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Conserved domains on  [gi|4835785|gb|AAD30251|]
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Strong similarity to gb|X95759 soluble-starch-synthase precursor (SSIII) from Solanum tuberosum [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
1-1025 0e+00

synthase/transferase


:

Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 1998.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785      1 MAASGPKSSGPRGFGRRTTVGSAQKRTQKKNGEKDSNATSTATNEVSGISKLPAAKVDVQ-----------------KQS 63
Cdd:PLN02316    1 MSTSKPKGSAPRGFAPRTTVESSQKRIQQNNGDKEDSSTSTSSLSVSAVEKTSNAKEEIQvdfqhnsesaveeveaeDEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     64 SVVLNERNVLDRSDIEDGSDRLDKKTTDDDDLLEQKLKLERENLRRKEIETLAAENLARGDRMFVYPVIVKPDEDIEVFL 143
Cdd:PLN02316   81 EVEQNQSDVLKSSSIVKEESISTDMDGIDDDSLDRKLKLERENLRKREIEELAEENFSRGNKLFVYPQVVKPDSDIEVYL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    144 NRNLSTLNNEPDVLIMGAFNEWRWKSFTRRLEKTWIHEDWLSCLLHIPKEAYKMDFVFFNGQSVYDNNDSKDFCVEIKGG 223
Cdd:PLN02316  161 NRSLSTLANEPDVLIMGAFNGWRWKSFTERLEKTELGGDWWSCKLHIPKEAYKMDFVFFNGQNVYDNNDHKDFCVEIEGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    224 MDKVDFENFLLEEKLREQEKLAKEEAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQPAIKKAVVSAENVWYI 303
Cdd:PLN02316  241 MDEHSFEDFLLEEKRRELEKLAKEEAERERQAEEQRRREEEKAAMEADRAQAKAEVEKRREKLQNLLKKASRSADNVWYI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    304 EPSDFKAEDTVKLYYNKRSGPLTNSKELWLHGGFNNWVDGLSIVVKLVNAELKDvdpksGNWWFAEVVVPGGALVIDWVF 383
Cdd:PLN02316  321 EPSEFKAGDTVKLYYNRSSGPLAHSTEIWIHGGYNNWIDGLSIVEKLVKSEEKD-----GDWWYAEVVVPERALVLDWVF 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    384 ADGPPKGAFLYDNNGYQDFHALVPQKLPEELYWLEEENMIFRKLQEDRRLKEEVMRAKMEKTARLKAETKERTLKKFLLS 463
Cdd:PLN02316  396 ADGPPGNARNYDNNGRQDFHAIVPNNIPEELYWVEEEHQIYRKLQEERRLREEAIRAKAEKTARMKAEMKEKTLKMFLLS 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    464 QKDVVYTEPLEIQAGNPVTVLYNPANTVLNGKPEVWFRGSFNRWTHRLGPLPPQKMEATDDeSSHVKTTAKVPLDAYMMD 543
Cdd:PLN02316  476 QKHIVYTEPLEVQAGTTVTVLYNPANTVLNGKPEVWFRGSFNRWTHRLGPLPPQKMVPADN-GSHLKATVKVPLDAYMMD 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    544 FVFSEKEDGGIFDNKNGLDYHLPVVGGISKEPPLHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCI 623
Cdd:PLN02316  555 FVFSEKEEGGIFDNRNGLDYHIPVFGGIAKEPPMHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDCL 634
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    624 KHNFVKDLQFNRSYHWGGTEIKVWHGKVEGLSVYFLDPQNGLFQRGCVYGCADDAGRFGFFCHAALEFLLQGGFHPDILH 703
Cdd:PLN02316  635 NLSHVKDLHYQRSYSWGGTEIKVWFGKVEGLSVYFLEPQNGMFWAGCVYGCRNDGERFGFFCHAALEFLLQSGFHPDIIH 714
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    704 CHDWSSAPVSWLFKDHYTQYGLIKTRIVFTIHNLEFGANAIGKAMTFADKATTVSPTYAKEVAGNSVISAHLYKFHGIIN 783
Cdd:PLN02316  715 CHDWSSAPVAWLFKDHYAHYGLSKARVVFTIHNLEFGANHIGKAMAYADKATTVSPTYSREVSGNSAIAPHLYKFHGILN 794
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    784 GIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEELQNRLGLKSADFPVVGIITRLTHQKGIHLIKHAIWRTLERNGQVVL 863
Cdd:PLN02316  795 GIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEALQQRLGLKQADLPLVGIITRLTHQKGIHLIKHAIWRTLERNGQVVL 874
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    864 LGSAPDPRIQNDFVNLANQLHSSHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYGAVPVVRKTGGL 943
Cdd:PLN02316  875 LGSAPDPRIQNDFVNLANQLHSSHHDRARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIPVVRKTGGL 954
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    944 FDTVFDVDHDKERAQAQVLEPNGFSFDGADAPGVDYALNRAISAWYDGREWFNSLCKTVMEQDWSWNRPALEYLELYHSA 1023
Cdd:PLN02316  955 FDTVFDVDHDKERAQAQGLEPNGFSFDGADAAGVDYALNRAISAWYDGRDWFNSLCKRVMEQDWSWNRPALDYMELYHSA 1034

                  ..
gi 4835785   1024 RK 1025
Cdd:PLN02316 1035 RK 1036
 
Name Accession Description Interval E-value
PLN02316 PLN02316
synthase/transferase
1-1025 0e+00

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 1998.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785      1 MAASGPKSSGPRGFGRRTTVGSAQKRTQKKNGEKDSNATSTATNEVSGISKLPAAKVDVQ-----------------KQS 63
Cdd:PLN02316    1 MSTSKPKGSAPRGFAPRTTVESSQKRIQQNNGDKEDSSTSTSSLSVSAVEKTSNAKEEIQvdfqhnsesaveeveaeDEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     64 SVVLNERNVLDRSDIEDGSDRLDKKTTDDDDLLEQKLKLERENLRRKEIETLAAENLARGDRMFVYPVIVKPDEDIEVFL 143
Cdd:PLN02316   81 EVEQNQSDVLKSSSIVKEESISTDMDGIDDDSLDRKLKLERENLRKREIEELAEENFSRGNKLFVYPQVVKPDSDIEVYL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    144 NRNLSTLNNEPDVLIMGAFNEWRWKSFTRRLEKTWIHEDWLSCLLHIPKEAYKMDFVFFNGQSVYDNNDSKDFCVEIKGG 223
Cdd:PLN02316  161 NRSLSTLANEPDVLIMGAFNGWRWKSFTERLEKTELGGDWWSCKLHIPKEAYKMDFVFFNGQNVYDNNDHKDFCVEIEGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    224 MDKVDFENFLLEEKLREQEKLAKEEAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQPAIKKAVVSAENVWYI 303
Cdd:PLN02316  241 MDEHSFEDFLLEEKRRELEKLAKEEAERERQAEEQRRREEEKAAMEADRAQAKAEVEKRREKLQNLLKKASRSADNVWYI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    304 EPSDFKAEDTVKLYYNKRSGPLTNSKELWLHGGFNNWVDGLSIVVKLVNAELKDvdpksGNWWFAEVVVPGGALVIDWVF 383
Cdd:PLN02316  321 EPSEFKAGDTVKLYYNRSSGPLAHSTEIWIHGGYNNWIDGLSIVEKLVKSEEKD-----GDWWYAEVVVPERALVLDWVF 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    384 ADGPPKGAFLYDNNGYQDFHALVPQKLPEELYWLEEENMIFRKLQEDRRLKEEVMRAKMEKTARLKAETKERTLKKFLLS 463
Cdd:PLN02316  396 ADGPPGNARNYDNNGRQDFHAIVPNNIPEELYWVEEEHQIYRKLQEERRLREEAIRAKAEKTARMKAEMKEKTLKMFLLS 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    464 QKDVVYTEPLEIQAGNPVTVLYNPANTVLNGKPEVWFRGSFNRWTHRLGPLPPQKMEATDDeSSHVKTTAKVPLDAYMMD 543
Cdd:PLN02316  476 QKHIVYTEPLEVQAGTTVTVLYNPANTVLNGKPEVWFRGSFNRWTHRLGPLPPQKMVPADN-GSHLKATVKVPLDAYMMD 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    544 FVFSEKEDGGIFDNKNGLDYHLPVVGGISKEPPLHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCI 623
Cdd:PLN02316  555 FVFSEKEEGGIFDNRNGLDYHIPVFGGIAKEPPMHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDCL 634
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    624 KHNFVKDLQFNRSYHWGGTEIKVWHGKVEGLSVYFLDPQNGLFQRGCVYGCADDAGRFGFFCHAALEFLLQGGFHPDILH 703
Cdd:PLN02316  635 NLSHVKDLHYQRSYSWGGTEIKVWFGKVEGLSVYFLEPQNGMFWAGCVYGCRNDGERFGFFCHAALEFLLQSGFHPDIIH 714
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    704 CHDWSSAPVSWLFKDHYTQYGLIKTRIVFTIHNLEFGANAIGKAMTFADKATTVSPTYAKEVAGNSVISAHLYKFHGIIN 783
Cdd:PLN02316  715 CHDWSSAPVAWLFKDHYAHYGLSKARVVFTIHNLEFGANHIGKAMAYADKATTVSPTYSREVSGNSAIAPHLYKFHGILN 794
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    784 GIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEELQNRLGLKSADFPVVGIITRLTHQKGIHLIKHAIWRTLERNGQVVL 863
Cdd:PLN02316  795 GIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEALQQRLGLKQADLPLVGIITRLTHQKGIHLIKHAIWRTLERNGQVVL 874
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    864 LGSAPDPRIQNDFVNLANQLHSSHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYGAVPVVRKTGGL 943
Cdd:PLN02316  875 LGSAPDPRIQNDFVNLANQLHSSHHDRARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIPVVRKTGGL 954
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    944 FDTVFDVDHDKERAQAQVLEPNGFSFDGADAPGVDYALNRAISAWYDGREWFNSLCKTVMEQDWSWNRPALEYLELYHSA 1023
Cdd:PLN02316  955 FDTVFDVDHDKERAQAQGLEPNGFSFDGADAAGVDYALNRAISAWYDGRDWFNSLCKRVMEQDWSWNRPALDYMELYHSA 1034

