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Conserved domains on  [gi|446306096|ref|WP_000383951|]
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MULTISPECIES: cyclic di-3',5'-guanylate-activated glycosyltransferase NrfB [Enterobacteriaceae]

Protein Classification

phage adsorption protein NrfB( domain architecture ID 11485276)

phage adsorption protein NrfB is required for bacteriophage N4 adsorption

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
nfrB PRK11234
phage adsorption protein NrfB;
7-737 0e+00

phage adsorption protein NrfB;


:

Pssm-ID: 236884 [Multi-domain]  Cd Length: 727  Bit Score: 1303.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096   7 VFATWLYGLKVIAITLAVIMFISGLDDFFIDVVYWVRRIKRKLSVYRRYPRMSYRELYKPDEKPLAIMVPAWNETGVIGN 86
Cdd:PRK11234   1 VLATWLYGLKVIAITLAVLMFISGLDDLFIDVVYWVRRIKRKLSVYRRYPRMSYRELYKPDEKPLAIMVPAWNETGVIGN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096  87 MAELAATTLDYENYHIFVGTYPNDPDTQRDVDEVCARFPNVHKVVCARPGPTSKADCLNNVLDAITQFERSANFAFAGFI 166
Cdd:PRK11234  81 MAELAATTLDYENYHIFVGTYPNDPATQADVDAVCARFPNVHKVVCARPGPTSKADCLNNVLDAITQFERSANFAFAGFI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 167 LHDAEDVISPMELRLFNYLVERKDLIQIPVYPFEREWTHFTSMTYIDEFSELHGKDVPVREALAGQVPSAGVGTCFSRRA 246
Cdd:PRK11234 161 LHDAEDVISPMELRLFNYLVERKDLIQIPVYPFEREWTHFTSGTYIDEFAELHGKDVPVREALAGQVPSAGVGTCFSRRA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 247 VTALLADGDGIAFDVQSLTEDYDIGFRLKEKGMTEIFVRFPVVDEAKEREQRKFLQHARTSNMICVREYFPDTFSTAVRQ 326
Cdd:PRK11234 241 VTALLEDGDGIAFDVQSLTEDYDIGFRLKEKGMREIFVRFPVVDEAKEREQRKFLQHARTSNMICVREYFPDTFSAAVRQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 327 KSRWIIGIVFQGFKTHKWTSSLTLNYFLWRDRKGAISNFVSFLAMLVMLQLLLLLAYESLWPNAWHFLSIFSGSAWLMTL 406
Cdd:PRK11234 321 KSRWIIGIVFQGFKTLGWTSSLTLNYFLWRDRKGAITNFVSFLAMLLMLQLLLLLLYESLWPDAWHFLSIFSGSAWLMTL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 407 LWLNFGLMVNRIVQRVIFVTGYYGLTQGLLSVLRLFWGNLINFMANWRALKQVLQHGDPRRVAWDKTTHDFPSVTGDTRS 486
Cdd:PRK11234 401 LWLNFGLMVNRIVQRVIFVTGYYGLTQGLLSVLRLLWGNLINFMANWRALRQVLQHGDPRRVAWDKTTHDFPSVTGDTRS 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 487 LRPLGQILLENQVITEEQLDTALRNRVEGLRLGGSMLMQGLISAEQLAQALAEQNGVAWESIDAWQIPSSLIAEMPASVA 566
Cdd:PRK11234 481 LRPLGQILLENGVITEEQLDTALRNRVRGLRLGQSLLMQGLISAEQLAQALAEQNGVAWESLDPWQIPSSLIAEMPASVA 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 567 LHYAVLPLRLENDELIVGSEDGIDPVSLAALTRKVGRKVRYVIVLRGQIVTGLRHWYARRRGHDPRAMLYNAVQHQwlte 646
Cdd:PRK11234 561 LHYAVLPLREEGDELIVASEDGISPVSLAALTRKLGRKVRYVIVPRGQVTTGLRHWYARRRGHDPRAMLYNAVQHQ---- 636
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 647 QQTGEIWRQYVPHQFLFAEILTTLGHINRSAINVLLLRHERSSLPLGKFLVTEGVISQETLDRVLTIQRELQVSMQSLLL 726
Cdd:PRK11234 637 QQAGEIWRQYVPHQFLFAEILTTLGHIPRSAINVLLLRHERSSLPLGKFLVTEGVISQETLDRALTIQRELQVSMQSLLL 716
                        730
                 ....*....|.
gi 446306096 727 KAGLNTEQVAQ 737
Cdd:PRK11234 717 KAGLNTEQVAQ 727
 
