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Conserved domains on  [gi|486159208|ref|WP_001522863|]
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MULTISPECIES: flagellar assembly peptidoglycan hydrolase FlgJ [Enterobacteriaceae]

Protein Classification

flagellar assembly peptidoglycan hydrolase FlgJ( domain architecture ID 11481497)

flagellar assembly peptidoglycan hydrolase FlgJ acts as a flagellum-specific muramidase which hydrolyzes the peptidoglycan layer to assemble the rod structure in the periplasmic space

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
flgJ PRK05684
flagellar assembly peptidoglycan hydrolase FlgJ;
2-309 0e+00

flagellar assembly peptidoglycan hydrolase FlgJ;


:

Pssm-ID: 235559 [Multi-domain]  Cd Length: 312  Bit Score: 510.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208   2 ISDSKLLASAAWDAQSLNELKAKTGEDPAANIRPVALQVEGMFVQMMLKSMRDALPKDGLFSSEHTRLYTSMYDQQIAQQ 81
Cdd:PRK05684   1 MSDSLSDSGAAYDLQSLNSLKAKAGKDPKANLRAVAQQFEGMFVQMMLKSMRDANPKDGLMNSQQTKLYTSMYDQQIAQQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208  82 MTAGKGLGLAEMMVKQMTPEQ-PLPEESTPAAPMKFPLETVVRYQNQTLSQLVQKAV---PRNYDDSLPGDSKAFLAQLS 157
Cdd:PRK05684  81 LSAGGGLGLADMMVKQLSPEQsPAPEESAGAVPMKFDLETVQSYQNQALAQLVRKAIpqpPLASDKPLFGSSDDFVARLS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 158 LPAQLASQQSGVPHHLILAQAALESGWGQRQIRRENGEPSYNLFGVKASGNWKGPVTEITTTEYENGEAKKVKAKFRVYS 237
Cdd:PRK05684 161 PPAQKAAQQSGVPHHLLLAQAALESGWGQREIRTADGSPSHNLFGIKADGSWKGPVTEITTTEYENGVAVKVKAAFRVYD 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 486159208 238 SYLEALSDYVGLLTRNPRYAAVTTAASAEQGAQALQDAGYATDPHYARKLTNMIQQMKSISDKVSKTYSMNI 309
Cdd:PRK05684 241 SYLESFNDYVSLLTNNPRYAAVTQAASPEQFARALQDAGYATDPNYARKLVSVIQQMKSMGEKVSKAYSHDL 312
 
Name Accession Description Interval E-value
flgJ PRK05684
flagellar assembly peptidoglycan hydrolase FlgJ;
2-309 0e+00

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 235559 [Multi-domain]  Cd Length: 312  Bit Score: 510.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208   2 ISDSKLLASAAWDAQSLNELKAKTGEDPAANIRPVALQVEGMFVQMMLKSMRDALPKDGLFSSEHTRLYTSMYDQQIAQQ 81
Cdd:PRK05684   1 MSDSLSDSGAAYDLQSLNSLKAKAGKDPKANLRAVAQQFEGMFVQMMLKSMRDANPKDGLMNSQQTKLYTSMYDQQIAQQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208  82 MTAGKGLGLAEMMVKQMTPEQ-PLPEESTPAAPMKFPLETVVRYQNQTLSQLVQKAV---PRNYDDSLPGDSKAFLAQLS 157
Cdd:PRK05684  81 LSAGGGLGLADMMVKQLSPEQsPAPEESAGAVPMKFDLETVQSYQNQALAQLVRKAIpqpPLASDKPLFGSSDDFVARLS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 158 LPAQLASQQSGVPHHLILAQAALESGWGQRQIRRENGEPSYNLFGVKASGNWKGPVTEITTTEYENGEAKKVKAKFRVYS 237
Cdd:PRK05684 161 PPAQKAAQQSGVPHHLLLAQAALESGWGQREIRTADGSPSHNLFGIKADGSWKGPVTEITTTEYENGVAVKVKAAFRVYD 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 486159208 238 SYLEALSDYVGLLTRNPRYAAVTTAASAEQGAQALQDAGYATDPHYARKLTNMIQQMKSISDKVSKTYSMNI 309
Cdd:PRK05684 241 SYLESFNDYVSLLTNNPRYAAVTQAASPEQFARALQDAGYATDPNYARKLVSVIQQMKSMGEKVSKAYSHDL 312
flagell_FlgJ TIGR02541
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ...
 11-295 5.09e-159

flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts directly in flagellar rod assembly. The C-terminal region is a flagellum-specific muramidase (peptidoglycan hydrolase) required for formation of the outer membrane L ring.