                  ..
gi 4835785   1024 RK 1025
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 ...
578-1022 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 4835785   578 HIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKHNFVKDLQFNRS---YHWGGTEIKVWHGKVEGL 654
Cdd:cd03791    1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLGLevkVGGRGEEVGVFELPVDGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   655 SVYFLDPQNGLFQRG----CVYGCADDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYTQYGLIKTRI 730
Cdd:cd03791   81 DYYFLDNPEFFDRPGlpgpPGYDYPDNAERFAFFSRAALELLRRLGFQPDIIHANDWHTALVPAYLKTRYRGPGFKKIKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   731 VFTIHNLEFGA----------------------------NAIGKAMTFADKATTVSPTYAKEVA-------GNSVISAHL 775
Cdd:cd03791  161 VFTIHNLAYQGlfpldtlaelglppelfhidglefygqiNFLKAGIVYADRVTTVSPTYAKEILtpeygegLDGVLRARA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   776 YKFHGIINGIDPDIWDPYNDNFIPVPYtSENVVEGKRAAKEELQNRLGLK-SADFPVVGIITRLTHQKGIHLIKHAIWRT 854
Cdd:cd03791  241 GKLSGILNGIDYDEWNPATDKLIPANY-SANDLEGKAENKAALQKELGLPvDPDAPLFGFVGRLTEQKGVDLILDALPEL 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   855 LERNGQVVLLGSApDPRIQNDFVNLANQlhssHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYGAV 934
Cdd:cd03791  320 LEEGGQLVVLGSG-DPEYEQAFRELAER----YPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRYGTL 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   935 PVVRKTGGLFDTVFDVDHDKEraqaqvlEPNGFSFDGADAPGVDYALNRAISAWYDgREWFNSLCKTVMEQDWSWNRPAL 1014
Cdd:cd03791  395 PIVRRTGGLADTVFDYDPETG-------EGTGFVFEDYDAEALLAALRRALALYRN-PELWRKLQKNAMKQDFSWDKSAK 466

                 ....*...
gi 4835785  1015 EYLELYHS 1022
Cdd:cd03791  467 EYLELYRS 474
GlgA COG0297
Glycogen synthase [Carbohydrate transport and metabolism];
577-1023 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 4835785   577 LHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIK---HNFVKDLQFNRSYHWGGTEIKVWHGKVEG 653
Cdd:COG0297    1 MKILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSIDdklKDLEVVASLEVPLGGRTYYARVLEGPDDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   654 LSVYFLDpQNGLFQRGCVYG-----CADDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYTQYGLIKT 728
Cdd:COG0297   81 VPVYFID-NPELFDRPGPYGdpdrdYPDNAERFAFFSRAALELLKGLDWKPDIIHCHDWQTGLIPALLKTRYADDPFKRI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   729 RIVFTIHNLE----FGANAIGK------------------------AMTFADKATTVSPTYAKEV------AG-NSVISA 773
Cdd:COG0297  160 KTVFTIHNLAyqgiFPAEILELlglppelftpdglefygqinflkaGIVYADRVTTVSPTYAREIqtpefgEGlDGLLRA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   774 HLYKFHGIINGIDPDIWDPYNDNFIPVPYTSENVvEGKRAAKEELQNRLGLK-SADFPVVGIITRLTHQKGIHLIKHAIW 852
Cdd:COG0297  240 RSGKLSGILNGIDYDVWNPATDPYLPANYSADDL-EGKAANKAALQEELGLPvDPDAPLIGMVSRLTEQKGLDLLLEALD 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   853 RTLERNGQVVLLGSApDPRIQNDFVNLANQlhssHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYG 932
Cdd:COG0297  319 ELLEEDVQLVVLGSG-DPEYEEAFRELAAR----YPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMYALRYG 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   933 AVPVVRKTGGLFDTVFDVDHDKERAqaqvlepNGFSFDGADAPGVDYALNRAISAWYDGREWfNSLCKTVMEQDWSWNRP 1012
Cdd:COG0297  394 TVPIVRRTGGLADTVIDYNEATGEG-------TGFVFDEYTAEALLAAIRRALALYRDPEAW-RKLQRNAMKQDFSWEKS 465
                        490
                 ....*....|.
gi 4835785  1013 ALEYLELYHSA 1023
Cdd:COG0297  466 AKEYLELYREL 476
glgA TIGR02095
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ...
577-1023 5.19e-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: 5.19e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     577 LHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKHNFVKDLQFNRSY---HWGGTE-IKVWHGKVE 652
Cdd:TIGR02095    1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVDDQVKVVELVdlsVGPRTLyVKVFEGVVE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     653 GLSVYFLDPQnGLFQR-GCVYGCA--DDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYTQyglIKTR 729
Cdd:TIGR02095   81 GVPVYFIDNP-SLFDRpGGIYGDDypDNAERFAFFSRAAAELLSGLGWQPDVVHAHDWHTALVPALLKAVYRP---NPIK 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     730 IVFTIHNLE----FGANAIGK------------------------AMTFADKATTVSPTYAKEV----AG---NSVISAH 774
Cdd:TIGR02095  157 TVFTIHNLAyqgvFPADDFSElglppeyfhmeglefygrvnflkgGIVYADRVTTVSPTYAREIltpeFGyglDGVLKAR 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     775 LYKFHGIINGIDPDIWDPYNDNFIPVPYTSENVvEGKRAAKEELQNRLGLK-SADFPVVGIITRLTHQKGIHLIKHAIWR 853
Cdd:TIGR02095  237 SGKLRGILNGIDTEVWNPATDPYLKANYSADDL-AGKAENKEALQEELGLPvDDDVPLFGVISRLTQQKGVDLLLAALPE 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     854 TLERNGQVVLLGSApDPRIQNDFVNLANQlhssHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYGA 933
Cdd:TIGR02095  316 LLELGGQLVVLGTG-DPELEEALRELAER----YPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYAMRYGT 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     934 VPVVRKTGGLFDTVFDVDHDKERAqaqvlepNGFSFDGADAPGVDYALNRAISAWYDGREWFNSLCKTVMEQDWSWNRPA 1013
Cdd:TIGR02095  391 VPIVRRTGGLADTVVDGDPEAESG-------TGFLFEEYDPGALLAALSRALRLYRQDPSLWEALQKNAMSQDFSWDKSA 463
                          490
                   ....*....|
gi 4835785    1014 LEYLELYHSA 1023
Cdd:TIGR02095  464 KQYVELYRSL 473
Glyco_transf_5 pfam08323
Starch synthase catalytic domain;
579-765 7.98e-63

Starch synthase catalytic domain;


Pssm-ID: 400563 [Multi-domain]  Cd Length: 239  Bit Score: 212.96  E-value: 7.98e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     579 IVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKHN-----FVKDLQFNRSYHWGGTEIKVWHGKVEG 653
Cdd:pfam08323    1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPEErnqleDVIRLSVAAGVPVRPLTVGVARLELDG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     654 LSVYFLDPQNgLFQRGCVYGC-----ADDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYTQYGLIKT 728
Cdd:pfam08323   81 VDVYFLDNPD-YFDRPGLYGDdgrdyEDNAERFAFFSRAALELAKKLGWIPDIIHCHDWHTALVPAYLKEAYADDPFKNI 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4835785     729 RIVFTIHNLEFG----------------------------ANAIGKAMTFADKATTVSPTYAKEV 765
Cdd:pfam08323  160 KTVFTIHNLAYQgrfpadlldllglppedfnldglefygqINFLKAGIVYADAVTTVSPTYAEEI 224
CBM_25 smart01066
Carbohydrate binding domain;
136-221 2.99e-23

Carbohydrate binding domain;


Pssm-ID: 198134 [Multi-domain]  Cd Length: 83  Bit Score: 94.35  E-value: 2.99e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785      136 DEDIEVFLNRNLSTLNNEPDVLIMGaFNEWRWKSFTRRLEKTWiHEDWLSCLLHIpKEAYKMDFVFFNGQSVYDNNDSKD 215
Cdd:smart01066    1 GNTVTVYYNGLLATSGAKNVYLHYG-FGENNWTDVPDVRMEKT-GEGWVKATIPV-KEAYKLNFCFKDGAGNWDNNGGAN 77

                    ....*.
gi 4835785      216 FCVEIK 221
Cdd:smart01066   78 YHFEIG 83
 
Name Accession Description Interval E-value
PLN02316 PLN02316
synthase/transferase
1-1025 0e+00