Name Accession Description Interval E-value
nfrB PRK11234
phage adsorption protein NrfB;
7-737 0e+00

phage adsorption protein NrfB;


Pssm-ID: 236884 [Multi-domain]  Cd Length: 727  Bit Score: 1303.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096   7 VFATWLYGLKVIAITLAVIMFISGLDDFFIDVVYWVRRIKRKLSVYRRYPRMSYRELYKPDEKPLAIMVPAWNETGVIGN 86
Cdd:PRK11234   1 VLATWLYGLKVIAITLAVLMFISGLDDLFIDVVYWVRRIKRKLSVYRRYPRMSYRELYKPDEKPLAIMVPAWNETGVIGN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096  87 MAELAATTLDYENYHIFVGTYPNDPDTQRDVDEVCARFPNVHKVVCARPGPTSKADCLNNVLDAITQFERSANFAFAGFI 166
Cdd:PRK11234  81 MAELAATTLDYENYHIFVGTYPNDPATQADVDAVCARFPNVHKVVCARPGPTSKADCLNNVLDAITQFERSANFAFAGFI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 167 LHDAEDVISPMELRLFNYLVERKDLIQIPVYPFEREWTHFTSMTYIDEFSELHGKDVPVREALAGQVPSAGVGTCFSRRA 246
Cdd:PRK11234 161 LHDAEDVISPMELRLFNYLVERKDLIQIPVYPFEREWTHFTSGTYIDEFAELHGKDVPVREALAGQVPSAGVGTCFSRRA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 247 VTALLADGDGIAFDVQSLTEDYDIGFRLKEKGMTEIFVRFPVVDEAKEREQRKFLQHARTSNMICVREYFPDTFSTAVRQ 326
Cdd:PRK11234 241 VTALLEDGDGIAFDVQSLTEDYDIGFRLKEKGMREIFVRFPVVDEAKEREQRKFLQHARTSNMICVREYFPDTFSAAVRQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 327 KSRWIIGIVFQGFKTHKWTSSLTLNYFLWRDRKGAISNFVSFLAMLVMLQLLLLLAYESLWPNAWHFLSIFSGSAWLMTL 406
Cdd:PRK11234 321 KSRWIIGIVFQGFKTLGWTSSLTLNYFLWRDRKGAITNFVSFLAMLLMLQLLLLLLYESLWPDAWHFLSIFSGSAWLMTL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 407 LWLNFGLMVNRIVQRVIFVTGYYGLTQGLLSVLRLFWGNLINFMANWRALKQVLQHGDPRRVAWDKTTHDFPSVTGDTRS 486
Cdd:PRK11234 401 LWLNFGLMVNRIVQRVIFVTGYYGLTQGLLSVLRLLWGNLINFMANWRALRQVLQHGDPRRVAWDKTTHDFPSVTGDTRS 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 487 LRPLGQILLENQVITEEQLDTALRNRVEGLRLGGSMLMQGLISAEQLAQALAEQNGVAWESIDAWQIPSSLIAEMPASVA 566
Cdd:PRK11234 481 LRPLGQILLENGVITEEQLDTALRNRVRGLRLGQSLLMQGLISAEQLAQALAEQNGVAWESLDPWQIPSSLIAEMPASVA 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 567 LHYAVLPLRLENDELIVGSEDGIDPVSLAALTRKVGRKVRYVIVLRGQIVTGLRHWYARRRGHDPRAMLYNAVQHQwlte 646
Cdd:PRK11234 561 LHYAVLPLREEGDELIVASEDGISPVSLAALTRKLGRKVRYVIVPRGQVTTGLRHWYARRRGHDPRAMLYNAVQHQ---- 636
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 647 QQTGEIWRQYVPHQFLFAEILTTLGHINRSAINVLLLRHERSSLPLGKFLVTEGVISQETLDRVLTIQRELQVSMQSLLL 726
Cdd:PRK11234 637 QQAGEIWRQYVPHQFLFAEILTTLGHIPRSAINVLLLRHERSSLPLGKFLVTEGVISQETLDRALTIQRELQVSMQSLLL 716
                        730
                 ....*....|.
gi 446306096 727 KAGLNTEQVAQ 737
Cdd:PRK11234 717 KAGLNTEQVAQ 727
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
164-368 2.67e-33

Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 126.68  E-value: 2.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096  164 GFILHDAEDVISPMELRLFNYLVER--KDLIQIPVYPfeREWTHFTSMTYIDEFSELHGKDVPVREALAGQVPSAGVGTC 241
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMASpeVAIIQGPILP--MNVGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096  242 FSRRAVTALladgdgIAFDVQSLTEDYDIGFRLKEKGMTEIFVrfpvvdeakereqrkflqhartsNMICVREYFPDTFS 321
Cdd:pfam13632  79 LRRSALQEV------GGWDDGSVSEDFDFGLRLQRAGYRVRFA-----------------------PYSAVYEKSPLTFR 129
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 446306096  322 TAVRQKSRWIIGI-VFQGFKTHKWTSSLTLNYFLWRDRKGAISNFVSF 368
Cdd:pfam13632 130 DFLRQRRRWAYGClLILLIRLLGYLGTLLWSGLPLALLLLLLFSISSL 177
PulE COG2804
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ...
485-627 2.89e-20

Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442055 [Multi-domain]  Cd Length: 561  Bit Score: 95.26  E-value: 2.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 485 RSLRPLGQILLENQVITEEQLDTALR-NRVEGLRLGGSMLMQGLISAEQLAQALAEQNGVAWESIDAWQIPSSLIAEMPA 563
Cdd:COG2804    4 SLLLRLGDLLVEAGLISEEQLLAALAeQKKTGKPLGELLVELGLVTEELLAEALAEQLGLPFVDLDELEIDPEVLELLPE 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446306096 564 SVALHYAVLPLRLENDELIVGSEDGIDPVSLAALTRKVGRKVRYVIVLRGQIVTGLRHWYARRR 627
Cdd:COG2804   84 ELARRHRVLPLRLEGGTLTVAMADPLDLEALDELRRLTGRPVEPVVATESDIERALDRLYGSES 147
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
73-267 8.82e-06

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 46.84  E-value: 8.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096  73 IMVPAWNETGVIGNMAElAATTLDYENYHIFVGTYpNDPDTQRDVDEVCARFPNVHKVVCARPGPTSKADCLNNVLdait 152
Cdd:cd06423    1 IIVPAYNEEAVIERTIE-SLLALDYPKLEVIVVDD-GSTDDTLEILEELAALYIRRVLVVRDKENGGKAGALNAGL---- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 153 qfeRSANFAFAGFIlhDAEDVISP-----MELRLFNYlverKDLIQI-----PVYPFEREWTHFTSMtyidEFSELHGKD 222
Cdd:cd06423   75 ---RHAKGDIVVVL--DADTILEPdalkrLVVPFFAD----PKVGAVqgrvrVRNGSENLLTRLQAI----EYLSIFRLG 141
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446306096 223 VPVREALAGQVPSAGVGTCFSRRAVTALLadgdgiAFDVQSLTED 267
Cdd:cd06423  142 RRAQSALGGVLVLSGAFGAFRREALREVG------GWDEDTLTED 180
 
Name Accession Description Interval E-value
nfrB PRK11234
phage adsorption protein NrfB;
7-737 0e+00

phage adsorption protein NrfB;


