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Conserved domains on  [gi|334182477|ref|NP_172637|]
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starch synthase 3 [Arabidopsis thaliana]

Protein Classification

PLN02316 family protein( domain architecture ID 11476621)

PLN02316 family protein

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PLN02316 PLN02316
synthase/transferase
18-1042 0e+00

synthase/transferase


:

Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 1998.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   18 MAASGPKSSGPRGFGRRTTVGSAQKRTQKKNGEKDSNATSTATNEVSGISKLPAAKVDVQ-----------------KQS 80
Cdd:PLN02316    1 MSTSKPKGSAPRGFAPRTTVESSQKRIQQNNGDKEDSSTSTSSLSVSAVEKTSNAKEEIQvdfqhnsesaveeveaeDEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   81 SVVLNERNVLDRSDIEDGSDRLDKKTTDDDDLLEQKLKLERENLRRKEIETLAAENLARGDRMFVYPVIVKPDEDIEVFL 160
Cdd:PLN02316   81 EVEQNQSDVLKSSSIVKEESISTDMDGIDDDSLDRKLKLERENLRKREIEELAEENFSRGNKLFVYPQVVKPDSDIEVYL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  161 NRNLSTLNNEPDVLIMGAFNEWRWKSFTRRLEKTWIHEDWLSCLLHIPKEAYKMDFVFFNGQSVYDNNDSKDFCVEIKGG 240
Cdd:PLN02316  161 NRSLSTLANEPDVLIMGAFNGWRWKSFTERLEKTELGGDWWSCKLHIPKEAYKMDFVFFNGQNVYDNNDHKDFCVEIEGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  241 MDKVDFENFLLEEKLREQEKLAKEEAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQPAIKKAVVSAENVWYI 320
Cdd:PLN02316  241 MDEHSFEDFLLEEKRRELEKLAKEEAERERQAEEQRRREEEKAAMEADRAQAKAEVEKRREKLQNLLKKASRSADNVWYI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  321 EPSDFKAEDTVKLYYNKRSGPLTNSKELWLHGGFNNWVDGLSIVVKLVNAELKDvdpksGNWWFAEVVVPGGALVIDWVF 400
Cdd:PLN02316  321 EPSEFKAGDTVKLYYNRSSGPLAHSTEIWIHGGYNNWIDGLSIVEKLVKSEEKD-----GDWWYAEVVVPERALVLDWVF 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  401 ADGPPKGAFLYDNNGYQDFHALVPQKLPEELYWLEEENMIFRKLQEDRRLKEEVMRAKMEKTARLKAETKERTLKKFLLS 480
Cdd:PLN02316  396 ADGPPGNARNYDNNGRQDFHAIVPNNIPEELYWVEEEHQIYRKLQEERRLREEAIRAKAEKTARMKAEMKEKTLKMFLLS 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  481 QKDVVYTEPLEIQAGNPVTVLYNPANTVLNGKPEVWFRGSFNRWTHRLGPLPPQKMEATDDeSSHVKTTAKVPLDAYMMD 560
Cdd:PLN02316  476 QKHIVYTEPLEVQAGTTVTVLYNPANTVLNGKPEVWFRGSFNRWTHRLGPLPPQKMVPADN-GSHLKATVKVPLDAYMMD 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  561 FVFSEKEDGGIFDNKNGLDYHLPVVGGISKEPPLHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCI 640
Cdd:PLN02316  555 FVFSEKEEGGIFDNRNGLDYHIPVFGGIAKEPPMHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDCL 634
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  641 KHNFVKDLQFNRSYHWGGTEIKVWHGKVEGLSVYFLDPQNGLFQRGCVYGCADDAGRFGFFCHAALEFLLQGGFHPDILH 720
Cdd:PLN02316  635 NLSHVKDLHYQRSYSWGGTEIKVWFGKVEGLSVYFLEPQNGMFWAGCVYGCRNDGERFGFFCHAALEFLLQSGFHPDIIH 714
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  721 CHDWSSAPVSWLFKDHYTQYGLIKTRIVFTIHNLEFGANAIGKAMTFADKATTVSPTYAKEVAGNSVISAHLYKFHGIIN 800
Cdd:PLN02316  715 CHDWSSAPVAWLFKDHYAHYGLSKARVVFTIHNLEFGANHIGKAMAYADKATTVSPTYSREVSGNSAIAPHLYKFHGILN 794
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  801 GIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEELQNRLGLKSADFPVVGIITRLTHQKGIHLIKHAIWRTLERNGQVVL 880
Cdd:PLN02316  795 GIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEALQQRLGLKQADLPLVGIITRLTHQKGIHLIKHAIWRTLERNGQVVL 874
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  881 LGSAPDPRIQNDFVNLANQLHSSHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYGAVPVVRKTGGL 960
Cdd:PLN02316  875 LGSAPDPRIQNDFVNLANQLHSSHHDRARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIPVVRKTGGL 954
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  961 FDTVFDVDHDKERAQAQVLEPNGFSFDGADAPGVDYALNRAISAWYDGREWFNSLCKTVMEQDWSWNRPALEYLELYHSA 1040
Cdd:PLN02316  955 FDTVFDVDHDKERAQAQGLEPNGFSFDGADAAGVDYALNRAISAWYDGRDWFNSLCKRVMEQDWSWNRPALDYMELYHSA 1034

                  ..
gi 334182477 1041 RK 1042
Cdd:PLN02316 1035 RK 1036
 
Name Accession Description Interval E-value
PLN02316 PLN02316
synthase/transferase
18-1042 0e+00

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 1998.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   18 MAASGPKSSGPRGFGRRTTVGSAQKRTQKKNGEKDSNATSTATNEVSGISKLPAAKVDVQ-----------------KQS 80
Cdd:PLN02316    1 MSTSKPKGSAPRGFAPRTTVESSQKRIQQNNGDKEDSSTSTSSLSVSAVEKTSNAKEEIQvdfqhnsesaveeveaeDEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   81 SVVLNERNVLDRSDIEDGSDRLDKKTTDDDDLLEQKLKLERENLRRKEIETLAAENLARGDRMFVYPVIVKPDEDIEVFL 160
Cdd:PLN02316   81 EVEQNQSDVLKSSSIVKEESISTDMDGIDDDSLDRKLKLERENLRKREIEELAEENFSRGNKLFVYPQVVKPDSDIEVYL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  161 NRNLSTLNNEPDVLIMGAFNEWRWKSFTRRLEKTWIHEDWLSCLLHIPKEAYKMDFVFFNGQSVYDNNDSKDFCVEIKGG 240
Cdd:PLN02316  161 NRSLSTLANEPDVLIMGAFNGWRWKSFTERLEKTELGGDWWSCKLHIPKEAYKMDFVFFNGQNVYDNNDHKDFCVEIEGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  241 MDKVDFENFLLEEKLREQEKLAKEEAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQPAIKKAVVSAENVWYI 320
Cdd:PLN02316  241 MDEHSFEDFLLEEKRRELEKLAKEEAERERQAEEQRRREEEKAAMEADRAQAKAEVEKRREKLQNLLKKASRSADNVWYI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  321 EPSDFKAEDTVKLYYNKRSGPLTNSKELWLHGGFNNWVDGLSIVVKLVNAELKDvdpksGNWWFAEVVVPGGALVIDWVF 400
Cdd:PLN02316  321 EPSEFKAGDTVKLYYNRSSGPLAHSTEIWIHGGYNNWIDGLSIVEKLVKSEEKD-----GDWWYAEVVVPERALVLDWVF 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  401 ADGPPKGAFLYDNNGYQDFHALVPQKLPEELYWLEEENMIFRKLQEDRRLKEEVMRAKMEKTARLKAETKERTLKKFLLS 480
Cdd:PLN02316  396 ADGPPGNARNYDNNGRQDFHAIVPNNIPEELYWVEEEHQIYRKLQEERRLREEAIRAKAEKTARMKAEMKEKTLKMFLLS 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  481 QKDVVYTEPLEIQAGNPVTVLYNPANTVLNGKPEVWFRGSFNRWTHRLGPLPPQKMEATDDeSSHVKTTAKVPLDAYMMD 560
Cdd:PLN02316  476 QKHIVYTEPLEVQAGTTVTVLYNPANTVLNGKPEVWFRGSFNRWTHRLGPLPPQKMVPADN-GSHLKATVKVPLDAYMMD 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  561 FVFSEKEDGGIFDNKNGLDYHLPVVGGISKEPPLHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCI 640
Cdd:PLN02316  555 FVFSEKEEGGIFDNRNGLDYHIPVFGGIAKEPPMHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDCL 634
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  641 KHNFVKDLQFNRSYHWGGTEIKVWHGKVEGLSVYFLDPQNGLFQRGCVYGCADDAGRFGFFCHAALEFLLQGGFHPDILH 720
Cdd:PLN02316  635 NLSHVKDLHYQRSYSWGGTEIKVWFGKVEGLSVYFLEPQNGMFWAGCVYGCRNDGERFGFFCHAALEFLLQSGFHPDIIH 714
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  721 CHDWSSAPVSWLFKDHYTQYGLIKTRIVFTIHNLEFGANAIGKAMTFADKATTVSPTYAKEVAGNSVISAHLYKFHGIIN 800
Cdd:PLN02316  715 CHDWSSAPVAWLFKDHYAHYGLSKARVVFTIHNLEFGANHIGKAMAYADKATTVSPTYSREVSGNSAIAPHLYKFHGILN 794
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  801 GIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEELQNRLGLKSADFPVVGIITRLTHQKGIHLIKHAIWRTLERNGQVVL 880
Cdd:PLN02316  795 GIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEALQQRLGLKQADLPLVGIITRLTHQKGIHLIKHAIWRTLERNGQVVL 874
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  881 LGSAPDPRIQNDFVNLANQLHSSHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYGAVPVVRKTGGL 960
Cdd:PLN02316  875 LGSAPDPRIQNDFVNLANQLHSSHHDRARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIPVVRKTGGL 954
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  961 FDTVFDVDHDKERAQAQVLEPNGFSFDGADAPGVDYALNRAISAWYDGREWFNSLCKTVMEQDWSWNRPALEYLELYHSA 1040
Cdd:PLN02316  955 FDTVFDVDHDKERAQAQGLEPNGFSFDGADAAGVDYALNRAISAWYDGRDWFNSLCKRVMEQDWSWNRPALDYMELYHSA 1034

                  ..
gi 334182477 1041 RK 1042
Cdd:PLN02316 1035 RK 1036
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
595-1039 0e+00

Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.