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 1998.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785      1 MAASGPKSSGPRGFGRRTTVGSAQKRTQKKNGEKDSNATSTATNEVSGISKLPAAKVDVQ-----------------KQS 63
Cdd:PLN02316    1 MSTSKPKGSAPRGFAPRTTVESSQKRIQQNNGDKEDSSTSTSSLSVSAVEKTSNAKEEIQvdfqhnsesaveeveaeDEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     64 SVVLNERNVLDRSDIEDGSDRLDKKTTDDDDLLEQKLKLERENLRRKEIETLAAENLARGDRMFVYPVIVKPDEDIEVFL 143
Cdd:PLN02316   81 EVEQNQSDVLKSSSIVKEESISTDMDGIDDDSLDRKLKLERENLRKREIEELAEENFSRGNKLFVYPQVVKPDSDIEVYL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    144 NRNLSTLNNEPDVLIMGAFNEWRWKSFTRRLEKTWIHEDWLSCLLHIPKEAYKMDFVFFNGQSVYDNNDSKDFCVEIKGG 223
Cdd:PLN02316  161 NRSLSTLANEPDVLIMGAFNGWRWKSFTERLEKTELGGDWWSCKLHIPKEAYKMDFVFFNGQNVYDNNDHKDFCVEIEGG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    224 MDKVDFENFLLEEKLREQEKLAKEEAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQPAIKKAVVSAENVWYI 303
Cdd:PLN02316  241 MDEHSFEDFLLEEKRRELEKLAKEEAERERQAEEQRRREEEKAAMEADRAQAKAEVEKRREKLQNLLKKASRSADNVWYI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    304 EPSDFKAEDTVKLYYNKRSGPLTNSKELWLHGGFNNWVDGLSIVVKLVNAELKDvdpksGNWWFAEVVVPGGALVIDWVF 383
Cdd:PLN02316  321 EPSEFKAGDTVKLYYNRSSGPLAHSTEIWIHGGYNNWIDGLSIVEKLVKSEEKD-----GDWWYAEVVVPERALVLDWVF 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    384 ADGPPKGAFLYDNNGYQDFHALVPQKLPEELYWLEEENMIFRKLQEDRRLKEEVMRAKMEKTARLKAETKERTLKKFLLS 463
Cdd:PLN02316  396 ADGPPGNARNYDNNGRQDFHAIVPNNIPEELYWVEEEHQIYRKLQEERRLREEAIRAKAEKTARMKAEMKEKTLKMFLLS 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    464 QKDVVYTEPLEIQAGNPVTVLYNPANTVLNGKPEVWFRGSFNRWTHRLGPLPPQKMEATDDeSSHVKTTAKVPLDAYMMD 543
Cdd:PLN02316  476 QKHIVYTEPLEVQAGTTVTVLYNPANTVLNGKPEVWFRGSFNRWTHRLGPLPPQKMVPADN-GSHLKATVKVPLDAYMMD 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    544 FVFSEKEDGGIFDNKNGLDYHLPVVGGISKEPPLHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCI 623
Cdd:PLN02316  555 FVFSEKEEGGIFDNRNGLDYHIPVFGGIAKEPPMHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQDLNHNVDIILPKYDCL 634
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    624 KHNFVKDLQFNRSYHWGGTEIKVWHGKVEGLSVYFLDPQNGLFQRGCVYGCADDAGRFGFFCHAALEFLLQGGFHPDILH 703
Cdd:PLN02316  635 NLSHVKDLHYQRSYSWGGTEIKVWFGKVEGLSVYFLEPQNGMFWAGCVYGCRNDGERFGFFCHAALEFLLQSGFHPDIIH 714
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    704 CHDWSSAPVSWLFKDHYTQYGLIKTRIVFTIHNLEFGANAIGKAMTFADKATTVSPTYAKEVAGNSVISAHLYKFHGIIN 783
Cdd:PLN02316  715 CHDWSSAPVAWLFKDHYAHYGLSKARVVFTIHNLEFGANHIGKAMAYADKATTVSPTYSREVSGNSAIAPHLYKFHGILN 794
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    784 GIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEELQNRLGLKSADFPVVGIITRLTHQKGIHLIKHAIWRTLERNGQVVL 863
Cdd:PLN02316  795 GIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEALQQRLGLKQADLPLVGIITRLTHQKGIHLIKHAIWRTLERNGQVVL 874
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    864 LGSAPDPRIQNDFVNLANQLHSSHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYGAVPVVRKTGGL 943
Cdd:PLN02316  875 LGSAPDPRIQNDFVNLANQLHSSHHDRARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIPVVRKTGGL 954
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    944 FDTVFDVDHDKERAQAQVLEPNGFSFDGADAPGVDYALNRAISAWYDGREWFNSLCKTVMEQDWSWNRPALEYLELYHSA 1023
Cdd:PLN02316  955 FDTVFDVDHDKERAQAQGLEPNGFSFDGADAAGVDYALNRAISAWYDGRDWFNSLCKRVMEQDWSWNRPALDYMELYHSA 1034

                  ..
gi 4835785   1024 RK 1025
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 ...
578-1022 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 4835785   578 HIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKHNFVKDLQFNRS---YHWGGTEIKVWHGKVEGL 654
Cdd:cd03791    1 KVLFVTSEVAPFAKTGGLGDVAGALPKALAKLGHDVRVILPRYGQIPDELDGYLRVLGLevkVGGRGEEVGVFELPVDGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   655 SVYFLDPQNGLFQRG----CVYGCADDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYTQYGLIKTRI 730
Cdd:cd03791   81 DYYFLDNPEFFDRPGlpgpPGYDYPDNAERFAFFSRAALELLRRLGFQPDIIHANDWHTALVPAYLKTRYRGPGFKKIKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   731 VFTIHNLEFGA----------------------------NAIGKAMTFADKATTVSPTYAKEVA-------GNSVISAHL 775
Cdd:cd03791  161 VFTIHNLAYQGlfpldtlaelglppelfhidglefygqiNFLKAGIVYADRVTTVSPTYAKEILtpeygegLDGVLRARA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   776 YKFHGIINGIDPDIWDPYNDNFIPVPYtSENVVEGKRAAKEELQNRLGLK-SADFPVVGIITRLTHQKGIHLIKHAIWRT 854
Cdd:cd03791  241 GKLSGILNGIDYDEWNPATDKLIPANY-SANDLEGKAENKAALQKELGLPvDPDAPLFGFVGRLTEQKGVDLILDALPEL 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   855 LERNGQVVLLGSApDPRIQNDFVNLANQlhssHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYGAV 934
Cdd:cd03791  320 LEEGGQLVVLGSG-DPEYEQAFRELAER----YPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRYGTL 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   935 PVVRKTGGLFDTVFDVDHDKEraqaqvlEPNGFSFDGADAPGVDYALNRAISAWYDgREWFNSLCKTVMEQDWSWNRPAL 1014
Cdd:cd03791  395 PIVRRTGGLADTVFDYDPETG-------EGTGFVFEDYDAEALLAALRRALALYRN-PELWRKLQKNAMKQDFSWDKSAK 466

                 ....*...
gi 4835785  1015 EYLELYHS 1022
Cdd:cd03791  467 EYLELYRS 474
GlgA COG0297
Glycogen synthase [Carbohydrate transport and metabolism];
577-1023 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 4835785   577 LHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIK---HNFVKDLQFNRSYHWGGTEIKVWHGKVEG 653
Cdd:COG0297    1 MKILFVASEAAPFAKTGGLADVVGALPKALAKLGHDVRVVLPGYPSIDdklKDLEVVASLEVPLGGRTYYARVLEGPDDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   654 LSVYFLDpQNGLFQRGCVYG-----CADDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYTQYGLIKT 728
Cdd:COG0297   81 VPVYFID-NPELFDRPGPYGdpdrdYPDNAERFAFFSRAALELLKGLDWKPDIIHCHDWQTGLIPALLKTRYADDPFKRI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   729 RIVFTIHNLE----FGANAIGK------------------------AMTFADKATTVSPTYAKEV------AG-NSVISA 773
Cdd:COG0297  160 KTVFTIHNLAyqgiFPAEILELlglppelftpdglefygqinflkaGIVYADRVTTVSPTYAREIqtpefgEGlDGLLRA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   774 HLYKFHGIINGIDPDIWDPYNDNFIPVPYTSENVvEGKRAAKEELQNRLGLK-SADFPVVGIITRLTHQKGIHLIKHAIW 852
Cdd:COG0297  240 RSGKLSGILNGIDYDVWNPATDPYLPANYSADDL-EGKAANKAALQEELGLPvDPDAPLIGMVSRLTEQKGLDLLLEALD 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   853 RTLERNGQVVLLGSApDPRIQNDFVNLANQlhssHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYG 932
Cdd:COG0297  319 ELLEEDVQLVVLGSG-DPEYEEAFRELAAR----YPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMYALRYG 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   933 AVPVVRKTGGLFDTVFDVDHDKERAqaqvlepNGFSFDGADAPGVDYALNRAISAWYDGREWfNSLCKTVMEQDWSWNRP 1012
Cdd:COG0297  394 TVPIVRRTGGLADTVIDYNEATGEG-------TGFVFDEYTAEALLAAIRRALALYRDPEAW-RKLQRNAMKQDFSWEKS 465
                        490
                 ....*....|.
gi 4835785  1013 ALEYLELYHSA 1023
Cdd:COG0297  466 AKEYLELYREL 476
glgA PRK00654
glycogen synthase GlgA;
577-1025 5.54e-180

glycogen synthase GlgA;


Pssm-ID: 234809 [Multi-domain]  Cd Length: 466  Bit Score: 531.62  E-value: 5.54e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    577 LHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKHNFVKDLQFNRsyhWGGTEIKVWHGKVEGLSV 656
Cdd:PRK00654    1 MKILFVASECAPLIKTGGLGDVVGALPKALAALGHDVRVLLPGYPAIREKLRDAQVVGR---LDLFTVLFGHLEGDGVPV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    657 YFLDPQNgLFQRGCVYGCADDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSA--PVsWLFKDHYTQYGLIKTriVFTI 734
Cdd:PRK00654   78 YLIDAPH-LFDRPSGYGYPDNGERFAFFSWAAAEFAEGLDPRPDIVHAHDWHTGliPA-LLKEKYWRGYPDIKT--VFTI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    735 HNLE----FGANAIG-----------------------KA-MTFADKATTVSPTYAKEV---------AGnsVISAHLYK 777
Cdd:PRK00654  154 HNLAyqglFPAEILGelglpaeafhleglefygqisflKAgLYYADRVTTVSPTYAREIttpefgyglEG--LLRARSGK 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    778 FHGIINGIDPDIWDPYNDNFIPVPYTSENVvEGKRAAKEELQNRLGLKSADFPVVGIITRLTHQKGIHLIKHAIWRTLER 857
Cdd:PRK00654  232 LSGILNGIDYDIWNPETDPLLAANYSADDL-EGKAENKRALQERFGLPDDDAPLFAMVSRLTEQKGLDLVLEALPELLEQ 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    858 NGQVVLLGSaPDPRIQNDFVNLANQlhssHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYGAVPVV 937
Cdd:PRK00654  311 GGQLVLLGT-GDPELEEAFRALAAR----YPGKVGVQIGYDEALAHRIYAGADMFLMPSRFEPCGLTQLYALRYGTLPIV 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    938 RKTGGLFDTVFDVDHDKERAqaqvlepNGFSFDGADAPGVDYALNRAISAWYDGREWfNSLCKTVMEQDWSWNRPALEYL 1017
Cdd:PRK00654  386 RRTGGLADTVIDYNPEDGEA-------TGFVFDDFNAEDLLRALRRALELYRQPPLW-RALQRQAMAQDFSWDKSAEEYL 457

