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Conserved domains on  [gi|336019405|gb|EGN49130|]
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hypothetical protein HMPREF0990_00025 [Lachnospiraceae bacterium 1_1_57FAA]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CYK3 COG5279
Cytokinesis protein 3, contains TGc (transglutaminase/protease-like) domain [Cell cycle ...
 81-212 1.04e-34

Cytokinesis protein 3, contains TGc (transglutaminase/protease-like) domain [Cell cycle control, cell division, chromosome partitioning];


:

Pssm-ID: 444090 [Multi-domain]  Cd Length: 250  Bit Score: 131.29  E-value: 1.04e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019405  81 QAQEIKTFVDDQIVKGETEDYKKARLIYDWITKNVRYAGSNDTDIGL---APYDVFTKKVAVCGGYSNLYKAMLNAAGIP 157
Cdd:COG5279   82 ATIADESKDDDYIITPGMSDYEKVRAIHDWIVDNIEYDYEAYNSGKSdshSAYGALKNGKGVCEGYAKLFKLLCNKAGIE 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 336019405 158 AIYVIGWAGGQ-----GHAWNLVYADGKWFYSDTTWGVSNPN--------YYFAPDVKDFSGSHKTQD 212
Cdd:COG5279  162 CYIVTGYARGSggesgNHAWNAVKIDGKWYLVDATWDDGVPDngggdvnyDYFLLSDEEFAKDHLPED 229
LRR_5 super family cl37855
BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich ...
 340-458 2.75e-10

BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis.


The actual alignment was detected with superfamily member pfam13306:

Pssm-ID: 463839 [Multi-domain]  Cd Length: 127  Bit Score: 57.94  E-value: 2.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019405  340 EKETFVCEKLKDIHVEEGNSKYSSY--DGCIYNKEktllLTIPEaktevkvpGTVVLDNTTFNSrSNITKIELEEGITTV 417
Cdd:pfam13306   4 GSYAFYNCSLTSITIPSSLTSIGEYafSNCTSLKS----ITLPS--------SLTSIGSYAFYN-CSLTSITIPSSLTSI 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 336019405  418 MPYVFNYCTGIKELYLPDSLESIEADAFNGVNLKQVTVYGN 458
Cdd:pfam13306  71 GEYAFSNCSNLKSITLPSNLTSIGSYAFSNCSLKSITIPSS 111
Dockerin_I cd14256
Type I dockerin repeat domain; Bacterial cohesin domains bind to a complementary protein ...
 483-538 1.10e-08

Type I dockerin repeat domain; Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.


:

Pssm-ID: 271215 [Multi-domain]  Cd Length: 57  Bit Score: 51.39  E-value: 1.10e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 336019405 483 KGDVDLDGNVAIGDVRVVLRSICQKIELNEMQELAADVEKDDKVDIKDLRKILRYV 538
Cdd:cd14256    1 YGDVNGDGKVNSADAALLKKYLLGKITLTEAQLKAADVNGDGKVNAIDLALLKKYL 56
 
Name Accession Description Interval E-value
CYK3 COG5279
Cytokinesis protein 3, contains TGc (transglutaminase/protease-like) domain [Cell cycle ...
 81-212 1.04e-34

Cytokinesis protein 3, contains TGc (transglutaminase/protease-like) domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444090 [Multi-domain]  Cd Length: 250  Bit Score: 131.29  E-value: 1.04e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019405  81 QAQEIKTFVDDQIVKGETEDYKKARLIYDWITKNVRYAGSNDTDIGL---APYDVFTKKVAVCGGYSNLYKAMLNAAGIP 157
Cdd:COG5279   82 ATIADESKDDDYIITPGMSDYEKVRAIHDWIVDNIEYDYEAYNSGKSdshSAYGALKNGKGVCEGYAKLFKLLCNKAGIE 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 336019405 158 AIYVIGWAGGQ-----GHAWNLVYADGKWFYSDTTWGVSNPN--------YYFAPDVKDFSGSHKTQD 212
Cdd:COG5279  162 CYIVTGYARGSggesgNHAWNAVKIDGKWYLVDATWDDGVPDngggdvnyDYFLLSDEEFAKDHLPED 229
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 91-185 2.80e-22

Transglutaminase-like superfamily; This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterized transglutaminase, the human blood clotting factor XIIIa'. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase, it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease.