Pssm-ID: 236884 [Multi-domain]  Cd Length: 727  Bit Score: 1303.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096   7 VFATWLYGLKVIAITLAVIMFISGLDDFFIDVVYWVRRIKRKLSVYRRYPRMSYRELYKPDEKPLAIMVPAWNETGVIGN 86
Cdd:PRK11234   1 VLATWLYGLKVIAITLAVLMFISGLDDLFIDVVYWVRRIKRKLSVYRRYPRMSYRELYKPDEKPLAIMVPAWNETGVIGN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096  87 MAELAATTLDYENYHIFVGTYPNDPDTQRDVDEVCARFPNVHKVVCARPGPTSKADCLNNVLDAITQFERSANFAFAGFI 166
Cdd:PRK11234  81 MAELAATTLDYENYHIFVGTYPNDPATQADVDAVCARFPNVHKVVCARPGPTSKADCLNNVLDAITQFERSANFAFAGFI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 167 LHDAEDVISPMELRLFNYLVERKDLIQIPVYPFEREWTHFTSMTYIDEFSELHGKDVPVREALAGQVPSAGVGTCFSRRA 246
Cdd:PRK11234 161 LHDAEDVISPMELRLFNYLVERKDLIQIPVYPFEREWTHFTSGTYIDEFAELHGKDVPVREALAGQVPSAGVGTCFSRRA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 247 VTALLADGDGIAFDVQSLTEDYDIGFRLKEKGMTEIFVRFPVVDEAKEREQRKFLQHARTSNMICVREYFPDTFSTAVRQ 326
Cdd:PRK11234 241 VTALLEDGDGIAFDVQSLTEDYDIGFRLKEKGMREIFVRFPVVDEAKEREQRKFLQHARTSNMICVREYFPDTFSAAVRQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 327 KSRWIIGIVFQGFKTHKWTSSLTLNYFLWRDRKGAISNFVSFLAMLVMLQLLLLLAYESLWPNAWHFLSIFSGSAWLMTL 406
Cdd:PRK11234 321 KSRWIIGIVFQGFKTLGWTSSLTLNYFLWRDRKGAITNFVSFLAMLLMLQLLLLLLYESLWPDAWHFLSIFSGSAWLMTL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 407 LWLNFGLMVNRIVQRVIFVTGYYGLTQGLLSVLRLFWGNLINFMANWRALKQVLQHGDPRRVAWDKTTHDFPSVTGDTRS 486
Cdd:PRK11234 401 LWLNFGLMVNRIVQRVIFVTGYYGLTQGLLSVLRLLWGNLINFMANWRALRQVLQHGDPRRVAWDKTTHDFPSVTGDTRS 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 487 LRPLGQILLENQVITEEQLDTALRNRVEGLRLGGSMLMQGLISAEQLAQALAEQNGVAWESIDAWQIPSSLIAEMPASVA 566
Cdd:PRK11234 481 LRPLGQILLENGVITEEQLDTALRNRVRGLRLGQSLLMQGLISAEQLAQALAEQNGVAWESLDPWQIPSSLIAEMPASVA 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 567 LHYAVLPLRLENDELIVGSEDGIDPVSLAALTRKVGRKVRYVIVLRGQIVTGLRHWYARRRGHDPRAMLYNAVQHQwlte 646
Cdd:PRK11234 561 LHYAVLPLREEGDELIVASEDGISPVSLAALTRKLGRKVRYVIVPRGQVTTGLRHWYARRRGHDPRAMLYNAVQHQ---- 636
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 647 QQTGEIWRQYVPHQFLFAEILTTLGHINRSAINVLLLRHERSSLPLGKFLVTEGVISQETLDRVLTIQRELQVSMQSLLL 726
Cdd:PRK11234 637 QQAGEIWRQYVPHQFLFAEILTTLGHIPRSAINVLLLRHERSSLPLGKFLVTEGVISQETLDRALTIQRELQVSMQSLLL 716
                        730
                 ....*....|.
gi 446306096 727 KAGLNTEQVAQ 737
Cdd:PRK11234 717 KAGLNTEQVAQ 727
nfrB PRK15489
glycosyl transferase family protein;
8-620 0e+00

glycosyl transferase family protein;