                  ....*...
gi 4835785   1018 ELYHSARK 1025
Cdd:PRK00654  458 ELYRRLLG 465
glgA TIGR02095
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ...
577-1023 5.19e-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: 5.19e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     577 LHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKHNFVKDLQFNRSY---HWGGTE-IKVWHGKVE 652
Cdd:TIGR02095    1 MRVLFVAAEMAPFAKTGGLADVVGALPKALAALGHDVRVLLPAYGCIEDEVDDQVKVVELVdlsVGPRTLyVKVFEGVVE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     653 GLSVYFLDPQnGLFQR-GCVYGCA--DDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYTQyglIKTR 729
Cdd:TIGR02095   81 GVPVYFIDNP-SLFDRpGGIYGDDypDNAERFAFFSRAAAELLSGLGWQPDVVHAHDWHTALVPALLKAVYRP---NPIK 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     730 IVFTIHNLE----FGANAIGK------------------------AMTFADKATTVSPTYAKEV----AG---NSVISAH 774
Cdd:TIGR02095  157 TVFTIHNLAyqgvFPADDFSElglppeyfhmeglefygrvnflkgGIVYADRVTTVSPTYAREIltpeFGyglDGVLKAR 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     775 LYKFHGIINGIDPDIWDPYNDNFIPVPYTSENVvEGKRAAKEELQNRLGLK-SADFPVVGIITRLTHQKGIHLIKHAIWR 853
Cdd:TIGR02095  237 SGKLRGILNGIDTEVWNPATDPYLKANYSADDL-AGKAENKEALQEELGLPvDDDVPLFGVISRLTQQKGVDLLLAALPE 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     854 TLERNGQVVLLGSApDPRIQNDFVNLANQlhssHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYGA 933
Cdd:TIGR02095  316 LLELGGQLVVLGTG-DPELEEALRELAER----YPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYAMRYGT 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     934 VPVVRKTGGLFDTVFDVDHDKERAqaqvlepNGFSFDGADAPGVDYALNRAISAWYDGREWFNSLCKTVMEQDWSWNRPA 1013
Cdd:TIGR02095  391 VPIVRRTGGLADTVVDGDPEAESG-------TGFLFEEYDPGALLAALSRALRLYRQDPSLWEALQKNAMSQDFSWDKSA 463
                          490
                   ....*....|
gi 4835785    1014 LEYLELYHSA 1023
Cdd:TIGR02095  464 KQYVELYRSL 473
PLN02939 PLN02939
transferase, transferring glycosyl groups
577-1023 9.52e-153

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 478.63  E-value: 9.52e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    577 LHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKHNFVKDLQ----FNRSYHWGGT-EIKVWHGKV 651
Cdd:PLN02939  482 LHIVHIAAEMAPVAKVGGLADVVSGLGKALQKKGHLVEIVLPKYDCMQYDQIRNLKvldvVVESYFDGNLfKNKIWTGTV 561
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    652 EGLSVYFLDPQN--GLFQRGCVYGCADDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYTQYGLIKTR 729
Cdd:PLN02939  562 EGLPVYFIEPQHpsKFFWRAQYYGEHDDFKRFSYFSRAALELLYQSGKKPDIIHCHDWQTAFVAPLYWDLYAPKGFNSAR 641
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    730 IVFTIHNLEFGA-------------------------------NAIGKAMTFADKATTVSPTYAKEVAG------NSVIS 772
Cdd:PLN02939  642 ICFTCHNFEYQGtapasdlascgldvhqldrpdrmqdnahgriNVVKGAIVYSNIVTTVSPTYAQEVRSeggrglQDTLK 721
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    773 AHLYKFHGIINGIDPDIWDPYNDNFIPVPYtSENVVEGKRAAKEELQNRLGLKSADF--PVVGIITRLTHQKGIHLIKHA 850
Cdd:PLN02939  722 FHSKKFVGILNGIDTDTWNPSTDRFLKVQY-NANDLQGKAANKAALRKQLGLSSADAsqPLVGCITRLVPQKGVHLIRHA 800
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    851 IWRTLERNGQVVLLGSAPDPRIQNDFVNLANQLHSShgDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMR 930
Cdd:PLN02939  801 IYKTAELGGQFVLLGSSPVPHIQREFEGIADQFQSN--NNIRLILKYDEALSHSIYAASDMFIIPSMFEPCGLTQMIAMR 878
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    931 YGAVPVVRKTGGLFDTVFDVDHDKERAQAQvlepNGFSFDGADAPGVDYALNRAISAWYDGREWFNSLCKTVMEQDWSWN 1010
Cdd:PLN02939  879 YGSVPIVRKTGGLNDSVFDFDDETIPVELR----NGFTFLTPDEQGLNSALERAFNYYKRKPEVWKQLVQKDMNIDFSWD 954
                         490
                  ....*....|...
gi 4835785   1011 RPALEYLELYHSA 1023
Cdd:PLN02939  955 SSASQYEELYQRA 967
PRK14099 PRK14099
glycogen synthase GlgA;
576-1022 5.50e-78

glycogen synthase GlgA;


Pssm-ID: 237610 [Multi-domain]  Cd Length: 485  Bit Score: 263.89  E-value: 5.50e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    576 PLHIVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKHNFVKDLQFNRSYHWGGTEIKVWHGKVEGLS 655
Cdd:PRK14099    3 PLRVLSVASEIFPLIKTGGLADVAGALPAALKAHGVEVRTLVPGYPAVLAGIEDAEQVHSFPDLFGGPARLLAARAGGLD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    656 VYFLDPQNgLFQR-GCVY------GCADDAGRFGFFCHAA--LEFLLQGGFHPDILHCHDWSSAPV-SWLfkdHYTQYGL 725
Cdd:PRK14099   83 LFVLDAPH-LYDRpGNPYvgpdgkDWPDNAQRFAALARAAaaIGQGLVPGFVPDIVHAHDWQAGLApAYL---HYSGRPA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    726 IKTriVFTIHNLEF---------GA----------------NAIG--KA-MTFADKATTVSPTYAKEVAG-------NSV 770
Cdd:PRK14099  159 PGT--VFTIHNLAFqgqfprellGAlglppsafsldgveyyGGIGylKAgLQLADRITTVSPTYALEIQGpeagmglDGL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    771 ISAHLYKFHGIINGIDPDIWDPYNDNFIPVPYTSENVvEGKRAAKEELQNRLGLKSA-DFPVVGIITRLTHQKGIHLIKH 849
Cdd:PRK14099  237 LRQRADRLSGILNGIDTAVWNPATDELIAATYDVETL-AARAANKAALQARFGLDPDpDALLLGVISRLSWQKGLDLLLE 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    850 AIwRTLERNG-QVVLLGSApDPRIQNDFVNLAnqlhSSHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIA 928
Cdd:PRK14099  316 AL-PTLLGEGaQLALLGSG-DAELEARFRAAA----QAYPGQIGVVIGYDEALAHLIQAGADALLVPSRFEPCGLTQLCA 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    929 MRYGAVPVVRKTGGLFDTVFDVDhdkERAQAQVLePNGFSFDGADAPGVDYALNRAISAWYDGREWFNsLCKTVMEQDWS 1008
Cdd:PRK14099  390 LRYGAVPVVARVGGLADTVVDAN---EMAIATGV-ATGVQFSPVTADALAAALRKTAALFADPVAWRR-LQRNGMTTDVS 464
                         490
                  ....*....|....
gi 4835785   1009 WNRPALEYLELYHS 1022
Cdd:PRK14099  465 WRNPAQHYAALYRS 478
Glyco_transf_5 pfam08323
Starch synthase catalytic domain;
579-765 7.98e-63

Starch synthase catalytic domain;


Pssm-ID: 400563 [Multi-domain]  Cd Length: 239  Bit Score: 212.96  E-value: 7.98e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     579 IVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKHN-----FVKDLQFNRSYHWGGTEIKVWHGKVEG 653
Cdd:pfam08323    1 ILFVASEVAPFAKTGGLADVVGALPKALAALGHDVRVIMPRYGNIPEErnqleDVIRLSVAAGVPVRPLTVGVARLELDG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     654 LSVYFLDPQNgLFQRGCVYGC-----ADDAGRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYTQYGLIKT 728
Cdd:pfam08323   81 VDVYFLDNPD-YFDRPGLYGDdgrdyEDNAERFAFFSRAALELAKKLGWIPDIIHCHDWHTALVPAYLKEAYADDPFKNI 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4835785     729 RIVFTIHNLEFG----------------------------ANAIGKAMTFADKATTVSPTYAKEV 765
Cdd:pfam08323  160 KTVFTIHNLAYQgrfpadlldllglppedfnldglefygqINFLKAGIVYADAVTTVSPTYAEEI 224
PRK14098 PRK14098
starch synthase;
579-1020 6.57e-56

starch synthase;