Pssm-ID: 274188 [Multi-domain]  Cd Length: 294  Bit Score: 445.45  E-value: 5.09e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208   11 AAWDAQSLNELKAKTGEDPAANIRPVALQVEGMFVQMMLKSMRDALPKDGLFSSEHTRLYTSMYDQQIAQQMTAGKGLGL 90
Cdd:TIGR02541   1 LAHDAQSLDSLKAKAVKDPKEQEKEAARQFEALFLNMMLKSMREATPKDGLFDSQQTRFYTQMLDQQMAQQLSANGGIGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208   91 AEMMVKQMTPEQP-LPEESTP--AAPMKFP----LETVVRYQNQTLSQLVQKAVPRN--YDDSLPGDSKAFLAQLSLPAQ 161
Cdd:TIGR02541  81 ADMIVAQLTKGQGnEPSEGAArgAAPSPLVyrprLDPKPRRIVKALIESVELSRPRGrsHAESVPGHPKSFVNSMLPHAR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208  162 LASQQSGVPHHLILAQAALESGWGQRQIRRENGEPSYNLFGVKASGNWKGPVTEITTTEYENGEAKKVKAKFRVYSSYLE 241
Cdd:TIGR02541 161 KAAQQLGVPPHLILAQAALESGWGQRQIRNADGSPSYNLFGIKASGSWQGKVVTTMTTEYVDGVAQKLTAKFRSYSSYEE 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 486159208  242 ALSDYVGLLTRNPRYAAVTTAASAEQGAQALQDAGYATDPHYARKLTNMIQQMK 295
Cdd:TIGR02541 241 AFSDYARLLNNNPRYEAVLQQRSAESFARGLQRAGYATDPRYARKLLQVIQSLA 294
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 37-295 9.18e-69

Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 215.60  E-value: 9.18e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208  37 ALQVEGMFVQMMLKSMRDALPKDGLFSSEHTRLYTSMYDQQIAQQMTAGKGLGLAEMMVKQMTPEQPLPEESTPAAPMKF 116
Cdd:COG1705   17 AQAKAAAQAAASAMASLEAAASSALSSSTSSSSKGASSSQSLEGLASALGGGASALSSAAALALKSAAKSATEAGGGLAS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 117 PLETVVRYQNQTLSQLVQKAVPRNYDDSLPGDSKAFLAQLSLPAQLASQQSGVPHHLILAQAALESGWGQRQIrreNGEP 196
Cdd:COG1705   97 ANAAATSAAALAASLSGAAALAASATAAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSEL---DGSP 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 197 SYNLFGVKASGNWKGPVTEITTTEYENGEAKKVKAKFRVYSSYLEALSDYVGLLTRNPRYA-AVTTAASAEQGAQALQDA 275
Cdd:COG1705  174 SNNLFGIKAGGSWQGKSVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLKNNPRYAgALANAKDYEAFAKALQKA 253

                        250       260
                 ....*....|....*....|
gi 486159208 276 GYATDPHYARKLTNMIQQMK 295
Cdd:COG1705  254 GYATDPKYADKLISIIESYN 273
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
 142-306 1.85e-50

Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 164.15  E-value: 1.85e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208   142 DDSLPGDSKAFLAQLSLPAQLASQQSGVPHHLILAQAALESGWGQRQIRRengePSYNLFGVKasGNWKGPVTEITTTEY 221
Cdd:smart00047   1 KLLAGGSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAK----KYNNLFGIK--GAYDGRPVRMGTLEY 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208   222 ENGEAKKVKAKFRVYSSYLEALSDYVgLLTRNPRYAAVTtaasaeqGAQALQDAGYATDPHYARKLTNMIQQMksisDKV 301
Cdd:smart00047  75 LNGGWVTVKAAFRGYFGEKFIDYAYV-LRGQNPLYKKRW-------GSNALQTAGYATDPDYAKKLIRIIALY----DEK 142


                   ....*
gi 486159208   302 SKTYS 306
Cdd:smart00047 143 LKGYD 147
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 146-293 6.96e-25

sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.


