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Conserved domains on  [gi|1532638322|gb|AZL41285|]
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isoprene monooxygenase hydroxylase alpha subunit, partial [Rhodococcus sp. WS1]

Protein Classification

aromatic/alkene/methane monooxygenase hydroxylase/oxygenase subunit alpha( domain architecture ID 10099411)

aromatic/alkene/methane monooxygenase (MO) hydroxylase/oxygenase subunit alpha is part of a multicomponent MO system such as toluene-4-MO that catalyzes the O2- and NADH-dependent hydroxylation of toluene to form p-cresol

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAMH_A cd01057
Aromatic and Alkene Monooxygenase Hydroxylase, subunit A, ferritin-like diiron-binding domain; ...
 12-478 0e+00

Aromatic and Alkene Monooxygenase Hydroxylase, subunit A, ferritin-like diiron-binding domain; Aromatic and Alkene Monooxygenase Hydroxylases, subunit A (AAMH_A). Subunit A of the soluble hydroxylase of multicomponent, aromatic and alkene monooxygenases are members of a superfamily of ferritin-like iron-storage proteins. AAMH exists as a hexamer (an alpha2-beta2-gamma2 homodimer) with each alpha-subunit housing one nonheme diiron center embedded in a four-helix bundle. The N-terminal domain of the alpha- and noncatalytic beta-subunits possess nearly identical folds, however, the beta-subunit lacks critical diiron ligands and a C-terminal domain found in the alpha-subunit. Methane monooxygenase is a multicomponent enzyme found in methanotrophic bacteria that catalyzes the hydroxylation of methane and higher alkenes (as large as octane). Phenol monooxygenase, found in a diverse group of bacteria, catalyses the hydroxylation of phenol, chloro- and methyl-phenol and naphthol. Both enzyme systems consist of three components: the hydroxylase, a coupling protein and a reductase. In the MMO hydroxylase, dioxygen and substrate interact with the diiron center in a hydrophobic cavity at the active site. The reductase component and protein coupling factor provide electrons from NADH for reducing the oxidized binuclear iron-oxo cluster to its reduced form. Reaction with dioxygen produces a peroxy-bridged complex and dehydration leads to the formation of complex Q, which is thought to be the oxygenating species that carries out the insertion of an oxygen atom into a C-H bond of the substrate. The toluene monooxygenase systems, toluene 2-, 3-, and 4-monooxygenase, are similar to MMO but with an additional component, a Rieske-type ferredoxin. The alkene monooxygenase from Xanthobacter strain Py2 is closely related to aromatic monooxygenases and catalyzes aromatic monohydroxylation of benzene, toluene, and phenol. Alkane omega-hydroxylase (AlkB) and xylene monooxygenase are members of a distinct class of integral membrane diiron proteins and are not included in this CD.


:

Pssm-ID: 153115 [Multi-domain]  Cd Length: 465  Bit Score: 602.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532638322  12 SRDLDWELSYVDPAVAFPTSWSGAGDVPKeaWDKWDEPFRVSYRDYVRIQREKESGVRAVSNALGRSGIFEKLDPAHVAA 91
Cdd:cd01057     1 TRDLDWDFSYVDEDDKFPTKYKMPIKIPD--WDKWKDPFKLTMREYVKMQAEKDKRVYGVLDAAVRSGAYEKVDPRWVEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532638322  92 SHLHMGTTCMVEHMAVTMQSRFCRFAPTPRWRNLGVFGMLDETRHTQLDLRFSHDLLKQDPRFDWAQKAFHTNEWgVLAV 171
Cdd:cd01057    79 MKLFLGAITPGEYAAVRGMAMLGRFAPAAELRNGYLMQMLDELRHTQIQLYLPHYYAKNYAGFDWAQKAFHGNWY-AGAA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532638322 172 KNFFDDAMLNADCVEAALATSLTVEHGFTNLQFVALAADAMAAGDINWSNLLSSIQTDEARHAQQGFPTLsILMEHDP-- 249
Cdd:cd01057   158 KRFFFDGFITGDAVEAALALQFVFETAFTNLLFVALASDAAANGDYATPTVFLSIQSDEARHMANGYPTL-VLLENDPdn 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532638322 250 -ARAQKALDIAFWRSTRLFQTLTGPAMDYYTPldQRKMSFKEFMLEWIVNHHERILED---YGLKKPWYWDQFMYSLENG 325
Cdd:cd01057   237 vPLLQRDLDKAFWRQHRLFDALVGMLMDYGTP--KRVMSWKEFWEEWIEEDFGSYFKDlekYGLKKPWYWDDAKKEKDWY 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532638322 326 HHAMHLGTWFWRPTLFWKPNAgVSKDEREWLREKYPTWEENWGGMWDEIIKNVNDDRIENTLPDTLPALCNLTQLPLGSA 405
Cdd:cd01057   315 HHQLALGFYAWWPTNFWRPDA-PTPEEMEWFEEKYPGWYKYYGKFWEEIRKNAAEGKRELFYPETLPPLCNVCQVPCVFT 393