Pssm-ID: 172588 [Multi-domain]  Cd Length: 489  Bit Score: 201.89  E-value: 6.57e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    579 IVHIAVEMAPIAKVGGLGDVVTSLSRAVQELNHNVDIVFPKYDCIKhnfvkDLQFNRSYHWGGTEIKV--------WHGK 650
Cdd:PRK14098    8 VLYVSGEVSPFVRVSALADFMASFPQALEEEGFEARIMMPKYGTIN-----DRKFRLHDVLRLSDIEVplkektdlLHVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    651 VEGL-----SVYFL-----DPQNGLF----QRGCVYGCADdagRFGFFCHAALEFLLQGGFHPDILHCHDWSSAPVSWLF 716
Cdd:PRK14098   83 VTALpsskiQTYFLynekyFKRNGLFtdmsLGGDLKGSAE---KVIFFNVGVLETLQRLGWKPDIIHCHDWYAGLVPLLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    717 KDHYTQYGLIK-TRIVFTIHN------LEFGA--------------------NAIGKAMTFADKATTVSPTYAKEVAGNS 769
Cdd:PRK14098  160 KTVYADHEFFKdIKTVLTIHNvyrqgvLPFKVfqkllpeevcsglhregdevNMLYTGVEHADLLTTTSPRYAEEIAGDG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    770 --------VISAHLYKFHGIINGIDPDIWDPYNDNFIPVPYTSENVvEGKRAAKEELQNRLGLK-SADFPVVGIITRLTH 840
Cdd:PRK14098  240 eeafgldkVLEERKMRLHGILNGIDTRQWNPSTDKLIKKRYSIERL-DGKLENKKALLEEVGLPfDEETPLVGVIINFDD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    841 QKGIHLIKHAIWRTLERNGQVVLLGSApDPRIQNDFVNLANQlhssHGDRARLVLTYDEPLSHLIYAGADFILVPSIFEP 920
Cdd:PRK14098  319 FQGAELLAESLEKLVELDIQLVICGSG-DKEYEKRFQDFAEE----HPEQVSVQTEFTDAFFHLAIAGLDMLLMPGKIES 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    921 CGLTQLIAMRYGAVPVVRKTGGLFDTVFDVDHDKeraqaqvlePNGFSFDGADAPGVDYALNRAISAWYDGREWfNSLCK 1000
Cdd:PRK14098  394 CGMLQMFAMSYGTIPVAYAGGGIVETIEEVSEDK---------GSGFIFHDYTPEALVAKLGEALALYHDEERW-EELVL 463
                         490       500
                  ....*....|....*....|
gi 4835785   1001 TVMEQDWSWNRPALEYLELY 1020
Cdd:PRK14098  464 EAMERDFSWKNSAEEYAQLY 483
CBM_25 smart01066
Carbohydrate binding domain;
136-221 2.99e-23

Carbohydrate binding domain;


Pssm-ID: 198134 [Multi-domain]  Cd Length: 83  Bit Score: 94.35  E-value: 2.99e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785      136 DEDIEVFLNRNLSTLNNEPDVLIMGaFNEWRWKSFTRRLEKTWiHEDWLSCLLHIpKEAYKMDFVFFNGQSVYDNNDSKD 215
Cdd:smart01066    1 GNTVTVYYNGLLATSGAKNVYLHYG-FGENNWTDVPDVRMEKT-GEGWVKATIPV-KEAYKLNFCFKDGAGNWDNNGGAN 77

                    ....*.
gi 4835785      216 FCVEIK 221
Cdd:smart01066   78 YHFEIG 83
CBM_25 smart01066
Carbohydrate binding domain;
478-567 2.00e-19

Carbohydrate binding domain;


Pssm-ID: 198134 [Multi-domain]  Cd Length: 83  Bit Score: 83.56  E-value: 2.00e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785      478 GNPVTVLYNPANTVlNGKPEVWFRGSF--NRWTHrlgpLPPQKMEATDDesSHVKTTAKVpLDAYMMDFVFseKEDGGIF 555
Cdd:smart01066    1 GNTVTVYYNGLLAT-SGAKNVYLHYGFgeNNWTD----VPDVRMEKTGE--GWVKATIPV-KEAYKLNFCF--KDGAGNW 70
                            90
                    ....*....|..
gi 4835785      556 DNKNGLDYHLPV 567
Cdd:smart01066   71 DNNGGANYHFEI 82
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
697-1021 3.06e-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: 87.59  E-value: 3.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   697 FHPDILHCHDWSSAPVSWLFKdhytqyGLIKTRIVFTIHNLEFGAN------------AIGKAMTFADKATTVSPTYAKE 764
Cdd:cd03801   81 RKFDVVHAHGLLAALLAALLA------LLLGAPLVVTLHGAEPGRLllllaaerrllaRAEALLRRADAVIAVSEALRDE 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   765 VAGNSVISAHlyKFHGIINGIDPDIWDPyndnfipvpytsenvvegkraakeeLQNRLGLKSADFPVVGIITRLTHQKGI 844
Cdd:cd03801  155 LRALGGIPPE--KIVVIPNGVDLERFSP-------------------------PLRRKLGIPPDRPVLLFVGRLSPRKGV 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   845 HLIKHAIWRTLERNGQVVLLGSAPDPRIQNDFVNLANQLhsshGDRARLV--LTYDEPLShlIYAGADFILVPSIFEPCG 922
Cdd:cd03801  208 DLLLEALAKLLRRGPDVRLVIVGGDGPLRAELEELELGL----GDRVRFLgfVPDEELPA--LYAAADVFVLPSRYEGFG 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   923 LTQLIAMRYGaVPVVrktgglfdtVFDVDHDKEraqAQVLEPNGFSFDGADAPgvdyALNRAISAWYDGREWFNSLCK-- 1000
Cdd:cd03801  282 LVVLEAMAAG-LPVV---------ATDVGGLPE---VVEDGEGGLVVPPDDVE----ALADALLRLLADPELRARLGRaa 344
                        330       340
                 ....*....|....*....|..
gi 4835785  1001 -TVMEQDWSWNRPALEYLELYH 1021
Cdd:cd03801  345 rERVAERFSWERVAERLLDLYR 366
CBM53 pfam16760
Starch/carbohydrate-binding module (family 53);
315-404 1.54e-17

Starch/carbohydrate-binding module (family 53);


Pssm-ID: 465261 [Multi-domain]  Cd Length: 76  Bit Score: 78.10  E-value: 1.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     315 KLYYNKrsgplTNSKELWLHGGFNNWVDGLSIVVKlvnaelKDVDPKSGNWWFAEVVVPGGALVIDWVFADgppkGAFLY 394
Cdd:pfam16760    1 NIYYNG-----SLAKEVYIHGGFNGWKNVQDVPME------KLPPTGGGDWFSATVPVPEDAYVLDFVFKD----GAGNW 65
                           90
                   ....*....|
gi 4835785     395 DNNGYQDFHA 404
Cdd:pfam16760   66 DNNNGQNYHI 75
CBM_25 smart01066
Carbohydrate binding domain;
311-407 1.81e-17

Carbohydrate binding domain;


Pssm-ID: 198134 [Multi-domain]  Cd Length: 83  Bit Score: 78.17  E-value: 1.81e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785      311 EDTVKLYYNKRSGPlTNSKELWLHGGF--NNWVDglsivvkLVNAELKdvdpKSGNWWFAEVVVPGGALVIDWVFADgpp 388
Cdd:smart01066    1 GNTVTVYYNGLLAT-SGAKNVYLHYGFgeNNWTD-------VPDVRME----KTGEGWVKATIPVKEAYKLNFCFKD--- 65
                            90
                    ....*....|....*....
gi 4835785      389 kGAFLYDNNGYQDFHALVP 407
Cdd:smart01066   66 -GAGNWDNNGGANYHFEIG 83
CBM53 pfam16760
Starch/carbohydrate-binding module (family 53);
141-219 3.08e-17

Starch/carbohydrate-binding module (family 53);


Pssm-ID: 465261 [Multi-domain]  Cd Length: 76  Bit Score: 76.95  E-value: 3.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     141 VFLNRNLStlnnePDVLIMGAFNEWRWKSFTRrLEKT--WIHEDWLSCLLHIPKEAYKMDFVFFNGQSVYDNNDSKDFCV 218
Cdd:pfam16760    2 IYYNGSLA-----KEVYIHGGFNGWKNVQDVP-MEKLppTGGGDWFSATVPVPEDAYVLDFVFKDGAGNWDNNNGQNYHI 75

                   .
gi 4835785     219 E 219
Cdd:pfam16760   76 P 76
CBM53 pfam16760
Starch/carbohydrate-binding module (family 53);
482-566 1.68e-16

Starch/carbohydrate-binding module (family 53);


Pssm-ID: 465261 [Multi-domain]  Cd Length: 76  Bit Score: 75.02  E-value: 1.68e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     482 TVLYNPANtvlngKPEVWFRGSFNRWTHRLGpLPPQKMEATDDESsHVKTTAKVPLDAYMMDFVFseKEDGGIFDNKNGL 561
Cdd:pfam16760    1 NIYYNGSL-----AKEVYIHGGFNGWKNVQD-VPMEKLPPTGGGD-WFSATVPVPEDAYVLDFVF--KDGAGNWDNNNGQ 71

                   ....*
gi 4835785     562 DYHLP 566
Cdd:pfam16760   72 NYHIP 76
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
697-947 8.62e-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: 73.93  E-value: 8.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   697 FHPDILHCHDWSSAPVSWLFKdhytqyGLIKTRIVFTIHNLEFgANAIGKA-----MTFADKATTVSPTYAKEVAGNsvI 771
Cdd:cd03819   75 ERIDLIHAHSRAPAWLGWLAS------RLTGVPLVTTVHGSYL-ATYHPKDfalavRARGDRVIAVSELVRDHLIEA--L 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   772 SAHLYKFHGIINGIDPDIWDPyndnfipvpytsenvvegkrAAKEELQNRLGLKSaDFPVVGIITRLTHQKGIHLIKHAI 851
Cdd:cd03819  146 GVDPERIRVIPNGVDTDRFPP--------------------EAEAEERAQLGLPE-GKPVVGYVGRLSPEKGWLLLVDAA 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   852 WRtLERNGQVVLL--GSAPdpriQNDFV-NLANQLhsshGDRARLVLT-YDEPLSHLiYAGADFILVPSIFEPCGLTQLI 927
Cdd:cd03819  205 AE-LKDEPDFRLLvaGDGP----ERDEIrRLVERL----GLRDRVTFTgFREDVPAA-LAASDVVVLPSLHEEFGRVALE 274
                        250       260
                 ....*....|....*....|.
gi 4835785   928 AMRYGaVPVVRKT-GGLFDTV 947
Cdd:cd03819  275 AMACG-TPVVATDvGGAREIV 294
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
684-1017 1.10e-09