Pssm-ID: 411609 [Multi-domain]  Cd Length: 312  Bit Score: 101.74  E-value: 6.96e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 146 PGDSKAFLAQLSLPAQLASQQSGVPHHLILAQAALESGWGQRQIRRENgepsYNLFGVKASGnWKGPVT----EITTTEY 221
Cdd:NF038016 157 RGTPAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLTRED----HNYFGIKCFG-SPGPIAvgcrSYATFEC 231

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 486159208 222 E-NGEAKKVKAKFRVYSSYLEALSDYVGLLTRNPRYA-AVTTAASAEQGAQALQDAGYATDPHYARKLTNMIQQ 293
Cdd:NF038016 232 SpTGGCFDTTATFRAYASAADSFRDHGRFLSVNSRYApAFAYTDDPDQFAREIHKAGYATDPTYADKLIGLMKQ 305
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
 160-295 4.64e-21

Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyse peptidoglycan.


Pssm-ID: 460354 [Multi-domain]  Cd Length: 91  Bit Score: 85.70  E-value: 4.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208  160 AQLASQQSGVPHHLILAQAALESGWGQRQIRREngepSYNLFGVKASgnWKGPVTeITTTEYengeakKVKAKFRVYSSY 239
Cdd:pfam01832   4 AIEAAKKYGIPASVLLAQAALESGWGTSRLAKE----SNNLFGIKAS--WKGKVA-YDTDEV------TVAARFRKYDSV 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 486159208  240 LEALSDyvglltrnpryaavttaasaeqgaqalqdagyatdpHYARKLTNMIQQMK 295
Cdd:pfam01832  71 EESIRD------------------------------------YYAEKLIAIIERYN 90
 
Name Accession Description Interval E-value
flgJ PRK05684
flagellar assembly peptidoglycan hydrolase FlgJ;
2-309 0e+00

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 235559 [Multi-domain]  Cd Length: 312  Bit Score: 510.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208   2 ISDSKLLASAAWDAQSLNELKAKTGEDPAANIRPVALQVEGMFVQMMLKSMRDALPKDGLFSSEHTRLYTSMYDQQIAQQ 81
Cdd:PRK05684   1 MSDSLSDSGAAYDLQSLNSLKAKAGKDPKANLRAVAQQFEGMFVQMMLKSMRDANPKDGLMNSQQTKLYTSMYDQQIAQQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208  82 MTAGKGLGLAEMMVKQMTPEQ-PLPEESTPAAPMKFPLETVVRYQNQTLSQLVQKAV---PRNYDDSLPGDSKAFLAQLS 157
Cdd:PRK05684  81 LSAGGGLGLADMMVKQLSPEQsPAPEESAGAVPMKFDLETVQSYQNQALAQLVRKAIpqpPLASDKPLFGSSDDFVARLS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 158 LPAQLASQQSGVPHHLILAQAALESGWGQRQIRRENGEPSYNLFGVKASGNWKGPVTEITTTEYENGEAKKVKAKFRVYS 237
Cdd:PRK05684 161 PPAQKAAQQSGVPHHLLLAQAALESGWGQREIRTADGSPSHNLFGIKADGSWKGPVTEITTTEYENGVAVKVKAAFRVYD 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 486159208 238 SYLEALSDYVGLLTRNPRYAAVTTAASAEQGAQALQDAGYATDPHYARKLTNMIQQMKSISDKVSKTYSMNI 309
Cdd:PRK05684 241 SYLESFNDYVSLLTNNPRYAAVTQAASPEQFARALQDAGYATDPNYARKLVSVIQQMKSMGEKVSKAYSHDL 312
flagell_FlgJ TIGR02541
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ...
 11-295 5.09e-159

flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts directly in flagellar rod assembly. The C-terminal region is a flagellum-specific muramidase (peptidoglycan hydrolase) required for formation of the outer membrane L ring.