Pssm-ID: 237974 [Multi-domain]  Cd Length: 703  Bit Score: 612.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096   8 FATWLYGLKVIAITLAVIMFISGLDDFFIDVVYWVRRIKRKLSVYRRYPRMSYRELYKPDEKPLAIMVPAWNETGVIGNM 87
Cdd:PRK15489  10 LAHYYAVLETAAVATALVILISSLDDLFIDAWYWVRELYRWLTRERRYRPLTAEQLRERDEQPLAIMVPAWKEYDVIAKM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096  88 AELAATTLDYENYHIFVGTYPNDPDTQRDVDEVCARFPNVHKVVCARPGPTSKADCLNNVLDAITQFERSANFAFAGFIL 167
Cdd:PRK15489  90 IENMLATLDYRRYVIFVGTYPNDAETITEVERMRRRYKRLVRVEVPHDGPTCKADCLNWIIQAIFRYEAGHGIEFAGVIL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 168 HDAEDVISPMELRLFNYLVERKDLIQIPVYPFEREWTHFTSMTYIDEFSELHGKDVPVREALAGQVPSAGVGTCFSRRAV 247
Cdd:PRK15489 170 HDSEDVLHPLELKYFNYLLPRKDLVQLPVLSLERKWYEWVAGTYMDEFAEWHQKDLVVRESLTGTVPSAGVGTCFSRRAL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 248 TALLADGDGIAFDVQSLTEDYDIGFRLKEKGMTEIFVRFPVVDEAKEREQRKFLQHARTSNMICVREYFPDTFSTAVRQK 327
Cdd:PRK15489 250 LALMKERGNQPFNTSSLTEDYDFSFRLAELGMQEIFVRFPVQFRVRRTSWFGPRRERTREMLLCVREYFPDTFRTAYRQK 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 328 SRWIIGIVFQGFKTHKWTSSLTLNYFLWRDRKGAISNFVSFLAMLVMLQLLLLLAYESL-WpnaWH--FLSIFSGSAWLM 404
Cdd:PRK15489 330 ARWVLGIAFQGWEQMGWRGSLATRYLLFRDRKGIVTSLVSIIAYVLLLNFLLLAVLRRAgW---WTmsFPSLFVTGGWMQ 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 405 TLLWLNFGLMVNRIVQRVIFVTGYYGLTQGLLSVLRLFWGNLINFMANWRALKQVLQH---GdpRRVAWDKTTHDFPSVT 481
Cdd:PRK15489 407 YLLAANAVALANRLAQRFYFVGRLYGWEQGLLSIPRMVVGNFINFMAVCRAWRIFLIYlvtG--KPIVWDKTMHDFPSND 484
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 482 GDTRSLRPLGQILLENQVITEEQLDTALRNRVE-GLRLGGSMLMQGLISAEQLAQALAEQNGVAWESIDAwQIPSSLIAE 560
Cdd:PRK15489 485 ALGQTRRRLGELLLTWQAVTPEQLQAALAEQQTrGKPLGRILLSQGWLDDETLAEAIAFQADLPRVSLDN-VVLGALADC 563
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446306096 561 MPASVALHYAVLPLRLEND---ELIVGSEdgIDPVSLAALTRKVGRKVRYVIVLRGQIVTGLR 620
Cdd:PRK15489 564 LPRDLCVRWRVVPFSIGEDgtlNIAVASP--LPGEALQEVARAAGRKVAQFIARDSEISAELR 624
PRK14716 PRK14716
glycosyl transferase family protein;
1-512 0e+00

glycosyl transferase family protein;