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: 61.49  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   684 FCHAALEFLLQGGFHPDILHCHDWSSAPVSWLFKDHYtqygliKTRIVFTIHNLE------------------FGANAIg 745
Cdd:cd03800   87 FADGLLRFIAREGGRYDLIHSHYWDSGLVGALLARRL------GVPLVHTFHSLGrvkyrhlgaqdtyhpslrITAEEQ- 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   746 kAMTFADKATTVSPtyaKEVAGN-SVISAHLYKFHGIINGIDPDIWDPYNDnfipvpytsenvvegkraaKEELQNRLGL 824
Cdd:cd03800  160 -ILEAADRVIASTP---QEADELiSLYGADPSRINVVPPGVDLERFFPVDR-------------------AEARRARLLL 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   825 KSaDFPVVGIITRLTHQKGIH-LIK-HAIWRTLERNGQVVLLGSAPDPRIQNDFVNLAnQLHSSHG--DRARLVLTYDEP 900
Cdd:cd03800  217 PP-DKPVVLALGRLDPRKGIDtLVRaFAQLPELRELANLVLVGGPSDDPLSMDREELA-ELAEELGliDRVRFPGRVSRD 294
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   901 LSHLIYAGADFILVPSIFEPCGLTQLIAMRYGaVPVV-RKTGGLFDTVFDvdhdkeraqaqvlEPNGFSFDGADAPgvdy 979
Cdd:cd03800  295 DLPELYRAADVFVVPSLYEPFGLTAIEAMACG-TPVVaTAVGGLQDIVRD-------------GRTGLLVDPHDPE---- 356
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 4835785   980 ALNRAISAWYDGREWFNSLCKTVME---QDWSWNRPALEYL 1017
Cdd:cd03800  357 ALAAALRRLLDDPALWQRLSRAGLErarAHYTWESVADQLL 397
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
697-937 1.60e-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: 57.72  E-value: 1.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   697 FHPDILHCHDWSSAPVSWLfkDHYTQYGLiktRIVFTIHNLEFGAnaIGKAMTFADKATTVSPT--YAKEVAGNSVISAH 774
Cdd:cd03823   95 FRPDVVHTHNLSGLGASLL--DAARDLGI---PVVHTLHDYWLLC--PRQFLFKKGGDAVLAPSrfTANLHEANGLFSAR 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   775 LYKfhgIINGIDPD-IWDPyndnfIPVPYTSENVVegkraakeelqnrlglksadfpvvGIITRLTHQKGIHLIKHAIWR 853
Cdd:cd03823  168 ISV---IPNAVEPDlAPPP-----RRRPGTERLRF------------------------GYIGRLTEEKGIDLLVEAFKR 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   854 TLERNGQVVLLGSAPDPRIQNDFVNLANQLHSShgdrarlvLTYDEPLSHliYAGADFILVPSIF-EPCGLTQLIAMRYG 932
Cdd:cd03823  216 LPREDIELVIAGHGPLSDERQIEGGRRIAFLGR--------VPTDDIKDF--YEKIDVLVVPSIWpEPFGLVVREAIAAG 285

                 ....*
gi 4835785   933 aVPVV 937
Cdd:cd03823  286 -LPVI 289
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
903-1025 1.80e-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: 1.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   903 HLIYAGADFILVPSIFEPCGLTQLIAMRYGAVPVVRKTGGLFDTVFDvdhdkeraqaqvlEPNGFSFDGADAPgvdyALN 982
Cdd:COG0438   15 EALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIED-------------GETGLLVPPGDPE----ALA 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 4835785   983 RAISAWYDGREWFNSL---CKTVMEQDWSWNRPALEYLELYHSARK 1025
Cdd:COG0438   78 EAILRLLEDPELRRRLgeaARERAEERFSWEAIAERLLALYEELLA 123
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
818-949 3.59e-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: 3.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   818 LQNRLGLKSADFPVVGiitRLTHQKGIHLIKHAIWRTLER--NGQVVLLGSAPDPRIQNdfvnlANQLHSSHGDRARLV- 894
Cdd:cd01635  102 ARLLVSLPLADKVSVG---RLVPEKGIDLLLEALALLKARlpDLVLVLVGGGGEREEEE-----ALAAALGLLERVVIIg 173
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 4835785   895 LTYDEPLSHLIYAGADFILVPSIFEPCGLTQLIAMRYGAVPVVRKTGGLFDTVFD 949
Cdd:cd01635  174 GLVDDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVD 228
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
233-284 1.02e-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: 1.02e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4835785     233 LLEEKLR---------EQEKLAKEEAERERQKEEKRRIEAQKAAIEAdRAQAKAETQKRRE 284
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 ...
699-937 2.10e-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: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   699 PDILHCHDWSSApvSWLFKDhytqyGLIKTRIVFTIHN-------LEFGANAIGKAMTFADKATTVSPTYAKEVAGNSVI 771
Cdd:cd03811   84 PDVVISFLGFAT--YIVAKL-----AAARSKVIAWIHSslsklyyLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLGPS 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   772 SAHlyKFHGIINGIDPDiwdpyndnFIpvpytsenvvegKRAAKEELQNRLGlksaDFPVVGIITRLTHQKGIHLIKHAI 851
Cdd:cd03811  157 PPE--KIEVIYNPIDID--------RI------------RALAKEPILNEPE----DGPVILAVGRLDPQKGHDLLIEAF 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   852 WRTLERNGQV--VLLGSAPDpriQNDFVNLANQLHSShgDRARLVLTYDEPLShlIYAGADFILVPSIFEPCGLTQLIAM 929
Cdd:cd03811  211 AKLRKKYPDVklVILGDGPL---REELEKLAKELGLA--ERVIFLGFQSNPYP--YLKKADLFVLSSRYEGFPNVLLEAM 283

                 ....*...
gi 4835785   930 RYGaVPVV 937
Cdd:cd03811  284 ALG-TPVV 290
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
830-951 2.83e-06

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 47.89  E-value: 2.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     830 PVVGIITRLTH-QKGIHLIKHAIWRTLERNGQVVLL--GSAPDPRIQNDFVNLANQLHsshgdrarlVLTYDEPLSHLiY 906
Cdd:pfam13692    2 PVILFVGRLHPnVKGVDYLLEAVPLLRKRDNDVRLVivGDGPEEELEELAAGLEDRVI---------FTGFVEDLAEL-L 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 4835785     907 AGADFILVPSIFEPCGLTQLIAMRYGaVPVV-RKTGGLFDTVFDVD 951
Cdd:pfam13692   72 AAADVFVLPSLYEGFGLKLLEAMAAG-LPVVaTDVGGIPELVDGEN 116
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
683-1023 1.27e-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: 48.53  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   683 FFCHAALEFLLQG--GFHPDILHCH-DWSSAPVSWLFKdhytqyGLIKTRIVFTIH--------NLEFGANAIGKAMTFA 751
Cdd:cd03798   78 PLRAPSLAKLLKRrrRGPPDLIHAHfAYPAGFAAALLA------RLYGVPYVVTEHgsdinvfpPRSLLRKLLRWALRRA 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   752 DKATTVSPTYAKEVAGNSVIsahLYKFHGIINGIDPDIWDPyndnfipvpytsenvvegkraakeeLQNRLGLKsADFPV 831
Cdd:cd03798  152 ARVIAVSKALAEELVALGVP---RDRVDVIPNGVDPARFQP-------------------------EDRGLGLP-LDAFV 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   832 VGIITRLTHQKGIHLIKHAIWRTLERNGQVVLLgsapdprIQNDFVNLA--NQLHSSHGDRARLVLTydEPLSH----LI 905
Cdd:cd03798  203 ILFVGRLIPRKGIDLLLEAFARLAKARPDVVLL-------IVGDGPLREalRALAEDLGLGDRVTFT--GRLPHeqvpAY 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   906 YAGADFILVPSIFEPCGLTQLIAMRYGaVPVV-RKTGGLFDTVFDvdhdkeraqaqvlEPNGFSFDGADAPGVDYALNRA 984
Cdd:cd03798  274 YRACDVFVLPSRHEGFGLVLLEAMACG-LPVVaTDVGGIPEVVGD-------------PETGLLVPPGDADALAAALRRA 339
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 4835785   985 ISAWYDGREWfNSLCKTVMEQdWSWNRPALEYLELYHSA 1023
Cdd:cd03798  340 LAEPYLRELG-EAARARVAER-FSWVKAADRIAAAYRDV 376
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
593-788 1.50e-05