Pssm-ID: 274188 [Multi-domain]  Cd Length: 294  Bit Score: 445.45  E-value: 5.09e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208   11 AAWDAQSLNELKAKTGEDPAANIRPVALQVEGMFVQMMLKSMRDALPKDGLFSSEHTRLYTSMYDQQIAQQMTAGKGLGL 90
Cdd:TIGR02541   1 LAHDAQSLDSLKAKAVKDPKEQEKEAARQFEALFLNMMLKSMREATPKDGLFDSQQTRFYTQMLDQQMAQQLSANGGIGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208   91 AEMMVKQMTPEQP-LPEESTP--AAPMKFP----LETVVRYQNQTLSQLVQKAVPRN--YDDSLPGDSKAFLAQLSLPAQ 161
Cdd:TIGR02541  81 ADMIVAQLTKGQGnEPSEGAArgAAPSPLVyrprLDPKPRRIVKALIESVELSRPRGrsHAESVPGHPKSFVNSMLPHAR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208  162 LASQQSGVPHHLILAQAALESGWGQRQIRRENGEPSYNLFGVKASGNWKGPVTEITTTEYENGEAKKVKAKFRVYSSYLE 241
Cdd:TIGR02541 161 KAAQQLGVPPHLILAQAALESGWGQRQIRNADGSPSYNLFGIKASGSWQGKVVTTMTTEYVDGVAQKLTAKFRSYSSYEE 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 486159208  242 ALSDYVGLLTRNPRYAAVTTAASAEQGAQALQDAGYATDPHYARKLTNMIQQMK 295
Cdd:TIGR02541 241 AFSDYARLLNNNPRYEAVLQQRSAESFARGLQRAGYATDPRYARKLLQVIQSLA 294
flgJ PRK12712
flagellar rod assembly protein/muramidase FlgJ; Provisional
 12-298 5.20e-91

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139172 [Multi-domain]  Cd Length: 344  Bit Score: 274.58  E-value: 5.20e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208  12 AWDAQSLNELK--AKTGEDpAANIRPVALQVEGMFVQMMLKSMRDALPKDGLFSSEHTRLYTSMYDQQIAQQMTAgKGLG 89
Cdd:PRK12712  17 ALDTQGFEALKhsARGGAD-AGTLQAAARQFEAVFTQMVLKSMRDATPQDGLFDNEQSKLYMSMMDQQLAQQMSS-RGIG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208  90 LAEMMVKQMTPE--QPLPE--------ESTPAAPMKF--------------------PLETVVRYQNQTLSQLVQKAVPR 139
Cdd:PRK12712  95 LADVMVRQLARAtgTQMPPgmnaaggaTAGSAADAEMarlldgrgagaadadagdlpAIGTIVPGQAWNPTAGLRQYQPQ 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 140 NYDDS---------LPGDS----KAFLAQLSLPAQLASQQSGVPHHLILAQAALESGWGQRQIRRENGEPSYNLFGVKAS 206
Cdd:PRK12712 175 AYADQgqgedrlgrLPDDApahvSAFVARMAGPAEAASRASGVPARLIVGQAALESGWGRREITHADGSTTFNVFGIKAG 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 207 GNWKGPVTEITTTEYENGEAKKVKAKFRVYSSYLEALSDYVGLLTRNPRYAAVTTAASAEQGAQALQDAGYATDPHYARK 286
Cdd:PRK12712 255 ANWKGRVAEVTTTEYVDGQPQKVRARFRAYGSYDEACADYARLLTSNPRYAGVVSAASADEAAHGLQRAGYATDPAYGHK 334

                        330
                 ....*....|..
gi 486159208 287 LtnmIQQMKSIS 298
Cdd:PRK12712 335 L---VKIMKKVS 343
flgJ PRK12709
flagellar rod assembly protein/muramidase FlgJ; Provisional
 12-294 1.32e-83

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 237179 [Multi-domain]  Cd Length: 320  Bit Score: 254.85  E-value: 1.32e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208  12 AWDAQSLNELKAKTGEDPAANIRPVALQVEGMFVQMMLKSMRDALPKDGLFSSEHTRLYTSMYDQQIAQQMTAgKGLGLA 91
Cdd:PRK12709  15 ALDVQGFDALRAQAKASPQAGAKMVAGQFDAMFTQMMLKSMRDATPSDGLFDSHTSKMYTSMLDQQLAQQMSS-KGIGVA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208  92 EMMVKQ-MTPEQPLPEESTPAAPMKFPLETVVRYQNQTLSQLVQK----------AVPRNYD-----------DSLPGDS 149
Cdd:PRK12709  94 DALMKQlLRNAGVAAGAQGDAGAGGMGGLGGNEGGLAAMNALAKAyanaanngalAGTRGYSagsaltpplkgNGGSPDA 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 150 KAFLAQLSLPAQLASQQSGVPHHLILAQAALESGWGQRQIRRENGEPSYNLFGVKASGNWKGPVTEITTTEYENGEAKKV 229
Cdd:PRK12709 174 DAFVDKLAAPAQAASAATGIPARFIVGQAALESGWGKREIRGADGSTSYNVFGIKATKGWTGRTVSAVTTEYVNGKPRRV 253

