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Conserved domains on  [gi|672087703|ref|XP_008771498|]
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glycerol kinase isoform X4 [Rattus norvegicus]

Protein Classification

glycerol kinase( domain architecture ID 10167374)

glycerol kinase converts glycerol and ATP to glycerol-3-phosphate and ADP as part of the synthesis of triglycerides and glycerophospholipid

CATH:  3.30.420.40
EC:  2.7.1.30
SCOP:  3000092

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_NBD_FGGY_GK1-3-like cd07792
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ...
11-544 0e+00

nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


:

Pssm-ID: 466802 [Multi-domain]  Cd Length: 499  Bit Score: 983.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  11 PLVGAVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQLNIDISNIKAIGV 90
Cdd:cd07792    1 PLVGAIDQGTTSTRFIVFDS-TGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKALGISPSDIKAIGI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  91 SNQRETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNNNFVKSKTG 170
Cdd:cd07792   80 TNQRETTVVWDKSTGKPLYNAI----------------------------VWLDTRTSDTVEELSAKTPGGKDHFRKKTG 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 171 LPLSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGINGGVHCTDVTNASRTMLFNIHSLEWDKELCEF 250
Cdd:cd07792  132 LPISTYFSAVKLRWLLDNVPEVKKAVDDGRLLFGTVDSWLIWNLTGGKNGGVHVTDVTNASRTMLMNLRTLQWDPELCEF 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 251 FGIPMEILPNVRSSSEIYGLMKIshslkaGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFS 330
Cdd:cd07792  212 FGIPMSILPEIRSSSEVYGKIAS------GPLAGVPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFS 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 331 EHGLLTTVAYKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSA 410
Cdd:cd07792  286 KHGLLTTVAYKLGPDAPPVYALEGSIAIAGAAVQWLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDA 365
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 411 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTA 490
Cdd:cd07792  366 RGTIVGLTQFTTKAHIARAALEAVCFQTREILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTA 445
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 672087703 491 LGAAMAAGAAEGVGVWSLEPEDLSAVTMERFEPQINAEESEIRYSTWKKAVMKS 544
Cdd:cd07792  446 LGAAIAAGLAVGVWKSLDELKSLNEGGRTVFEPQISEEERERRYKRWKKAVERS 499
 
Name Accession Description Interval E-value
ASKHA_NBD_FGGY_GK1-3-like cd07792
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ...
11-544 0e+00

nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466802 [Multi-domain]  Cd Length: 499  Bit Score: 983.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  11 PLVGAVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQLNIDISNIKAIGV 90
Cdd:cd07792    1 PLVGAIDQGTTSTRFIVFDS-TGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKALGISPSDIKAIGI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  91 SNQRETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNNNFVKSKTG 170
Cdd:cd07792   80 TNQRETTVVWDKSTGKPLYNAI----------------------------VWLDTRTSDTVEELSAKTPGGKDHFRKKTG 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 171 LPLSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGINGGVHCTDVTNASRTMLFNIHSLEWDKELCEF 250
Cdd:cd07792  132 LPISTYFSAVKLRWLLDNVPEVKKAVDDGRLLFGTVDSWLIWNLTGGKNGGVHVTDVTNASRTMLMNLRTLQWDPELCEF 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 251 FGIPMEILPNVRSSSEIYGLMKIshslkaGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFS 330
Cdd:cd07792  212 FGIPMSILPEIRSSSEVYGKIAS------GPLAGVPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFS 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 331 EHGLLTTVAYKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSA 410
Cdd:cd07792  286 KHGLLTTVAYKLGPDAPPVYALEGSIAIAGAAVQWLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDA 365
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 411 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTA 490
Cdd:cd07792  366 RGTIVGLTQFTTKAHIARAALEAVCFQTREILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTA 445
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 672087703 491 LGAAMAAGAAEGVGVWSLEPEDLSAVTMERFEPQINAEESEIRYSTWKKAVMKS 544
Cdd:cd07792  446 LGAAIAAGLAVGVWKSLDELKSLNEGGRTVFEPQISEEERERRYKRWKKAVERS 499
glycerol_kin TIGR01311
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ...
11-547 0e+00

glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of carbohydrate kinases. [Energy metabolism, Other]


Pssm-ID: 273549 [Multi-domain]  Cd Length: 493  Bit Score: 813.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703   11 PLVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGV 90
Cdd:TIGR01311   1 PYILAIDQGTTSSRAIVFD-KDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAG---IKPDDIAAIGI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703   91 SNQRETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNnnFVKSKTG 170
Cdd:TIGR01311  77 TNQRETTVVWDKATGKPLYNAI----------------------------VWQDRRTASICEELKAEGYGE--FIREKTG 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  171 LPLSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGingGVHCTDVTNASRTMLFNIHSLEWDKELCEF 250
Cdd:TIGR01311 127 LPLDPYFSATKLRWLLDNVPGVREAAERGELLFGTIDTWLIWNLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLEL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  251 FGIPMEILPNVRSSSEIYGLMKISHSLkagalEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFS 330
Cdd:TIGR01311 204 FGIPREILPEVRSSSEVYGYTDPGLLG-----AEIPITGVLGDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVIS 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  331 EHGLLTTVAYKLGRDKPVYyALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSA 410
Cdd:TIGR01311 279 KHGLLTTVAYQLGGKKPVY-ALEGSVFVAGAAVQWLRDNLKLIKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDA 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  411 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTA 490
Cdd:TIGR01311 358 RGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDAGVEITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTA 437
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 672087703  491 LGAAMAAGAAEGVGVWSLEPEDLSAVTmERFEPQINAEESEIRYSTWKKAVMKSIGW 547
Cdd:TIGR01311 438 LGAAYAAGLAVGYWKSLEEIEALWRVE-KTFEPEMDEEEREARYAGWKEAVKRSLGW 493
GlpK COG0554
Glycerol kinase [Energy production and conversion];
13-548 0e+00

Glycerol kinase [Energy production and conversion];


Pssm-ID: 440320 [Multi-domain]  Cd Length: 496  Bit Score: 741.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  13 VGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVSN 92
Cdd:COG0554    5 ILAIDQGTTSTRAILFDRD-GNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAG---ISAEDIAAIGITN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  93 QRETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRipGNNNFVKSKTGLP 172
Cdd:COG0554   81 QRETTVVWDRKTGKPLYNAI----------------------------VWQDRRTADICEELKAD--GLEDLIREKTGLV 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 173 LSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGingGVHCTDVTNASRTMLFNIHSLEWDKELCEFFG 252
Cdd:COG0554  131 LDPYFSATKIKWILDNVPGARERAEAGELLFGTIDSWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFG 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 253 IPMEILPNVRSSSEIYGlmkisHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEH 332
Cdd:COG0554  208 IPRSMLPEVRPSSEVFG-----ETDPDLFGAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKN 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 333 GLLTTVAYKLGrDKPVYyALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARG 412
Cdd:COG0554  283 GLLTTIAWGLG-GKVTY-ALEGSIFVAGAAVQWLRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARG 360
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 413 IICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalg 492
Cdd:COG0554  361 AIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTalg 440
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 672087703 493 aamaagaaegvgVWSlEPEDLSAV--TMERFEPQINAEESEIRYSTWKKAVMKSIGWV 548
Cdd:COG0554  441 aayl--aglavgFWK-SLEELAALwkVDRRFEPQMDEEERERLYAGWKKAVERTLGWA 495
PTZ00294 PTZ00294
glycerol kinase-like protein; Provisional
11-548 0e+00

glycerol kinase-like protein; Provisional


Pssm-ID: 240348 [Multi-domain]  Cd Length: 504  Bit Score: 712.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  11 PLVGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQLNIDISnIKAIGV 90
Cdd:PTZ00294   2 KYIGSIDQGTTSTRFIIFDEK-GNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPSFK-IKAIGI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  91 SNQRETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNNNFVKsKTG 170
Cdd:PTZ00294  80 TNQRETVVAWDKVTGKPLYNAI----------------------------VWLDTRTYDIVNELTKKYGGSNFFQK-ITG 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 171 LPLSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGingGVHCTDVTNASRTMLFNIHSLEWDKELCEF 250
Cdd:PTZ00294 131 LPISTYFSAFKIRWMLENVPAVKDAVKEGTLLFGTIDTWLIWNLTGG---KSHVTDVTNASRTFLMNIKTLKWDEELLNK 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 251 FGIPMEILPNVRSSSEIYGLMKishSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFS 330
Cdd:PTZ00294 208 FGIPKETLPEIKSSSENFGTIS---GEAVPLLEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFS 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 331 EHGLLTTVAYKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSA 410
Cdd:PTZ00294 285 KHGLLTTVCYQLGPNGPTVYALEGSIAVAGAGVEWLRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDA 364
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 411 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTa 490
Cdd:PTZ00294 365 RGTIVGMTLKTTRAHIVRAALEAIALQTNDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETT- 443
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 491 lGAAMAAGAAEGVGVW-SLEP-EDLSAVTMERFEPQINAEESEIRYSTWKKAVMKSIGWV 548
Cdd:PTZ00294 444 -ALGAALLAGLAVGVWkSLEEvKKLIRRSNSTFSPQMSAEERKAIYKEWNKAVERSLKWA 502
FGGY_N pfam00370
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ...
12-300 1.22e-107

FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.