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 46.37  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     593 GGLGDVVTSLSRAVQELNHNVDIVFPKYDcikhnfvkdlqfnrsyhwGGTEIKVWHGKVEGLSVYFLDPQNglfqrgcvy 672
Cdd:pfam13439    1 GGVERYVLELARALARRGHEVTVVTPGGP------------------GPLAEEVVRVVRVPRVPLPLPPRL--------- 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     673 gcaddagRFGFFCHAALEFLLQGgFHPDILHCHDWSSAPVSWLFKDHYTqygliKTRIVFTIHNLEFGANAIG------- 745
Cdd:pfam13439   54 -------LRSLAFLRRLRRLLRR-ERPDVVHAHSPFPLGLAALAARLRL-----GIPLVVTYHGLFPDYKRLGarlsplr 120
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 4835785     746 --------KAMTFADKATTVSPTYAKEVAGNSVISAHlyKFHGIINGIDPD 788
Cdd:pfam13439  121 rllrrlerRLLRRADRVIAVSEAVADELRRLYGVPPE--KIRVIPNGVDLE 169
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
233-293 1.59e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 48.26  E-value: 1.59e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4835785    233 LLEEKLREQEKLAKEEAERE------RQKEEKRRIEAQK-------AAIEADRAQAKAETQKRRelLQPAIKKA 293
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 ...
234-293 2.80e-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: 2.80e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     234 LEEKLREQEKLAKEEAEReRQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQPAIKKA 293
Cdd:TIGR02794   94 LEQRAAAEKAAKQAEQAA-KQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQA 152
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
234-287 5.44e-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: 5.44e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4835785     234 LEEKLREQEKLAKE------------EAERERQKEEKRRIEA---QKAAIEADRAQAKAETQKRRELLQ 287
Cdd:pfam13868  118 AEEKLEKQRQLREEidefneeqaewkELEKEEEREEDERILEylkEKAEREEEREAEREEIEEEKEREI 186
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
235-284 6.43e-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: 6.43e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 4835785     235 EEKLR---EQEKLAKEEAERERQ--KEEKRRIEAQKAAIEAdRAQAKAEtQKRRE 284
Cdd:pfam05672   68 EERRReeeERQRKAEEEAEEREQreQEEQERLQKQKEEAEA-KAREEAE-RQRQE 120
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
235-293 6.78e-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: 46.38  E-value: 6.78e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     235 EEKLR-EQEKLAKEEAERERQKEEkrriEAQKAAIEADRAQAKAETQKRREllqPAIKKA 293
Cdd:TIGR02794  123 EAKAKqAAEAKAKAEAEAERKAKE----EAAKQAEEEAKAKAAAEAKKKAE---EAKKKA 175
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
234-293 6.89e-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: 6.89e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4835785     234 LEEKLR---EQEKLAKEEAERERQK----EEKRRiEAQKAAIEADRAQAKAETQKRReLLQPAIKKA 293
Cdd:pfam20492   11 LEERLKqyeEETKKAQEELEESEETaeelEEERR-QAEEEAERLEQKRQEAEEEKER-LEESAEMEA 75
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
686-937 7.60e-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: 7.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   686 HAALEFLLQGGFHPDILHCHDwssapvswlfkdHYTQYGLIKTRIVFTIHNL------EFGANAIGKAMTF--------A 751
Cdd:cd03809   72 LRWLQILLPKKDKPDLLHSPH------------NTAPLLLKGCPQVVTIHDLiplrypEFFPKRFRLYYRLllpislrrA 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   752 DKATTVSPTYAKEVAGNSVISAHlyKFHGIINGIDPDIWdpyndnfipvpytsenvvegKRAAKEELQNRLGLKSADFPV 831
Cdd:cd03809  140 DAIITVSEATRDDIIKFYGVPPE--KIVVIPLGVDPSFF--------------------PPESAAVLIAKYLLPEPYFLY 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   832 VGIITRlthQKGIH-LIK-HAIWRTLERNGQVVLLGSAPDPRIQNDFVNLANQLHsshgDRARLV--LTYDEpLSHLiYA 907
Cdd:cd03809  198 VGTLEP---RKNHErLLKaFALLKKQGGDLKLVIVGGKGWEDEELLDLVKKLGLG----GRVRFLgyVSDED-LPAL-YR 268
                        250       260       270
                 ....*....|....*....|....*....|
gi 4835785   908 GADFILVPSIFEPCGLTQLIAMRYGaVPVV 937
Cdd:cd03809  269 GARAFVFPSLYEGFGLPVLEAMACG-TPVI 297
MRP-L20 pfam12824
Mitochondrial ribosomal protein subunit L20; This family is the essential mitochondrial ...
237-286 8.31e-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: 44.25  E-value: 8.31e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4835785     237 KLREQE-------KLAKE------------EAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELL 286
Cdd:pfam12824   93 RLRAEDpekwtrkKLAKKfgcsplfvsmvtEAPKEKKKEMKAELEAIKSRWGPKRRIAREDRKKRKELW 161
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
233-284 8.68e-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: 8.68e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     233 LLEEKLR----EQEKLAKE----EAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRE 284
Cdd:pfam20492   38 ELEEERRqaeeEAERLEQKrqeaEEEKERLEESAEMEAEEKEQLEAELAEAQEEIARLEE 97
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
235-292 1.00e-04

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: 1.00e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     235 EEKLREQEKLAKEEAERERQKEEKRRIEAQKAAIEAD--RAQAKAETQKRRELLQPAIKK 292
Cdd:pfam15927    2 RLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQdrRAEELEELKHLLEERKEALEK 61
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
235-298 1.03e-04

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: 1.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4835785   235 EEKLREQEKLAKEEAERERQKEEKRRIEAQKAAieadrAQAKAETQKRRELLQPAIKKAVVSAE 298
Cdd:COG3064   25 KRAAAEAEQKAKEEAEEERLAELEAKRQAEEEA-----REAKAEAEQRAAELAAEAAKKLAEAE 83
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
239-293 1.60e-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: 1.60e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 4835785     239 REQEKLAKE-EAERERQKEEKRRIEAQKAAIEADrAQAKAETQKRRELLQPAIKKA 293
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 ...
235-298 1.67e-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: 1.67e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4835785     235 EEKLREQEKLAKEEAERERQKEE-KRRIEA-QKAAIEADRAQ-AKAETQKRREllQPAIKKAVVSAE 298
Cdd:TIGR02794  101 EKAAKQAEQAAKQAEEKQKQAEEaKAKQAAeAKAKAEAEAERkAKEEAAKQAE--EEAKAKAAAEAK 165
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
230-293 2.13e-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: 2.13e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4835785     230 ENFLLEEKLRE-QEKLAKEEAERERQKEEKRRI-----------EAQKAAIE---ADRAQAKAETQKRRELLQPAIKKA 293
Cdd:pfam13868  153 EDERILEYLKEkAEREEEREAEREEIEEEKEREiarlraqqekaQDEKAERDelrAKLYQEEQERKERQKEREEAEKKA 231
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
828-947 2.50e-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: 2.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     828 DFPVVGIITRLTHQKGIHLIKHAIWRTLERNGQVVLL--GSAPDpriQNDFVNLANQLHSshGDRARLVL-TYDEPLSHL 904
Cdd:pfam00534    1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLViaGDGEE---EKRLKKLAEKLGL--GDNVIFLGfVSDEDLPEL 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 4835785     905 iYAGADFILVPSIFEPCGLTQLIAMRYGAVPVVRKTGGLFDTV 947
Cdd:pfam00534   76 -LKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVV 117
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
235-298 3.06e-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: 42.34  E-value: 3.06e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4835785     235 EEKLREQEKLAKEEAERERQKEEKRRIEAQKAAIEADRAQAKAET-QKRREllqPAIKKAVVSAE 298
Cdd:pfam05672   54 EERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERlQKQKE---EAEAKAREEAE 115
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
236-287 3.15e-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: 3.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 4835785   236 EKLREQE----KLAKEEAERERQKEEKRRiEAQKAAIEADRAQAKAETQKRRELLQ 287
Cdd:COG2268  227 ELEQEREietaRIAEAEAELAKKKAEERR-EAETARAEAEAAYEIAEANAEREVQR 281
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
235-298 3.44e-04