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 486159208 230 KAKFRVYSSYLEALSDYVGLLTRNPRYAAVTTAA-SAEQGAQALQDAGYATDPHYARKLTNMIQQM 294
Cdd:PRK12709 254 VAKFRAYDSYEHAMTDYANLLKNNPRYAGVLNASrSVEGFAHGMQKAGYATDPHYAKKLISIMQQI 319
flgJ PRK12713
flagellar rod assembly protein/muramidase FlgJ; Provisional
 11-296 1.58e-77

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139173 [Multi-domain]  Cd Length: 339  Bit Score: 240.03  E-value: 1.58e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208  11 AAWDAQSLNELKAKTGEDP--AANIRPVALQVEGMFVQMMLKSMRDALPKDGLFSSEHTRLYTSMYDQQIAQQMtAGKGL 88
Cdd:PRK12713  15 SVFDLGRLADLKRDAVKAPdgQRQQTEVARQFEALFLQMMLKRMREATPKEGLFDSQQTEMLQGMADEQLALQL-ASPGI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208  89 GLAEMMVKQMTPEQPlPEESTPA---------------APMKFPLETVVRYQNQ---------TLSQLVQKAVPRNYD-- 142
Cdd:PRK12713  94 GLAQALLGQMQQGQP-PVPAAAAaggdaaaaralagtaAPAPLVRDLRGNYVQPdpaprrevnALLDVLRSNRARDRAma 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 143 --DSLPGDSKAFLAQLSLPAQLASQQSGVPHHLILAQAALESGWGQRQIRRENGEPSYNLFGVKASGNWKGPVTEITTTE 220
Cdd:PRK12713 173 aaEGAPSHVVDFVSRMSRAANVAAQQSGVPARLILGQAALESGWGRRELRHEDGSTSYNLFGIKAGASWKGKVVNVMTTE 252

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 486159208 221 YENGEAKKVKAKFRVYSSYLEALSDYVGLLTRNPRYAAVTTAASAEQGAQALQDAGYATDPHYARKLTNMIQQMKS 296
Cdd:PRK12713 253 YVDGVAQKLVQPFRAYSSYEESFSDYARLIGNSPRYEAVTQAGNEIEAARRIQEAGYATDPRYAEKLISIMGQLRT 328
FlgJ COG1705
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ...
 37-295 9.18e-69

Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];


Pssm-ID: 441311 [Multi-domain]  Cd Length: 276  Bit Score: 215.60  E-value: 9.18e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208  37 ALQVEGMFVQMMLKSMRDALPKDGLFSSEHTRLYTSMYDQQIAQQMTAGKGLGLAEMMVKQMTPEQPLPEESTPAAPMKF 116
Cdd:COG1705   17 AQAKAAAQAAASAMASLEAAASSALSSSTSSSSKGASSSQSLEGLASALGGGASALSSAAALALKSAAKSATEAGGGLAS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 117 PLETVVRYQNQTLSQLVQKAVPRNYDDSLPGDSKAFLAQLSLPAQLASQQSGVPHHLILAQAALESGWGQRQIrreNGEP 196
Cdd:COG1705   97 ANAAATSAAALAASLSGAAALAASATAAASASPEEFIAKIAPAAQKAAKKYGVPASVLIAQAALESGWGKSEL---DGSP 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 197 SYNLFGVKASGNWKGPVTEITTTEYENGEAKKVKAKFRVYSSYLEALSDYVGLLTRNPRYA-AVTTAASAEQGAQALQDA 275
Cdd:COG1705  174 SNNLFGIKAGGSWQGKSVEVTTTEYVNGKAVKIKARFRAYDSYAESFRDYARLLKNNPRYAgALANAKDYEAFAKALQKA 253

                        250       260
                 ....*....|....*....|
gi 486159208 276 GYATDPHYARKLTNMIQQMK 295
Cdd:COG1705  254 GYATDPKYADKLISIIESYN 273
LYZ2 smart00047
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
 142-306 1.85e-50

Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.


