12
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 297265931  478 STQTDFNELDLETLAPYIPMDgEDFQLSPICPEER 512
Cdd:pfam11413   1 FTSQDMEDLDLEMLAPYIPMD-DDFQLTPIDQLEP 34
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
84-145 2.59e-09

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 54.71  E-value: 2.59e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297265931    84 QMDNLYLKALEGFIAVVTQDGDMIFLSENISKFMGLTQVELTGHSIFDFTHPCDHEEIRENL 145
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEAL 62
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
204-259 8.97e-09

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 53.17  E-value: 8.97e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 297265931   204 SKTFLSRHSMDMKFTYCDDRITELIGYHPEELLGRSAYEFYHALDSENMTKSHQNL 259
Cdd:smart00091  10 LPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRL 65
HLH smart00353
helix loop helix domain;
20-65 7.57e-08

helix loop helix domain;


Pssm-ID: 197674  Cd Length: 53  Bit Score: 50.29  E-value: 7.57e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 297265931    20 RDAARCRRSKETEVFYELAHELPlPHSVSSHLDKASIMRLAISFLR 65
Cdd:smart00353   1 NARERRRRRKINEAFDELRSLLP-TLPKNKKLSKAEILRLAIEYIK 45
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
267-309 7.12e-07

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 47.18  E-value: 7.12e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 297265931   267 SGQYRMLAKHGGYVWLETQGTVIYNPRNlQPQCIMCVNYVLSE 309
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDEDG-EVEGILGVVRDITE 42
DAG1 pfam05454
Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the ...
541-763 6.25e-04

Dystroglycan (Dystrophin-associated glycoprotein 1); Dystroglycan is one of the dystrophin-associated glycoproteins, which is encoded by a 5.5 kb transcript in human. The protein product is cleaved into two non-covalently associated subunits, [alpha] (N-terminal) and [beta] (C-terminal). In skeletal muscle the dystroglycan complex works as a transmembrane linkage between the extracellular matrix and the cytoskeleton. [alpha]-dystroglycan is extracellular and binds to merosin ([alpha]-2 laminin) in the basement membrane, while [beta]-dystroglycan is a transmembrane protein and binds to dystrophin, which is a large rod-like cytoskeletal protein, absent in Duchenne muscular dystrophy patients. Dystrophin binds to intracellular actin cables. In this way, the dystroglycan complex, which links the extracellular matrix to the intracellular actin cables, is thought to provide structural integrity in muscle tissues. The dystroglycan complex is also known to serve as an agrin receptor in muscle, where it may regulate agrin-induced acetylcholine receptor clustering at the neuromuscular junction. There is also evidence which suggests the function of dystroglycan as a part of the signal transduction pathway because it is shown that Grb2, a mediator of the Ras-related signal pathway, can interact with the cytoplasmic domain of dystroglycan. In general, aberrant expression of dystrophin-associated protein complex underlies the pathogenesis of Duchenne muscular dystrophy, Becker muscular dystrophy and severe childhood autosomal recessive muscular dystrophy. Interestingly, no genetic disease has been described for either [alpha]- or [beta]-dystroglycan. Dystroglycan is widely distributed in non-muscle tissues as well as in muscle tissues. During epithelial morphogenesis of kidney, the dystroglycan complex is shown to act as a receptor for the basement membrane. Dystroglycan expression in mouse brain and neural retina has also been reported. However, the physiological role of dystroglycan in non-muscle tissues has remained unclear.


Pssm-ID: 147567  Cd Length: 290  Bit Score: 41.14  E-value: 6.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265931  541 PHSPFLLDKFQQqLESKKTEPEHRPmSSIFfdagsKASLPPCCGQASTPLSSMGGRSNTQWPPDPPLHFGPTKwavgdqr 620
Cdd:pfam05454  60 PHEPCPKEQVAM-LSKKILDSDGSP-REAF-----KNALEPEFKLTNISVVGTGSCRHTEFIPTNPLDYIPSR------- 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265931  621 teflgAAPLGPPVSPPHISTFKTRSAKGFGArgPDVLSPAM------VALSNKLKLKRQLEYEEQA----------FQD- 683
Cdd:pfam05454 126 -----TPPTGTPDRPPEKSSEDDVYLHTVIP--AVVVAAILliagiiAMICYRKKRKGKLTLEDQAtfikkgvpiiFADe 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265931  684 LSGGDPPGGSTSHLMWKRMKnlrggsCPLMPDKPLSANVPNGKFTQNPVRGLGHPLRHL-----PLPQPPSAVSPGENSK 758
Cdd:pfam05454 199 LDDSKPPPSSSMPLILKEEK------PPLPPPEYPNQNVPETTPLNQDLLGEYTPLRDEdpnapPYQPPPPFTTPMEGKG 272

                  ....*
gi 297265931  759 SRFPA 763
Cdd:pfam05454 273 SRPKN 277
PAS_11 pfam14598
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
207-309 2.88e-23

PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), which binds to an LXXLL motif in the C-terminal region of STAT6 (Signal transducer and activator of transcription 6).