Pssm-ID: 395295 [Multi-domain]  Cd Length: 245  Bit Score: 322.36  E-value: 1.22e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703   12 LVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEklgQLNIDISNIKAIGVS 91
Cdd:pfam00370   1 YYLGIDCGTTSTKAILFN-EQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLS---QLGISLKQIKGIGIS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703   92 NQRETTVVWDKLTgEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKriPGNNNFVKSKTGL 171
Cdd:pfam00370  77 NQGHGTVLLDKND-KPLYNAI----------------------------LWKDRRTAEIVENLKE--EGNNQKLYEITGL 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  172 PLSTYFSAVKLRWLLDNVKKVQEAVEenraLFGTIDSWLIWSLTGginggVHCTDVTNASRTMLFNIHSLEWDKELCEFF 251
Cdd:pfam00370 126 PIWPGFTLSKLRWIKENEPEVFEKIH----KFLTIHDYLRWRLTG-----VFVTDHTNASRSMMFNIHKLDWDPELLAAL 196
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 672087703  252 GIPMEILPNVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVG 300
Cdd:pfam00370 197 GIPRDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
 
Name Accession Description Interval E-value
ASKHA_NBD_FGGY_GK1-3-like cd07792
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ...
11-544 0e+00

nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466802 [Multi-domain]  Cd Length: 499  Bit Score: 983.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  11 PLVGAVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQLNIDISNIKAIGV 90
Cdd:cd07792    1 PLVGAIDQGTTSTRFIVFDS-TGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKALGISPSDIKAIGI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  91 SNQRETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNNNFVKSKTG 170
Cdd:cd07792   80 TNQRETTVVWDKSTGKPLYNAI----------------------------VWLDTRTSDTVEELSAKTPGGKDHFRKKTG 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 171 LPLSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGINGGVHCTDVTNASRTMLFNIHSLEWDKELCEF 250
Cdd:cd07792  132 LPISTYFSAVKLRWLLDNVPEVKKAVDDGRLLFGTVDSWLIWNLTGGKNGGVHVTDVTNASRTMLMNLRTLQWDPELCEF 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 251 FGIPMEILPNVRSSSEIYGLMKIshslkaGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFS 330
Cdd:cd07792  212 FGIPMSILPEIRSSSEVYGKIAS------GPLAGVPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFS 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 331 EHGLLTTVAYKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSA 410
Cdd:cd07792  286 KHGLLTTVAYKLGPDAPPVYALEGSIAIAGAAVQWLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDA 365
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 411 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTA 490
Cdd:cd07792  366 RGTIVGLTQFTTKAHIARAALEAVCFQTREILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTA 445
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 672087703 491 LGAAMAAGAAEGVGVWSLEPEDLSAVTMERFEPQINAEESEIRYSTWKKAVMKS 544
Cdd:cd07792  446 LGAAIAAGLAVGVWKSLDELKSLNEGGRTVFEPQISEEERERRYKRWKKAVERS 499
glycerol_kin TIGR01311
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ...
11-547 0e+00

glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of carbohydrate kinases. [Energy metabolism, Other]


Pssm-ID: 273549 [Multi-domain]  Cd Length: 493  Bit Score: 813.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703   11 PLVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGV 90
Cdd:TIGR01311   1 PYILAIDQGTTSSRAIVFD-KDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAG---IKPDDIAAIGI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703   91 SNQRETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNnnFVKSKTG 170
Cdd:TIGR01311  77 TNQRETTVVWDKATGKPLYNAI----------------------------VWQDRRTASICEELKAEGYGE--FIREKTG 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  171 LPLSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGingGVHCTDVTNASRTMLFNIHSLEWDKELCEF 250
Cdd:TIGR01311 127 LPLDPYFSATKLRWLLDNVPGVREAAERGELLFGTIDTWLIWNLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLEL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  251 FGIPMEILPNVRSSSEIYGLMKISHSLkagalEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFS 330
Cdd:TIGR01311 204 FGIPREILPEVRSSSEVYGYTDPGLLG-----AEIPITGVLGDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVIS 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  331 EHGLLTTVAYKLGRDKPVYyALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSA 410
Cdd:TIGR01311 279 KHGLLTTVAYQLGGKKPVY-ALEGSVFVAGAAVQWLRDNLKLIKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDA 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  411 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTA 490
Cdd:TIGR01311 358 RGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDAGVEITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTA 437
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 672087703  491 LGAAMAAGAAEGVGVWSLEPEDLSAVTmERFEPQINAEESEIRYSTWKKAVMKSIGW 547
Cdd:TIGR01311 438 LGAAYAAGLAVGYWKSLEEIEALWRVE-KTFEPEMDEEEREARYAGWKEAVKRSLGW 493
ASKHA_NBD_FGGY_GK cd07769
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ...
13-541 0e+00

nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466789 [Multi-domain]  Cd Length: 486  Bit Score: 747.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  13 VGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVSN 92
Cdd:cd07769    2 ILAIDQGTTSTRAILFDED-GNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAG---ISASDIAAIGITN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  93 QRETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRipGNNNFVKSKTGLP 172
Cdd:cd07769   78 QRETTVVWDKKTGKPLYNAI----------------------------VWQDRRTADICEELKAK--GLEERIREKTGLP 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 173 LSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGingGVHCTDVTNASRTMLFNIHSLEWDKELCEFFG 252
Cdd:cd07769  128 LDPYFSATKIKWILDNVPGARERAERGELLFGTIDTWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLEWDDELLELFG 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 253 IPMEILPNVRSSSEIYGlmkisHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEH 332
Cdd:cd07769  205 IPRSMLPEVRPSSEVFG-----YTDPEGLGAGIPIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKN 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 333 GLLTTVAYKLgrDKPVYYALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARG 412
Cdd:cd07769  280 GLLTTIAWQI--GGKVTYALEGSIFIAGAAIQWLRDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARG 357
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 413 IICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalg 492
Cdd:cd07769  358 AIVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTalg 437
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 672087703 493 aamaagaaegvgVWSLEPEDLSAVTMER-FEPQINAEESEIRYSTWKKAV 541
Cdd:cd07769  438 aayl--aglavgFWKDLDELASLWQVDKrFEPSMDEEERERLYRGWKKAV 485
GlpK COG0554
Glycerol kinase [Energy production and conversion];
13-548 0e+00

Glycerol kinase [Energy production and conversion];


Pssm-ID: 440320 [Multi-domain]  Cd Length: 496  Bit Score: 741.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  13 VGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVSN 92
Cdd:COG0554    5 ILAIDQGTTSTRAILFDRD-GNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAG---ISAEDIAAIGITN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  93 QRETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRipGNNNFVKSKTGLP 172
Cdd:COG0554   81 QRETTVVWDRKTGKPLYNAI----------------------------VWQDRRTADICEELKAD--GLEDLIREKTGLV 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 173 LSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGingGVHCTDVTNASRTMLFNIHSLEWDKELCEFFG 252
Cdd:COG0554  131 LDPYFSATKIKWILDNVPGARERAEAGELLFGTIDSWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFG 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 253 IPMEILPNVRSSSEIYGlmkisHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEH 332
Cdd:COG0554  208 IPRSMLPEVRPSSEVFG-----ETDPDLFGAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKN 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 333 GLLTTVAYKLGrDKPVYyALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARG 412
Cdd:COG0554  283 GLLTTIAWGLG-GKVTY-ALEGSIFVAGAAVQWLRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARG 360
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 413 IICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalg 492
Cdd:COG0554  361 AIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTalg 440
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 672087703 493 aamaagaaegvgVWSlEPEDLSAV--TMERFEPQINAEESEIRYSTWKKAVMKSIGWV 548
Cdd:COG0554  441 aayl--aglavgFWK-SLEELAALwkVDRRFEPQMDEEERERLYAGWKKAVERTLGWA 495
PTZ00294 PTZ00294
glycerol kinase-like protein; Provisional
11-548 0e+00

glycerol kinase-like protein; Provisional


Pssm-ID: 240348 [Multi-domain]  Cd Length: 504  Bit Score: 712.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  11 PLVGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQLNIDISnIKAIGV 90
Cdd:PTZ00294   2 KYIGSIDQGTTSTRFIIFDEK-GNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPSFK-IKAIGI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  91 SNQRETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNNNFVKsKTG 170
Cdd:PTZ00294  80 TNQRETVVAWDKVTGKPLYNAI----------------------------VWLDTRTYDIVNELTKKYGGSNFFQK-ITG 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 171 LPLSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGingGVHCTDVTNASRTMLFNIHSLEWDKELCEF 250
Cdd:PTZ00294 131 LPISTYFSAFKIRWMLENVPAVKDAVKEGTLLFGTIDTWLIWNLTGG---KSHVTDVTNASRTFLMNIKTLKWDEELLNK 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 251 FGIPMEILPNVRSSSEIYGLMKishSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFS 330
Cdd:PTZ00294 208 FGIPKETLPEIKSSSENFGTIS---GEAVPLLEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFS 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 331 EHGLLTTVAYKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSA 410
Cdd:PTZ00294 285 KHGLLTTVCYQLGPNGPTVYALEGSIAVAGAGVEWLRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDA 364
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 411 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTa 490
Cdd:PTZ00294 365 RGTIVGMTLKTTRAHIVRAALEAIALQTNDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETT- 443
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 491 lGAAMAAGAAEGVGVW-SLEP-EDLSAVTMERFEPQINAEESEIRYSTWKKAVMKSIGWV 548
Cdd:PTZ00294 444 -ALGAALLAGLAVGVWkSLEEvKKLIRRSNSTFSPQMSAEERKAIYKEWNKAVERSLKWA 502
PLN02295 PLN02295
glycerol kinase
12-548 0e+00

glycerol kinase


Pssm-ID: 215166 [Multi-domain]  Cd Length: 512  Bit Score: 698.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  12 LVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQ--LNIDiSNIKAIG 89
Cdd:PLN02295   1 FVGAIDQGTTSTRFIIYD-RDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAkgHNVD-SGLKAIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  90 VSNQRETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNNNFVKSKT 169
Cdd:PLN02295  79 ITNQRETTVAWSKSTGRPLYNAI----------------------------VWMDSRTSSICRRLEKELSGGRKHFVETC 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 170 GLPLSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGINGGVHCTDVTNASRTMLFNIHSLEWDKELCE 249
Cdd:PLN02295 131 GLPISTYFSATKLLWLLENVDAVKEAVKSGDALFGTIDSWLIWNLTGGASGGVHVTDVTNASRTMLMNLKTLDWDKPTLE 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 250 FFGIPMEILPNVRSSSEIYGlmKISHSlkaGALEGVPISGCLGDQSAALVGQMCfQDGQAKNTYGTGCFLLCNTGHKCVF 329
Cdd:PLN02295 211 ALGIPAEILPKIVSNSEVIG--TIAKG---WPLAGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVP 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 330 SEHGLLTTVAYKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPS 409
Cdd:PLN02295 285 SKHGLLTTVAYKLGPDAPTNYALEGSVAIAGAAVQWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDD 364
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 410 ARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSH-----LQVDGGMTSNKILMQLQADILYIPVVKPS 484
Cdd:PLN02295 365 ARGVCVGITRFTNKAHIARAVLESMCFQVKDVLDAMRKDAGEEKSHkglflLRVDGGATANNLLMQIQADLLGSPVVRPA 444
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672087703 485 MPETTalGAAMAAGAAEGVGVWSlePEDLSAVTMER----FEPQINAEESEIRYSTWKKAVMKSIGWV 548
Cdd:PLN02295 445 DIETT--ALGAAYAAGLAVGLWT--EEEIFASEKWKntttFRPKLDEEERAKRYASWCKAVERSFDLA 508
glpK PRK00047
glycerol kinase GlpK;
13-548 0e+00

glycerol kinase GlpK;