Pssm-ID: 376628 [Multi-domain]  Cd Length: 108  Bit Score: 91.70  E-value: 2.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019405   91 DQIVKGETEDYKKARLIYDWITKNVRYAGSNDTDIGLAPYDVFTKKVAVCGGYSNLYKAMLNAAGIPAIYVIGWAGGQG- 169
Cdd:pfam01841   5 DRITGGATDPLEKARAIYDYVRKNITYDLPGRSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGIPARYVTGYLRGPDt 84

                          90       100
                  ....*....|....*....|...
gi 336019405  170 ------HAWNLVY-ADGKWFYSD 185
Cdd:pfam01841  85 vrggdaHAWVEVYlPGYGWVPVD 107
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 132-188 4.09e-13

Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish covalent links between proteins. A subset of transglutaminase homologues appear to catalyse the reverse reaction, the hydrolysis of peptide bonds. Proteins with this domain are both extracellular and intracellular, and it is likely that the eukaryotic intracellular proteins are involved in signalling events.


Pssm-ID: 214673  Cd Length: 68  Bit Score: 64.33  E-value: 4.09e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 336019405   132 VFTKKVAVCGGYSNLYKAMLNAAGIPAIYVIGWAGGQG-----------HAWNLVYADGKWFYSDTTW 188
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDtigglrsiweaHAWAEVYLEGGWVPVDPTP 68
LRR_5 pfam13306
BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich ...
 340-458 2.75e-10

BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis.


Pssm-ID: 463839 [Multi-domain]  Cd Length: 127  Bit Score: 57.94  E-value: 2.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019405  340 EKETFVCEKLKDIHVEEGNSKYSSY--DGCIYNKEktllLTIPEaktevkvpGTVVLDNTTFNSrSNITKIELEEGITTV 417
Cdd:pfam13306   4 GSYAFYNCSLTSITIPSSLTSIGEYafSNCTSLKS----ITLPS--------SLTSIGSYAFYN-CSLTSITIPSSLTSI 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 336019405  418 MPYVFNYCTGIKELYLPDSLESIEADAFNGVNLKQVTVYGN 458
Cdd:pfam13306  71 GEYAFSNCSNLKSITLPSNLTSIGSYAFSNCSLKSITIPSS 111
Dockerin_I cd14256
Type I dockerin repeat domain; Bacterial cohesin domains bind to a complementary protein ...
 483-538 1.10e-08

Type I dockerin repeat domain; Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.


Pssm-ID: 271215 [Multi-domain]  Cd Length: 57  Bit Score: 51.39  E-value: 1.10e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 336019405 483 KGDVDLDGNVAIGDVRVVLRSICQKIELNEMQELAADVEKDDKVDIKDLRKILRYV 538
Cdd:cd14256    1 YGDVNGDGKVNSADAALLKKYLLGKITLTEAQLKAADVNGDGKVNAIDLALLKKYL 56
Dockerin_1 pfam00404
Dockerin type I domain; The dockerin repeat is the binding partner of the cohesin domain ...
 484-538 2.03e-04

Dockerin type I domain; The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium. This family contains two copies of the repeat.


Pssm-ID: 459805 [Multi-domain]  Cd Length: 56  Bit Score: 39.47  E-value: 2.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 336019405  484 GDVDLDGNVAIGDVRVVLRSICQKIELNEMQELAADVEKDDKVDIKDLRKILRYV 538
Cdd:pfam00404   1 GDVNGDGKVNALDALLLKNYLLGSGTGSSINKKAADVNGDGKVNALDALLLKNYL 55
 
Name Accession Description Interval E-value
CYK3 COG5279
Cytokinesis protein 3, contains TGc (transglutaminase/protease-like) domain [Cell cycle ...
 81-212 1.04e-34