Pssm-ID: 340822 [Multi-domain]  Cd Length: 474  Bit Score: 575.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  595 HIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKHNFVKDLQFNRS---YHWGGTEIKVWHGKVEGL 671
Cdd:cd03791     1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLGLevkVGGRGEEVGVFELPVDGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  672 SVYFLDPQNGLFQRG----CVYGCADDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYTQYGLIKTRI 747
Cdd:cd03791    81 DYYFLDNPEFFDRPGlpgpPGYDYPDNAERFAFFSRAALELLRRLGFQPDIIHANDWHTALVPAYLKTRYRGPGFKKIKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  748 VFTIHNLEFGA----------------------------NAIGKAMTFADKATTVSPTYAKEVA-------GNSVISAHL 792
Cdd:cd03791   161 VFTIHNLAYQGlfpldtlaelglppelfhidglefygqiNFLKAGIVYADRVTTVSPTYAKEILtpeygegLDGVLRARA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  793 YKFHGIINGIDPDIWDPYNDNFIPVPYtSENVVEGKRAAKEELQNRLGLK-SADFPVVGIITRLTHQKGIHLIKHAIWRT 871
Cdd:cd03791   241 GKLSGILNGIDYDEWNPATDKLIPANY-SANDLEGKAENKAALQKELGLPvDPDAPLFGFVGRLTEQKGVDLILDALPEL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  872 LERNGQVVLLGSApDPRIQNDFVNLANQlhssHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYGAV 951
Cdd:cd03791   320 LEEGGQLVVLGSG-DPEYEQAFRELAER----YPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRYGTL 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  952 PVVRKTGGLFDTVFDVDHDKEraqaqvlEPNGFSFDGADAPGVDYALNRAISAWYDgREWFNSLCKTVMEQDWSWNRPAL 1031
Cdd:cd03791   395 PIVRRTGGLADTVFDYDPETG-------EGTGFVFEDYDAEALLAALRRALALYRN-PELWRKLQKNAMKQDFSWDKSAK 466

                  ....*...
gi 334182477 1032 EYLELYHS 1039
Cdd:cd03791   467 EYLELYRS 474
GlgA COG0297
Glycogen synthase [Carbohydrate transport and metabolism];
594-1040 0e+00

Glycogen synthase [Carbohydrate transport and metabolism];


Pssm-ID: 440066 [Multi-domain]  Cd Length: 476  Bit Score: 540.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  594 LHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIK---HNFVKDLQFNRSYHWGGTEIKVWHGKVEG 670
Cdd:COG0297     1 MKILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSIDdklKDLEVVASLEVPLGGRTYYARVLEGPDDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  671 LSVYFLDpQNGLFQRGCVYG-----CADDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYTQYGLIKT 745
Cdd:COG0297    81 VPVYFID-NPELFDRPGPYGdpdrdYPDNAERFAFFSRAALELLKGLDWKPDIIHCHDWQTGLIPALLKTRYADDPFKRI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  746 RIVFTIHNLE----FGANAIGK------------------------AMTFADKATTVSPTYAKEV------AG-NSVISA 790
Cdd:COG0297   160 KTVFTIHNLAyqgiFPAEILELlglppelftpdglefygqinflkaGIVYADRVTTVSPTYAREIqtpefgEGlDGLLRA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  791 HLYKFHGIINGIDPDIWDPYNDNFIPVPYTSENVvEGKRAAKEELQNRLGLK-SADFPVVGIITRLTHQKGIHLIKHAIW 869
Cdd:COG0297   240 RSGKLSGILNGIDYDVWNPATDPYLPANYSADDL-EGKAANKAALQEELGLPvDPDAPLIGMVSRLTEQKGLDLLLEALD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  870 RTLERNGQVVLLGSApDPRIQNDFVNLANQlhssHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYG 949
Cdd:COG0297   319 ELLEEDVQLVVLGSG-DPEYEEAFRELAAR----YPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMYALRYG 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  950 AVPVVRKTGGLFDTVFDVDHDKERAqaqvlepNGFSFDGADAPGVDYALNRAISAWYDGREWfNSLCKTVMEQDWSWNRP 1029
Cdd:COG0297   394 TVPIVRRTGGLADTVIDYNEATGEG-------TGFVFDEYTAEALLAAIRRALALYRDPEAW-RKLQRNAMKQDFSWEKS 465
                         490
                  ....*....|.
gi 334182477 1030 ALEYLELYHSA 1040
Cdd:COG0297   466 AKEYLELYREL 476
glgA TIGR02095
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ...
594-1040 6.81e-164

glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 273969 [Multi-domain]  Cd Length: 473  Bit Score: 490.62  E-value: 6.81e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   594 LHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKHNFVKDLQFNRSY---HWGGTE-IKVWHGKVE 669
Cdd:TIGR02095    1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVDDQVKVVELVdlsVGPRTLyVKVFEGVVE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   670 GLSVYFLDPQnGLFQR-GCVYGCA--DDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYTQyglIKTR 746
Cdd:TIGR02095   81 GVPVYFIDNP-SLFDRpGGIYGDDypDNAERFAFFSRAAAELLSGLGWQPDVVHAHDWHTALVPALLKAVYRP---NPIK 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   747 IVFTIHNLE----FGANAIGK------------------------AMTFADKATTVSPTYAKEV----AG---NSVISAH 791
Cdd:TIGR02095  157 TVFTIHNLAyqgvFPADDFSElglppeyfhmeglefygrvnflkgGIVYADRVTTVSPTYAREIltpeFGyglDGVLKAR 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   792 LYKFHGIINGIDPDIWDPYNDNFIPVPYTSENVvEGKRAAKEELQNRLGLK-SADFPVVGIITRLTHQKGIHLIKHAIWR 870
Cdd:TIGR02095  237 SGKLRGILNGIDTEVWNPATDPYLKANYSADDL-AGKAENKEALQEELGLPvDDDVPLFGVISRLTQQKGVDLLLAALPE 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   871 TLERNGQVVLLGSApDPRIQNDFVNLANQlhssHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYGA 950
Cdd:TIGR02095  316 LLELGGQLVVLGTG-DPELEEALRELAER----YPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYAMRYGT 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   951 VPVVRKTGGLFDTVFDVDHDKERAqaqvlepNGFSFDGADAPGVDYALNRAISAWYDGREWFNSLCKTVMEQDWSWNRPA 1030
Cdd:TIGR02095  391 VPIVRRTGGLADTVVDGDPEAESG-------TGFLFEEYDPGALLAALSRALRLYRQDPSLWEALQKNAMSQDFSWDKSA 463
                          490
                   ....*....|
gi 334182477  1031 LEYLELYHSA 1040
Cdd:TIGR02095  464 KQYVELYRSL 473
Glyco_transf_5 pfam08323
Starch synthase catalytic domain;
596-782 6.72e-63

Starch synthase catalytic domain;


Pssm-ID: 400563 [Multi-domain]  Cd Length: 239  Bit Score: 213.35  E-value: 6.72e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   596 IVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKHN-----FVKDLQFNRSYHWGGTEIKVWHGKVEG 670
Cdd:pfam08323    1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPEErnqleDVIRLSVAAGVPVRPLTVGVARLELDG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   671 LSVYFLDPQNgLFQRGCVYGC-----ADDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYTQYGLIKT 745
Cdd:pfam08323   81 VDVYFLDNPD-YFDRPGLYGDdgrdyEDNAERFAFFSRAALELAKKLGWIPDIIHCHDWHTALVPAYLKEAYADDPFKNI 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334182477   746 RIVFTIHNLEFG----------------------------ANAIGKAMTFADKATTVSPTYAKEV 782
Cdd:pfam08323  160 KTVFTIHNLAYQgrfpadlldllglppedfnldglefygqINFLKAGIVYADAVTTVSPTYAEEI 224
CBM_25 smart01066
Carbohydrate binding domain;
153-238 2.90e-23

Carbohydrate binding domain;


Pssm-ID: 198134 [Multi-domain]  Cd Length: 83  Bit Score: 94.73  E-value: 2.90e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477    153 DEDIEVFLNRNLSTLNNEPDVLIMGaFNEWRWKSFTRRLEKTWiHEDWLSCLLHIpKEAYKMDFVFFNGQSVYDNNDSKD 232
Cdd:smart01066    1 GNTVTVYYNGLLATSGAKNVYLHYG-FGENNWTDVPDVRMEKT-GEGWVKATIPV-KEAYKLNFCFKDGAGNWDNNGGAN 77

                    ....*.
gi 334182477    233 FCVEIK 238
Cdd:smart01066   78 YHFEIG 83
 
Name Accession Description Interval E-value
PLN02316 PLN02316
synthase/transferase
18-1042 0e+00