Pssm-ID: 234594 [Multi-domain]  Cd Length: 498  Bit Score: 688.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  13 VGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEktcEKLGQLNIDISNIKAIGVSN 92
Cdd:PRK00047   7 ILALDQGTTSSRAIIFD-HDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIA---EALAKAGISPDQIAAIGITN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  93 QRETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRipGNNNFVKSKTGLP 172
Cdd:PRK00047  83 QRETTVVWDKETGRPIYNAI----------------------------VWQDRRTADICEELKRD--GYEDYIREKTGLV 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 173 LSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGingGVHCTDVTNASRTMLFNIHSLEWDKELCEFFG 252
Cdd:PRK00047 133 IDPYFSGTKIKWILDNVEGARERAEKGELLFGTIDTWLVWKLTGG---KVHVTDYTNASRTMLFNIHTLDWDDELLELLD 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 253 IPMEILPNVRSSSEIYGLMKISHSLKAGalegVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEH 332
Cdd:PRK00047 210 IPRSMLPEVRPSSEVYGKTNPYGFFGGE----VPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSEN 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 333 GLLTTVAYKLGrDKPVYyALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARG 412
Cdd:PRK00047 286 GLLTTIAWGID-GKVVY-ALEGSIFVAGSAIQWLRDGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARG 363
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 413 IICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalg 492
Cdd:PRK00047 364 AIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETT--- 440
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672087703 493 aamaagaaegvgvwSL--------------EPEDLSAVTME--RFEPQINAEESEIRYSTWKKAVMKSIGWV 548
Cdd:PRK00047 441 --------------ALgaaylaglavgfwkDLDELKEQWKIdrRFEPQMDEEEREKLYAGWKKAVKRTLAWA 498
FGGY_EcGK_like cd07786
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ...
15-541 0e+00

Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases


Pssm-ID: 198361 [Multi-domain]  Cd Length: 486  Bit Score: 682.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  15 AVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEktcEKLGQLNIDISNIKAIGVSNQR 94
Cdd:cd07786    4 AIDQGTTSSRAILFD-HDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAR---EALAKAGIRASDIAAIGITNQR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  95 ETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRipGNNNFVKSKTGLPLS 174
Cdd:cd07786   80 ETTVVWDRETGKPVYNAI----------------------------VWQDRRTADICEELKAE--GHEEMIREKTGLVLD 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 175 TYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGingGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIP 254
Cdd:cd07786  130 PYFSATKIRWILDNVPGARERAERGELAFGTIDSWLIWKLTGG---KVHATDVTNASRTMLFNIHTLEWDDELLELFGIP 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 255 MEILPNVRSSSEIYGlmkisHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEHGL 334
Cdd:cd07786  207 ASMLPEVKPSSEVFG-----YTDPDLLGAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGL 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 335 LTTVAYKLGrdKPVYYALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGII 414
Cdd:cd07786  282 LTTIAWQLG--GKVTYALEGSIFIAGAAVQWLRDGLGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAI 359
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 415 CGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTAL--- 491
Cdd:cd07786  360 FGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALgaa 439
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 672087703 492 -----GAAMAAGAAEGVGVWSLEpedlsavtmERFEPQINAEESEIRYSTWKKAV 541
Cdd:cd07786  440 ylaglAVGLWKSLDELAKLWQVD---------RRFEPSMSEEEREALYAGWKKAV 485
ASKHA_NBD_FGGY_GK5-like cd07793
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ...
15-541 5.08e-146

nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466803 [Multi-domain]  Cd Length: 501  Bit Score: 430.06  E-value: 5.08e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  15 AVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVSNQR 94
Cdd:cd07793    4 AVDVGTTNIRCHIFDKK-GKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAG---LTPEDIAAIGISTQR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  95 ETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSK---------------RIP 159
Cdd:cd07793   80 NTFLTWDKKTGKPLHNFI----------------------------TWQDLRAAELCESWNRslllkalrggskflhFLT 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 160 GNNNFVKSKTgLPLSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGingGVHCTDVTNASRTMLFNIH 239
Cdd:cd07793  132 RNKRFLAASV-LKFSTAHVSIRLLWILQNNPELKEAAEKGELLFGTIDTWLLWKLTGG---KVHATDYSNASATGLFDPF 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 240 SLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKISHSLKAgalegVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFL 319
Cdd:cd07793  208 TLEWSPILLSLFGIPSSILPEVKDTSGDFGSTDPSIFGAE-----IPITAVVADQQAALFGECCFDKGDVKITMGTGTFI 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 320 LCNTGHKCVFSEHGLLTTVAYKLGrDKPVYyALEGSVAIAGAVIRWLRDNLGIiKSSEEIEKLAKEVGTSYGCYFVPAFS 399
Cdd:cd07793  283 DINTGSKPHASVKGLYPLVGWKIG-GEITY-LAEGNASDTGTVIDWAKSIGLF-DDPSETEDIAESVEDTNGVYFVPAFS 359
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 400 GLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIP 479
Cdd:cd07793  360 GLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKP 439
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672087703 480 VVKPSMPETTalGAAMAAGAAEGVGVWSlEPEDLSAV--TMERFEPQINAEESEIRYSTWKKAV 541
Cdd:cd07793  440 VERPKNTEMS--ALGAAFLAGLASGIWK-SKEELKKLrkIEKIFEPKMDNEKREELYKNWKKAV 500
FGGY_N pfam00370
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ...
12-300 1.22e-107

FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.


Pssm-ID: 395295 [Multi-domain]  Cd Length: 245  Bit Score: 322.36  E-value: 1.22e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703   12 LVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEklgQLNIDISNIKAIGVS 91
Cdd:pfam00370   1 YYLGIDCGTTSTKAILFN-EQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLS---QLGISLKQIKGIGIS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703   92 NQRETTVVWDKLTgEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKriPGNNNFVKSKTGL 171
Cdd:pfam00370  77 NQGHGTVLLDKND-KPLYNAI----------------------------LWKDRRTAEIVENLKE--EGNNQKLYEITGL 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  172 PLSTYFSAVKLRWLLDNVKKVQEAVEenraLFGTIDSWLIWSLTGginggVHCTDVTNASRTMLFNIHSLEWDKELCEFF 251
Cdd:pfam00370 126 PIWPGFTLSKLRWIKENEPEVFEKIH----KFLTIHDYLRWRLTG-----VFVTDHTNASRSMMFNIHKLDWDPELLAAL 196
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 672087703  252 GIPMEILPNVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVG 300
Cdd:pfam00370 197 GIPRDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
XylB COG1070
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ...
6-489 1.16e-91

Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440688 [Multi-domain]  Cd Length: 494  Bit Score: 290.20  E-value: 1.16e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703   6 KAVLGplvgaVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNI 85
Cdd:COG1070    1 KYVLG-----IDIGTTSVKAVLFDA-DGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAG---VDPEEI 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  86 KAIGVSNQRETTVVWDKlTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNNNFv 165
Cdd:COG1070   72 AAIGVSGQMHGLVLLDA-DGEPLRPAI----------------------------LWNDTRAAAEAAELREELGEEALY- 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 166 kSKTGLPLSTYFSAVKLRWLLDNvkkvQEAVEENRALFGTIDSWLIWSLTGginggVHCTDVTNASRTMLFNIHSLEWDK 245
Cdd:COG1070  122 -EITGNPLHPGFTAPKLLWLKEN----EPEIFARIAKVLLPKDYLRYRLTG-----EFVTDYSDASGTGLLDVRTRDWSD 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 246 ELCEFFGIPMEILPNVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGH 325
Cdd:COG1070  192 ELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDK 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 326 KcVFSEHGLLTTVAYKL-GRdkpvyYALEGSVAIAGAVIRWLRDNLGIIKSS--EEIEKLAKEVGT-SYGCYFVPAFSGL 401
Cdd:COG1070  272 P-LPDPEGRVHTFCHAVpGR-----WLPMGATNNGGSALRWFRDLFADGELDdyEELNALAAEVPPgADGLLFLPYLSGE 345
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 402 YAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVV 481
Cdd:COG1070  346 RTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRPVE 424

                 ....*...
gi 672087703 482 KPSMPETT 489
Cdd:COG1070  425 VPEAEEGG 432
ASKHA_NBD_FGGY cd00366
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ...
15-489 7.54e-88

nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466787 [Multi-domain]  Cd Length: 392  Bit Score: 276.75  E-value: 7.54e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  15 AVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVSNQR 94
Cdd:cd00366    4 GIDIGTTSVKAALFDE-DGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAG---IDPSDIAAIGISGQM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  95 ETTVVWDKlTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDlrtqstveklskripgnnnfvksktglpls 174
Cdd:cd00366   80 PGVVLVDA-DGNPLRPAI----------------------------IWLD------------------------------ 100
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 175 tyfsavklrwlldnvkkvqeaveeNRALFGTIDSWLIWSLTGginggVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIP 254
Cdd:cd00366  101 ------------------------RRAKFLQPNDYIVFRLTG-----EFAIDYSNASGTGLYDIKTGDWSEELLDALGIP 151
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 255 MEILPNVRSSSEIYGlmKISH--SLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGhKCVFSEH 332
Cdd:cd00366  152 REKLPPIVESGEVVG--RVTPeaAEETGLPAGTPVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTD-EPVPPDP 228
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 333 GLLTTVAYKLGRdkpvyYALEGSVAIAGAVIRWLRDNLGIIKSSEE----IEKLAKEVGT-SYGCYFVPAFSGLYAPYWE 407
Cdd:cd00366  229 RLLNRCHVVPGL-----WLLEGAINTGGASLRWFRDEFGEEEDSDAeyegLDELAAEVPPgSDGLIFLPYLSGERSPIWD 303
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 408 PSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPE 487
Cdd:cd00366  304 PAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEIL-EELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAE 382