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1532638322 406 FARHDLADHSLTYKGRLYHFDSEISKWCFEQDPDRYAGHQNFIDRFIDGQVLPADLAGGLLYMGlTPDVMGDD 478
Cdd:cd01057   394 EDLTAEAPRVLEYNGRKYHFCSEGCEWIFEQEPERYAGHWNPVDRFLGGELADVILELGLLRSD-GKTLIGQP 465
 
Name Accession Description Interval E-value
AAMH_A cd01057
Aromatic and Alkene Monooxygenase Hydroxylase, subunit A, ferritin-like diiron-binding domain; ...
 12-478 0e+00

Aromatic and Alkene Monooxygenase Hydroxylase, subunit A, ferritin-like diiron-binding domain; Aromatic and Alkene Monooxygenase Hydroxylases, subunit A (AAMH_A). Subunit A of the soluble hydroxylase of multicomponent, aromatic and alkene monooxygenases are members of a superfamily of ferritin-like iron-storage proteins. AAMH exists as a hexamer (an alpha2-beta2-gamma2 homodimer) with each alpha-subunit housing one nonheme diiron center embedded in a four-helix bundle. The N-terminal domain of the alpha- and noncatalytic beta-subunits possess nearly identical folds, however, the beta-subunit lacks critical diiron ligands and a C-terminal domain found in the alpha-subunit. Methane monooxygenase is a multicomponent enzyme found in methanotrophic bacteria that catalyzes the hydroxylation of methane and higher alkenes (as large as octane). Phenol monooxygenase, found in a diverse group of bacteria, catalyses the hydroxylation of phenol, chloro- and methyl-phenol and naphthol. Both enzyme systems consist of three components: the hydroxylase, a coupling protein and a reductase. In the MMO hydroxylase, dioxygen and substrate interact with the diiron center in a hydrophobic cavity at the active site. The reductase component and protein coupling factor provide electrons from NADH for reducing the oxidized binuclear iron-oxo cluster to its reduced form. Reaction with dioxygen produces a peroxy-bridged complex and dehydration leads to the formation of complex Q, which is thought to be the oxygenating species that carries out the insertion of an oxygen atom into a C-H bond of the substrate. The toluene monooxygenase systems, toluene 2-, 3-, and 4-monooxygenase, are similar to MMO but with an additional component, a Rieske-type ferredoxin. The alkene monooxygenase from Xanthobacter strain Py2 is closely related to aromatic monooxygenases and catalyzes aromatic monohydroxylation of benzene, toluene, and phenol. Alkane omega-hydroxylase (AlkB) and xylene monooxygenase are members of a distinct class of integral membrane diiron proteins and are not included in this CD.