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 1998.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   18 MAASGPKSSGPRGFGRRTTVGSAQKRTQKKNGEKDSNATSTATNEVSGISKLPAAKVDVQ-----------------KQS 80
Cdd:PLN02316    1 MSTSKPKGSAPRGFAPRTTVESSQKRIQQNNGDKEDSSTSTSSLSVSAVEKTSNAKEEIQvdfqhnsesaveeveaeDEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   81 SVVLNERNVLDRSDIEDGSDRLDKKTTDDDDLLEQKLKLERENLRRKEIETLAAENLARGDRMFVYPVIVKPDEDIEVFL 160
Cdd:PLN02316   81 EVEQNQSDVLKSSSIVKEESISTDMDGIDDDSLDRKLKLERENLRKREIEELAEENFSRGNKLFVYPQVVKPDSDIEVYL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  161 NRNLSTLNNEPDVLIMGAFNEWRWKSFTRRLEKTWIHEDWLSCLLHIPKEAYKMDFVFFNGQSVYDNNDSKDFCVEIKGG 240
Cdd:PLN02316  161 NRSLSTLANEPDVLIMGAFNGWRWKSFTERLEKTELGGDWWSCKLHIPKEAYKMDFVFFNGQNVYDNNDHKDFCVEIEGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  241 MDKVDFENFLLEEKLREQEKLAKEEAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQPAIKKAVVSAENVWYI 320
Cdd:PLN02316  241 MDEHSFEDFLLEEKRRELEKLAKEEAERERQAEEQRRREEEKAAMEADRAQAKAEVEKRREKLQNLLKKASRSADNVWYI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  321 EPSDFKAEDTVKLYYNKRSGPLTNSKELWLHGGFNNWVDGLSIVVKLVNAELKDvdpksGNWWFAEVVVPGGALVIDWVF 400
Cdd:PLN02316  321 EPSEFKAGDTVKLYYNRSSGPLAHSTEIWIHGGYNNWIDGLSIVEKLVKSEEKD-----GDWWYAEVVVPERALVLDWVF 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  401 ADGPPKGAFLYDNNGYQDFHALVPQKLPEELYWLEEENMIFRKLQEDRRLKEEVMRAKMEKTARLKAETKERTLKKFLLS 480
Cdd:PLN02316  396 ADGPPGNARNYDNNGRQDFHAIVPNNIPEELYWVEEEHQIYRKLQEERRLREEAIRAKAEKTARMKAEMKEKTLKMFLLS 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  481 QKDVVYTEPLEIQAGNPVTVLYNPANTVLNGKPEVWFRGSFNRWTHRLGPLPPQKMEATDDeSSHVKTTAKVPLDAYMMD 560
Cdd:PLN02316  476 QKHIVYTEPLEVQAGTTVTVLYNPANTVLNGKPEVWFRGSFNRWTHRLGPLPPQKMVPADN-GSHLKATVKVPLDAYMMD 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  561 FVFSEKEDGGIFDNKNGLDYHLPVVGGISKEPPLHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCI 640
Cdd:PLN02316  555 FVFSEKEEGGIFDNRNGLDYHIPVFGGIAKEPPMHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDCL 634
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  641 KHNFVKDLQFNRSYHWGGTEIKVWHGKVEGLSVYFLDPQNGLFQRGCVYGCADDAGRFGFFCHAALEFLLQGGFHPDILH 720
Cdd:PLN02316  635 NLSHVKDLHYQRSYSWGGTEIKVWFGKVEGLSVYFLEPQNGMFWAGCVYGCRNDGERFGFFCHAALEFLLQSGFHPDIIH 714
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  721 CHDWSSAPVSWLFKDHYTQYGLIKTRIVFTIHNLEFGANAIGKAMTFADKATTVSPTYAKEVAGNSVISAHLYKFHGIIN 800
Cdd:PLN02316  715 CHDWSSAPVAWLFKDHYAHYGLSKARVVFTIHNLEFGANHIGKAMAYADKATTVSPTYSREVSGNSAIAPHLYKFHGILN 794
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  801 GIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEELQNRLGLKSADFPVVGIITRLTHQKGIHLIKHAIWRTLERNGQVVL 880
Cdd:PLN02316  795 GIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEALQQRLGLKQADLPLVGIITRLTHQKGIHLIKHAIWRTLERNGQVVL 874
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  881 LGSAPDPRIQNDFVNLANQLHSSHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYGAVPVVRKTGGL 960
Cdd:PLN02316  875 LGSAPDPRIQNDFVNLANQLHSSHHDRARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIPVVRKTGGL 954
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  961 FDTVFDVDHDKERAQAQVLEPNGFSFDGADAPGVDYALNRAISAWYDGREWFNSLCKTVMEQDWSWNRPALEYLELYHSA 1040
Cdd:PLN02316  955 FDTVFDVDHDKERAQAQGLEPNGFSFDGADAAGVDYALNRAISAWYDGRDWFNSLCKRVMEQDWSWNRPALDYMELYHSA 1034

                  ..
gi 334182477 1041 RK 1042
Cdd:PLN02316 1035 RK 1036
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
595-1039 0e+00

Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.


Pssm-ID: 340822 [Multi-domain]  Cd Length: 474  Bit Score: 575.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  595 HIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKHNFVKDLQFNRS---YHWGGTEIKVWHGKVEGL 671
Cdd:cd03791     1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLGLevkVGGRGEEVGVFELPVDGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  672 SVYFLDPQNGLFQRG----CVYGCADDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYTQYGLIKTRI 747
Cdd:cd03791    81 DYYFLDNPEFFDRPGlpgpPGYDYPDNAERFAFFSRAALELLRRLGFQPDIIHANDWHTALVPAYLKTRYRGPGFKKIKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  748 VFTIHNLEFGA----------------------------NAIGKAMTFADKATTVSPTYAKEVA-------GNSVISAHL 792
Cdd:cd03791   161 VFTIHNLAYQGlfpldtlaelglppelfhidglefygqiNFLKAGIVYADRVTTVSPTYAKEILtpeygegLDGVLRARA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  793 YKFHGIINGIDPDIWDPYNDNFIPVPYtSENVVEGKRAAKEELQNRLGLK-SADFPVVGIITRLTHQKGIHLIKHAIWRT 871
Cdd:cd03791   241 GKLSGILNGIDYDEWNPATDKLIPANY-SANDLEGKAENKAALQKELGLPvDPDAPLFGFVGRLTEQKGVDLILDALPEL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  872 LERNGQVVLLGSApDPRIQNDFVNLANQlhssHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYGAV 951
Cdd:cd03791   320 LEEGGQLVVLGSG-DPEYEQAFRELAER----YPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRYGTL 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  952 PVVRKTGGLFDTVFDVDHDKEraqaqvlEPNGFSFDGADAPGVDYALNRAISAWYDgREWFNSLCKTVMEQDWSWNRPAL 1031
Cdd:cd03791   395 PIVRRTGGLADTVFDYDPETG-------EGTGFVFEDYDAEALLAALRRALALYRN-PELWRKLQKNAMKQDFSWDKSAK 466

                  ....*...
gi 334182477 1032 EYLELYHS 1039
Cdd:cd03791   467 EYLELYRS 474
GlgA COG0297
Glycogen synthase [Carbohydrate transport and metabolism];
594-1040 0e+00

Glycogen synthase [Carbohydrate transport and metabolism];


Pssm-ID: 440066 [Multi-domain]  Cd Length: 476  Bit Score: 540.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  594 LHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIK---HNFVKDLQFNRSYHWGGTEIKVWHGKVEG 670
Cdd:COG0297     1 MKILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSIDdklKDLEVVASLEVPLGGRTYYARVLEGPDDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  671 LSVYFLDpQNGLFQRGCVYG-----CADDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYTQYGLIKT 745
Cdd:COG0297    81 VPVYFID-NPELFDRPGPYGdpdrdYPDNAERFAFFSRAALELLKGLDWKPDIIHCHDWQTGLIPALLKTRYADDPFKRI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  746 RIVFTIHNLE----FGANAIGK------------------------AMTFADKATTVSPTYAKEV------AG-NSVISA 790
Cdd:COG0297   160 KTVFTIHNLAyqgiFPAEILELlglppelftpdglefygqinflkaGIVYADRVTTVSPTYAREIqtpefgEGlDGLLRA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  791 HLYKFHGIINGIDPDIWDPYNDNFIPVPYTSENVvEGKRAAKEELQNRLGLK-SADFPVVGIITRLTHQKGIHLIKHAIW 869
Cdd:COG0297   240 RSGKLSGILNGIDYDVWNPATDPYLPANYSADDL-EGKAANKAALQEELGLPvDPDAPLIGMVSRLTEQKGLDLLLEALD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  870 RTLERNGQVVLLGSApDPRIQNDFVNLANQlhssHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYG 949
Cdd:COG0297   319 ELLEEDVQLVVLGSG-DPEYEEAFRELAAR----YPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMYALRYG 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  950 AVPVVRKTGGLFDTVFDVDHDKERAqaqvlepNGFSFDGADAPGVDYALNRAISAWYDGREWfNSLCKTVMEQDWSWNRP 1029
Cdd:COG0297   394 TVPIVRRTGGLADTVIDYNEATGEG-------TGFVFDEYTAEALLAAIRRALALYRDPEAW-RKLQRNAMKQDFSWEKS 465
                         490
                  ....*....|.
gi 334182477 1030 ALEYLELYHSA 1040
Cdd:COG0297   466 AKEYLELYREL 476
glgA PRK00654
glycogen synthase GlgA;
594-1042 7.44e-180

glycogen synthase GlgA;


Pssm-ID: 234809 [Multi-domain]  Cd Length: 466  Bit Score: 531.62  E-value: 7.44e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  594 LHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKHNFVKDLQFNRsyhWGGTEIKVWHGKVEGLSV 673
Cdd:PRK00654    1 MKILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGYPAIREKLRDAQVVGR---LDLFTVLFGHLEGDGVPV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  674 YFLDPQNgLFQRGCVYGCADDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSA--PVsWLFKDHYTQYGLIKTriVFTI 751
Cdd:PRK00654   78 YLIDAPH-LFDRPSGYGYPDNGERFAFFSWAAAEFAEGLDPRPDIVHAHDWHTGliPA-LLKEKYWRGYPDIKT--VFTI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  752 HNLE----FGANAIG-----------------------KA-MTFADKATTVSPTYAKEV---------AGnsVISAHLYK 794
Cdd:PRK00654  154 HNLAyqglFPAEILGelglpaeafhleglefygqisflKAgLYYADRVTTVSPTYAREIttpefgyglEG--LLRARSGK 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  795 FHGIINGIDPDIWDPYNDNFIPVPYTSENVvEGKRAAKEELQNRLGLKSADFPVVGIITRLTHQKGIHLIKHAIWRTLER 874
Cdd:PRK00654  232 LSGILNGIDYDIWNPETDPLLAANYSADDL-EGKAENKRALQERFGLPDDDAPLFAMVSRLTEQKGLDLVLEALPELLEQ 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  875 NGQVVLLGSaPDPRIQNDFVNLANQlhssHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYGAVPVV 954
Cdd:PRK00654  311 GGQLVLLGT-GDPELEEAFRALAAR----YPGKVGVQIGYDEALAHRIYAGADMFLMPSRFEPCGLTQLYALRYGTLPIV 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  955 RKTGGLFDTVFDVDHDKERAqaqvlepNGFSFDGADAPGVDYALNRAISAWYDGREWfNSLCKTVMEQDWSWNRPALEYL 1034
Cdd:PRK00654  386 RRTGGLADTVIDYNPEDGEA-------TGFVFDDFNAEDLLRALRRALELYRQPPLW-RALQRQAMAQDFSWDKSAEEYL 457