                 ..
gi 672087703 488 TT 489
Cdd:cd00366  383 GA 384
ASKHA_NBD_FGGY_YgcE-like cd07779
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ...
15-489 1.68e-87

nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466798 [Multi-domain]  Cd Length: 433  Bit Score: 277.09  E-value: 1.68e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  15 AVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVSNQR 94
Cdd:cd07779    4 GIDVGTTSTRAIIFD-LDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAG---VDPEDIAAIGLTSQR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  95 ETTVVWDKlTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTqstveklskripgnnnfvksktglpls 174
Cdd:cd07779   80 STFVPVDE-DGRPLRPAI----------------------------SWQDKRT--------------------------- 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 175 tyfsavklrwlldnvkkvqeaveenrALFGTIDSWLIWSLTggingGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIP 254
Cdd:cd07779  104 --------------------------AKFLTVQDYLLYRLT-----GEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGID 152
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 255 MEILPNVRSSSEIYGlmKISH--SLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTgHKCVFSEH 332
Cdd:cd07779  153 RDKLPELVPPGTVIG--TLTKeaAEETGLPEGTPVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVS-DKPVEDPE 229
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 333 GLLTTVAYKLgrdkPVYYALEGSVAIAGAVIRWLRDNLG--------IIKSSEE-IEKLAKEVGT-SYGCYFVPAFSGLY 402
Cdd:cd07779  230 RRIPCNPSAV----PGKWVLEGSINTGGSAVRWFRDEFGqdevaekeLGVSPYElLNEEAAKSPPgSDGLLFLPYLAGAG 305
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 403 APYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVK 482
Cdd:cd07779  306 TPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRDNLEAM-EKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVER 384

                 ....*..
gi 672087703 483 PSMPETT 489
Cdd:cd07779  385 PETSEAT 391
ASKHA_NBD_FGGY_FK cd07773
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ...
12-489 3.35e-78

nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466793 [Multi-domain]  Cd Length: 443  Bit Score: 253.28  E-value: 3.35e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  12 LVGaVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQlnidiSNIKAIGVS 91
Cdd:cd07773    2 LLG-IDIGTTNVKAVLFD-EDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGP-----DPIAAISVS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  92 NQRETTVVWDKlTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNNNFvkSKTGL 171
Cdd:cd07773   75 SQGESGVPVDR-DGEPLGPAI----------------------------VWFDPRGKEEAEELAERIGAEELY--RITGL 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 172 PLSTYFSAVKLRWLLDNVKKVQEAVeenrALFGTIDSWLIWSLTGginggVHCTDVTNASRTMLFNIHSLEWDKELCEFF 251
Cdd:cd07773  124 PPSPMYSLAKLLWLREHEPEIFAKA----AKWLSVADYIAYRLTG-----EPVTDYSLASRTMLFDIRKRTWSEELLEAA 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 252 GIPMEILPNVRSSSEIYGLMKISHSLKAGALEGVPIsgCLG--DQSAALVGQMCFQDGQAKNTYGTG-CFLLC-NTGHKC 327
Cdd:cd07773  195 GIDASLLPELVPSGTVIGTVTPEAAEELGLPAGTPV--VVGghDHLCAALGAGVIEPGDVLDSTGTAeALLAVvDEPPLD 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 328 VFSEHGLLTTVAYKLGRdkpvYYALEGSVAiAGAVIRWLRDNLGI--IKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPY 405
Cdd:cd07773  273 EMLAEGGLSYGHHVPGG----YYYLAGSLP-GGALLEWFRDLFGGdeSDLAAADELAEAAPPGPTGLLFLPHLSGSGTPD 347
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 406 WEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSM 485
Cdd:cd07773  348 FDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEAL-EKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEV 426

                 ....
gi 672087703 486 PETT 489
Cdd:cd07773  427 PEAT 430
ASKHA_NBD_FGGY_EcXK-like cd07808
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ...
8-489 1.61e-75

nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466808 [Multi-domain]  Cd Length: 482  Bit Score: 247.45  E-value: 1.61e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703   8 VLGplvgaVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTcekLGQLNIDISNIKA 87
Cdd:cd07808    2 LLG-----IDLGTSSVKAVLVDED-GRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALREL---LAKAGISPSDIAA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  88 IGVSNQRETTVVWDKlTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPgnnNFVKS 167
Cdd:cd07808   73 IGLTGQMHGLVLLDK-NGRPLRPAI----------------------------LWNDQRSAAECEELEARLG---DEILI 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 168 KTGLPLSTYFSAVKLRWLL----DNVKKVqeaveenRALFGTIDsWLIWSLTGginggVHCTDVTNASRTMLFNIHSLEW 243
Cdd:cd07808  121 ITGNPPLPGFTLPKLLWLKenepEIFARI-------RKILLPKD-YLRYRLTG-----ELATDPSDASGTLLFDVEKREW 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 244 DKELCEFFGIPMEILPNVRSSSEIYGlmKISHSLkAGAL---EGVP-ISGClGDQSAALVGQMCFQDGQAKNTYGTGCFL 319
Cdd:cd07808  188 SEELLEALGLDPSILPPIVESTEIVG--TLTPEA-AEELglpEGTPvVAGA-GDNAAAALGAGVVEPGDALISLGTSGVV 263
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 320 LCNTgHKCVFSEHGLLTTVAYKLGrdkPVYYALeGSVAIAGAVIRWLRDNLGIIKSS-EEIEKLAKEVG-TSYGCYFVPA 397
Cdd:cd07808  264 FAPT-DKPVPDPKGRLHTFPHAVP---GKWYAM-GVTLSAGLSLRWLRDLFGPDRESfDELDAEAAKVPpGSEGLLFLPY 338
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 398 FSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILY 477
Cdd:cd07808  339 LSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVL-KELGIKVKEIRLIGGGAKSPLWRQILADVLG 417
                        490
                 ....*....|..
gi 672087703 478 IPVVKPSMPETT 489
Cdd:cd07808  418 VPVVVPAEEEGS 429
ASKHA_NBD_FGGY_GntK cd07770
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ...
15-489 3.77e-72

nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466790 [Multi-domain]  Cd Length: 478  Bit Score: 238.61  E-value: 3.77e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  15 AVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQLNIDisnikAIGVSNQR 94
Cdd:cd07770    4 GIDIGTTSTKAVLFDED-GRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVD-----AIGFSSAM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  95 ETTVVWDKlTGEPLynavaAPVSPgssvpvavvpsgspvpaagassvWLDLRTQSTVEKLSKRIPGNNnfVKSKTGLPLS 174
Cdd:cd07770   78 HSLLGVDE-DGEPL-----TPVIT-----------------------WADTRAAEEAERLRKEGDGSE--LYRRTGCPIH 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 175 TYFSAVKLRWLldnvKKVQEAVEENRALFGTIDSWLIWSLTGginggVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIP 254
Cdd:cd07770  127 PMYPLAKLLWL----KEERPELFAKAAKFVSIKEYLLYRLTG-----ELVTDYSTASGTGLLNIHTLDWDEEALELLGID 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 255 MEILPNVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTgcfllcnTGHKCVFSEHGL 334
Cdd:cd07770  198 EEQLPELVDPTEVLPGLKPEFAERLGLLAGTPVVLGASDGALANLGSGALDPGRAALTVGT-------SGAIRVVSDRPV 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 335 LT----TVAYKLGRDKPVyyaLEGSVAIAGAVIRWLRDNLGIIKSS-EEIEKLAKEVG-TSYGCYFVPAFSGLYAPYWEP 408
Cdd:cd07770  271 LDppgrLWCYRLDENRWL---VGGAINNGGNVLDWLRDTLLLSGDDyEELDKLAEAVPpGSHGLIFLPYLAGERAPGWNP 347
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 409 SARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPET 488
Cdd:cd07770  348 DARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEAL-EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEA 426

                 .
gi 672087703 489 T 489
Cdd:cd07770  427 S 427
ASKHA_NBD_FGGY_RrXK-like cd07804
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ...
12-484 4.34e-65

nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Rhodospirillum rubrum xylulose kinase (RrXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466806 [Multi-domain]  Cd Length: 451  Bit Score: 218.93  E-value: 4.34e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  12 LVGaVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVS 91
Cdd:cd07804    2 LLG-IDIGTTGTKGVLVDED-GKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAG---ISPKEIAAIGVS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  92 NQRETTVVWDKlTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNNNFvkSKTGL 171
Cdd:cd07804   77 GLVPALVPVDE-NGKPLRPAI----------------------------LYGDRRATEEIEWLNENIGEDRIF--EITGN 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 172 PLSTYFSAVKLRWLLDNvkkvQEAVEENRALFGTIDSWLIWSLTGginggVHCTDVTNASRTM-LFNIHSLEWDKELCEF 250
Cdd:cd07804  126 PLDSQSVGPKLLWIKRN----EPEVFKKTRKFLGAYDYIVYKLTG-----EYVIDYSSAGNEGgLFDIRKRTWDEELLEA 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 251 FGIPMEILPNVRSSSEIYGlmKISH--SLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGT-GCFLLCntgHKC 327
Cdd:cd07804  197 LGIDPDLLPELVPSTEIVG--EVTKeaAEETGLAEGTPVVAGTVDAAASALSAGVVEPGDLLLMLGTaGDIGVV---TDK 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 328 VFSEHGLLTTVAyklgrDKPVYYALEGSVAIAGAVIRWLRDNLGIIKSSEE----------IEKLAKEVG-TSYGCYFVP 396
Cdd:cd07804  272 LPTDPRLWLDYH-----DIPGTYVLNGGMATSGSLLRWFRDEFAGEEVEAEksggdsaydlLDEEAEKIPpGSDGLIVLP 346
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 397 AFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDcGIPLSHLQVDGGMTSNKILMQLQADIL 476
Cdd:cd07804  347 YFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRHHLEVIREA-GLPIKRLVAVGGGAKSPLWRQIVADVT 425