Pssm-ID: 237800 [Multi-domain]  Cd Length: 504  Bit Score: 607.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096   1 MDWLLDVFATWLYGLKVIAITLAVIMFISGLDDFFIDVVYWVRRIKRKLsvyRRYPRMSYRELYKPDEKPLAIMVPAWNE 80
Cdd:PRK14716   1 RGWLVELIAAMLDALRVVLLVVAVLILLSGLDDLFIDAVYLARRLYRRR---SRIPRLSLATLRSVPEKRIAIFVPAWRE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096  81 TGVIGNMAELAATTLDYENYHIFVGTYPNDPDTQRDVDEVCARFPNVHKVVCARPGPTSKADCLNNVLDAITQFERSANF 160
Cdd:PRK14716  78 ADVIGRMLEHNLATLDYENYRIFVGTYPNDPATLREVDRLAARYPRVHLVIVPHDGPTSKADCLNWIYQAIFAFERERGI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 161 AFAGFILHDAEDVISPMELRLFNYLVERKDLIQIPVYPFEREWTHFTSMTYIDEFSELHGKDVPVREALAGQVPSAGVGT 240
Cdd:PRK14716 158 RFAIIVLHDAEDVIHPLELRLYNYLLPRHDFVQLPVFSLPRDWGEWVAGTYMDEFAESHLKDLPVREALGGLIPSAGVGT 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 241 CFSRRAVTALLADGDGIAFDVQSLTEDYDIGFRLKEKGMTEIFVRFPVVDEAKEREQRKflqhartsNMICVREYFPDTF 320
Cdd:PRK14716 238 AFSRRALERLAAERGGQPFDSDSLTEDYDIGLRLKRAGFRQIFVRVRADDTTDRPDRRG--------EPIATREFFPDTF 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 321 STAVRQKSRWIIGIVFQGFKTHKWTSSLTLNYFLWRDRKGAISNFVSFLAMLVMLQLLLLLAYESLWPNAWHFLSIFSGS 400
Cdd:PRK14716 310 KAAVRQKARWIYGIAFQGWERLGWKGPAATKYMLWRDRKGLLTNLLLFLAYLLLLLVALVLFGSWLGGWAWSYGSPLPPG 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 401 AWLMTLLWLNFGLMVNRIVQRVIFVTGYYGLTQGLLSVLRLFWGNLINFMANWRALKQVLQH-GDPRRVAWDKTTHDFPS 479
Cdd:PRK14716 390 PWLQALLWVNLAILLLRVLVRAYFVGRLYGWREALLSIPRMVVGNIINFAATARAWRLYIRSlLTGKPLVWDKTEHDFPS 469
                        490       500       510
                 ....*....|....*....|....*....|...
gi 446306096 480 VTGDTRSLRPLGQILLENQVITEEQLDTALRNR 512
Cdd:PRK14716 470 AEALAGVRRRLGDLLLSWRAASSADLPVALALR 502
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
164-368 2.67e-33

Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 126.68  E-value: 2.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096  164 GFILHDAEDVISPMELRLFNYLVER--KDLIQIPVYPfeREWTHFTSMTYIDEFSELHGKDVPVREALAGQVPSAGVGTC 241
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMASpeVAIIQGPILP--MNVGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096  242 FSRRAVTALladgdgIAFDVQSLTEDYDIGFRLKEKGMTEIFVrfpvvdeakereqrkflqhartsNMICVREYFPDTFS 321
Cdd:pfam13632  79 LRRSALQEV------GGWDDGSVSEDFDFGLRLQRAGYRVRFA-----------------------PYSAVYEKSPLTFR 129
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 446306096  322 TAVRQKSRWIIGI-VFQGFKTHKWTSSLTLNYFLWRDRKGAISNFVSF 368
Cdd:pfam13632 130 DFLRQRRRWAYGClLILLIRLLGYLGTLLWSGLPLALLLLLLFSISSL 177
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
71-333 4.19e-29

