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Conserved domains on  [gi|739292236|ref|WP_037154920|]
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MULTISPECIES: benzoate 1,2-dioxygenase small subunit [Nocardiaceae]

Protein Classification

nuclear transport factor 2 family protein( domain architecture ID 233)

nuclear transport factor 2 (NTF2) family protein, similar to Aspergillus flavus scytalone dehydratases, Pseudomonas putida benzene 1,2-dioxygenase subunit beta, and many other members with similar structural details but divergent functions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NTF2_like super family cl09109
Nuclear transport factor 2 (NTF2-like) superfamily. This family includes members of the NTF2 ...
 24-178 3.87e-92

Nuclear transport factor 2 (NTF2-like) superfamily. This family includes members of the NTF2 family, Delta-5-3-ketosteroid isomerases, Scytalone Dehydratases, and the beta subunit of Ring hydroxylating dioxygenases. This family is a classic example of divergent evolution wherein the proteins have many common structural details but diverge greatly in their function. For example, nuclear transport factor 2 (NTF2) mediates the nuclear import of RanGDP and binds to both RanGDP and FxFG repeat-containing nucleoporins while Ketosteroid isomerases catalyze the isomerization of delta-5-3-ketosteroid to delta-4-3-ketosteroid, by intramolecular transfer of the C4-beta proton to the C6-beta position. While the function of the beta sub-unit of the Ring hydroxylating dioxygenases is not known, Scytalone Dehydratases catalyzes two reactions in the biosynthetic pathway that produces fungal melanin. Members of the NTF2-like superfamily are widely distributed among bacteria, archaea and eukaryotes.


The actual alignment was detected with superfamily member TIGR03232:

Pssm-ID: 471850  Cd Length: 155  Bit Score: 265.14  E-value: 3.87e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739292236   24 IEQFLYREARYLDDREFEKWLTCYADDVEYWMPCWDDNDLLTEDPQTDISLIYYENKGGLEDRVFRIRTERSSATsIPEP 103
Cdd:TIGR03232   1 IQAFLYREARLLDDEQWDDWLECYRADASFWMPAWDDDDQLTEDPQSEISLIYYPNRQGLEDRVFRIKTERSSAT-VPDT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739292236  104 RTSHNISNVEVIERRGDIVDVRFNWHTMYFRYKTIDPYYGTSFYTIDFSGDSPLIRRKTVVLKNDYIHHVVDIYH 178
Cdd:TIGR03232  80 RTSHNISNVEIEEQDGDVITVRFNWHTLSFRYKTTDSYFGMSRYTIDFSGESPKIKSKYVVLKNDYINQVIDIYH 154
 
Name Accession Description Interval E-value
benzo_1_2_benB TIGR03232
benzoate 1,2-dioxygenase, small subunit; Benzoate 1,2-dioxygenase (EC 1.14.12.10) belongs to ...
 24-178 3.87e-92

benzoate 1,2-dioxygenase, small subunit; Benzoate 1,2-dioxygenase (EC 1.14.12.10) belongs to the larger family of aromatic ring-hydroxylating dioxygenases. Members of this family should all act on benzoate, but several have additional known activities on various benozate analogs. Some members actually may be named more suitably according to such alternate an activity, such as 2-chlorobenzoate 1,2-dioxygenase (1.14.12.13).


Pssm-ID: 132276  Cd Length: 155  Bit Score: 265.14  E-value: 3.87e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739292236   24 IEQFLYREARYLDDREFEKWLTCYADDVEYWMPCWDDNDLLTEDPQTDISLIYYENKGGLEDRVFRIRTERSSATsIPEP 103
Cdd:TIGR03232   1 IQAFLYREARLLDDEQWDDWLECYRADASFWMPAWDDDDQLTEDPQSEISLIYYPNRQGLEDRVFRIKTERSSAT-VPDT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739292236  104 RTSHNISNVEVIERRGDIVDVRFNWHTMYFRYKTIDPYYGTSFYTIDFSGDSPLIRRKTVVLKNDYIHHVVDIYH 178
Cdd:TIGR03232  80 RTSHNISNVEIEEQDGDVITVRFNWHTLSFRYKTTDSYFGMSRYTIDFSGESPKIKSKYVVLKNDYINQVIDIYH 154
ring_hydroxylating_dioxygenases_beta cd00667
Ring hydroxylating dioxygenase beta subunit. This subunit has a similar structure to NTF-2, ...
 20-178 3.99e-59