                 ....*...
gi 672087703 477 YIPVVKPS 484
Cdd:cd07804  426 GVPQEYVK 433
ASKHA_NBD_FGGY_CvXK-like cd07805
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ...
15-487 9.53e-63

nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Chromobacterium violaceum xylulose kinase (CvXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466807 [Multi-domain]  Cd Length: 485  Bit Score: 213.92  E-value: 9.53e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  15 AVDQGTSSTrflvfnsKTA------ELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECiekTCEKLGQLNIDISNIKAI 88
Cdd:cd07805    4 AIDLGTSGV-------KAAlvdldgELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRA---TRALLEKSGIDPSDIAAI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  89 GVSNQRETTVVWDKlTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNNnFVKSK 168
Cdd:cd07805   74 AFSGQMQGVVPVDK-DGNPLRNAI----------------------------IWSDTRAAEEAEEIAGGLGGIE-GYRLG 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 169 TGLPLSTYFSAVKLRWLLDNVKkvqEAVEENRALFGTIDsWLIWSLTGginggVHCTDVTNASRTMLFNIHSLEWDKELC 248
Cdd:cd07805  124 GGNPPSGKDPLAKILWLKENEP---EIYAKTHKFLDAKD-YLNFRLTG-----RAATDPSTASTTGLMDLRKRRWSEELL 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 249 EFFGIPMEILPNVRSSSEIYG--LMKISHSLkaGALEGVPISGCLGDQSAALVGQMCFQDGQAkNTY-GTGCFLLCNTGH 325
Cdd:cd07805  195 RAAGIDPDKLPELVPSTEVVGelTPEAAAEL--GLPAGTPVVGGGGDAAAAALGAGAVEEGDA-HIYlGTSGWVAAHVPK 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 326 KCVFSEHGlLTTVAYKLgrdkPVYYALEGSVAIAGAVIRWLRDNLGIIKSS-----EEIEKLAKEVGT-SYGCYFVPAFS 399
Cdd:cd07805  272 PKTDPDHG-IFTLASAD----PGRYLLAAEQETAGGALEWARDNLGGDEDLgaddyELLDELAAEAPPgSNGLLFLPWLN 346
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 400 GLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGiPLSHLQVDGGMTSNKILMQLQADILYIP 479
Cdd:cd07805  347 GERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRP 425

                 ....*...
gi 672087703 480 VVKPSMPE 487
Cdd:cd07805  426 VEVPENPQ 433
FGGY_C pfam02782
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ...
309-492 5.15e-46

FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.


Pssm-ID: 426979 [Multi-domain]  Cd Length: 197  Bit Score: 160.18  E-value: 5.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  309 AKNTYGTGCFLLCNTGHKCVFsEHGLLTTVAyklGRDKPVYYALEGSVAIAGAVIRWLRDNLGI---------IKSSEEI 379
Cdd:pfam02782   1 LAISAGTSSFVLVETPEPVLS-VHGVWGPYT---NEMLPGYWGLEGGQSAAGSLLAWLLQFHGLreelrdagnVESLAEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  380 EKLAKEVGTSyGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVD 459
Cdd:pfam02782  77 AALAAVAPAG-GLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVS 155
                         170       180       190
                  ....*....|....*....|....*....|...
gi 672087703  460 GGMTSNKILMQLQADILYIPVVKPSMPETTALG 492
Cdd:pfam02782 156 GGGSRNPLLLQLLADALGLPVVVPGPDEATALG 188
ASKHA_NBD_FGGY_EcLyxK-like cd07802
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ...
12-489 1.09e-44

nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466805 [Multi-domain]  Cd Length: 444  Bit Score: 163.88  E-value: 1.09e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  12 LVGaVDQGTSSTRFLVFNSKTAELLSHHqVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVS 91
Cdd:cd07802    2 LLG-IDNGTTNVKAVLFDLDGREIAVAS-RPTPVISPRPGWAERDMDELWQATAEAIRELLEKSG---VDPSDIAGVGVT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  92 NQRETTVVWDKlTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRipGNNNFVKSKTGL 171
Cdd:cd07802   77 GHGNGLYLVDK-DGKPVRNAI----------------------------LSNDSRAADIVDRWEED--GTLEKVYPLTGQ 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 172 PLSTYFSAVKLRWLLDNVKKVQEAVeenRALFGTIDsWLIWSLTggingGVHCTDVTNASrTMLFNIHSLEWDKELCEFF 251
Cdd:cd07802  126 PLWPGQPVALLRWLKENEPERYDRI---RTVLFCKD-WIRYRLT-----GEISTDYTDAG-SSLLDLDTGEYDDELLDLL 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 252 GIP--MEILPNVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCfllCNTG--HKC 327
Cdd:cd07802  196 GIEelKDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVvtDEP 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 328 VFSEHGLLTTvaykLGRDKPVYYALEGSVAIAGaVIRWLRDNLG------IIKSSEEIEKLAKEVG-TSYGCYFVPaFsg 400
Cdd:cd07802  273 VVPDSVGSNS----LHADPGLYLIVEASPTSAS-NLDWFLDTLLgeekeaGGSDYDELDELIAAVPpGSSGVIFLP-Y-- 344
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 401 LYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCgiPLSHLQVDGGMTSNKILMQLQADILYIPV 480
Cdd:cd07802  345 LYGSGANPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLVAR--KPETIRLTGGGARSPVWAQIFADVLGLPV 422

                 ....*....
gi 672087703 481 VKPSMPETT 489
Cdd:cd07802  423 EVPDGEELG 431
ASKHA_NBD_FGGY_YoaC-like cd07798
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ...
15-489 1.06e-42

nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466804 [Multi-domain]  Cd Length: 448  Bit Score: 158.54  E-value: 1.06e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  15 AVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPREGW-VEQDPKEILQSVYECIEKTcekLGQLNIDISNIKAIGVSNQ 93
Cdd:cd07798    4 VIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPDaKEFDPEELWEKICEAIREA---LKKAGISPEDISAVSSTSQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  94 RETTVVWDKlTGEPLYnavaapvspgssvpvaVVPSgspvpaagassvwLDLRTqstvEKLSKRIPGNNNFVKSK-TGLP 172
Cdd:cd07798   81 REGIVFLDK-DGRELY----------------AGPN-------------IDARG----VEEAAEIDDEFGEEIYTtTGHW 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 173 LSTYFSAVKLRWLldnvKKVQEAVEENRALFGTIDSWLIWSLTGGInggvhCTDVTNASRTMLFNIHSLEWDKELCEFFG 252
Cdd:cd07798  127 PTELFPAARLLWF----KENRPEIFERIATVLSISDWIGYRLTGEL-----VSEPSQASETQLFDIKKREWSQELLEALG 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 253 IPMEILPNVRSSSEIYGlmKISHSLKA--GALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGhKCVFS 330
Cdd:cd07798  198 LPPEILPEIVPSGTVLG--TVSEEAARelGLPEGTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTD-EPIID 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 331 EHGLLTTVAYkLGRDKpvyYALEGSVAIAGAVIRWLRDNL--GIIKSSEEIEKLAKEVG-TSYGCYfvpAFSGLYAPYwe 407
Cdd:cd07798  275 PERRLWTGCH-LVPGK---WVLESNAGVTGLNYQWLKELLygDPEDSYEVLEEEASEIPpGANGVL---AFLGPQIFD-- 345
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 408 PSARGIICGLTQFT--------NKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIP 479
Cdd:cd07798  346 ARLSGLKNGGFLFPtplsaselTRGDFARAILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKP 425
                        490
                 ....*....|
gi 672087703 480 VVKPSMPETT 489
Cdd:cd07798  426 VLVPEGREAS 435
ASKHA_NBD_FGGY_SePSK_AtXK1-like cd07783
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ...
15-488 1.39e-42

nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466801 [Multi-domain]  Cd Length: 429  Bit Score: 157.77  E-value: 1.39e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  15 AVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLgqlniDISNIKAIGVSNQR 94
Cdd:cd07783    4 GIDLGTSGVRAVVVDED-GTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAEL-----RPRRVVAIAVDGTS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  95 ETTVVWDKlTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPgnnnFVKSKTGLPLS 174
Cdd:cd07783   78 GTLVLVDR-EGEPLRPAI----------------------------MYNDARAVAEAEELAEAAG----AVAPRTGLAVS 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 175 TYFSAVKLRWLLDNVKKVQEAVeenrALFGTIDSWLIWSLTGGinggVHCTDVTNASRTmLFNIHSLEWDKELCEFFGIP 254
Cdd:cd07783  125 PSSSLAKLLWLKRHEPEVLAKT----AKFLHQADWLAGRLTGD----RGVTDYNNALKL-GYDPETGRWPSWLLALLGIP 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 255 MEILPNVRSSSEIYG--LMKISHSLkaGALEGVPIsgCLG--DQSAALVGQMCFQDGQAKNTYGTgcfllcntghkcvfs 330
Cdd:cd07783  196 PDLLPRVVAPGTVIGtlTAEAAEEL--GLPAGTPV--VAGttDSIAAFLASGAVRPGDAVTSLGT--------------- 256
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 331 ehglltTVAYKLGRDKPV---------------YYALEGSVAIAGAVIRWLrdnlgiiKSSEEIEKLAKEVGTSY--GCY 393
Cdd:cd07783  257 ------TLVLKLLSDKRVpdpgggvyshrhgdgYWLVGGASNTGGAVLRWF-------FSDDELAELSAQADPPGpsGLI 323
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 394 FVP-AFSGLYAPYWEPSARGIICGLTqfTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQ 472
Cdd:cd07783  324 YYPlPLRGERFPFWDPDARGFLLPRP--HDRAEFLRALLEGIAFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIR 401
                        490
                 ....*....|....*.
gi 672087703 473 ADILYIPVVKPSMPET 488
Cdd:cd07783  402 ADVLGVPVVIAEEEEA 417
ASKHA_NBD_FGGY_BaXK-like cd07809
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ...
8-488 2.19e-34

nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466809 [Multi-domain]  Cd Length: 443  Bit Score: 135.37  E-value: 2.19e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703   8 VLGplvgaVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTcekLGQLNIDISNIKA 87
Cdd:cd07809    2 VLG-----IDLGTQSIKAVLIDAETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQL---LKDAGAELRDVAA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  88 IGVSNQRETTVVWDKlTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNNnfvKS 167
Cdd:cd07809   74 IGISGQMHGLVALDA-DGKVLRPAK----------------------------LWCDTRTAPEAEELTEALGGKK---CL 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 168 KTGLPLSTYFSAVKLRWLLDN----VKKVqeaveenrALFGTIDSWLIWSLTGGinggvHCTDVTNASRTMLFNIHSLEW 243
Cdd:cd07809  122 LVGLNIPARFTASKLLWLKENepehYARI--------AKILLPHDYLNWKLTGE-----KVTGLGDASGTFPIDPRTRDY 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 244 DKELCEFF---GIPMEILPNVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGT-GCfl 319
Cdd:cd07809  189 DAELLAAIdpsRDLRDLLPEVLPAGEVAGRLTPEGAEELGLPAGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTsGT-- 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 320 LCNTGHKCVFSEHGLLTTVAyklgrDKPVYYALegSVAIAGAVIRWLRDNLGIIKSS-EEIEKLAKEV-GTSYGCYFVPA 397
Cdd:cd07809  267 AYGVSDKPVSDPHGRVATFC-----DSTGGMLP--LINTTNCLTAWTELFRELLGVSyEELDELAAQApPGAGGLLLLPF 339
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 398 FSGLYAPYWePSARGIICGLTQF-TNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADIL 476
Cdd:cd07809  340 LNGERTPNL-PHGRASLVGLTLSnFTRANLARAALEGATFGLRYGLDIL-RELGVEIDEIRLIGGGSKSPVWRQILADVF 417
                        490
                 ....*....|..
gi 672087703 477 YIPVVKPSMPET 488
Cdd:cd07809  418 GVPVVVPETGEG 429
ASKHA_NBD_FGGY_BaEryA-like cd24121
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ...
12-488 2.44e-28

nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). It catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466971 [Multi-domain]  Cd Length: 452  Bit Score: 117.73  E-value: 2.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  12 LVGaVDQGTSSTRFLVFNSKTAELlSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQLNidiSNIKAIGVS 91
Cdd:cd24121    2 LIG-IDAGTSVVKAVAFDLDGREL-AVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLP---DRVAAIGVT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  92 NQRETTvvWdkLTGEplynavaapvspgssvpvavvpSGSPV-PAAgassVWLDLRTQSTVEKLSKRipGNNNFVKSKTG 170
Cdd:cd24121   77 GQGDGT--W--LVDE----------------------DGRPVrDAI----LWLDGRAADIVERWQAD--GIAEAVFEITG 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 171 LPLSTYFSAVKLRWLLDNVKkvqEAVEENRALFGTIDsWLIWSLTGGInggvhCTDVTNASRTMlFNIHSLEWDKELCEF 250
Cdd:cd24121  125 TGLFPGSQAAQLAWLKENEP---ERLERARTALHCKD-WLFYKLTGEI-----ATDPSDASLTF-LDFRTRQYDDEVLDL 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 251 FGIP--MEILPNVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFllcntghkcv 328
Cdd:cd24121  195 LGLEelRHLLPPIRPGTEVIGPLTPEAAAATGLPAGTPVVLGPFDVVATALGSGAIEPGDACSILGTTGV---------- 264
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 329 fseHGLLTTVAYkLGRDKP---VYYALEGSV-----AIAG-AVIRWLRDNLGIIKSSE----------EIEKLAKEV--- 386
Cdd:cd24121  265 ---HEVVVDEPD-LEPEGVgytICLGVPGRWlramaNMAGtPNLDWFLRELGEVLKEGaepagsdlfqDLEELAASSppg 340
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 387 --GTSYGCYFVPAfsGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnrdcGIPLSHLQVDGGMTS 464
Cdd:cd24121  341 aeGVLYHPYLSPA--GERAPFVNPNARAQFTGLSLEHTRADLLRAVYEGVALAMRDCYEHM----GEDPGELRLSGGGAR 414
                        490       500
                 ....*....|....*....|....
gi 672087703 465 NKILMQLQADILYIPVVKPSMPET 488
Cdd:cd24121  415 SDTWCQILADALGVPVRVPAGEEF 438
ASKHA_NBD_FGGY_SHK cd07777
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ...
15-489 1.03e-27

nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466796 [Multi-domain]  Cd Length: 436  Bit Score: 115.78  E-value: 1.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  15 AVDQGTSSTRFLVFNSKTAELLS----HHQVEIKQEFPreGWVEQDPKEILQSVYECIEKTCEKLGqlnidiSNIKAIGV 90
Cdd:cd07777    4 GIDIGTTSIKAALLDLESGRILEsvsrPTPAPISSDDP--GRSEQDPEKILEAVRNLIDELPREYL------SDVTGIGI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  91 SNQRETTVVWDKlTGEPLYNAVAapvspgssvpvavvpsgspvpaagassvWLDLRtqSTVEKLSKRIPGNNNFvKSKTG 170
Cdd:cd07777   76 TGQMHGIVLWDE-DGNPVSPLIT----------------------------WQDQR--CSEEFLGGLSTYGEEL-LPKSG 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 171 LPLSTYFSAVKLRWLLdnvkkVQEAVEENRALFGTIDSWLIWSLTGGINggvHCTDVTNASRTMLFNIHSLEWDKELCEF 250
Cdd:cd07777  124 MRLKPGYGLATLFWLL-----RNGPLPSKADRAGTIGDYIVARLTGLPK---PVMHPTNAASWGLFDLETGTWNKDLLEA 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 251 FGIPMEILPNVRSSSEIYGlmkishSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTG---CFLLC-NTGHK 326
Cdd:cd07777  196 LGLPVILLPEIVPSGEIVG------TLSSALPKGIPVYVALGDNQASVLGSGLNEENDAVLNIGTGaqlSFLTPkFELSG 269
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 327 CV----FSEHGLLTTVAyKL--GRdkpVYYALEGSVAiagaviRWLRDnLGIIKSSEEI-EKLAKEVGTSYGC--YFVPA 397
Cdd:cd07777  270 SVeirpFFDGRYLLVAA-SLpgGR---ALAVLVDFLR------EWLRE-LGGSLSDDEIwEKLDELAESEESSdlSVDPT 338
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 398 FSGlyaPYWEPSARGIICGLTQ--FTNKcHIAFAALEAVCfqtREILDAMNRDC--GIPLSHLQVDGGM-TSNKILMQLQ 472
Cdd:cd07777  339 FFG---ERHDPEGRGSITNIGEsnFTLG-NLFRALCRGIA---ENLHEMLPRLDldLSGIERIVGSGGAlRKNPVLRRII 411
                        490
                 ....*....|....*..
gi 672087703 473 ADILYIPVVKPSMPETT 489
Cdd:cd07777  412 EKRFGLPVVLSEGSEEA 428
ASKHA_NBD_FGGY_L-RBK cd07781
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ...
8-489 1.07e-25

nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466799 [Multi-domain]  Cd Length: 504  Bit Score: 110.70  E-value: 1.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703   8 VLGplvgaVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEF--PREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNI 85
Cdd:cd07781    2 VIG-----IDFGTQSVRAGLVDLADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAEAG---VDPEDV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  86 KAIGVSnqreTTvvwdkltgeplynavaapvspgSSVPVAVVPSGSPV-PAAgassVWLDLRTQSTVEKLSKRIPGNNNF 164
Cdd:cd07781   74 VGIGVD----TT----------------------SSTVVPVDEDGNPLaPAI----LWMDHRAQEEAAEINETAHPALEY 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 165 VKSKTGLPLS--TYFSavKLRWLLDNVKKVQEA----VEEnralfgtIDsWLIWSLTGGINGGVhCtdvtNASRTMLFNI 238
Cdd:cd07781  124 YLAYYGGVYSseWMWP--KALWLKRNAPEVYDAaytiVEA-------CD-WINARLTGRWVRSR-C----AAGHKWMYNE 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 239 HSLEWDKELCEFFGIPM----EILP-NVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTY 313
Cdd:cd07781  189 WGGGPPREFLAALDPGLlklrEKLPgEVVPVGEPAGTLTAEAAERLGLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIM 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 314 GT-GCFLLcnTGHKCVFSEhGLLTTVayklgrDKPV---YYALEGSVAIAGAVIRWLRDNLGI------IKSSEEIEKLA 383
Cdd:cd07781  269 GTsTCHLM--VSPKPVDIP-GICGPV------PDAVvpgLYGLEAGQSAVGDIFAWFVRLFVPpaeergDSIYALLSEEA 339
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 384 KEVGTsyGCyfvpafSGLYA---------PYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLS 454
Cdd:cd07781  340 AKLPP--GE------SGLVAldwfngnrtPLVDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERF-EEAGVPVN 410
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 672087703 455 HLQVDGGMTS-NKILMQLQADILYIPVVKPSMPETT 489
Cdd:cd07781  411 RVVACGGIAEkNPLWMQIYADVLGRPIKVPKSDQAP 446
ASKHA_NBD_FGGY_AI-2K cd07775
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ...
15-489 1.82e-24

nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466794 [Multi-domain]  Cd Length: 492  Bit Score: 106.65  E-value: 1.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  15 AVDQGTSSTRFLVFNsKTAELLSHHQVE-IKQEFPR-EGWVEQDPKEILQSVYECIEKTCEklgQLNIDISNIKAIGVSN 92
Cdd:cd07775    4 ALDAGTGSGRAVIFD-LEGNQIAVAQREwRHKEVPDvPGSMDFDTEKNWKLICECIREALK---KAGIAPKSIAAISTTS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  93 QRETTVVWDKlTGEPLYnAVAApvspgssvpvavvpsgspvpaagassvwLDLRTQSTVEKLSKRIPGNNNFVKSKTGLP 172
Cdd:cd07775   80 MREGIVLYDN-EGEEIW-ACAN----------------------------VDARAAEEVSELKELYNTLEEEVYRISGQT 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 173 LStyFSAV-KLRWLLDNVKKVQEAVeenrALFGTIDSWLIWSLTGGInggvhCTDVTNASRTMLFNIHSLEWDKELCEFF 251
Cdd:cd07775  130 FA--LGAIpRLLWLKNNRPEIYRKA----AKITMLSDWIAYKLSGEL-----AVEPSNGSTTGLFDLKTRDWDPEILEMA 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 252 GIPMEILPNVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKcVFSE 331
Cdd:cd07775  199 GLKADILPPVVESGTVIGKVTKEAAEETGLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAP-VTDP 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 332 HGLLTTVAYKLgrdkPVYYALEGSVAIAGAVIRWLRDNLGI----------IKSSEEIEKLAKEVGTsyGCY-FVPAFSG 400
Cdd:cd07775  278 AMNIRVNCHVI----PDMWQAEGISFFPGLVMRWFRDAFCAeekeiaerlgIDAYDLLEEMAKDVPP--GSYgIMPIFSD 351
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 401 L--YApYWEPSARGIIcGLTQFTNKCHIA--FAAL-EAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADI 475
Cdd:cd07775  352 VmnYK-NWRHAAPSFL-NLDIDPEKCNKAtfFRAImENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADV 429
                        490
                 ....*....|....
gi 672087703 476 LYIPVVKPSMPETT 489
Cdd:cd07775  430 LGLPVKVPVVKEAT 443
PRK10331 PRK10331
L-fuculokinase; Provisional
17-490 1.88e-21