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 115.93  E-value: 4.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096   71 LAIMVPAWNETGVIGNMAElAATTLDYENYHIFVGTYPNDPDTQRDVDEVCARFPNVHKVVCAR---PGPTSKADCLNNV 147
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLE-AILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNarlLGPTGKSRGLNHG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096  148 LDAItqfersanfAFAGFILHDAEDVISPMELRLFNYLVERKDLIQIPVYPFEREWTHFTSMTYIDEFSELHGKDVPVRE 227
Cdd:pfam13641  83 FRAV---------KSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSLNRSTMLSALGALEFALRHLRMMSLRL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096  228 ALaGQVPSAGVGTCFSRRAVTALLadgdgiAFDVQ-SLTEDYDIGFRLKEKGmteifvrFPVVdeakereqrkFLQHARt 306
Cdd:pfam13641 154 AL-GVLPLSGAGSAIRREVLKELG------LFDPFfLLGDDKSLGRRLRRHG-------WRVA----------YAPDAA- 208
                         250       260
                  ....*....|....*....|....*..
gi 446306096  307 snmicVREYFPDTFSTAVRQKSRWIIG 333
Cdd:pfam13641 209 -----VRTVFPTYLAASIKQRARWVYG 230
T2SSE_N pfam05157
Type II secretion system (T2SS), protein E, N-terminal domain; This domain is found at the ...
522-629 1.18e-22

Type II secretion system (T2SS), protein E, N-terminal domain; This domain is found at the N-terminus of members of the Type II secretion system protein E. Proteins in this subfamily are typically involved in Type 4 pilus biogenesis, though some are involved in other processes; for instance aggregation in Myxococcus xanthus. The structure of this domain is now known.


Pssm-ID: 428339 [Multi-domain]  Cd Length: 108  Bit Score: 93.17  E-value: 1.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096  522 MLMQGLISAEQLAQALAEQNGVAWESIDAWQIPSSLIAEMPASVALHYAVLPLRLENDELIVGSEDGIDPVSLAALTRKV 601
Cdd:pfam05157   1 LVELGLLSEEQLAQALAEQLGLPFVDLEALEIDPELLRLLPREFARRHRVLPLREDGGTLVVAVADPLDLALLDELRFLT 80
                          90       100
                  ....*....|....*....|....*...
gi 446306096  602 GRKVRYVIVLRGQIVTGLRHWYARRRGH 629
Cdd:pfam05157  81 GKRVEPVLATPSDIRRALERLYGSEESL 108
PulE COG2804
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ...
485-627 2.89e-20

Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442055 [Multi-domain]  Cd Length: 561  Bit Score: 95.26  E-value: 2.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 485 RSLRPLGQILLENQVITEEQLDTALR-NRVEGLRLGGSMLMQGLISAEQLAQALAEQNGVAWESIDAWQIPSSLIAEMPA 563
Cdd:COG2804    4 SLLLRLGDLLVEAGLISEEQLLAALAeQKKTGKPLGELLVELGLVTEELLAEALAEQLGLPFVDLDELEIDPEVLELLPE 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446306096 564 SVALHYAVLPLRLENDELIVGSEDGIDPVSLAALTRKVGRKVRYVIVLRGQIVTGLRHWYARRR 627
Cdd:COG2804   84 ELARRHRVLPLRLEGGTLTVAMADPLDLEALDELRRLTGRPVEPVVATESDIERALDRLYGSES 147
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
57-355 1.14e-14

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 75.55  E-value: 1.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096  57 RMSYRELYKPDEKPLAIMVPAWNETGVIGNMAElAATTLDY--ENYHIFVGTYPNDPDTQRDVDEVCARFPNVHkvVCAR 134
Cdd:COG1215   17 ALARRRRAPADLPRVSVIIPAYNEEAVIEETLR-SLLAQDYpkEKLEVIVVDDGSTDETAEIARELAAEYPRVR--VIER 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 135 PGPTSKADCLNNVLDAitqfersANFAFagFILHDAEDVISPMELRLFnylverkdliqipVYPFEREwthftsmtyide 214
Cdd:COG1215   94 PENGGKAAALNAGLKA-------ARGDI--VVFLDADTVLDPDWLRRL-------------VAAFADP------------ 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 215 fselhgkdvpvrealagQVPSAGVGTCFSRRAVTALladgDGiaFDVQSLTEDYDIGFRLKEKGMTEIFVRFPVvdeake 294
Cdd:COG1215  140 -----------------GVGASGANLAFRREALEEV----GG--FDEDTLGEDLDLSLRLLRAGYRIVYVPDAV------ 190
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446306096 295 reqrkflqhartsnmicVREYFPDTFSTAVRQKSRWIIGIVFQGFKTHKWTSSLTLNYFLW 355
Cdd:COG1215  191 -----------------VYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPRRLLLFLL 234
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
73-267 8.82e-06