Pssm-ID: 214488 [Multi-domain]  Cd Length: 147  Bit Score: 164.15  E-value: 1.85e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208   142 DDSLPGDSKAFLAQLSLPAQLASQQSGVPHHLILAQAALESGWGQRQIRRengePSYNLFGVKasGNWKGPVTEITTTEY 221
Cdd:smart00047   1 KLLAGGSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAK----KYNNLFGIK--GAYDGRPVRMGTLEY 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208   222 ENGEAKKVKAKFRVYSSYLEALSDYVgLLTRNPRYAAVTtaasaeqGAQALQDAGYATDPHYARKLTNMIQQMksisDKV 301
Cdd:smart00047  75 LNGGWVTVKAAFRGYFGEKFIDYAYV-LRGQNPLYKKRW-------GSNALQTAGYATDPDYAKKLIRIIALY----DEK 142


                   ....*
gi 486159208   302 SKTYS 306
Cdd:smart00047 143 LKGYD 147
flgJ PRK12711
flagellar assembly peptidoglycan hydrolase FlgJ;
20-287 7.31e-48

flagellar assembly peptidoglycan hydrolase FlgJ;


Pssm-ID: 237180 [Multi-domain]  Cd Length: 392  Bit Score: 164.75  E-value: 7.31e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208  20 ELKAKTGEDPAaNIRPVALQVEGMFVQMMLKSMRDALPKDGLFSSEHtRLYTSMYDQQIAQQMTAGKGLGLAEMMVKQMT 99
Cdd:PRK12711   9 DLNPSTKADPA-KIDKVSRQLEGQFAQMLVKSMRDASSGDPMFPGEN-QMFREMYDQQMAKALTDGKGLGLSAMISKQLS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 100 PEQPLPEEST---PA--------------APMKFPLE---TVVRYQNQT--------------LSQLVQKAVPRN----- 140
Cdd:PRK12711  87 GDTGGPALNTalnTAkaakayslvagkrdASLPLPARdgaAAGITTSSVaaaalsagnlsgigMSQVLDLIAGRTgagea 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 141 YDDSLPGDS----------------------------------------KAFLAQLSLPAQLASQQSGVPHHLILAQAAL 180
Cdd:PRK12711 167 GSDDAAALSwpsandrwsdvaasdaadanaavnasaastaaaslgertpEGFVAKIWTHAQKAARELGVDPRALVAQAAL 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 181 ESGWGQRQIrrENGEPSYNLFGVKASGnWKGPVTEITTTEYENGEAKKVKAKFRVYSSYLEALSDYVGLLTRNPRYAAVT 260
Cdd:PRK12711 247 ETGWGRRGI--GNGGDSNNLFGIKATG-WNGDKVTTGTHEYVNGVKTTETADFRAYGSAEESFADYVRLLKNNSRYQQAL 323

                        330       340
                 ....*....|....*....|....*...
gi 486159208 261 TAASAEQG-AQALQDAGYATDPHYARKL 287
Cdd:PRK12711 324 QAGTDIKGfARGLQQAGYATDPGYAAKI 351
FlgJ1 COG3951
Rod binding protein domain [Cell motility];
1-103 2.03e-40

Rod binding protein domain [Cell motility];


Pssm-ID: 443151 [Multi-domain]  Cd Length: 107  Bit Score: 136.59  E-value: 2.03e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208   1 MISDSKLLASAAWDAQSLNELKAKTGEDPAANIRPVALQVEGMFVQMMLKSMRDALPKDGLFSSEHTRLYTSMYDQQIAQ 80
Cdd:COG3951    1 MSISSSLSSSLALDAQSLNALKAAAKADDDAALKEAAQQFEALFLQMMLKSMRKAVPEDGLFGSQAEDMFRDMLDQQLAK 80

                         90       100
                 ....*....|....*....|...
gi 486159208  81 QMTAGKGLGLAEMMVKQMTPEQP 103
Cdd:COG3951   81 ELAKGGGLGLADMIYRQLSRQQE 103
flgJ PRK12710
flagellar rod assembly protein/muramidase FlgJ; Provisional
 11-290 1.16e-32

flagellar rod assembly protein/muramidase FlgJ; Provisional


Pssm-ID: 139170 [Multi-domain]  Cd Length: 291  Bit Score: 122.21  E-value: 1.16e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208  11 AAWDAQSLNELKAKTGEDPAANIRPVALQVEGMFVQMMLKSMRDA---LPKDGLFSSEHTRLYTSMYDQQIAQQMTAGKG 87
Cdd:PRK12710   7 ATSDFQGLNELKVQAKNNAKEALPEVAKQFEGIFLQSMLKSMRMGqhfLDESSPFSGKNEATFQEMLDTQYASTIAESKG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208  88 LGLAEMMVKQMtpeqplpeESTPAAPMKFPLETVVRYQNQTLSqlvqkavprNYDDSLpGDSKAFLAQLSLPAQLASQQS 167
Cdd:PRK12710  87 IGLAALLAKQL--------ENSVGDKANNPVNSSTEVSNTKVT---------NSEESL-SVVDDFVKSVWPTAKQAASLI 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 168 GVPHHLILAQAALESGWGQRQIRRENGEPSYNLFGVKASGNWKGPVTEITTTEYENGEAKKVKAKFRVYSSYLEALSDYV 247
Cdd:PRK12710 149 GLDPKLLVAQAALETGWGKFVTRDADGSSSNNLFNIKTGSHSEVESIQVKTTEYIADTPIKINASFRKYPSIEHSFHDYV 228