                  ....*...
gi 334182477 1035 ELYHSARK 1042
Cdd:PRK00654  458 ELYRRLLG 465
glgA TIGR02095
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ...
594-1040 6.81e-164

glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 273969 [Multi-domain]  Cd Length: 473  Bit Score: 490.62  E-value: 6.81e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   594 LHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKHNFVKDLQFNRSY---HWGGTE-IKVWHGKVE 669
Cdd:TIGR02095    1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVDDQVKVVELVdlsVGPRTLyVKVFEGVVE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   670 GLSVYFLDPQnGLFQR-GCVYGCA--DDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYTQyglIKTR 746
Cdd:TIGR02095   81 GVPVYFIDNP-SLFDRpGGIYGDDypDNAERFAFFSRAAAELLSGLGWQPDVVHAHDWHTALVPALLKAVYRP---NPIK 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   747 IVFTIHNLE----FGANAIGK------------------------AMTFADKATTVSPTYAKEV----AG---NSVISAH 791
Cdd:TIGR02095  157 TVFTIHNLAyqgvFPADDFSElglppeyfhmeglefygrvnflkgGIVYADRVTTVSPTYAREIltpeFGyglDGVLKAR 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   792 LYKFHGIINGIDPDIWDPYNDNFIPVPYTSENVvEGKRAAKEELQNRLGLK-SADFPVVGIITRLTHQKGIHLIKHAIWR 870
Cdd:TIGR02095  237 SGKLRGILNGIDTEVWNPATDPYLKANYSADDL-AGKAENKEALQEELGLPvDDDVPLFGVISRLTQQKGVDLLLAALPE 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   871 TLERNGQVVLLGSApDPRIQNDFVNLANQlhssHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYGA 950
Cdd:TIGR02095  316 LLELGGQLVVLGTG-DPELEEALRELAER----YPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYAMRYGT 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   951 VPVVRKTGGLFDTVFDVDHDKERAqaqvlepNGFSFDGADAPGVDYALNRAISAWYDGREWFNSLCKTVMEQDWSWNRPA 1030
Cdd:TIGR02095  391 VPIVRRTGGLADTVVDGDPEAESG-------TGFLFEEYDPGALLAALSRALRLYRQDPSLWEALQKNAMSQDFSWDKSA 463
                          490
                   ....*....|
gi 334182477  1031 LEYLELYHSA 1040
Cdd:TIGR02095  464 KQYVELYRSL 473
PLN02939 PLN02939
transferase, transferring glycosyl groups
594-1040 1.67e-152

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 478.24  E-value: 1.67e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  594 LHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKHNFVKDLQ----FNRSYHWGGT-EIKVWHGKV 668
Cdd:PLN02939  482 LHIVHIAAEMAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKYDCMQYDQIRNLKvldvVVESYFDGNLfKNKIWTGTV 561
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  669 EGLSVYFLDPQN--GLFQRGCVYGCADDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYTQYGLIKTR 746
Cdd:PLN02939  562 EGLPVYFIEPQHpsKFFWRAQYYGEHDDFKRFSYFSRAALELLYQSGKKPDIIHCHDWQTAFVAPLYWDLYAPKGFNSAR 641
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  747 IVFTIHNLEFGA-------------------------------NAIGKAMTFADKATTVSPTYAKEVAG------NSVIS 789
Cdd:PLN02939  642 ICFTCHNFEYQGtapasdlascgldvhqldrpdrmqdnahgriNVVKGAIVYSNIVTTVSPTYAQEVRSeggrglQDTLK 721
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  790 AHLYKFHGIINGIDPDIWDPYNDNFIPVPYtSENVVEGKRAAKEELQNRLGLKSADF--PVVGIITRLTHQKGIHLIKHA 867
Cdd:PLN02939  722 FHSKKFVGILNGIDTDTWNPSTDRFLKVQY-NANDLQGKAANKAALRKQLGLSSADAsqPLVGCITRLVPQKGVHLIRHA 800
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  868 IWRTLERNGQVVLLGSAPDPRIQNDFVNLANQLHSShgDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMR 947
Cdd:PLN02939  801 IYKTAELGGQFVLLGSSPVPHIQREFEGIADQFQSN--NNIRLILKYDEALSHSIYAASDMFIIPSMFEPCGLTQMIAMR 878
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  948 YGAVPVVRKTGGLFDTVFDVDHDKERAQAQvlepNGFSFDGADAPGVDYALNRAISAWYDGREWFNSLCKTVMEQDWSWN 1027
Cdd:PLN02939  879 YGSVPIVRKTGGLNDSVFDFDDETIPVELR----NGFTFLTPDEQGLNSALERAFNYYKRKPEVWKQLVQKDMNIDFSWD 954
                         490
                  ....*....|...
gi 334182477 1028 RPALEYLELYHSA 1040
Cdd:PLN02939  955 SSASQYEELYQRA 967
PRK14099 PRK14099
glycogen synthase GlgA;
593-1039 6.63e-78

glycogen synthase GlgA;


Pssm-ID: 237610 [Multi-domain]  Cd Length: 485  Bit Score: 263.89  E-value: 6.63e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  593 PLHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKHNFVKDLQFNRSYHWGGTEIKVWHGKVEGLS 672
Cdd:PRK14099    3 PLRVLSVASEIFPLIKTGGLADVAGALPAALKAHGVEVRTLVPGYPAVLAGIEDAEQVHSFPDLFGGPARLLAARAGGLD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  673 VYFLDPQNgLFQR-GCVY------GCADDAGRFGFFCHAA--LEFLLQGGFHPDILHCHDWSSAPV-SWLfkdHYTQYGL 742
Cdd:PRK14099   83 LFVLDAPH-LYDRpGNPYvgpdgkDWPDNAQRFAALARAAaaIGQGLVPGFVPDIVHAHDWQAGLApAYL---HYSGRPA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  743 IKTriVFTIHNLEF---------GA----------------NAIG--KA-MTFADKATTVSPTYAKEVAG-------NSV 787
Cdd:PRK14099  159 PGT--VFTIHNLAFqgqfprellGAlglppsafsldgveyyGGIGylKAgLQLADRITTVSPTYALEIQGpeagmglDGL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  788 ISAHLYKFHGIINGIDPDIWDPYNDNFIPVPYTSENVvEGKRAAKEELQNRLGLKSA-DFPVVGIITRLTHQKGIHLIKH 866
Cdd:PRK14099  237 LRQRADRLSGILNGIDTAVWNPATDELIAATYDVETL-AARAANKAALQARFGLDPDpDALLLGVISRLSWQKGLDLLLE 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  867 AIwRTLERNG-QVVLLGSApDPRIQNDFVNLAnqlhSSHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIA 945
Cdd:PRK14099  316 AL-PTLLGEGaQLALLGSG-DAELEARFRAAA----QAYPGQIGVVIGYDEALAHLIQAGADALLVPSRFEPCGLTQLCA 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  946 MRYGAVPVVRKTGGLFDTVFDVDhdkERAQAQVLePNGFSFDGADAPGVDYALNRAISAWYDGREWFNsLCKTVMEQDWS 1025
Cdd:PRK14099  390 LRYGAVPVVARVGGLADTVVDAN---EMAIATGV-ATGVQFSPVTADALAAALRKTAALFADPVAWRR-LQRNGMTTDVS 464
                         490
                  ....*....|....
gi 334182477 1026 WNRPALEYLELYHS 1039
Cdd:PRK14099  465 WRNPAQHYAALYRS 478
Glyco_transf_5 pfam08323
Starch synthase catalytic domain;
596-782 6.72e-63

Starch synthase catalytic domain;


Pssm-ID: 400563 [Multi-domain]  Cd Length: 239  Bit Score: 213.35  E-value: 6.72e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   596 IVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKHN-----FVKDLQFNRSYHWGGTEIKVWHGKVEG 670
Cdd:pfam08323    1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPEErnqleDVIRLSVAAGVPVRPLTVGVARLELDG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   671 LSVYFLDPQNgLFQRGCVYGC-----ADDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYTQYGLIKT 745
Cdd:pfam08323   81 VDVYFLDNPD-YFDRPGLYGDdgrdyEDNAERFAFFSRAALELAKKLGWIPDIIHCHDWHTALVPAYLKEAYADDPFKNI 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334182477   746 RIVFTIHNLEFG----------------------------ANAIGKAMTFADKATTVSPTYAKEV 782
Cdd:pfam08323  160 KTVFTIHNLAYQgrfpadlldllglppedfnldglefygqINFLKAGIVYADAVTTVSPTYAEEI 224
PRK14098 PRK14098
starch synthase;
596-1037 7.89e-56

starch synthase;


Pssm-ID: 172588 [Multi-domain]  Cd Length: 489  Bit Score: 201.89  E-value: 7.89e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  596 IVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKhnfvkDLQFNRSYHWGGTEIKV--------WHGK 667
Cdd:PRK14098    8 VLYVSGEVSPFVRVSALADFMASFPQALEEEGFEARIMMPKYGTIN-----DRKFRLHDVLRLSDIEVplkektdlLHVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  668 VEGL-----SVYFL-----DPQNGLF----QRGCVYGCADdagRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLF 733
Cdd:PRK14098   83 VTALpsskiQTYFLynekyFKRNGLFtdmsLGGDLKGSAE---KVIFFNVGVLETLQRLGWKPDIIHCHDWYAGLVPLLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  734 KDHYTQYGLIK-TRIVFTIHN------LEFGA--------------------NAIGKAMTFADKATTVSPTYAKEVAGNS 786
Cdd:PRK14098  160 KTVYADHEFFKdIKTVLTIHNvyrqgvLPFKVfqkllpeevcsglhregdevNMLYTGVEHADLLTTTSPRYAEEIAGDG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  787 --------VISAHLYKFHGIINGIDPDIWDPYNDNFIPVPYTSENVvEGKRAAKEELQNRLGLK-SADFPVVGIITRLTH 857
Cdd:PRK14098  240 eeafgldkVLEERKMRLHGILNGIDTRQWNPSTDKLIKKRYSIERL-DGKLENKKALLEEVGLPfDEETPLVGVIINFDD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  858 QKGIHLIKHAIWRTLERNGQVVLLGSApDPRIQNDFVNLANQlhssHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEP 937
Cdd:PRK14098  319 FQGAELLAESLEKLVELDIQLVICGSG-DKEYEKRFQDFAEE----HPEQVSVQTEFTDAFFHLAIAGLDMLLMPGKIES 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  938 CGLTQLIAMRYGAVPVVRKTGGLFDTVFDVDHDKEraqaqvlepNGFSFDGADAPGVDYALNRAISAWYDGREWfNSLCK 1017
Cdd:PRK14098  394 CGMLQMFAMSYGTIPVAYAGGGIVETIEEVSEDKG---------SGFIFHDYTPEALVAKLGEALALYHDEERW-EELVL 463
                         490       500
                  ....*....|....*....|
gi 334182477 1018 TVMEQDWSWNRPALEYLELY 1037
Cdd:PRK14098  464 EAMERDFSWKNSAEEYAQLY 483
CBM_25 smart01066
Carbohydrate binding domain;
153-238 2.90e-23