Pssm-ID: 153115 [Multi-domain]  Cd Length: 465  Bit Score: 602.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532638322  12 SRDLDWELSYVDPAVAFPTSWSGAGDVPKeaWDKWDEPFRVSYRDYVRIQREKESGVRAVSNALGRSGIFEKLDPAHVAA 91
Cdd:cd01057     1 TRDLDWDFSYVDEDDKFPTKYKMPIKIPD--WDKWKDPFKLTMREYVKMQAEKDKRVYGVLDAAVRSGAYEKVDPRWVEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532638322  92 SHLHMGTTCMVEHMAVTMQSRFCRFAPTPRWRNLGVFGMLDETRHTQLDLRFSHDLLKQDPRFDWAQKAFHTNEWgVLAV 171
Cdd:cd01057    79 MKLFLGAITPGEYAAVRGMAMLGRFAPAAELRNGYLMQMLDELRHTQIQLYLPHYYAKNYAGFDWAQKAFHGNWY-AGAA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532638322 172 KNFFDDAMLNADCVEAALATSLTVEHGFTNLQFVALAADAMAAGDINWSNLLSSIQTDEARHAQQGFPTLsILMEHDP-- 249
Cdd:cd01057   158 KRFFFDGFITGDAVEAALALQFVFETAFTNLLFVALASDAAANGDYATPTVFLSIQSDEARHMANGYPTL-VLLENDPdn 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532638322 250 -ARAQKALDIAFWRSTRLFQTLTGPAMDYYTPldQRKMSFKEFMLEWIVNHHERILED---YGLKKPWYWDQFMYSLENG 325
Cdd:cd01057   237 vPLLQRDLDKAFWRQHRLFDALVGMLMDYGTP--KRVMSWKEFWEEWIEEDFGSYFKDlekYGLKKPWYWDDAKKEKDWY 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532638322 326 HHAMHLGTWFWRPTLFWKPNAgVSKDEREWLREKYPTWEENWGGMWDEIIKNVNDDRIENTLPDTLPALCNLTQLPLGSA 405
Cdd:cd01057   315 HHQLALGFYAWWPTNFWRPDA-PTPEEMEWFEEKYPGWYKYYGKFWEEIRKNAAEGKRELFYPETLPPLCNVCQVPCVFT 393

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1532638322 406 FARHDLADHSLTYKGRLYHFDSEISKWCFEQDPDRYAGHQNFIDRFIDGQVLPADLAGGLLYMGlTPDVMGDD 478
Cdd:cd01057   394 EDLTAEAPRVLEYNGRKYHFCSEGCEWIFEQEPERYAGHWNPVDRFLGGELADVILELGLLRSD-GKTLIGQP 465
Phenol_Hydrox pfam02332
Methane/Phenol/Toluene Hydroxylase; Bacterial phenol hydroxylase is a multicomponent enzyme ...
 17-248 7.07e-63

Methane/Phenol/Toluene Hydroxylase; Bacterial phenol hydroxylase is a multicomponent enzyme that catabolizes phenol and some of its methylated derivatives. This Pfam family contains both the P1 and P3 polypeptides of phenol hydroxylase and the alpha and beta chain of methane hydroxylase protein A.


Pssm-ID: 426724  Cd Length: 229  Bit Score: 204.79  E-value: 7.07e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532638322  17 WELSYVDPAVAFPTSwsgagDVPKEAWDKWDEPFRVSYRDYVRIQREKESGVRAVSNALGRSGIFEKLDPAHVAASHLHM 96
Cdd:pfam02332   1 WTPSYVDGDPSYPYT-----ALRMSDWYAFRDPDRLTYRTYVKMQAEKEERVYGVLDAAERSGLFARLDPAWREVLKLHL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532638322  97 GTTCMVEHMAVTMQSRFCRFAPTPRWRNLGVFGMLDETRHTQLDLRFSHDLLKQ-DPRFDWAQ-KAFHTNEWGVLAVKNF 174
Cdd:pfam02332  76 GPLRHLEYGAQMANAYLARYGPGTAIRNAATFQALDELRHAQIITYLGLELAKAyPGAFDGSLdKAAWLNDPAWQPLRRL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1532638322 175 FDDAMLNADCVEAALATSLTVEHGFTNLQFVALAADAMAAGDINWSNLLSSIQTDEARHAQQGFPTLSILMEHD 248
Cdd:pfam02332 156 VEDILVAYDWFEALVALNLVFEPLLTNLLFVAFMEVAAANGDFLTPTLISSAQSDEARHARWGDALLKFLLEDD 229
YHS COG3350
Heavy metal-bindng TRASH/YHS domain, predicted Cu/Ag metallochaperone [Inorganic ion transport ...
 412-446 2.70e-07

Heavy metal-bindng TRASH/YHS domain, predicted Cu/Ag metallochaperone [Inorganic ion transport and metabolism];


Pssm-ID: 442578  Cd Length: 56  Bit Score: 47.39  E-value: 2.70e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1532638322 412 ADHSLTYKGRLYHFDSEISKWCFEQDPDRYAGHQN 446
Cdd:COG3350    21 AAYTAEYDGKTYYFCSEECRDKFKANPEKYLPQYG 55
 