Ring hydroxylating dioxygenase beta subunit. This subunit has a similar structure to NTF-2, Ketosteroid isomerase and scytalone dehydratase.The degradation of aromatic compounds by aerobic bacteria frequently begins with the dihydroxylation of the substrate by nonheme iron-containing dioxygenases. These enzymes consist of two or three soluble proteins that interact to form an electron-transport chain that transfers electrons from reduced nucleotides (NADH) via flavin and [2Fe-2S] redox centers to a terminal dioxygenase. Aromatic-ring-hydroxylating dioxygenases oxidize aromatic hydrocarbons and related compounds to cis-arene diols. These enzymes utilize a mononuclear non-heme iron center to catalyze the addition of dioxygen to their respective substrates. The active site of these enzymes however is in the alpha sub-unit. No functional role has been attributed to the beta sub-unit except for a structural role.


Pssm-ID: 238357  Cd Length: 160  Bit Score: 181.69  E-value: 3.99e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739292236  20 TQSSIEQFLYREARYLDDREFEKWLTCYADDVEYWMPCWDDNDLLTEDPQTDISLIYYENKGGLEDRVFRIRTERSSATS 99
Cdd:cd00667    2 LQAEVEQFLYREARLLDDRRWDEWLALFAEDCHYWVPARENRERRDEDPGLELSAIYDDDRRMLEDRVVRLRTGRAWSED 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739292236 100 iPEPRTSHNISNVEVIERRGDIVDVRFNWHTMYFRYK-TIDPYYGTSFYTIDFSGDSPLIRRKTVVLKNDYIHHVVDIYH 178
Cdd:cd00667   82 -PPSRTRHLVSNVRVLEGDGGEIEVRSNFVVVRTRLDgESDVFAGGRYDDLRRSEDGLRIASRRVVLDNDRIPTVNLSPF 160
HcaF COG5517
3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites ...
 14-179 1.19e-54

3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 444268  Cd Length: 162  Bit Score: 170.41  E-value: 1.19e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739292236  14 APSRLITQSSIEQFLYREARYLDDREFEKWLTCYADDVEYWMPCWDDNDlltEDPQTDISLIyYENKGGLEDRVFRIRTE 93
Cdd:COG5517    1 AAVDLELRAEVEQFLYREARLLDERRFDEWLALFTEDGHYWVPARENRD---TDPGLPLSLI-YDDRAMLEDRVARLRTG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739292236  94 RSSAtSIPEPRTSHNISNVEVIERRGDIVDVRFNWHTMYFRYKTIDPYY-GTSFYTIDFSGDSPLIRRKTVVLKNDYIHH 172
Cdd:COG5517   77 NAWA-EDPPSRTRHLVSNVRVEETDGGEIEVRSNFLVYRTRRDGQTDLFvGRYEDRLRRTGGGLRIARRRVVLDNSVIPT 155


                 ....*..
gi 739292236 173 VVDIYHF 179
Cdd:COG5517  156 KNLSYPL 162
Ring_hydroxyl_B pfam00866
Ring hydroxylating beta subunit; This subunit has a similar structure to NTF-2 and scytalone ...
 30-170 8.56e-52

Ring hydroxylating beta subunit; This subunit has a similar structure to NTF-2 and scytalone dehydratase.


Pssm-ID: 425916  Cd Length: 144  Bit Score: 162.46  E-value: 8.56e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739292236   30 REARYLDDREFEKWLTCYADDVEYWMPCWDDNDLLTEDPQTDISLIYYENKGGLEDRVFRIRTERSSATSiPEPRTSHNI 109
Cdd:pfam00866   1 REARLLDDRDWDAWLALLAEDIHYWMPQREDRQRRDRDPQREESAIFDDDRAGLEDRVFRIRTGRAWAED-PPSRTRHLV 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739292236  110 SNVEVIER-RGDIVDVRFNWHTMYFRYK-TIDPYYGTSFYTIDFSGDSPLIRRKTVVLKNDYI 170
Cdd:pfam00866  80 SNVRVEETeADGELEVRSNFIVYRNRLErQVDSFAGRRTDVLRRSGDGFKIARRTILLDNSVI 142
PRK10069 PRK10069
3-phenylpropionate/cinnamic acid dioxygenase subunit beta;
3-167 2.14e-15