Cytokinesis protein 3, contains TGc (transglutaminase/protease-like) domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444090 [Multi-domain]  Cd Length: 250  Bit Score: 131.29  E-value: 1.04e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019405  81 QAQEIKTFVDDQIVKGETEDYKKARLIYDWITKNVRYAGSNDTDIGL---APYDVFTKKVAVCGGYSNLYKAMLNAAGIP 157
Cdd:COG5279   82 ATIADESKDDDYIITPGMSDYEKVRAIHDWIVDNIEYDYEAYNSGKSdshSAYGALKNGKGVCEGYAKLFKLLCNKAGIE 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 336019405 158 AIYVIGWAGGQ-----GHAWNLVYADGKWFYSDTTWGVSNPN--------YYFAPDVKDFSGSHKTQD 212
Cdd:COG5279  162 CYIVTGYARGSggesgNHAWNAVKIDGKWYLVDATWDDGVPDngggdvnyDYFLLSDEEFAKDHLPED 229
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 91-185 2.80e-22

Transglutaminase-like superfamily; This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterized transglutaminase, the human blood clotting factor XIIIa'. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase, it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease.


Pssm-ID: 376628 [Multi-domain]  Cd Length: 108  Bit Score: 91.70  E-value: 2.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019405   91 DQIVKGETEDYKKARLIYDWITKNVRYAGSNDTDIGLAPYDVFTKKVAVCGGYSNLYKAMLNAAGIPAIYVIGWAGGQG- 169
Cdd:pfam01841   5 DRITGGATDPLEKARAIYDYVRKNITYDLPGRSPGDGDAEEFLFTGKGDCEDFASLFVALLRALGIPARYVTGYLRGPDt 84

                          90       100
                  ....*....|....*....|...
gi 336019405  170 ------HAWNLVY-ADGKWFYSD 185
Cdd:pfam01841  85 vrggdaHAWVEVYlPGYGWVPVD 107
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 84-187 9.43e-21

Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 89.68  E-value: 9.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019405  84 EIKTFVDdQIVKGETEDYKKARLIYDWITKNVRYaGSNDTDIGLAPYDVFTKKVAVCGGYSNLYKAMLNAAGIPAIYVIG 163
Cdd:COG1305   62 ELRALAA-ELTGGATTPYEKARALYDWVRDNIRY-DPGSTGVGTTALETLERRRGVCRDFAHLLVALLRALGIPARYVSG 139

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 336019405 164 WAGGQG----------HAWNLVYADGK-WFYSDTT 187
Cdd:COG1305  140 YLPGEPppgggraddaHAWVEVYLPGAgWVPFDPT 174
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 132-188 4.09e-13

Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish covalent links between proteins. A subset of transglutaminase homologues appear to catalyse the reverse reaction, the hydrolysis of peptide bonds. Proteins with this domain are both extracellular and intracellular, and it is likely that the eukaryotic intracellular proteins are involved in signalling events.


Pssm-ID: 214673  Cd Length: 68  Bit Score: 64.33  E-value: 4.09e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 336019405   132 VFTKKVAVCGGYSNLYKAMLNAAGIPAIYVIGWAGGQG-----------HAWNLVYADGKWFYSDTTW 188
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDtigglrsiweaHAWAEVYLEGGWVPVDPTP 68
LRR_5 pfam13306
BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich ...
 340-458 2.75e-10

BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis.


Pssm-ID: 463839 [Multi-domain]  Cd Length: 127  Bit Score: 57.94  E-value: 2.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019405  340 EKETFVCEKLKDIHVEEGNSKYSSY--DGCIYNKEktllLTIPEaktevkvpGTVVLDNTTFNSrSNITKIELEEGITTV 417
Cdd:pfam13306   4 GSYAFYNCSLTSITIPSSLTSIGEYafSNCTSLKS----ITLPS--------SLTSIGSYAFYN-CSLTSITIPSSLTSI 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 336019405  418 MPYVFNYCTGIKELYLPDSLESIEADAFNGVNLKQVTVYGN 458
Cdd:pfam13306  71 GEYAFSNCSNLKSITLPSNLTSIGSYAFSNCSLKSITIPSS 111
Dockerin_I cd14256
Type I dockerin repeat domain; Bacterial cohesin domains bind to a complementary protein ...
 483-538 1.10e-08

Type I dockerin repeat domain; Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.