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 46.84  E-value: 8.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096  73 IMVPAWNETGVIGNMAElAATTLDYENYHIFVGTYpNDPDTQRDVDEVCARFPNVHKVVCARPGPTSKADCLNNVLdait 152
Cdd:cd06423    1 IIVPAYNEEAVIERTIE-SLLALDYPKLEVIVVDD-GSTDDTLEILEELAALYIRRVLVVRDKENGGKAGALNAGL---- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 153 qfeRSANFAFAGFIlhDAEDVISP-----MELRLFNYlverKDLIQI-----PVYPFEREWTHFTSMtyidEFSELHGKD 222
Cdd:cd06423   75 ---RHAKGDIVVVL--DADTILEPdalkrLVVPFFAD----PKVGAVqgrvrVRNGSENLLTRLQAI----EYLSIFRLG 141
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446306096 223 VPVREALAGQVPSAGVGTCFSRRAVTALLadgdgiAFDVQSLTED 267
Cdd:cd06423  142 RRAQSALGGVLVLSGAFGAFRREALREVG------GWDEDTLTED 180
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
73-333 8.70e-04

CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, Glucan Biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of glucan.


Pssm-ID: 133049 [Multi-domain]  Cd Length: 241  Bit Score: 41.47  E-value: 8.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096  73 IMVPAWNETGVIGN-MAELAAttLDY--ENYHIFVGTYPNDPDTQRDVdEVCARFPNVHKVVCARPGPTSKADCLNNVLd 149
Cdd:cd06427    5 ILVPLYKEAEVLPQlIASLSA--LDYprSKLDVKLLLEEDDEETIAAA-RALRLPSIFRVVVVPPSQPRTKPKACNYAL- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 150 aitqfersaNFAFAGFI-LHDAEDVISPMELR----LFNYLVERKDLIQIPVYPFEREWTHFTSMTYIdEFSELHGKDVP 224
Cdd:cd06427   81 ---------AFARGEYVvIYDAEDAPDPDQLKkavaAFARLDDKLACVQAPLNYYNARENWLTRMFAL-EYAAWFDYLLP 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096 225 VREALAGQVPSAGVGTCFSRRAVTALladgdGiAFDVQSLTEDYDIGFRLKEKGMTEIFVRFPVVDEAkereqrkflqha 304
Cdd:cd06427  151 GLARLGLPIPLGGTSNHFRTDVLREL-----G-GWDPFNVTEDADLGLRLARAGYRTGVLNSTTLEEA------------ 212
                        250       260
                 ....*....|....*....|....*....
gi 446306096 305 rtsnmicvreyfPDTFSTAVRQKSRWIIG 333
Cdd:cd06427  213 ------------NNALGNWIRQRSRWIKG 229
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
73-174 9.71e-03

N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine; N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase.


Pssm-ID: 133058 [Multi-domain]  Cd Length: 191  Bit Score: 38.13  E-value: 9.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446306096  73 IMVPAWNETGVIGnmAELAATTLDYENYHIFVGTYPNDPDTQRDVdEVCARFPNVHkvVCARPGP---TSKADCLNNVLD 149
Cdd:cd06436    1 VLVPCLNEEAVIQ--RTLASLLRNKPNFLVLVIDDASDDDTAGIV-RLAITDSRVH--LLRRHLPnarTGKGDALNAAYD 75
                         90       100
                 ....*....|....*....|....*
gi 446306096 150 AITQFERSANFafagfilhDAEDVI 174
Cdd:cd06436   76 QIRQILIEEGA--------DPERVI 92
 
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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