3-phenylpropionate/cinnamic acid dioxygenase subunit beta;


Pssm-ID: 236647  Cd Length: 183  Bit Score: 70.06  E-value: 2.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739292236   3 ATVDNTDSRQTAPSRLITQSSIEQFLYREARYLDDREFEKWLTCYADDVEYWMPC-----WDDNDLLTEDPQTDISLIYY 77
Cdd:PRK10069   1 ATGGAASRRQRAQVSLELHHEISQFLYREARLLDEWRYDDWLALLAEDIHYTMPMrttvnAQRRDRREGVQTPPTMAWFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739292236  78 ENKGGLEDRVFRIRTERSSATSiPEPRTSHNISNVEVIErrGDIVDVrFNWHTMYFRYKT-----IDPYYGTSFYTIDFS 152
Cdd:PRK10069  81 DNKDQLERRVARLETGMAWAEE-PPSRLRHLITNVRVEE--TDIPDE-FAVRSNFLLYRSrgerdEDFLVGRREDVLRRE 156

                        170
                 ....*....|....*
gi 739292236 153 GDSPLIRRKTVVLKN 167
Cdd:PRK10069 157 GDGWRLARRRIVLDQ 171
 
Name Accession Description Interval E-value
benzo_1_2_benB TIGR03232
benzoate 1,2-dioxygenase, small subunit; Benzoate 1,2-dioxygenase (EC 1.14.12.10) belongs to ...
 24-178 3.87e-92

benzoate 1,2-dioxygenase, small subunit; Benzoate 1,2-dioxygenase (EC 1.14.12.10) belongs to the larger family of aromatic ring-hydroxylating dioxygenases. Members of this family should all act on benzoate, but several have additional known activities on various benozate analogs. Some members actually may be named more suitably according to such alternate an activity, such as 2-chlorobenzoate 1,2-dioxygenase (1.14.12.13).


Pssm-ID: 132276  Cd Length: 155  Bit Score: 265.14  E-value: 3.87e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739292236   24 IEQFLYREARYLDDREFEKWLTCYADDVEYWMPCWDDNDLLTEDPQTDISLIYYENKGGLEDRVFRIRTERSSATsIPEP 103
Cdd:TIGR03232   1 IQAFLYREARLLDDEQWDDWLECYRADASFWMPAWDDDDQLTEDPQSEISLIYYPNRQGLEDRVFRIKTERSSAT-VPDT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739292236  104 RTSHNISNVEVIERRGDIVDVRFNWHTMYFRYKTIDPYYGTSFYTIDFSGDSPLIRRKTVVLKNDYIHHVVDIYH 178
Cdd:TIGR03232  80 RTSHNISNVEIEEQDGDVITVRFNWHTLSFRYKTTDSYFGMSRYTIDFSGESPKIKSKYVVLKNDYINQVIDIYH 154
ring_hydroxylating_dioxygenases_beta cd00667
Ring hydroxylating dioxygenase beta subunit. This subunit has a similar structure to NTF-2, ...
 20-178 3.99e-59

Ring hydroxylating dioxygenase beta subunit. This subunit has a similar structure to NTF-2, Ketosteroid isomerase and scytalone dehydratase.The degradation of aromatic compounds by aerobic bacteria frequently begins with the dihydroxylation of the substrate by nonheme iron-containing dioxygenases. These enzymes consist of two or three soluble proteins that interact to form an electron-transport chain that transfers electrons from reduced nucleotides (NADH) via flavin and [2Fe-2S] redox centers to a terminal dioxygenase. Aromatic-ring-hydroxylating dioxygenases oxidize aromatic hydrocarbons and related compounds to cis-arene diols. These enzymes utilize a mononuclear non-heme iron center to catalyze the addition of dioxygen to their respective substrates. The active site of these enzymes however is in the alpha sub-unit. No functional role has been attributed to the beta sub-unit except for a structural role.