Carbohydrate binding domain;


Pssm-ID: 198134 [Multi-domain]  Cd Length: 83  Bit Score: 94.73  E-value: 2.90e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477    153 DEDIEVFLNRNLSTLNNEPDVLIMGaFNEWRWKSFTRRLEKTWiHEDWLSCLLHIpKEAYKMDFVFFNGQSVYDNNDSKD 232
Cdd:smart01066    1 GNTVTVYYNGLLATSGAKNVYLHYG-FGENNWTDVPDVRMEKT-GEGWVKATIPV-KEAYKLNFCFKDGAGNWDNNGGAN 77

                    ....*.
gi 334182477    233 FCVEIK 238
Cdd:smart01066   78 YHFEIG 83
CBM_25 smart01066
Carbohydrate binding domain;
495-584 1.90e-19

Carbohydrate binding domain;


Pssm-ID: 198134 [Multi-domain]  Cd Length: 83  Bit Score: 83.56  E-value: 1.90e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477    495 GNPVTVLYNPANTVlNGKPEVWFRGSF--NRWTHrlgpLPPQKMEATDDesSHVKTTAKVpLDAYMMDFVFseKEDGGIF 572
Cdd:smart01066    1 GNTVTVYYNGLLAT-SGAKNVYLHYGFgeNNWTD----VPDVRMEKTGE--GWVKATIPV-KEAYKLNFCF--KDGAGNW 70
                            90
                    ....*....|..
gi 334182477    573 DNKNGLDYHLPV 584
Cdd:smart01066   71 DNNGGANYHFEI 82
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
714-1038 2.49e-18

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 87.98  E-value: 2.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  714 FHPDILHCHDWSSAPVSWLFKdhytqyGLIKTRIVFTIHNLEFGAN------------AIGKAMTFADKATTVSPTYAKE 781
Cdd:cd03801    81 RKFDVVHAHGLLAALLAALLA------LLLGAPLVVTLHGAEPGRLllllaaerrllaRAEALLRRADAVIAVSEALRDE 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  782 VAGNSVISAHlyKFHGIINGIDPDIWDPyndnfipvpytsenvvegkraakeeLQNRLGLKSADFPVVGIITRLTHQKGI 861
Cdd:cd03801   155 LRALGGIPPE--KIVVIPNGVDLERFSP-------------------------PLRRKLGIPPDRPVLLFVGRLSPRKGV 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  862 HLIKHAIWRTLERNGQVVLLGSAPDPRIQNDFVNLANQLhsshGDRARLV--LTYDEPLShlIYAGADFILVPSIFEPCG 939
Cdd:cd03801   208 DLLLEALAKLLRRGPDVRLVIVGGDGPLRAELEELELGL----GDRVRFLgfVPDEELPA--LYAAADVFVLPSRYEGFG 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  940 LTQLIAMRYGaVPVVrktgglfdtVFDVDHDKEraqAQVLEPNGFSFDGADAPgvdyALNRAISAWYDGREWFNSLCK-- 1017
Cdd:cd03801   282 LVVLEAMAAG-LPVV---------ATDVGGLPE---VVEDGEGGLVVPPDDVE----ALADALLRLLADPELRARLGRaa 344
                         330       340
                  ....*....|....*....|..
gi 334182477 1018 -TVMEQDWSWNRPALEYLELYH 1038
Cdd:cd03801   345 rERVAERFSWERVAERLLDLYR 366
CBM53 pfam16760
Starch/carbohydrate-binding module (family 53);
332-421 1.58e-17

Starch/carbohydrate-binding module (family 53);


Pssm-ID: 465261 [Multi-domain]  Cd Length: 76  Bit Score: 78.10  E-value: 1.58e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   332 KLYYNKrsgplTNSKELWLHGGFNNWVDGLSIVVKlvnaelKDVDPKSGNWWFAEVVVPGGALVIDWVFADgppkGAFLY 411
Cdd:pfam16760    1 NIYYNG-----SLAKEVYIHGGFNGWKNVQDVPME------KLPPTGGGDWFSATVPVPEDAYVLDFVFKD----GAGNW 65
                           90
                   ....*....|
gi 334182477   412 DNNGYQDFHA 421
Cdd:pfam16760   66 DNNNGQNYHI 75
CBM_25 smart01066
Carbohydrate binding domain;
328-424 1.74e-17

Carbohydrate binding domain;


Pssm-ID: 198134 [Multi-domain]  Cd Length: 83  Bit Score: 78.17  E-value: 1.74e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477    328 EDTVKLYYNKRSGPlTNSKELWLHGGF--NNWVDglsivvkLVNAELKdvdpKSGNWWFAEVVVPGGALVIDWVFADgpp 405
Cdd:smart01066    1 GNTVTVYYNGLLAT-SGAKNVYLHYGFgeNNWTD-------VPDVRME----KTGEGWVKATIPVKEAYKLNFCFKD--- 65
                            90
                    ....*....|....*....
gi 334182477    406 kGAFLYDNNGYQDFHALVP 424
Cdd:smart01066   66 -GAGNWDNNGGANYHFEIG 83
CBM53 pfam16760
Starch/carbohydrate-binding module (family 53);
158-236 3.16e-17

Starch/carbohydrate-binding module (family 53);


Pssm-ID: 465261 [Multi-domain]  Cd Length: 76  Bit Score: 76.95  E-value: 3.16e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   158 VFLNRNLStlnnePDVLIMGAFNEWRWKSFTRrLEKT--WIHEDWLSCLLHIPKEAYKMDFVFFNGQSVYDNNDSKDFCV 235
Cdd:pfam16760    2 IYYNGSLA-----KEVYIHGGFNGWKNVQDVP-MEKLppTGGGDWFSATVPVPEDAYVLDFVFKDGAGNWDNNNGQNYHI 75

                   .
gi 334182477   236 E 236
Cdd:pfam16760   76 P 76
CBM53 pfam16760
Starch/carbohydrate-binding module (family 53);
499-583 1.72e-16

Starch/carbohydrate-binding module (family 53);


Pssm-ID: 465261 [Multi-domain]  Cd Length: 76  Bit Score: 75.02  E-value: 1.72e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   499 TVLYNPANtvlngKPEVWFRGSFNRWTHRLGpLPPQKMEATDDESsHVKTTAKVPLDAYMMDFVFseKEDGGIFDNKNGL 578
Cdd:pfam16760    1 NIYYNGSL-----AKEVYIHGGFNGWKNVQD-VPMEKLPPTGGGD-WFSATVPVPEDAYVLDFVF--KDGAGNWDNNNGQ 71

                   ....*
gi 334182477   579 DYHLP 583
Cdd:pfam16760   72 NYHIP 76
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
714-964 6.95e-14

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 74.31  E-value: 6.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  714 FHPDILHCHDWSSAPVSWLFKdhytqyGLIKTRIVFTIHNLEFgANAIGKA-----MTFADKATTVSPTYAKEVAGNsvI 788
Cdd:cd03819    75 ERIDLIHAHSRAPAWLGWLAS------RLTGVPLVTTVHGSYL-ATYHPKDfalavRARGDRVIAVSELVRDHLIEA--L 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  789 SAHLYKFHGIINGIDPDIWDPyndnfipvpytsenvvegkrAAKEELQNRLGLKSaDFPVVGIITRLTHQKGIHLIKHAI 868
Cdd:cd03819   146 GVDPERIRVIPNGVDTDRFPP--------------------EAEAEERAQLGLPE-GKPVVGYVGRLSPEKGWLLLVDAA 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  869 WRtLERNGQVVLL--GSAPdpriQNDFV-NLANQLhsshGDRARLVLT-YDEPLSHLiYAGADFILVPSIFEPCGLTQLI 944
Cdd:cd03819   205 AE-LKDEPDFRLLvaGDGP----ERDEIrRLVERL----GLRDRVTFTgFREDVPAA-LAASDVVVLPSLHEEFGRVALE 274
                         250       260
                  ....*....|....*....|.
gi 334182477  945 AMRYGaVPVVRKT-GGLFDTV 964
Cdd:cd03819   275 AMACG-TPVVATDvGGAREIV 294
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
701-1034 9.72e-10

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 61.87  E-value: 9.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  701 FCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYtqygliKTRIVFTIHNLE------------------FGANAIg 762
Cdd:cd03800    87 FADGLLRFIAREGGRYDLIHSHYWDSGLVGALLARRL------GVPLVHTFHSLGrvkyrhlgaqdtyhpslrITAEEQ- 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  763 kAMTFADKATTVSPtyaKEVAGN-SVISAHLYKFHGIINGIDPDIWDPYNDnfipvpytsenvvegkraaKEELQNRLGL 841
Cdd:cd03800   160 -ILEAADRVIASTP---QEADELiSLYGADPSRINVVPPGVDLERFFPVDR-------------------AEARRARLLL 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  842 KSaDFPVVGIITRLTHQKGIH-LIK-HAIWRTLERNGQVVLLGSAPDPRIQNDFVNLAnQLHSSHG--DRARLVLTYDEP 917
Cdd:cd03800   217 PP-DKPVVLALGRLDPRKGIDtLVRaFAQLPELRELANLVLVGGPSDDPLSMDREELA-ELAEELGliDRVRFPGRVSRD 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  918 LSHLIYAGADFILVPSIFEPCGLTQLIAMRYGaVPVV-RKTGGLFDTVFDvdhdkeraqaqvlEPNGFSFDGADAPgvdy 996
Cdd:cd03800   295 DLPELYRAADVFVVPSLYEPFGLTAIEAMACG-TPVVaTAVGGLQDIVRD-------------GRTGLLVDPHDPE---- 356
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 334182477  997 ALNRAISAWYDGREWFNSLCKTVME---QDWSWNRPALEYL 1034
Cdd:cd03800   357 ALAAALRRLLDDPALWQRLSRAGLErarAHYTWESVADQLL 397
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
714-954 1.45e-08