L-fuculokinase; Provisional


Pssm-ID: 182383 [Multi-domain]  Cd Length: 470  Bit Score: 97.41  E-value: 1.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  17 DQGTSSTRFLVFNSKTAELLSHHQ---VEIKQEFPRegWVEQDPKEILQSVYECIEKTCEKLGQlnidiSNIKAIGVsnq 93
Cdd:PRK10331   8 DCGATNVRAIAVDRQGKIVARASTpnaSDIAAENSD--WHQWSLDAILQRFADCCRQINSELTE-----CHIRGITV--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  94 reTTVVWDkltgeplynavaapvspgssvpvavvpsGSPVPAAGA------SsvWLDLRTQSTVEKLSKRIPGNNNFVKS 167
Cdd:PRK10331  78 --TTFGVD----------------------------GALVDKQGNllypiiS--WKCPRTAAVMENIERYISAQQLQQIS 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 168 KTG-LPLSTYFsavKLRWLldnvkkvqeavEENRA-LFGTIDSWL-IWSLtggIN---GGVHCTDVTNASRTMLFNIHSL 241
Cdd:PRK10331 126 GVGaFSFNTLY---KLVWL-----------KENHPqLLEQAHAWLfISSL---INhrlTGEFTTDITMAGTSQMLDIQQR 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 242 EWDKELCEFFGIPMEILPNVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDgQAKNTYGTGCFLLC 321
Cdd:PRK10331 189 DFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAAALLGLPVGIPVISAGHDTQFALFGSGAGQN-QPVLSSGTWEILMV 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 322 NTGH---KCVFSEHGLLTTVAYKLGRDKPvyyaleGSVAIAGAVIRWLRDNLGiikSSEE-----IEKlAKEVGT-SYGC 392
Cdd:PRK10331 268 RSAQvdtSLLSQYAGSTCELDSQSGLYNP------GMQWLASGVLEWVRKLFW---TAETpyqtmIEE-ARAIPPgADGV 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 393 YFVPAFSGlyapywepSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQ 472
Cdd:PRK10331 338 KMQCDLLA--------CQNAGWQGVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIK 409
                        490
                 ....*....|....*...
gi 672087703 473 ADILYIPVVKPSMPETTA 490
Cdd:PRK10331 410 ANMLDIPIKVLDDAETTV 427
ASKHA_NBD_FGGY_RBK-like cd07768
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ...
16-488 1.34e-18

nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466788 [Multi-domain]  Cd Length: 522  Bit Score: 88.84  E-value: 1.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  16 VDQGTSSTRFLVFNSKTAELLSHHQVEIKQ-EFPREGWVEQDPKEILQSVYECIEKTcekLGQLNIDISNIKAIGVSNQR 94
Cdd:cd07768    5 VDVGTSSARAGVYDLYAGLEMAQEPVPYYQdSSKKSWKFWQKSTEIIKALQKCVQKL---NIREGVDAYEVKGCGVDATC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  95 eTTVVWDKlTGEPlyNAVAAPVSPGSSVpvavvpsgspvpaagasSVWLDLRTQSTVEKLskripgnnNFVKSKTGLP-- 172
Cdd:cd07768   82 -SLAIFDR-EGTP--LMALIPYPNEDNV-----------------IFWMDHSAVNEAQWI--------NMQCPQQLLDyl 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 173 ---LSTYFSAVKLRWLLDNVKKVQEAVEEnraLFGTIDsWLIWSLTGGINGGVhCTDVTNASrtmlFNIHSLEWDKELCE 249
Cdd:cd07768  133 ggkISPEMGVPKLKYFLDEYSHLRDKHFH---IFDLHD-YIAYELTRLYEWNI-CGLLGKEN----LDGEESGWSSSFFK 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 250 FFGIPME------ILPNVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVgqmcfqdGQAKNTYGTGCFLLCNT 323
Cdd:cd07768  204 NIDPRLEhltttkNLPSNVPIGTTSGVALPEMAEKMGLHPGTAVVVSCIDAHASWF-------AVASPHLETSLFMIAGT 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 324 GhkcvfSEHGLLTTVAYKL-GRDKPVYYAL-------EGSVAIAGAVIRWL-------RDNLGIIKSSEEI--------E 380
Cdd:cd07768  277 S-----SCHMYGTTISDRIpGVWGPFDTIIdpdysvyEAGQSATGKLIEHLfeshpcaRKFDEALKKGADIyqvleqtiR 351
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 381 KLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFT---NKCHIAFAALEAVCFQTREILDAMNRDcGIPLSHLQ 457
Cdd:cd07768  352 QIEKNNGLSIHILTLDMFFGNRSEFADPRLKGSFIGESLDTsmlNLTYKYIAILEALAFGTRLIIDTFQNE-GIHIKELR 430
                        490       500       510
                 ....*....|....*....|....*....|.
gi 672087703 458 VDGGMTSNKILMQLQADILYIPVVKPSMPET 488
Cdd:cd07768  431 ASGGQAKNERLLQLIALVTNVAIIKPKENMM 461
PRK15027 PRK15027
xylulokinase; Provisional
16-475 1.31e-17

xylulokinase; Provisional


Pssm-ID: 184987 [Multi-domain]  Cd Length: 484  Bit Score: 85.79  E-value: 1.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  16 VDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVyeciEKTCEKLGQLNiDISNIKAIGVSNQRE 95
Cdd:PRK15027   5 IDLGTSGVKVILLNEQ-GEVVASQTEKLTVSRPHPLWSEQDPEQWWQAT----DRAMKALGDQH-SLQDVKALGIAGQMH 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  96 TTVVWDKltgeplYNAVAAPvspgssvpvavvpsgspvpaagaSSVWLDLRTQSTVEKLSKRIPGNnnfvKSKTGLPLST 175
Cdd:PRK15027  79 GATLLDA------QQRVLRP-----------------------AILWNDGRCAQECALLEARVPQS----RVITGNLMMP 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 176 YFSAVKLRWlldnVKKVQEAVEENRALFGTIDSWLIWSLTGginggVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPM 255
Cdd:PRK15027 126 GFTAPKLLW----VQRHEPEIFRQIDKVLLPKDYLRLRMTG-----EFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSR 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 256 EILPNVRSSSEIYGLMkISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTgcfllcnTGHKCVFSEhGLL 335
Cdd:PRK15027 197 DQMPALYEGSEITGAL-LPEVAKAWGMATVPVVAGGGDNAAGAVGVGMVDANQAMLSLGT-------SGVYFAVSE-GFL 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 336 T---TVAYKLGRDKPVYYALEGSVAIAGAVIRW------LRDNLGIIKSSEEIEKLAKEVgtsygcYFVPAFSGLYAPYW 406
Cdd:PRK15027 268 SkpeSAVHSFCHALPQRWHLMSVMLSAASCLDWaakltgLSNVPALIAAAQQADESAEPV------WFLPYLSGERTPHN 341
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672087703 407 EPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNrDCGIPLSHLQVDGGMTSNKILMQLQADI 475
Cdd:PRK15027 342 NPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVH-ACGIKPQSVTLIGGGARSEYWRQMLADI 409
ASKHA_NBD_FGGY_D-RBK cd07782
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ...
15-488 1.81e-16

nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.


Pssm-ID: 466800 [Multi-domain]  Cd Length: 540  Bit Score: 82.58  E-value: 1.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  15 AVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVsnqr 94
Cdd:cd07782    4 GVDVGTGSARAGLFDL-DGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAG---VDPEQVKGIGF---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  95 ETT---VVWDKlTGEPlynavaapvspgssvpVAVVPSGSP----VpaagassVWLDLRTQSTVEklskRIpgnnnfvkS 167
Cdd:cd07782   76 DATcslVVLDA-EGKP----------------VSVSPSGDDernvI-------LWMDHRAVEEAE----RI--------N 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 168 KTGLPLSTYFSAV--------KLRWLldnvKKVQEAVEENRALFGTIDSWLIWSLTGGINGGVhCTDVtnASRTMLFNIH 239
Cdd:cd07782  120 ATGHEVLKYVGGKispemeppKLLWL----KENLPETWAKAGHFFDLPDFLTWKATGSLTRSL-CSLV--CKWTYLAHEG 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 240 SLE-WDKELCEFFG-----------IPMEILPNVRSSSEiyGLmkishSLKA----GALEGVPIS--------GCLGDQS 295
Cdd:cd07782  193 SEGgWDDDFFKEIGledlvednfakIGSVVLPPGEPVGG--GL-----TAEAakelGLPEGTPVGvslidahaGGLGTLG 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 296 AALVGQMC-FQDGQAKntygtgCFLLCNTG--HkCVFSEHGLLttVA-----YKlGRDKPVYYALEGSVAIAGAVIRWlr 367
Cdd:cd07782  266 ADVGGLPCeADPLTRR------LALICGTSscH-MAVSPEPVF--VPgvwgpYY-SAMLPGLWLNEGGQSATGALLDH-- 333
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 368 dnlgIIKS---SEEIEKLAKEVGTSY------------------------GCYFVPAFSGLYAPYWEPSARGIICGLTQF 420
Cdd:cd07782  334 ----IIEThpaYPELKEEAKAAGKSIyeylnerleqlaeekglplayltrDLHVLPDFHGNRSPLADPTLRGMISGLTLD 409
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672087703 421 TNKCHIA---FAALEAVCFQTREILDAMNRdCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPET 488
Cdd:cd07782  410 TSLDDLAllyLATLQALAYGTRHIIEAMNA-AGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEA 479
ASKHA_NBD_FGGY_RhaB-like cd07771
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ...
144-481 3.11e-16

nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.