Name Accession Description Interval E-value
AAMH_A cd01057
Aromatic and Alkene Monooxygenase Hydroxylase, subunit A, ferritin-like diiron-binding domain; ...
 12-478 0e+00

Aromatic and Alkene Monooxygenase Hydroxylase, subunit A, ferritin-like diiron-binding domain; Aromatic and Alkene Monooxygenase Hydroxylases, subunit A (AAMH_A). Subunit A of the soluble hydroxylase of multicomponent, aromatic and alkene monooxygenases are members of a superfamily of ferritin-like iron-storage proteins. AAMH exists as a hexamer (an alpha2-beta2-gamma2 homodimer) with each alpha-subunit housing one nonheme diiron center embedded in a four-helix bundle. The N-terminal domain of the alpha- and noncatalytic beta-subunits possess nearly identical folds, however, the beta-subunit lacks critical diiron ligands and a C-terminal domain found in the alpha-subunit. Methane monooxygenase is a multicomponent enzyme found in methanotrophic bacteria that catalyzes the hydroxylation of methane and higher alkenes (as large as octane). Phenol monooxygenase, found in a diverse group of bacteria, catalyses the hydroxylation of phenol, chloro- and methyl-phenol and naphthol. Both enzyme systems consist of three components: the hydroxylase, a coupling protein and a reductase. In the MMO hydroxylase, dioxygen and substrate interact with the diiron center in a hydrophobic cavity at the active site. The reductase component and protein coupling factor provide electrons from NADH for reducing the oxidized binuclear iron-oxo cluster to its reduced form. Reaction with dioxygen produces a peroxy-bridged complex and dehydration leads to the formation of complex Q, which is thought to be the oxygenating species that carries out the insertion of an oxygen atom into a C-H bond of the substrate. The toluene monooxygenase systems, toluene 2-, 3-, and 4-monooxygenase, are similar to MMO but with an additional component, a Rieske-type ferredoxin. The alkene monooxygenase from Xanthobacter strain Py2 is closely related to aromatic monooxygenases and catalyzes aromatic monohydroxylation of benzene, toluene, and phenol. Alkane omega-hydroxylase (AlkB) and xylene monooxygenase are members of a distinct class of integral membrane diiron proteins and are not included in this CD.


Pssm-ID: 153115 [Multi-domain]  Cd Length: 465  Bit Score: 602.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532638322  12 SRDLDWELSYVDPAVAFPTSWSGAGDVPKeaWDKWDEPFRVSYRDYVRIQREKESGVRAVSNALGRSGIFEKLDPAHVAA 91
Cdd:cd01057     1 TRDLDWDFSYVDEDDKFPTKYKMPIKIPD--WDKWKDPFKLTMREYVKMQAEKDKRVYGVLDAAVRSGAYEKVDPRWVEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532638322  92 SHLHMGTTCMVEHMAVTMQSRFCRFAPTPRWRNLGVFGMLDETRHTQLDLRFSHDLLKQDPRFDWAQKAFHTNEWgVLAV 171
Cdd:cd01057    79 MKLFLGAITPGEYAAVRGMAMLGRFAPAAELRNGYLMQMLDELRHTQIQLYLPHYYAKNYAGFDWAQKAFHGNWY-AGAA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532638322 172 KNFFDDAMLNADCVEAALATSLTVEHGFTNLQFVALAADAMAAGDINWSNLLSSIQTDEARHAQQGFPTLsILMEHDP-- 249
Cdd:cd01057   158 KRFFFDGFITGDAVEAALALQFVFETAFTNLLFVALASDAAANGDYATPTVFLSIQSDEARHMANGYPTL-VLLENDPdn 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532638322 250 -ARAQKALDIAFWRSTRLFQTLTGPAMDYYTPldQRKMSFKEFMLEWIVNHHERILED---YGLKKPWYWDQFMYSLENG 325
Cdd:cd01057   237 vPLLQRDLDKAFWRQHRLFDALVGMLMDYGTP--KRVMSWKEFWEEWIEEDFGSYFKDlekYGLKKPWYWDDAKKEKDWY 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532638322 326 HHAMHLGTWFWRPTLFWKPNAgVSKDEREWLREKYPTWEENWGGMWDEIIKNVNDDRIENTLPDTLPALCNLTQLPLGSA 405
Cdd:cd01057   315 HHQLALGFYAWWPTNFWRPDA-PTPEEMEWFEEKYPGWYKYYGKFWEEIRKNAAEGKRELFYPETLPPLCNVCQVPCVFT 393