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 58.11  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  714 FHPDILHCHDWSSAPVSWLfkDHYTQYGLiktRIVFTIHNLEFGAnaIGKAMTFADKATTVSPT--YAKEVAGNSVISAH 791
Cdd:cd03823    95 FRPDVVHTHNLSGLGASLL--DAARDLGI---PVVHTLHDYWLLC--PRQFLFKKGGDAVLAPSrfTANLHEANGLFSAR 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  792 LYKfhgIINGIDPD-IWDPyndnfIPVPYTSENVVegkraakeelqnrlglksadfpvvGIITRLTHQKGIHLIKHAIWR 870
Cdd:cd03823   168 ISV---IPNAVEPDlAPPP-----RRRPGTERLRF------------------------GYIGRLTEEKGIDLLVEAFKR 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  871 TLERNGQVVLLGSAPDPRIQNDFVNLANQLHSShgdrarlvLTYDEPLSHliYAGADFILVPSIF-EPCGLTQLIAMRYG 949
Cdd:cd03823   216 LPREDIELVIAGHGPLSDERQIEGGRRIAFLGR--------VPTDDIKDF--YEKIDVLVVPSIWpEPFGLVVREAIAAG 285

                  ....*
gi 334182477  950 aVPVV 954
Cdd:cd03823   286 -LPVI 289
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
920-1042 1.82e-08

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 53.84  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  920 HLIYAGADFILVPSIFEPCGLTQLIAMRYGAVPVVRKTGGLFDTVFDvdhdkeraqaqvlEPNGFSFDGADAPgvdyALN 999
Cdd:COG0438    15 EALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIED-------------GETGLLVPPGDPE----ALA 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 334182477 1000 RAISAWYDGREWFNSL---CKTVMEQDWSWNRPALEYLELYHSARK 1042
Cdd:COG0438    78 EAILRLLEDPELRRRLgeaARERAEERFSWEAIAERLLALYEELLA 123
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
835-966 3.19e-07

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 52.41  E-value: 3.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  835 LQNRLGLKSADFPVVGiitRLTHQKGIHLIKHAIWRTLER--NGQVVLLGSAPDPRIQNdfvnlANQLHSSHGDRARLV- 911
Cdd:cd01635   102 ARLLVSLPLADKVSVG---RLVPEKGIDLLLEALALLKARlpDLVLVLVGGGGEREEEE-----ALAAALGLLERVVIIg 173
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 334182477  912 LTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYGAVPVVRKTGGLFDTVFD 966
Cdd:cd01635   174 GLVDDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVD 228
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
250-301 1.17e-06

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 49.27  E-value: 1.17e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334182477   250 LLEEKLR---------EQEKLAKEEAERERQKEEKRRIEAQKAAIEAdRAQAKAETQKRRE 301
Cdd:pfam05672   15 ILAEKRRqareqrereEQERLEKEEEERLRKEELRRRAEEERARREE-EARRLEEERRREE 74
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
716-954 2.17e-06

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 51.20  E-value: 2.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  716 PDILHCHDWSSApvSWLFKDhytqyGLIKTRIVFTIHN-------LEFGANAIGKAMTFADKATTVSPTYAKEVAGNSVI 788
Cdd:cd03811    84 PDVVISFLGFAT--YIVAKL-----AAARSKVIAWIHSslsklyyLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLGPS 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  789 SAHlyKFHGIINGIDPDiwdpyndnFIpvpytsenvvegKRAAKEELQNRLGlksaDFPVVGIITRLTHQKGIHLIKHAI 868
Cdd:cd03811   157 PPE--KIEVIYNPIDID--------RI------------RALAKEPILNEPE----DGPVILAVGRLDPQKGHDLLIEAF 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  869 WRTLERNGQV--VLLGSAPDpriQNDFVNLANQLHSShgDRARLVLTYDEPLShlIYAGADFILVPSIFEPCGLTQLIAM 946
Cdd:cd03811   211 AKLRKKYPDVklVILGDGPL---REELEKLAKELGLA--ERVIFLGFQSNPYP--YLKKADLFVLSSRYEGFPNVLLEAM 283

                  ....*...
gi 334182477  947 RYGaVPVV 954
Cdd:cd03811   284 ALG-TPVV 290
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
847-968 2.45e-06

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 47.89  E-value: 2.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   847 PVVGIITRLTH-QKGIHLIKHAIWRTLERNGQVVLL--GSAPDPRIQNDFVNLANQLHsshgdrarlVLTYDEPLSHLiY 923
Cdd:pfam13692    2 PVILFVGRLHPnVKGVDYLLEAVPLLRKRDNDVRLVivGDGPEEELEELAAGLEDRVI---------FTGFVEDLAEL-L 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 334182477   924 AGADFILVPSIFEPCGLTQLIAMRYGaVPVV-RKTGGLFDTVFDVD 968
Cdd:pfam13692   72 AAADVFVLPSLYEGFGLKLLEAMAAG-LPVVaTDVGGIPELVDGEN 116
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
700-1040 1.17e-05

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 48.92  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  700 FFCHAALEFLLQG--GFHPDILHCH-DWSSAPVSWLFKdhytqyGLIKTRIVFTIH--------NLEFGANAIGKAMTFA 768
Cdd:cd03798    78 PLRAPSLAKLLKRrrRGPPDLIHAHfAYPAGFAAALLA------RLYGVPYVVTEHgsdinvfpPRSLLRKLLRWALRRA 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  769 DKATTVSPTYAKEVAGNSVIsahLYKFHGIINGIDPDIWDPyndnfipvpytsenvvegkraakeeLQNRLGLKsADFPV 848
Cdd:cd03798   152 ARVIAVSKALAEELVALGVP---RDRVDVIPNGVDPARFQP-------------------------EDRGLGLP-LDAFV 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  849 VGIITRLTHQKGIHLIKHAIWRTLERNGQVVLLgsapdprIQNDFVNLA--NQLHSSHGDRARLVLTydEPLSH----LI 922
Cdd:cd03798   203 ILFVGRLIPRKGIDLLLEAFARLAKARPDVVLL-------IVGDGPLREalRALAEDLGLGDRVTFT--GRLPHeqvpAY 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  923 YAGADFILVPSIFEPCGLTQLIAMRYGaVPVV-RKTGGLFDTVFDvdhdkeraqaqvlEPNGFSFDGADAPGVDYALNRA 1001
Cdd:cd03798   274 YRACDVFVLPSRHEGFGLVLLEAMACG-LPVVaTDVGGIPEVVGD-------------PETGLLVPPGDADALAAALRRA 339
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 334182477 1002 ISAWYDGREWfNSLCKTVMEQdWSWNRPALEYLELYHSA 1040
Cdd:cd03798   340 LAEPYLRELG-EAARARVAER-FSWVKAADRIAAAYRDV 376
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
610-805 1.33e-05

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 46.76  E-value: 1.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   610 GGLGDVVTSLSRAVQELNHNVDIVFPKYDcikhnfvkdlqfnrsyhwGGTEIKVWHGKVEGLSVYFLDPQNglfqrgcvy 689
Cdd:pfam13439    1 GGVERYVLELARALARRGHEVTVVTPGGP------------------GPLAEEVVRVVRVPRVPLPLPPRL--------- 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   690 gcaddagRFGFFCHAALEFLLQGgFHPDILHCHDWSSAPVSWLFKDHYTqygliKTRIVFTIHNLEFGANAIG------- 762
Cdd:pfam13439   54 -------LRSLAFLRRLRRLLRR-ERPDVVHAHSPFPLGLAALAARLRL-----GIPLVVTYHGLFPDYKRLGarlsplr 120
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 334182477   763 --------KAMTFADKATTVSPTYAKEVAGNSVISAHlyKFHGIINGIDPD 805
Cdd:pfam13439  121 rllrrlerRLLRRADRVIAVSEAVADELRRLYGVPPE--KIRVIPNGVDLE 169
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
250-310 1.62e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 48.26  E-value: 1.62e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334182477  250 LLEEKLREQEKLAKEEAERE------RQKEEKRRIEAQK-------AAIEADRAQAKAETQKRRelLQPAIKKA 310
Cdd:PRK09510   92 LQQKQAAEQERLKQLEKERLaaqeqkKQAEEAAKQAALKqkqaeeaAAKAAAAAKAKAEAEAKR--AAAAAKKA 163
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
251-310 2.78e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 47.53  E-value: 2.78e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   251 LEEKLREQEKLAKEEAEReRQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQPAIKKA 310
Cdd:TIGR02794   94 LEQRAAAEKAAKQAEQAA-KQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQA 152
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
251-304 6.44e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.45  E-value: 6.44e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334182477   251 LEEKLREQEKLAKE------------EAERERQKEEKRRIEA---QKAAIEADRAQAKAETQKRRELLQ 304
Cdd:pfam13868  118 AEEKLEKQRQLREEidefneeqaewkELEKEEEREEDERILEylkEKAEREEEREAEREEIEEEKEREI 186
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
252-310 6.85e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 46.38  E-value: 6.85e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   252 EEKLR-EQEKLAKEEAERERQKEEkrriEAQKAAIEADRAQAKAETQKRREllqPAIKKA 310
Cdd:TIGR02794  123 EAKAKqAAEAKAKAEAEAERKAKE----EAAKQAEEEAKAKAAAEAKKKAE---EAKKKA 175
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
252-301 6.93e-05

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 44.26  E-value: 6.93e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 334182477   252 EEKLR---EQEKLAKEEAERERQ--KEEKRRIEAQKAAIEAdRAQAKAEtQKRRE 301
Cdd:pfam05672   68 EERRReeeERQRKAEEEAEEREQreQEEQERLQKQKEEAEA-KAREEAE-RQRQE 120
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
251-310 7.28e-05