Pssm-ID: 238357  Cd Length: 160  Bit Score: 181.69  E-value: 3.99e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739292236  20 TQSSIEQFLYREARYLDDREFEKWLTCYADDVEYWMPCWDDNDLLTEDPQTDISLIYYENKGGLEDRVFRIRTERSSATS 99
Cdd:cd00667    2 LQAEVEQFLYREARLLDDRRWDEWLALFAEDCHYWVPARENRERRDEDPGLELSAIYDDDRRMLEDRVVRLRTGRAWSED 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739292236 100 iPEPRTSHNISNVEVIERRGDIVDVRFNWHTMYFRYK-TIDPYYGTSFYTIDFSGDSPLIRRKTVVLKNDYIHHVVDIYH 178
Cdd:cd00667   82 -PPSRTRHLVSNVRVLEGDGGEIEVRSNFVVVRTRLDgESDVFAGGRYDDLRRSEDGLRIASRRVVLDNDRIPTVNLSPF 160
HcaF COG5517
3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites ...
 14-179 1.19e-54

3-phenylpropionate/cinnamic acid dioxygenase, small subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 444268  Cd Length: 162  Bit Score: 170.41  E-value: 1.19e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739292236  14 APSRLITQSSIEQFLYREARYLDDREFEKWLTCYADDVEYWMPCWDDNDlltEDPQTDISLIyYENKGGLEDRVFRIRTE 93
Cdd:COG5517    1 AAVDLELRAEVEQFLYREARLLDERRFDEWLALFTEDGHYWVPARENRD---TDPGLPLSLI-YDDRAMLEDRVARLRTG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739292236  94 RSSAtSIPEPRTSHNISNVEVIERRGDIVDVRFNWHTMYFRYKTIDPYY-GTSFYTIDFSGDSPLIRRKTVVLKNDYIHH 172
Cdd:COG5517   77 NAWA-EDPPSRTRHLVSNVRVEETDGGEIEVRSNFLVYRTRRDGQTDLFvGRYEDRLRRTGGGLRIARRRVVLDNSVIPT 155


                 ....*..
gi 739292236 173 VVDIYHF 179
Cdd:COG5517  156 KNLSYPL 162
Ring_hydroxyl_B pfam00866
Ring hydroxylating beta subunit; This subunit has a similar structure to NTF-2 and scytalone ...
 30-170 8.56e-52

Ring hydroxylating beta subunit; This subunit has a similar structure to NTF-2 and scytalone dehydratase.


Pssm-ID: 425916  Cd Length: 144  Bit Score: 162.46  E-value: 8.56e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739292236   30 REARYLDDREFEKWLTCYADDVEYWMPCWDDNDLLTEDPQTDISLIYYENKGGLEDRVFRIRTERSSATSiPEPRTSHNI 109
Cdd:pfam00866   1 REARLLDDRDWDAWLALLAEDIHYWMPQREDRQRRDRDPQREESAIFDDDRAGLEDRVFRIRTGRAWAED-PPSRTRHLV 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739292236  110 SNVEVIER-RGDIVDVRFNWHTMYFRYK-TIDPYYGTSFYTIDFSGDSPLIRRKTVVLKNDYI 170
Cdd:pfam00866  80 SNVRVEETeADGELEVRSNFIVYRNRLErQVDSFAGRRTDVLRRSGDGFKIARRTILLDNSVI 142
anthran_1_2_B TIGR03231
anthranilate 1,2-dioxygenase, small subunit; Anthranilate (2-aminobenzoate) is an intermediate ...
 24-178 2.40e-48

anthranilate 1,2-dioxygenase, small subunit; Anthranilate (2-aminobenzoate) is an intermediate of tryptophan (Trp) biosynthesis and degradation. Members of this family are the small subunit of anthranilate 1,2-dioxygenase, which acts in Trp degradation by converting anthranilate to catechol. Closely related paralogs typically are the benzoate 1,2-dioxygenase small subunit, among the larger set of ring-hydroxylating dioxygenases. [Energy metabolism, Amino acids and amines]