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1532638322 406 FARHDLADHSLTYKGRLYHFDSEISKWCFEQDPDRYAGHQNFIDRFIDGQVLPADLAGGLLYMGlTPDVMGDD 478
Cdd:cd01057   394 EDLTAEAPRVLEYNGRKYHFCSEGCEWIFEQEPERYAGHWNPVDRFLGGELADVILELGLLRSD-GKTLIGQP 465
Phenol_Hydrox pfam02332
Methane/Phenol/Toluene Hydroxylase; Bacterial phenol hydroxylase is a multicomponent enzyme ...
 17-248 7.07e-63

Methane/Phenol/Toluene Hydroxylase; Bacterial phenol hydroxylase is a multicomponent enzyme that catabolizes phenol and some of its methylated derivatives. This Pfam family contains both the P1 and P3 polypeptides of phenol hydroxylase and the alpha and beta chain of methane hydroxylase protein A.


Pssm-ID: 426724  Cd Length: 229  Bit Score: 204.79  E-value: 7.07e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532638322  17 WELSYVDPAVAFPTSwsgagDVPKEAWDKWDEPFRVSYRDYVRIQREKESGVRAVSNALGRSGIFEKLDPAHVAASHLHM 96
Cdd:pfam02332   1 WTPSYVDGDPSYPYT-----ALRMSDWYAFRDPDRLTYRTYVKMQAEKEERVYGVLDAAERSGLFARLDPAWREVLKLHL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1532638322  97 GTTCMVEHMAVTMQSRFCRFAPTPRWRNLGVFGMLDETRHTQLDLRFSHDLLKQ-DPRFDWAQ-KAFHTNEWGVLAVKNF 174
Cdd:pfam02332  76 GPLRHLEYGAQMANAYLARYGPGTAIRNAATFQALDELRHAQIITYLGLELAKAyPGAFDGSLdKAAWLNDPAWQPLRRL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1532638322 175 FDDAMLNADCVEAALATSLTVEHGFTNLQFVALAADAMAAGDINWSNLLSSIQTDEARHAQQGFPTLSILMEHD 248
Cdd:pfam02332 156 VEDILVAYDWFEALVALNLVFEPLLTNLLFVAFMEVAAANGDFLTPTLISSAQSDEARHARWGDALLKFLLEDD 229
YHS pfam04945
YHS domain; This short presumed domain is about 50 amino acid residues long. It often contains ...
 412-444 3.33e-08

YHS domain; This short presumed domain is about 50 amino acid residues long. It often contains two cysteines that may be functionally important. This domain is found in copper transporting ATPases, some phenol hydroxylases and in a set of uncharacterized membrane proteins including Swiss:Q9CNI0. This domain is named after three of the most conserved amino acids it contains. The domain may be metal binding, possibly copper ions. This domain is duplicated in some copper transporting ATPases.


Pssm-ID: 461496 [Multi-domain]  Cd Length: 46  Bit Score: 49.67  E-value: 3.33e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1532638322 412 ADHSLTYKGRLYHFDSEISKWCFEQDPDRYAGH 444
Cdd:pfam04945  13 AQYKSEYKGKEYYFCSEGCLDIFDDDPEKYAGQ 45
YHS COG3350
Heavy metal-bindng TRASH/YHS domain, predicted Cu/Ag metallochaperone [Inorganic ion transport ...
 412-446 2.70e-07

Heavy metal-bindng TRASH/YHS domain, predicted Cu/Ag metallochaperone [Inorganic ion transport and metabolism];


Pssm-ID: 442578  Cd Length: 56  Bit Score: 47.39  E-value: 2.70e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1532638322 412 ADHSLTYKGRLYHFDSEISKWCFEQDPDRYAGHQN 446
Cdd:COG3350    21 AAYTAEYDGKTYYFCSEECRDKFKANPEKYLPQYG 55
 
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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