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 486159208 248 GLLTRNPRYA-AVTTAASAEQGAQALQDAGYATDPHYARKLTNM 290
Cdd:PRK12710 229 SLIKGSERYQmALANAENPEIYVSELNKAGYATDPNYSNKILSI 272
sporang_Gsm NF038016
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ...
 146-293 6.96e-25

sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.


Pssm-ID: 411609 [Multi-domain]  Cd Length: 312  Bit Score: 101.74  E-value: 6.96e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 146 PGDSKAFLAQLSLPAQLASQQSGVPHHLILAQAALESGWGQRQIRRENgepsYNLFGVKASGnWKGPVT----EITTTEY 221
Cdd:NF038016 157 RGTPAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLTRED----HNYFGIKCFG-SPGPIAvgcrSYATFEC 231

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 486159208 222 E-NGEAKKVKAKFRVYSSYLEALSDYVGLLTRNPRYA-AVTTAASAEQGAQALQDAGYATDPHYARKLTNMIQQ 293
Cdd:NF038016 232 SpTGGCFDTTATFRAYASAADSFRDHGRFLSVNSRYApAFAYTDDPDQFAREIHKAGYATDPTYADKLIGLMKQ 305
Glucosaminidase pfam01832
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ...
 160-295 4.64e-21

Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyse peptidoglycan.


Pssm-ID: 460354 [Multi-domain]  Cd Length: 91  Bit Score: 85.70  E-value: 4.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208  160 AQLASQQSGVPHHLILAQAALESGWGQRQIRREngepSYNLFGVKASgnWKGPVTeITTTEYengeakKVKAKFRVYSSY 239
Cdd:pfam01832   4 AIEAAKKYGIPASVLLAQAALESGWGTSRLAKE----SNNLFGIKAS--WKGKVA-YDTDEV------TVAARFRKYDSV 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 486159208  240 LEALSDyvglltrnpryaavttaasaeqgaqalqdagyatdpHYARKLTNMIQQMK 295
Cdd:pfam01832  71 EESIRD------------------------------------YYAEKLIAIIERYN 90
PRK08581 PRK08581
amidase domain-containing protein;
174-292 1.64e-18

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 86.00  E-value: 1.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 174 ILAQAALESGWGQRQIRREngePSYNLFGVKasGNWKGPVTEITTTEYENGEAKKVKAKFRVYSSYLEALSDYVGLL--- 250
Cdd:PRK08581 345 MIAQAILESDSGQSALAKS---PNHNLFGIK--GAYEGNSVSFNTLEADGNQLYSINAGFRKYPSTKESLEDYADLIkng 419

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 486159208 251 -TRNPRYAAVT---TAASAEQGAQALQDAgYATDPHYARKLTNMIQ 292
Cdd:PRK08581 420 iDGNSTIYKPTwksEAKSYKDATSHLSKT-YATDPNYAKKLNSIIK 464
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
95-291 5.76e-15

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 75.12  E-value: 5.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208  95 VKQMTPEQP-LPEESTPAAPM--KFPLE--TVVRYQNQTLS------QLVQKAVPRNyddslPGDSKAFLAQLSLPAQLA 163
Cdd:PRK06347  90 KQTETKEQTkTPEEKQPAAKQveKAPAEpaTVSNPDNATSSstpatyNLLQKSALRS-----GATVQSFIQTIQASSSQI 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 164 SQQSGVPHHLILAQAALESGWGQRQIrreNGEPSYNLFGVKASGNWKGpVTEITTTEYENGEAKKVKAKFRVYSSYLEAL 243
Cdd:PRK06347 165 AAENDLYASVMIAQAILESAYGTSEL---GSAPNYNLFGIKGAYNGQS-YTKQTLEDDGKGNYYTITAKFRKYPSYHQSL 240

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 486159208 244 SDYVGLLTRNPR-----YAAV--TTAASAEQGAQALQDAgYATDPHYARKLTNMI 291
Cdd:PRK06347 241 EDYAQVIRKGPSwnpnyYSKVwkSNTTSYKDATKALTGT-YATDTAYATKLNDLI 294
Rod-binding pfam10135
Rod binding protein; Members of this family are involved in the assembly of the prokaryotic ...
 50-97 2.46e-14

Rod binding protein; Members of this family are involved in the assembly of the prokaryotic flagellar rod.