Pssm-ID: 258736 [Multi-domain]  Cd Length: 110  Bit Score: 96.17  E-value: 2.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265931  207 FLSRHSMDMKFTYCDDRITELI-GYHPEELLGRSAYEFYHALDSENMTKSHQNLCTKGQVVSGQYRMLAKHGGYVWLETQ 285
Cdd:pfam14598   4 FTTRHDMDGKIIHIDTSGLRAVlGYLTEELVGRSIYDLCHPDDLRTLKKHLREVYDNGQARSSIYRLRLRDGDFVYVHTK 83
                          90       100
                  ....*....|....*....|....
gi 297265931  286 GTVIYNPRNLQPQCIMCVNYVLSE 309
Cdd:pfam14598  84 SKLFRNQKTNEQDFIMCTHTLLSE 107
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
217-304 1.41e-17

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 254805 [Multi-domain]  Cd Length: 90  Bit Score: 79.35  E-value: 1.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265931  217 FTYCDDRITELIGYHPEELLGRSA--YEFYHALDSENMTKSHQNLCTK-GQVVSGQYRMLAKHGGYVWLETQGTVIYNPR 293
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELKSSYEgwLDLVHPEDRERVRRALQELLLKkGEPYSGEYRIRRKDGSYRWVEARGRPIRDEN 80
                          90
                  ....*....|.
gi 297265931  294 NlQPQCIMCVN 304
Cdd:pfam08447  81 G-KPVRVIGVA 90
PAS_9 pfam13426
PAS domain;
212-303 3.27e-06

PAS domain;


Pssm-ID: 257751 [Multi-domain]  Cd Length: 104  Bit Score: 46.22  E-value: 3.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265931  212 SMDMKFTYCDDRITELIGYHPEELLGRSAYEFYHALDSENMTKSHQNLCTKGQVVSGQYRMLAKHGGYVWLETQGTVIYN 291
Cdd:pfam13426   8 DPEGRIVYANPAALRLLGYTREELLGKSIRDLFGPGTDEEAVARLREALRNGGEVEVELELRRKDGEPFPVLVSASPVRD 87
                          90
                  ....*....|..
gi 297265931  292 PRNlQPQCIMCV 303
Cdd:pfam13426  88 EDG-EVVGIVGI 98
PAS COG2202
PAS domain [Signal transduction mechanisms];
96-291 9.91e-06

PAS domain [Signal transduction mechanisms];


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 46.38  E-value: 9.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265931  96 FIAVVTQDGDMIFLSENISKFMGLTQVELTGhsIFDFTHPCDHEEIRENLSLK---NGILNCVLHCTGQVKVYNNCPPHN 172
Cdd:COG2202    1 LILVLDRDGRIIYANEAAEELLGYSAEELLG--LLLALHPEDRDRLRELLRRLlagEELLSEELRLVRKDGEERWVELSA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297265931 173 SLCGYKEPLLSCLIIMCEP----------IQHPSHMDIPLD-SKTFLSRHSMDMKFTYCDDRITELIGYHPEELLGRSAY 241
Cdd:COG2202   79 APLRDGEGRVLGLLGLRDIterkraeealRESEERLRALLEaSPDGIWVLDEDGRILYANPAAEELLGYSPEEELGRGLS 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 297265931 242 EFYHALDSEN--MTKSHQNLCTKGQVVSGQYRMLAKHGGYV-WLETQGTVIYN 291
Cdd:COG2202  159 DLIHPEDEERreLELARALAEGRGGPLEIEYRVRRKDGERVrWILSRISPVRD 211
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
216-292 3.54e-05

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 250275 [Multi-domain]  Cd Length: 111  Bit Score: 43.16  E-value: 3.54e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297265931  216 KFTYCDDRITELIGYHPEELLGRSAYEFYHALDSENMTKSHQNLCTKGQVVSGQYRMLAKHGGYVWLETQGTVIYNP 292
Cdd:pfam00989  22 RILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAVAELLRQALLQGEESRGFEVSFRVRDGRPRHVEVRASPVRDA 98
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
97-147 1.30e-03

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 38.43  E-value: 1.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 297265931   97 IAVVTQDGDMIFLSENISKFMGLTQVELTGHSIFDFTHPCDHEEIRENLSL 147
Cdd:TIGR00229  16 IIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIER 66
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
216-290 2.33e-03

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 37.66  E-value: 2.33e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297265931  216 KFTYCDDRITELIGYHPEELLGRSAYEFYHALDSENMTKSHQNLCTKGQ-VVSGQYRMLAKHGGYVWLETQGTVIY 290
Cdd:TIGR00229  24 NILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPePVSEERRVRRKDGSEIWVEVSVSPIR 99
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.14
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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