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 44.26  E-value: 3.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4835785   235 EEKLREQEKLAKEEAERERQK---EEKRRIEAQKAAIEADRAQAKAETQKRRE-LLQPAIKKAVVSAE 298
Cdd:COG3064   59 EAKAEAEQRAAELAAEAAKKLaeaEKAAAEAEKKAAAEKAKAAKEAEAAAAAEkAAAAAEKEKAEEAK 126
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
234-299 5.66e-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: 5.66e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4835785   234 LEEKLREQEKlAKEEAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQPAIKKAVVSAEN 299
Cdd:COG3064   75 AAKKLAEAEK-AAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEE 139
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
234-288 8.21e-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: 41.18  E-value: 8.21e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4835785     234 LEEKLR----EQEKLAKEEA------ERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQP 288
Cdd:pfam05672   29 REEQERlekeEEERLRKEELrrraeeERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQ 93
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
235-299 8.50e-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: 8.50e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4835785     235 EEKLREQEKLAKEEAERERQKEEKRRIEAQKAAI------EADRAQAKAETQKRRELLQ-PAIKKAVVSAEN 299
Cdd:pfam07767  215 EEKLERVLEKIAESAATAEAREEKRKTKAQRNKEkrrkeeEREAKEEKALKKKLAQLERlKEIAKEIAEKEK 286
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
235-293 1.46e-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: 42.21  E-value: 1.46e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4835785     235 EEKLREQEKLAKEEAERERQKEEKRRIEAQKAAIEAD---RAQAKAETQKRRELLQpAIKKA 293
Cdd:pfam13868  180 EEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQErkeRQKEREEAEKKARQRQ-ELQQA 240
PRK03963 PRK03963
V-type ATP synthase subunit E; Provisional
233-287 1.53e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 167649 [Multi-domain]  Cd Length: 198  Bit Score: 40.89  E-value: 1.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    233 LLEEKLREQEKLAK---EEAER--ERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQ 287
Cdd:PRK03963    7 IIQEINREAEQKIEyilEEAQKeaEKIKEEARKRAESKAEWILRKAKTQAELEKQRIIAN 66
Cgr1 pfam03879
Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA ...
233-292 1.54e-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: 1.54e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4835785     233 LLEEKlrEQEKLAKEEAERERQ--KEEKRRIEAQKAAIEAdraqAKAETQKRRELLQPAIKK 292
Cdd:pfam03879   52 LKDEK--EAERQRRIQAIKERReaKEEKERYEELAAKMHA----KKVERLKRKEKRNKLLKE 107
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
236-293 1.75e-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: 1.75e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4835785     236 EKLREQEKLAKEEAERERQKEE-KRRIEAQ-KAAIEADR------AQAKAETQKRRElLQPAIKKA 293
Cdd:TIGR02794  149 AKQAEEEAKAKAAAEAKKKAEEaKKKAEAEaKAKAEAEAkakaeeAKAKAEAAKAKA-AAEAAAKA 213
AhaH TIGR02926
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
239-284 2.17e-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: 2.17e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 4835785     239 REQEKLAKEEAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRE 284
Cdd:TIGR02926   30 REEARELLEEAEEEASKLGEEIIKEAEEEIEKEAEKIREEGEKEIE 75
PRK14474 PRK14474
F0F1 ATP synthase subunit B; Provisional
233-301 2.25e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184696 [Multi-domain]  Cd Length: 250  Bit Score: 40.96  E-value: 2.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4835785    233 LLEEKLRE---QEKLAKEEAERERQKEEKrrIEAQKAAIEAdRAQAKAETQKRRELLQpaIKKAVVSAENVW 301
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.
227-289 2.37e-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: 2.37e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4835785     227 VDFENFLLEEKLREQEKLAKEeAERERQKEEKRRIEAQKAAIEADRAQAKAETQKR--RELLQPA 289
Cdd:pfam05262  194 VNFRRDMTDLKERESQEDAKR-AQQLKEELDKKQIDADKAQQKADFAQDNADKQRDevRQKQQEA 257
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
235-293 2.37e-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: 2.37e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4835785     235 EEKLREQEKLAKEEAERERQKE--EKRRIEAQKAAIEADRAQAKAETQKRRELLQPAIKKA 293
Cdd:TIGR02794  163 EAKKKAEEAKKKAEAEAKAKAEaeAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAA 223
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
224-287 2.83e-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: 2.83e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4835785     224 MDKVDFENFLleEKLREQEKLAKEEAE--RERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQ 287
Cdd:pfam13868  258 REEEEFERML--RKQAEDEEIEQEEAEkrRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLR 321
NtpH COG2811
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ...
235-294 2.84e-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: 2.84e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4835785   235 EEKLREQEKLAKE---EAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRE-LLQPA---IKKAV 294
Cdd:COG2811   29 EERIAEAREEAEEiieQAEEEAEEEAQERLEEAREEAEAEAEEIIEEGEKEAEaLKKKAedkLDKAV 95
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
753-1022 3.13e-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: 3.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   753 KATTVSPT-YAKEVAGNSVISAHlYKFHGIINGIDPDIWDPYNdnfipvpytsenvvegkraaKEELQNRLGLkSADFPV 831
Cdd:cd03825  138 RLTIVAPSrWLADMVRRSPLLKG-LPVVVIPNGIDTEIFAPVD--------------------KAKARKRLGI-PQDKKV 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   832 VGIITRLTHQ--KGIHLIKHAIwRTL--ERNGQVVLLGSAPDPRIQNDFvnlanqLHSSHGdrarlVLTYDEPLsHLIYA 907
Cdd:cd03825  196 ILFGAESVTKprKGFDELIEAL-KLLatKDDLLLVVFGKNDPQIVILPF------DIISLG-----YIDDDEQL-VDIYS 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785   908 GADFILVPSIFEPCGLTQLIAMRYGaVPVVR-KTGGLFDTVFDvdhdkeraqaqvlEPNGFSFDGADAPGVDYALNRAIS 986
Cdd:cd03825  263 AADLFVHPSLADNLPNTLLEAMACG-TPVVAfDTGGSPEIVQH-------------GVTGYLVPPGDVQALAEAIEWLLA 328
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 4835785   987 AwYDGREWFNSLCKTVMEQDWSWNRPALEYLELYHS 1022
Cdd:cd03825  329 N-PKERESLGERARALAENHFDQRVQAQRYLELYKD 363
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
233-294 3.22e-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: 3.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4835785   233 LLEEKLRE-QEKLAKEEAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQPAIKKAV 294
Cdd:COG1579  107 DLEDEILElMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
235-294 3.44e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 41.47  E-value: 3.44e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    235 EEKLREQEKLAKEEAeRERQKEEKRRIEAQKAAIEAdRAQAKAEtqKRRELLQPAIKKAV 294
Cdd:PRK05035  437 EIRAIEQEKKKAEEA-KARFEARQARLEREKAAREA-RHKKAAE--ARAAKDKDAVAAAL 492
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
225-277 3.61e-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: 3.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 4835785   225 DKVDFENFLLEEKLR---EQEKLAKEEAERERQKEEKRRIEAQKAAIEAdRAQAKA 277
Cdd:cd03401  140 DDVLITNIDFPDEYEkaiEAKQVAEQEAERAKFELEKAEQEAERKVIEA-EGEAEA 194
PRK03963 PRK03963
V-type ATP synthase subunit E; Provisional
232-297 4.14e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 167649 [Multi-domain]  Cd Length: 198  Bit Score: 39.74  E-value: 4.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    232 FLLEEKLREQEKLaKEEAER--ERQKEEKRRIEAQKAAIEADR--AQAKAETQKRRELLQPAIKKAVVSA 297
Cdd:PRK03963   21 YILEEAQKEAEKI-KEEARKraESKAEWILRKAKTQAELEKQRiiANAKLEVRRKRLAVQEELISEVLEA 89
V-ATPase_G pfam03179
Vacuolar (H+)-ATPase G subunit; This family represents the eukaryotic vacuolar (H+)-ATPase ...
239-295 4.27e-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: 37.97  E-value: 4.27e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4835785     239 REQEKL--AKEEAERE----RQKEEK--RRIEAQKAAI-EADRAQAKAETQKRRELLQPAI---KKAVV 295
Cdd:pfam03179   26 RKQKRLkqAKEEAEKEieeyRAQREKefKEFEAKHMGSrEELEKKIEKETQEKIQEIKDSVnknKEAVV 94
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
241-299 5.84e-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: 5.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 4835785   241 QEKLAKEEAERERQkEEKRRIEAQKAAIEADRAQAKAETQKRRELLQPAIKKAVVSAEN 299
Cdd:COG3064    2 QEALEEKAAEAAAQ-ERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEARE 59
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
233-298 6.15e-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: 6.15e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4835785   233 LLEEKLRE---QEKLAKEEAERERQKEEKRR--IEAQKAAIEADRAQAKAETQKRRELLQPAIKKAVVSAE 298
Cdd:COG3064    4 ALEEKAAEaaaQERLEQAEAEKRAAAEAEQKakEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAE 74
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
234-282 6.17e-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: 6.17e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 4835785     234 LEEKLREQ--EKLAKEEAERERQKEEKR--RIEAQKAAIEADRaqaKAETQKR 282
Cdd:pfam11600   66 LKEKERREkkEKDEKEKAEKLRLKEEKRkeKQEALEAKLEEKR---KKEEEKR 115
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
237-287 6.36e-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: 6.36e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4835785   237 KLRE-QEKLAKEEAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQ 287
Cdd:COG1196  233 KLRElEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE 284
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
223-293 6.82e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.58  E-value: 6.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4835785    223 GMDKVDFENFL--LEEKLREQEKLAKE-EAERERQKEEKRRIEAQKAAIEADRAQAKAETQKRrelLQPAIKKA 293
Cdd:PRK00409  512 GEDKEKLNELIasLEELERELEQKAEEaEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKE---AQQAIKEA 582
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
235-293 6.93e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 38.78  E-value: 6.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785    235 EEKLR--------EQEKL--AKEEAERERQKEEKR------RIEAQK----------AAIEADRAQAKAETQKRRELLQP 288
Cdd:PRK07352   63 EERLRqaaqalaeAQQKLaqAQQEAERIRADAKARaeairaEIEKQAiedmarlkqtAAADLSAEQERVIAQLRREAAEL 142

                  ....*
gi 4835785    289 AIKKA 293
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 ...
235-282 7.50e-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: 7.50e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4835785   235 EEKLRE-----QEKL--AKEEAERERQ------KEEKRRIEAQ-KAAIEADRAQAKAETQKR 282
Cdd:cd06503   57 EEKLAEaraeaQEIIeeARKEAEKIKEeilaeaKEEAERILEQaKAEIEQEKEKALAELRKE 118
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
234-292 8.59e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 8.59e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4835785   234 LEEKLRE-QEKLAKEEAERERQKEEKRRIEAQKAAIEADRAQAKAET---QKRRELLQPAIKK 292
Cdd:COG4372   78 LEEELEElNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERqdlEQQRKQLEAQIAE 140
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
235-287 8.74e-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: 8.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 4835785     235 EEKLREQEKLAKEEAERERQKEEKRRIEAQKAAIEADraQAKAETQKRRELLQ 287
Cdd:pfam05672   47 ELRRRAEEERARREEEARRLEEERRREEEERQRKAEE--EAEEREQREQEEQE 97
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
234-287 9.26e-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: 39.52  E-value: 9.26e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 4835785     234 LEEKLREQEKLAKEEAErERQKEEKRRIEAQKAAIEADRAQAKAETQKRRELLQ 287
Cdd:pfam13868   78 LEEQIEEREQKRQEEYE-EKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLRE 130
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
219-300 9.27e-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: 9.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4835785     219 EIKGGMDKVDFenfLLEEKLREQEKLAKEEAERERQKE---------------EKRRIEAQKAAIEADRAQAKAETQKRR 283
Cdd:TIGR02169  181 EVEENIERLDL---IIDEKRQQLERLRREREKAERYQAllkekreyegyellkEKEALERQKEAIERQLASLEEELEKLT 257
                           90
                   ....*....|....*..
gi 4835785     284 ELLQpAIKKAVVSAENV 300
Cdd:TIGR02169  258 EEIS-ELEKRLEEIEQL 273
 
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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