Pssm-ID: 466791 [Multi-domain]  Cd Length: 460  Bit Score: 81.42  E-value: 3.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 144 DLRTQSTVEKLSKRIPGNNNFvkSKTGLPLSTYFSAVKLRWLldnvkkvqeaVEENRALFGTIDSWLI------WSLTGG 217
Cdd:cd07771   98 DPRTEGMMEELFEKISKEELY--ERTGIQFQPINTLYQLYAL----------KKEGPELLERADKLLMlpdllnYLLTGE 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 218 InggvhCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKISHSlKAGALEGVP-ISGCLGDQSA 296
Cdd:cd07771  166 K-----VAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVA-EELGLKGIPvIAVASHDTAS 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 297 ALVGQMCFQDGQAkntygtgcFLLCNT----GhkcVFSEHGLLTTVAYKLGrdkpvyYALEGSVA--------IAGaviR 364
Cdd:cd07771  240 AVAAVPAEDEDAA--------FISSGTwsliG---VELDEPVITEEAFEAG------FTNEGGADgtirllknITG---L 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 365 WL----RDNL---GIIKSSEEIEKLAKEVgTSYGCYFVPAFSGLYAPywePSARGIICGLTQFTN------KCHIAFAAL 431
Cdd:cd07771  300 WLlqecRREWeeeGKDYSYDELVALAEEA-PPFGAFIDPDDPRFLNP---GDMPEAIRAYCRETGqpvpesPGEIARCIY 375
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 672087703 432 EAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVV 481
Cdd:cd07771  376 ESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPVI 425
AraB COG1069
Ribulose kinase [Carbohydrate transport and metabolism];
5-492 1.10e-13

Ribulose kinase [Carbohydrate transport and metabolism];


Pssm-ID: 440687 [Multi-domain]  Cd Length: 532  Bit Score: 73.61  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703   5 KKAVLGplvgaVDQGTSSTRFLVFNSKTAELLSHHQVEIKQ------EFPREGWVEQDPKEILQSVYECIektCEKLGQL 78
Cdd:COG1069    1 EKYVIG-----VDFGTDSVRAVVVDAADGEELASAVHPYPRwviglyLPPPPDQARQHPLDYLEALEAAV---REALAQA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  79 NIDISNIKAIGVSNQRETTVVWDKlTGEPLynavaaPVSPG-SSVPVA-VVpsgspvpaagassVWLDLRTQSTVEklsk 156
Cdd:COG1069   73 GVDPADVVGIGVDATGCTPVPVDA-DGTPL------ALLPEfAENPHAmVI-------------LWKDHTAQEEAE---- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 157 RIpgnnNFVKSKTGLPLSTY---------FSAvKLRWLLdnvkkvqeavEENRALFGTIDS------WLIWSLTGGINGG 221
Cdd:COG1069  129 RI----NELAKARGEDYLRYvggiissewFWP-KILHLL----------REDPEVYEAADSfvelcdWITWQLTGSLKRS 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 222 VhCTdvtnASRTMLFNIHSLEWDKElcEFF---GIPMEILPNvRSSSEIYGLmkishSLKAGAL-----------EGVPI 287
Cdd:COG1069  194 R-CT----AGHKALWHAHEGGYPSE--EFFaalDPLLDGLAD-RLGTEIYPL-----GEPAGTLtaewaarlglpPGTAV 260
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 288 SGCLGDQSAALVGQMCFQDGQ-AKNtYGT-GCFLLCNTGHKC-------VFSehGLLttvayklgrdkPVYYALEGSVAI 358
Cdd:COG1069  261 AVGAIDAHAGAVGAGGVEPGTlVKV-MGTsTCHMLVSPEERFvpgicgqVDG--SIV-----------PGMWGYEAGQSA 326
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 359 AGAVIRWLRDNLGiikSSEEIEKLAKEVGTS----------------YGCYFVPAFSGLYAPYWEPSARGIICGLTQFTN 422
Cdd:COG1069  327 VGDIFAWFVRLLV---PPLEYEKEAEERGISlhpllteeaaklppgeSGLHALDWFNGNRSPLADQRLKGVILGLTLGTD 403
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672087703 423 KCHIAFAALEAVCFQTREILDAMNrDCGIPLSHLQVDGG-MTSNKILMQLQADILYIPVVKPSMPETTALG 492
Cdd:COG1069  404 AEDIYRALVEATAFGTRAIIERFE-EEGVPIDEIIACGGiATKNPLVMQIYADVTGRPIKVAASEQACALG 473
PRK10939 PRK10939
autoinducer-2 (AI-2) kinase; Provisional
15-292 1.13e-08

autoinducer-2 (AI-2) kinase; Provisional


Pssm-ID: 182853 [Multi-domain]  Cd Length: 520  Bit Score: 57.71  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  15 AVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPR-EGWVEQDPKEILQSVYECIEktcEKLGQLNIDISNIKAIGVSNQ 93
Cdd:PRK10939   7 ALDAGTGSIRAVIFDLNGNQIAVGQAEWRHLAVPDvPGSMEFDLEKNWQLACQCIR---QALQKAGIPASDIAAVSATSM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  94 RETTVVWDKlTGEPLYnAVAApvspgssvpvavvpsgspvpaagassvwLDLRTQSTVEKLSKRIPGNNNFVKSKTGLPL 173
Cdd:PRK10939  84 REGIVLYDR-NGTEIW-ACAN----------------------------VDARASREVSELKELHNNFEEEVYRCSGQTL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 174 StyFSAV-KLRWLldnvKKVQEAVEENRALFGTIDSWLIWSLTGGInggvhCTDVTNASRTMLFNIHSLEWDKELCEFFG 252
Cdd:PRK10939 134 A--LGALpRLLWL----AHHRPDIYRQAHTITMISDWIAYMLSGEL-----AVDPSNAGTTGLLDLVTRDWDPALLEMAG 202
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 672087703 253 IPMEILPNVRSSSEIYGLMKISHSLKAGALEGVPI--------SGCLG 292
Cdd:PRK10939 203 LRADILPPVKETGTVLGHVTAKAAAETGLRAGTPVvmgggdvqLGCLG 250
ASKHA_NBD_FGGY_MPA43-like cd07778
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ...
16-482 2.09e-07

nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466797 [Multi-domain]  Cd Length: 544  Bit Score: 53.56  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  16 VDQGTSSTRFLVFNSKTaELLSHHQVEI-KQEFPREGW-VEQDPKEILQSVYECIEKTCEKLGQLNIDISNIKA---IGV 90
Cdd:cd07778    5 IDVGSTSVRIGIFDYHG-TLLATSERPIsYKQDPKDLWfVTQSSTEIWKAIKTALKELIEELSDYIVSGIGVSAtcsMVV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703  91 SNQRETTvvwDKLTgePlYNAVAAPVSPGSSVpvavvpsgspvpaagasSVWLDLRTQSTVEKLskripgNNNFVKSKTG 170
Cdd:cd07778   84 MQRDSDT---SYLV--P-YNVIHEKSNPDQDI-----------------IFWMDHRASEETQWL------NNILPDDILD 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 171 LPLSTYF---SAVKLRWLLDNVKkvqEAVEENRALFGTIDsWLIWSL-TGGINGGVhcTDVTNASRTMLFNIHSLE-WDK 245
Cdd:cd07778  135 YLGGGFIpemAIPKLKYLIDLIK---EDTFKKLEVFDLHD-WISYMLaTNLGHSNI--VPVNAPPSIGIGIDGSLKgWSK 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 246 ELCEFFGIPMEILPNVRSSSEIYGLM----KISH-SLKAGALEGVPIS-----GCLgDQSAALVGQMC---FQDGQAKNT 312
Cdd:cd07778  209 DFYSKLKISTKVCNVGNTFKEAPPLPyagiPIGKvNVILASYLGIDKStvvghGCI-DCYAGWFSTFAaakTLDTTLFMV 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 313 YGTG-CFLLcntGHKCV-----------FSEhgllttvaykLGRDKPVYyalEGSVAIAG-----------AVIRWLRDN 369
Cdd:cd07778  288 AGTStCFLY---ATSSSqvgpipgiwgpFDQ----------LLKNYSVY---EGGQSATGklieklfnshpAIIELLKSD 351
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 370 LGIIKSSEE-IEKLAKEVGTS----YGCYFvpaFSGLYA----PYWEPSARGIICGLTQFTNKCHIAF---AALEAVCFQ 437
Cdd:cd07778  352 ANFFETVEEkIDKYERLLGQSihylTRHMF---FYGDYLgnrtPYNDPNMSGSFIGESTDSSLTDLVLkyiLILEFLAFQ 428
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 672087703 438 TREILDAMNRDCgIPLSHLQVDGGMTSNKILMQLQADILYIPVVK 482
Cdd:cd07778  429 TKLIIDNFQKEK-IIIQKVVISGSQAKNARLLQLLSTVLSKIHII 472
PRK04123 PRK04123
ribulokinase; Provisional
411-492 2.27e-04

ribulokinase; Provisional


Pssm-ID: 235221 [Multi-domain]  Cd Length: 548  Bit Score: 44.07  E-value: 2.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672087703 411 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGM-TSNKILMQLQADILYIPV-VKPSmPET 488
Cdd:PRK04123 398 KGVITGLTLGTDAPDIYRALIEATAFGTRAIMECF-EDQGVPVEEVIAAGGIaRKNPVLMQIYADVLNRPIqVVAS-DQC 475

                 ....
gi 672087703 489 TALG 492
Cdd:PRK04123 476 PALG 479
rhaB PRK10640
rhamnulokinase; Provisional
206-254 2.75e-03

rhamnulokinase; Provisional


Pssm-ID: 182609 [Multi-domain]  Cd Length: 471  Bit Score: 40.47  E-value: 2.75e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 672087703 206 IDSWLIWSLTGGINggvhcTDVTNASRTMLFNIHSLEWDKELCEFFGIP 254
Cdd:PRK10640 142 IPDYFSYRLTGKMN-----WEYTNATTTQLVNINSDDWDESLLAWSGAP 185
 
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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