Pssm-ID: 132275  Cd Length: 155  Bit Score: 154.29  E-value: 2.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739292236   24 IEQFLYREARYLDDREFEKWLTCYADDVEYWMPCWDDNDLLTEDPQTDISLIYYENKGGLEDRVFRIRTERSsATSIPEP 103
Cdd:TIGR03231   1 VEQFLYRKAELCDAQDWDAYLDLFDEDSEFHLPQWISEHNYTRDPKRELSLIYYEDRSGLEDRVFRIRTGKA-ASTTPMP 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739292236  104 RTSHNISNVEVIERRGDIVDVRFNWHTMYFRYKTIDPYYGTSFYTIDFSGDSPLIRRKTVVLKNDYIHHVVDIYH 178
Cdd:TIGR03231  80 RTLHNIHNVRIAELEDGLLRVRVNWRTLFNRLGLEGCFYGHATYVLKPTGDSWLIRRKHSVLLNDKIDSVLDFYH 154
NTF2_like cd00531
Nuclear transport factor 2 (NTF2-like) superfamily. This family includes members of the NTF2 ...
 24-165 2.28e-18

Nuclear transport factor 2 (NTF2-like) superfamily. This family includes members of the NTF2 family, Delta-5-3-ketosteroid isomerases, Scytalone Dehydratases, and the beta subunit of Ring hydroxylating dioxygenases. This family is a classic example of divergent evolution wherein the proteins have many common structural details but diverge greatly in their function. For example, nuclear transport factor 2 (NTF2) mediates the nuclear import of RanGDP and binds to both RanGDP and FxFG repeat-containing nucleoporins while Ketosteroid isomerases catalyze the isomerization of delta-5-3-ketosteroid to delta-4-3-ketosteroid, by intramolecular transfer of the C4-beta proton to the C6-beta position. While the function of the beta sub-unit of the Ring hydroxylating dioxygenases is not known, Scytalone Dehydratases catalyzes two reactions in the biosynthetic pathway that produces fungal melanin. Members of the NTF2-like superfamily are widely distributed among bacteria, archaea and eukaryotes.


Pssm-ID: 238296 [Multi-domain]  Cd Length: 124  Bit Score: 76.40  E-value: 2.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739292236  24 IEQFLYREARYLDDReFEKWLTCYADDVEYWMPCWDDndlltedpqtdiSLIYYEN-KGGLEDRVFRIRTERssatsipe 102
Cdd:cd00531    1 AEQFLYRYARLLDAG-DREWLALLYADDAYFEPPGGD------------GLIYPDDgREAIEDRVRRLPFGP-------- 59

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739292236 103 PRTSHNISNVEVIERRGDIVDVRFNWHTMYFRYKTI-DPYYGTSFYTIDFSGDSPLIRRKTVVL 165
Cdd:cd00531   60 SRTRHLVSNVDVQPGDDGEGVVVSVFGVLRTRGDGEqDVFAGGQTFVLRPQGGGGKIANRRFRL 123
PRK10069 PRK10069
3-phenylpropionate/cinnamic acid dioxygenase subunit beta;
3-167 2.14e-15

3-phenylpropionate/cinnamic acid dioxygenase subunit beta;


Pssm-ID: 236647  Cd Length: 183  Bit Score: 70.06  E-value: 2.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739292236   3 ATVDNTDSRQTAPSRLITQSSIEQFLYREARYLDDREFEKWLTCYADDVEYWMPC-----WDDNDLLTEDPQTDISLIYY 77
Cdd:PRK10069   1 ATGGAASRRQRAQVSLELHHEISQFLYREARLLDEWRYDDWLALLAEDIHYTMPMrttvnAQRRDRREGVQTPPTMAWFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739292236  78 ENKGGLEDRVFRIRTERSSATSiPEPRTSHNISNVEVIErrGDIVDVrFNWHTMYFRYKT-----IDPYYGTSFYTIDFS 152
Cdd:PRK10069  81 DNKDQLERRVARLETGMAWAEE-PPSRLRHLITNVRVEE--TDIPDE-FAVRSNFLLYRSrgerdEDFLVGRREDVLRRE 156

                        170
                 ....*....|....*
gi 739292236 153 GDSPLIRRKTVVLKN 167
Cdd:PRK10069 157 GDGWRLARRRIVLDQ 171
 
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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