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 43.37  E-value: 7.28e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334182477   251 LEEKLR---EQEKLAKEEAERERQK----EEKRRiEAQKAAIEADRAQAKAETQKRReLLQPAIKKA 310
Cdd:pfam20492   11 LEERLKqyeEETKKAQEELEESEETaeelEEERR-QAEEEAERLEQKRQEAEEEKER-LEESAEMEA 75
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
703-954 7.68e-05

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 46.20  E-value: 7.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  703 HAALEFLLQGGFHPDILHCHDwssapvswlfkdHYTQYGLIKTRIVFTIHNL------EFGANAIGKAMTF--------A 768
Cdd:cd03809    72 LRWLQILLPKKDKPDLLHSPH------------NTAPLLLKGCPQVVTIHDLiplrypEFFPKRFRLYYRLllpislrrA 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  769 DKATTVSPTYAKEVAGNSVISAHlyKFHGIINGIDPDIWdpyndnfipvpytsenvvegKRAAKEELQNRLGLKSADFPV 848
Cdd:cd03809   140 DAIITVSEATRDDIIKFYGVPPE--KIVVIPLGVDPSFF--------------------PPESAAVLIAKYLLPEPYFLY 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  849 VGIITRlthQKGIH-LIK-HAIWRTLERNGQVVLLGSAPDPRIQNDFVNLANQLHsshgDRARLV--LTYDEpLSHLiYA 924
Cdd:cd03809   198 VGTLEP---RKNHErLLKaFALLKKQGGDLKLVIVGGKGWEDEELLDLVKKLGLG----GRVRFLgyVSDED-LPAL-YR 268
                         250       260       270
                  ....*....|....*....|....*....|
gi 334182477  925 GADFILVPSIFEPCGLTQLIAMRYGaVPVV 954
Cdd:cd03809   269 GARAFVFPSLYEGFGLPVLEAMACG-TPVI 297
MRP-L20 pfam12824
Mitochondrial ribosomal protein subunit L20; This family is the essential mitochondrial ...
254-303 8.87e-05

Mitochondrial ribosomal protein subunit L20; This family is the essential mitochondrial ribosomal protein subunit L20 of fungi.


Pssm-ID: 432810  Cd Length: 161  Bit Score: 43.86  E-value: 8.87e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334182477   254 KLREQE-------KLAKE------------EAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELL 303
Cdd:pfam12824   93 RLRAEDpekwtrkKLAKKfgcsplfvsmvtEAPKEKKKEMKAELEAIKSRWGPKRRIAREDRKKRKELW 161
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
250-301 9.36e-05

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 42.98  E-value: 9.36e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   250 LLEEKLR----EQEKLAKE----EAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRE 301
Cdd:pfam20492   38 ELEEERRqaeeEAERLEQKrqeaEEEKERLEESAEMEAEEKEQLEAELAEAQEEIARLEE 97
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
252-315 9.74e-05

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 46.19  E-value: 9.74e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334182477  252 EEKLREQEKLAKEEAERERQKEEKRRIEAQKAAieadrAQAKAETQKRRELLQPAIKKAVVSAE 315
Cdd:COG3064    25 KRAAAEAEQKAKEEAEEERLAELEAKRQAEEEA-----REAKAEAEQRAAELAAEAAKKLAEAE 83
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
252-309 9.86e-05

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 44.66  E-value: 9.86e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   252 EEKLREQEKLAKEEAERERQKEEKRRIEAQKAAIEAD--RAQAKAETQKRRELLQPAIKK 309
Cdd:pfam15927    2 RLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQdrRAEELEELKHLLEERKEALEK 61
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
256-310 1.56e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 45.22  E-value: 1.56e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 334182477   256 REQEKLAKE-EAERERQKEEKRRIEAQKAAIEADrAQAKAETQKRRELLQPAIKKA 310
Cdd:TIGR02794   75 QQAEEAEKQrAAEQARQKELEQRAAAEKAAKQAE-QAAKQAEEKQKQAEEAKAKQA 129
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
252-315 1.64e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 45.22  E-value: 1.64e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334182477   252 EEKLREQEKLAKEEAERERQKEE-KRRIEA-QKAAIEADRAQ-AKAETQKRREllQPAIKKAVVSAE 315
Cdd:TIGR02794  101 EKAAKQAEQAAKQAEEKQKQAEEaKAKQAAeAKAKAEAEAERkAKEEAAKQAE--EEAKAKAAAEAK 165
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
845-964 2.43e-04

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 42.65  E-value: 2.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   845 DFPVVGIITRLTHQKGIHLIKHAIWRTLERNGQVVLL--GSAPDpriQNDFVNLANQLHSshGDRARLVL-TYDEPLSHL 921
Cdd:pfam00534    1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLViaGDGEE---EKRLKKLAEKLGL--GDNVIFLGfVSDEDLPEL 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 334182477   922 iYAGADFILVPSIFEPCGLTQLIAMRYGAVPVVRKTGGLFDTV 964
Cdd:pfam00534   76 -LKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVV 117
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
247-310 2.64e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.52  E-value: 2.64e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334182477   247 ENFLLEEKLRE-QEKLAKEEAERERQKEEKRRI-----------EAQKAAIE---ADRAQAKAETQKRRELLQPAIKKA 310
Cdd:pfam13868  153 EDERILEYLKEkAEREEEREAEREEIEEEKEREiarlraqqekaQDEKAERDelrAKLYQEEQERKERQKEREEAEKKA 231
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
253-304 3.05e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 44.48  E-value: 3.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 334182477  253 EKLREQE----KLAKEEAERERQKEEKRRiEAQKAAIEADRAQAKAETQKRRELLQ 304
Cdd:COG2268   227 ELEQEREietaRIAEAEAELAKKKAEERR-EAETARAEAEAAYEIAEANAEREVQR 281
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
252-315 3.05e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 44.65  E-value: 3.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334182477  252 EEKLREQEKLAKEEAERERQK---EEKRRIEAQKAAIEADRAQAKAETQKRRE-LLQPAIKKAVVSAE 315
Cdd:COG3064    59 EAKAEAEQRAAELAAEAAKKLaeaEKAAAEAEKKAAAEKAKAAKEAEAAAAAEkAAAAAEKEKAEEAK 126
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
252-315 3.49e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 41.95  E-value: 3.49e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334182477   252 EEKLREQEKLAKEEAERERQKEEKRRIEAQKAAIEADRAQAKAET-QKRREllqPAIKKAVVSAE 315
Cdd:pfam05672   54 EERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERlQKQKE---EAEAKAREEAE 115
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
251-316 5.16e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 43.87  E-value: 5.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334182477  251 LEEKLREQEKlAKEEAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQPAIKKAVVSAEN 316
Cdd:COG3064    75 AAKKLAEAEK-AAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEE 139
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
251-305 8.76e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 40.79  E-value: 8.76e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334182477   251 LEEKLR----EQEKLAKEEA------ERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQP 305
Cdd:pfam05672   29 REEQERlekeEEERLRKEELrrraeeERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQ 93
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
252-316 8.89e-04

Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.


Pssm-ID: 462259 [Multi-domain]  Cd Length: 353  Bit Score: 42.67  E-value: 8.89e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334182477   252 EEKLREQEKLAKEEAERERQKEEKRRIEAQKAAI------EADRAQAKAETQKRRELLQ-PAIKKAVVSAEN 316
Cdd:pfam07767  215 EEKLERVLEKIAESAATAEAREEKRKTKAQRNKEkrrkeeEREAKEEKALKKKLAQLERlKEIAKEIAEKEK 286
PRK03963 PRK03963
V-type ATP synthase subunit E; Provisional
250-304 1.52e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 167649 [Multi-domain]  Cd Length: 198  Bit Score: 40.89  E-value: 1.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  250 LLEEKLREQEKLAK---EEAER--ERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQ 304
Cdd:PRK03963    7 IIQEINREAEQKIEyilEEAQKeaEKIKEEARKRAESKAEWILRKAKTQAELEKQRIIAN 66
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
253-310 1.69e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 41.75  E-value: 1.69e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334182477   253 EKLREQEKLAKEEAERERQKEE-KRRIEAQ-KAAIEADR------AQAKAETQKRRElLQPAIKKA 310
Cdd:TIGR02794  149 AKQAEEEAKAKAAAEAKKKAEEaKKKAEAEaKAKAEAEAkakaeeAKAKAEAAKAKA-AAEAAAKA 213
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
252-310 1.70e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.83  E-value: 1.70e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334182477   252 EEKLREQEKLAKEEAERERQKEEKRRIEAQKAAIEAD---RAQAKAETQKRRELLQpAIKKA 310
Cdd:pfam13868  180 EEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQErkeRQKEREEAEKKARQRQ-ELQQA 240
Cgr1 pfam03879
Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA ...
250-309 1.76e-03

Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA processing.


Pssm-ID: 427562 [Multi-domain]  Cd Length: 107  Bit Score: 39.14  E-value: 1.76e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334182477   250 LLEEKlrEQEKLAKEEAERERQ--KEEKRRIEAQKAAIEAdraqAKAETQKRRELLQPAIKK 309
Cdd:pfam03879   52 LKDEK--EAERQRRIQAIKERReaKEEKERYEELAAKMHA----KKVERLKRKEKRNKLLKE 107
AhaH TIGR02926
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
256-301 2.09e-03

ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The hydrophilic A1 "stalk" complex (AhaABCDEFG) is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex. It is unclear precisely where AhaH fits into these complexes.