Pssm-ID: 271215 [Multi-domain]  Cd Length: 57  Bit Score: 51.39  E-value: 1.10e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 336019405 483 KGDVDLDGNVAIGDVRVVLRSICQKIELNEMQELAADVEKDDKVDIKDLRKILRYV 538
Cdd:cd14256    1 YGDVNGDGKVNSADAALLKKYLLGKITLTEAQLKAADVNGDGKVNAIDLALLKKYL 56
LRR_5 pfam13306
BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich ...
 327-451 1.14e-07

BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis.


Pssm-ID: 463839 [Multi-domain]  Cd Length: 127  Bit Score: 50.62  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336019405  327 ESFTLPKETEKYDEkETFV-CEKLKDIHVEEGNSKYSSY--DGCIYNKektllLTIPEAKTEvkvpgtvvLDNTTFNSRS 403
Cdd:pfam13306  14 TSITIPSSLTSIGE-YAFSnCTSLKSITLPSSLTSIGSYafYNCSLTS-----ITIPSSLTS--------IGEYAFSNCS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 336019405  404 NITKIELEEGITTVMPYVFNYCtGIKELYLPDSLESIEADAFNG-VNLK 451
Cdd:pfam13306  80 NLKSITLPSNLTSIGSYAFSNC-SLKSITIPSSVTTIGSYAFSNcSNLK 127
Dockerin cd14253
Dockerin repeat domain; Dockerins are modules in the cellulosome complex that often anchor ...
 484-537 6.01e-05

Dockerin repeat domain; Dockerins are modules in the cellulosome complex that often anchor catalytic subunits by binding to cohesin domains of scaffolding proteins. Three types of dockerins and their corresponding cohesin have been described in the literature. This alignment models two consecutive dockerin repeats, the functional unit.


Pssm-ID: 271212  Cd Length: 56  Bit Score: 40.87  E-value: 6.01e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 336019405 484 GDVDLDGNVAIGDVRVVLRSICQKIELNEMQELAADVEKDDKVDIKDLRKILRY 537
Cdd:cd14253    1 GDVNGDGTVDITDATAVKRYVAATITPDDDSKARGDVNGDGGINAIDAMIIAKY 54
Dockerin_1 pfam00404
Dockerin type I domain; The dockerin repeat is the binding partner of the cohesin domain ...
 484-538 2.03e-04

Dockerin type I domain; The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium. This family contains two copies of the repeat.


Pssm-ID: 459805 [Multi-domain]  Cd Length: 56  Bit Score: 39.47  E-value: 2.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 336019405  484 GDVDLDGNVAIGDVRVVLRSICQKIELNEMQELAADVEKDDKVDIKDLRKILRYV 538
Cdd:pfam00404   1 GDVNGDGKVNALDALLLKNYLLGSGTGSSINKKAADVNGDGKVNALDALLLKNYL 55
Gln_amidase pfam15644
Papain fold toxin 1, glutamine deamidase; A papain fold toxin domain found in bacterial ...
 140-185 2.29e-03

Papain fold toxin 1, glutamine deamidase; A papain fold toxin domain found in bacterial polymorphic toxin systems. In these systems they might function either as a releasing peptidase or toxin. In Shigella flexneri, UniProtKB:Q8VSD5, this protein is expressed from a plasmid, and delivered into the host via the type III secretion system where it deamidates the glutamine residue at position 100 in ubiquitin-activating enzyme E2, UBC13, to a glutamic acid residue. Invasion of host cells by pathogens normally invokes an acute inflammatory response through activating the TRAF6-mediated signalling pathway. UBC13 helps to activate TRAF6. Thus deamidation of UBC13 results in the dampening of the inflammatory response. The key glutaminase deamidase activity is mediated by a cys-his-glu triad, present in all members of the family.


Pssm-ID: 434830 [Multi-domain]  Cd Length: 113  Bit Score: 37.80  E-value: 2.29e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 336019405  140 CGGYSNLYKAMLNAA-GIPAIYVIGWAGGQ--GHAWNLVYADGKWFYSD 185
Cdd:pfam15644  61 DGAYDDLAQALRAAGpGSYAVVIVRWPGGGggGHAWNAVNPNGAVVWLD 109
 
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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