Pssm-ID: 431078 [Multi-domain]  Cd Length: 50  Bit Score: 66.08  E-value: 2.46e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 486159208   50 KSMRDALPK-DGLF-SSEHTRLYTSMYDQQIAQQMTAGKGLGLAEMMVKQ 97
Cdd:pfam10135   1 KSMRKTVPKeDGLFdGSEAEDMFRDMLDQQLAKQLAKGGGLGLADMLYRQ 50
flgJ PRK12708
peptidoglycan hydrolase; Reviewed
 18-120 3.47e-10

peptidoglycan hydrolase; Reviewed


Pssm-ID: 139168 [Multi-domain]  Cd Length: 134  Bit Score: 57.16  E-value: 3.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208  18 LNELKAKTGEDPAanIRPVALQVEGMFVQMMLKSMR---DALP-KDGLFSSEHTRLYTSMYDQQIAQQMTAGKGLGLAEM 93
Cdd:PRK12708  15 AGDLIPQNLEQGA--LKLAAQQFEAQFLQTVLKQMRsasDVMAdEDDPFNSKNQGMYRDFYDAELASRLSSQRSMGLAEV 92

                         90       100
                 ....*....|....*....|....*..
gi 486159208  94 MVKQMTPEQPLPEEstPAAPMKFPLET 120
Cdd:PRK12708  93 MIKQLSSKLKSAPE--VVALESQTLTT 117
LytD COG4193
Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism];
163-306 3.00e-07

Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism];


Pssm-ID: 443347 [Multi-domain]  Cd Length: 423  Bit Score: 51.51  E-value: 3.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 163 ASQQSGV-PHHLIlAQAALESGWGQRQI---RRENGEPSYNLFGVKASGNwkGPVTEITTTEYENGEAKKVK-----AKF 233
Cdd:COG4193  281 AAKKYGVnPLYLA-SHALLETGNGTSKLakgVEVNGKTYYNLFGIGAYDS--NPLENGAKYAYKQGWTSPEKaivggAKF 357

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 486159208 234 rVYSSYLEAlSDYVGLLTRNPRYAAVTTAASAEqgaqalqdagYATDPHYARKLTNMIQQMKSISDKVSKTYS 306
Cdd:COG4193  358 -IGSNYINN-TGYGQNTLYKMRWNPVNPGTNHQ----------YATDPFWAEKIAGHMYRAYKKLKDYNLYFD 418
PRK10356 PRK10356
protein bax;
169-292 2.58e-05

protein bax;


Pssm-ID: 182404  Cd Length: 274  Bit Score: 44.86  E-value: 2.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 169 VPHHLILAQAALESGWGQRQIRRENGepsyNLFGVKASgnwkgpvteittteyeNGEAKKVKAKFRVYSSYL---EALSD 245
Cdd:PRK10356 149 IPTSMVATMAAAESGWGTSKLARNNN----NLFGMKCM----------------KGRCTNAPGKVKGYSQFSsvkESVSA 208

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 486159208 246 YVGLLTRNPRYAAVTTAASAEQGAQALQDA--------GYAT-DPHYARKLTNMIQ 292
Cdd:PRK10356 209 YVTNLNTHPAYSSFRKSRAQLRKADQEVTAtamihklkGYSTkGSSYNNYLFAMYQ 264
Bax COG2992
Uncharacterized FlgJ-related protein [General function prediction only];
122-202 8.61e-04

Uncharacterized FlgJ-related protein [General function prediction only];


Pssm-ID: 442231  Cd Length: 253  Bit Score: 40.29  E-value: 8.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486159208 122 VRYQNQTLSQLVQ--KAVPRNYDDSLPGDSKAFLAQLS----LPAQLASQQS---------GVPHHLILAQAALESGWGQ 186
Cdd:COG2992   57 ILAENERILAERErlLALQAKLLKSLSPEEQAWLSALAkkyrVKNDLLDEADleellkrvdIIPPSLVLAQAANESGWGT 136

                         90
                 ....*....|....*.
gi 486159208 187 RQIRREngepSYNLFG 202
Cdd:COG2992  137 SRFARE----GNNLFG 148
 
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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