Pssm-ID: 131972 [Multi-domain]  Cd Length: 85  Bit Score: 38.29  E-value: 2.09e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 334182477   256 REQEKLAKEEAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRE 301
Cdd:TIGR02926   30 REEARELLEEAEEEASKLGEEIIKEAEEEIEKEAEKIREEGEKEIE 75
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
252-310 2.29e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 41.37  E-value: 2.29e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334182477   252 EEKLREQEKLAKEEAERERQKE--EKRRIEAQKAAIEADRAQAKAETQKRRELLQPAIKKA 310
Cdd:TIGR02794  163 EAKKKAEEAKKKAEAEAKAKAEaeAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAA 223
PRK14474 PRK14474
F0F1 ATP synthase subunit B; Provisional
250-318 2.45e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184696 [Multi-domain]  Cd Length: 250  Bit Score: 40.96  E-value: 2.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334182477  250 LLEEKLRE---QEKLAKEEAERERQKEEKrrIEAQKAAIEAdRAQAKAETQKRRELLQpaIKKAVVSAENVW 318
Cdd:PRK14474   40 RIANRWQDaeqRQQEAGQEAERYRQKQQS--LEQQRASFMA-QAQEAADEQRQHLLNE--AREDVATARDEW 106
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
244-306 2.54e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 41.53  E-value: 2.54e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334182477   244 VDFENFLLEEKLREQEKLAKEeAERERQKEEKRRIEAQKAAIEADRAQAKAETQKR--RELLQPA 306
Cdd:pfam05262  194 VNFRRDMTDLKERESQEDAKR-AQQLKEELDKKQIDADKAQQKADFAQDNADKQRDevRQKQQEA 257
NtpH COG2811
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ...
252-311 2.70e-03

Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit H is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 442060 [Multi-domain]  Cd Length: 108  Bit Score: 38.36  E-value: 2.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334182477  252 EEKLREQEKLAKE---EAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRE-LLQPA---IKKAV 311
Cdd:COG2811    29 EERIAEAREEAEEiieQAEEEAEEEAQERLEEAREEAEAEAEEIIEEGEKEAEaLKKKAedkLDKAV 95
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
770-1039 3.19e-03

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 41.16  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  770 KATTVSPT-YAKEVAGNSVISAHlYKFHGIINGIDPDIWDPYNdnfipvpytsenvvegkraaKEELQNRLGLkSADFPV 848
Cdd:cd03825   138 RLTIVAPSrWLADMVRRSPLLKG-LPVVVIPNGIDTEIFAPVD--------------------KAKARKRLGI-PQDKKV 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  849 VGIITRLTHQ--KGIHLIKHAIwRTL--ERNGQVVLLGSAPDPRIQNDFvnlanqLHSSHGdrarlVLTYDEPLsHLIYA 924
Cdd:cd03825   196 ILFGAESVTKprKGFDELIEAL-KLLatKDDLLLVVFGKNDPQIVILPF------DIISLG-----YIDDDEQL-VDIYS 262
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  925 GADFILVPSIFEPCGLTQLIAMRYGaVPVVR-KTGGLFDTVFDvdhdkeraqaqvlEPNGFSFDGADAPGVDYALNRAIS 1003
Cdd:cd03825   263 AADLFVHPSLADNLPNTLLEAMACG-TPVVAfDTGGSPEIVQH-------------GVTGYLVPPGDVQALAEAIEWLLA 328
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 334182477 1004 AwYDGREWFNSLCKTVMEQDWSWNRPALEYLELYHS 1039
Cdd:cd03825   329 N-PKERESLGERARALAENHFDQRVQAQRYLELYKD 363
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
241-304 3.20e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 3.20e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334182477   241 MDKVDFENFLleEKLREQEKLAKEEAE--RERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQ 304
Cdd:pfam13868  258 REEEEFERML--RKQAEDEEIEQEEAEkrRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLR 321
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
250-311 3.28e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 3.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334182477  250 LLEEKLRE-QEKLAKEEAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQPAIKKAV 311
Cdd:COG1579   107 DLEDEILElMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
252-311 3.51e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 41.47  E-value: 3.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  252 EEKLREQEKLAKEEAeRERQKEEKRRIEAQKAAIEAdRAQAKAEtqKRRELLQPAIKKAV 311
Cdd:PRK05035  437 EIRAIEQEKKKAEEA-KARFEARQARLEREKAAREA-RHKKAAE--ARAAKDKDAVAAAL 492
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
242-294 3.71e-03

Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prohibitin (a lipid raft-associated integral membrane protein). Individual proteins of the SPFH (band 7) domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. These microdomains, in addition to being stable scaffolds, may also be dynamic units with their own regulatory functions. Prohibitin is a mitochondrial inner-membrane protein which may act as a chaperone for the stabilization of mitochondrial proteins. Human prohibitin forms a hetero-oligomeric complex with Bap-37 (prohibitin 2, an SPFH domain carrying homolog). This complex may protect non-assembled membrane proteins against proteolysis by the m-AAA protease. Prohibitin and Bap-37 yeast homologs have been implicated in yeast longevity and in the maintenance of mitochondrial morphology.


Pssm-ID: 259799 [Multi-domain]  Cd Length: 195  Bit Score: 39.80  E-value: 3.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 334182477  242 DKVDFENFLLEEKLR---EQEKLAKEEAERERQKEEKRRIEAQKAAIEAdRAQAKA 294
Cdd:cd03401   140 DDVLITNIDFPDEYEkaiEAKQVAEQEAERAKFELEKAEQEAERKVIEA-EGEAEA 194
PRK03963 PRK03963
V-type ATP synthase subunit E; Provisional
249-314 4.07e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 167649 [Multi-domain]  Cd Length: 198  Bit Score: 39.74  E-value: 4.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  249 FLLEEKLREQEKLaKEEAER--ERQKEEKRRIEAQKAAIEADR--AQAKAETQKRRELLQPAIKKAVVSA 314
Cdd:PRK03963   21 YILEEAQKEAEKI-KEEARKraESKAEWILRKAKTQAELEKQRiiANAKLEVRRKRLAVQEELISEVLEA 89
V-ATPase_G pfam03179
Vacuolar (H+)-ATPase G subunit; This family represents the eukaryotic vacuolar (H+)-ATPase ...
256-312 4.98e-03

Vacuolar (H+)-ATPase G subunit; This family represents the eukaryotic vacuolar (H+)-ATPase (V-ATPase) G subunit. V-ATPases generate an acidic environment in several intracellular compartments. Correspondingly, they are found as membrane-attached proteins in several organelles. They are also found in the plasma membranes of some specialized cells. V-ATPases consist of peripheral (V1) and membrane integral (V0) heteromultimeric complexes. The G subunit is part of the V1 subunit, but is also thought to be strongly attached to the V0 complex. It may be involved in the coupling of ATP degradation to H+ translocation.


Pssm-ID: 460836 [Multi-domain]  Cd Length: 105  Bit Score: 37.58  E-value: 4.98e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334182477   256 REQEKL--AKEEAERE----RQKEEK--RRIEAQKAAI-EADRAQAKAETQKRRELLQPAI---KKAVV 312
Cdd:pfam03179   26 RKQKRLkqAKEEAEKEieeyRAQREKefKEFEAKHMGSrEELEKKIEKETQEKIQEIKDSVnknKEAVV 94
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
258-316 5.33e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 40.41  E-value: 5.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 334182477  258 QEKLAKEEAERERQkEEKRRIEAQKAAIEADRAQAKAETQKRRELLQPAIKKAVVSAEN 316
Cdd:COG3064     2 QEALEEKAAEAAAQ-ERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEARE 59
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
250-315 5.56e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 40.41  E-value: 5.56e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334182477  250 LLEEKLRE---QEKLAKEEAERERQKEEKRR--IEAQKAAIEADRAQAKAETQKRRELLQPAIKKAVVSAE 315
Cdd:COG3064     4 ALEEKAAEaaaQERLEQAEAEKRAAAEAEQKakEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAE 74
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
251-299 6.34e-03

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 38.52  E-value: 6.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 334182477   251 LEEKLREQ--EKLAKEEAERERQKEEKR--RIEAQKAAIEADRaqaKAETQKR 299
Cdd:pfam11600   66 LKEKERREkkEKDEKEKAEKLRLKEEKRkeKQEALEAKLEEKR---KKEEEKR 115
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
254-304 6.48e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 6.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 334182477  254 KLRE-QEKLAKEEAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQ 304
Cdd:COG1196   233 KLRElEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE 284
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
240-310 7.01e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.58  E-value: 7.01e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334182477  240 GMDKVDFENFL--LEEKLREQEKLAKE-EAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRrelLQPAIKKA 310
Cdd:PRK00409  512 GEDKEKLNELIasLEELERELEQKAEEaEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKE---AQQAIKEA 582
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
252-310 7.05e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 38.78  E-value: 7.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477  252 EEKLR--------EQEKL--AKEEAERERQKEEKR------RIEAQK----------AAIEADRAQAKAETQKRRELLQP 305
Cdd:PRK07352   63 EERLRqaaqalaeAQQKLaqAQQEAERIRADAKARaeairaEIEKQAiedmarlkqtAAADLSAEQERVIAQLRREAAEL 142

                  ....*
gi 334182477  306 AIKKA 310
Cdd:PRK07352  143 AIAKA 147
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
252-299 7.71e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 37.80  E-value: 7.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334182477  252 EEKLRE-----QEKL--AKEEAERERQ------KEEKRRIEAQ-KAAIEADRAQAKAETQKR 299
Cdd:cd06503    57 EEKLAEaraeaQEIIeeARKEAEKIKEeilaeaKEEAERILEQaKAEIEQEKEKALAELRKE 118
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
252-304 9.50e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 38.10  E-value: 9.50e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 334182477   252 EEKLREQEKLAKEEAERERQKEEKRRIEAQKAAIEADraQAKAETQKRRELLQ 304
Cdd:pfam05672   47 ELRRRAEEERARREEEARRLEEERRREEEERQRKAEE--EAEEREQREQEEQE 97
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
236-317 9.78e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 9.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182477   236 EIKGGMDKVDFenfLLEEKLREQEKLAKEEAERERQKE---------------EKRRIEAQKAAIEADRAQAKAETQKRR 300
Cdd:TIGR02169  181 EVEENIERLDL---IIDEKRQQLERLRREREKAERYQAllkekreyegyellkEKEALERQKEAIERQLASLEEELEKLT 257
                           90
                   ....*....|....*..
gi 334182477   301 ELLQpAIKKAVVSAENV 317
Cdd:TIGR02169  258 EEIS-ELEKRLEEIEQL 273
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
251-309 9.80e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 9.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334182477  251 LEEKLRE-QEKLAKEEAERERQKEEKRRIEAQKAAIEADRAQAKAET---QKRRELLQPAIKK 309
Cdd:COG4372    78 LEEELEElNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERqdlEQQRKQLEAQIAE 140
 
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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