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Conserved domains on  [gi|1034636798|ref|XP_016863086|]
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xylulose kinase isoform X4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 70-285 5.38e-107

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member cd07776:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 514  Bit Score: 331.44  E-value: 5.38e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798  70 VSLGTSDTLFLWLQEPMPALEGHIFCNPVDSQHYMALLCFKNGSLMREKIRNESVSRSWSDFSKALQSTEMGNGGNLGFY 149
Cdd:cd07776   290 VSLGTSDTVFLVLDEPKPGPEGHVFANPVDPGSYMAMLCYKNGSLARERVRDRYAGGSWEKFNELLESTPPGNNGNLGLY 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 150 FDVMEITPEIIGRHRFNTENHK-VAAFPGDVEVRALIEGQFMAKRIHAEGLGYRVmSKTKILATGGASHNREILQVLADV 228
Cdd:cd07776   370 FDEPEITPPVPGGGRRFFGDDGvDAFFDPAVEVRAVVESQFLSMRLHAERLGSDI-PPTRILATGGASANKAILQVLADV 448

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034636798 229 FDAPVYVIDTANSACVGSAYRAFHGLAGGTDVPFS--EVVKLAPNPRLAATPSPGASQR 285
Cdd:cd07776   449 FGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSpeFVVFSAEEPKLVAEPDPEAAEV 507
HIV_retropepsin_like cd05482
Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family ...
 451-537 5.83e-29

Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


:

Pssm-ID: 133149  Cd Length: 87  Bit Score: 110.05  E-value: 5.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 451 CEITIQGKKFKGLGDTGADVSIISLQHWPSVWPIQSAQFNIVGVGKAPEVYQSiYILHCEGPHE-QSGTIQPIVTSVPIN 529
Cdd:cd05482     1 LTLYINGKLFEGLLDTGADVSIIAENDWPKNWPIQPAPSNLTGIGGAITPSQS-SVLLLEIDGEgHLGTILVYVLSLPVN 79


                  ....*...
gi 1034636798 530 LWGRDLLQ 537
Cdd:cd05482    80 LWGRDILS 87
trimeric_dUTPase super family cl00493
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 355-431 1.25e-12

Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common family of dUTPase, found in bacteria, eukaryotes, and archaea. They catalyze the hydrolysis of the dUTP-Mg complex (dUTP-Mg) into dUMP and pyrophosphate. This reaction is crucial for the preservation of chromosomal integrity as it removes dUTP and therefore reduces the cellular dUTP/dTTP ratio, and prevents dUTP from being incorporated into DNA. It also provides dUMP as the precursor for dTTP synthesis via the thymidylate synthase pathway. dUTPases are homotrimeric, except some monomeric viral dUTPases, which have been shown to mimic a trimer. Active sites are located at the subunit interface.


The actual alignment was detected with superfamily member pfam00692:

Pssm-ID: 444938 [Multi-domain]  Cd Length: 129  Bit Score: 65.00  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 355 ASGMAGSLLGRSNLHLKGVQVQTGVIDSDYSGEIQIVI--STSVPWKAEPGECIAQLLIVPYVEMGRSETK-------QT 425
Cdd:pfam00692  43 PDGTYGRIFPRSGLAAKGLIVVPGVIDSDYRGEVKVVLfnLGKSDFTIKKGDRIAQLIFEPILHPELEPVEtldntdrGD 122


                  ....*.
gi 1034636798 426 GGSGST 431
Cdd:pfam00692 123 GGFGSS 128
G_patch smart00443
glycine rich nucleic binding domain; A predicted glycine rich nucleic binding domain found in ...
 562-595 3.33e-06

glycine rich nucleic binding domain; A predicted glycine rich nucleic binding domain found in the splicing factor 45, SON DNA binding protein and D-type Retrovirus- polyproteins.


:

Pssm-ID: 197727 [Multi-domain]  Cd Length: 47  Bit Score: 44.07  E-value: 3.33e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1034636798  562 MGYVPGMGLEKNLQGLKKPVQAEGKNSCQGLGYH 595
Cdd:smart00443  14 MGWKEGQGLGKNEQGIVEPISAEIKKDRKGLGAV 47
 
Name Accession Description Interval E-value
ASKHA_NBD_FGGY_SpXK-like cd07776
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ...
 70-285 5.38e-107

nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; 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. The subfamily includes XKs mainly from eukaryote. 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: 466795 [Multi-domain]  Cd Length: 514  Bit Score: 331.44  E-value: 5.38e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798  70 VSLGTSDTLFLWLQEPMPALEGHIFCNPVDSQHYMALLCFKNGSLMREKIRNESVSRSWSDFSKALQSTEMGNGGNLGFY 149
Cdd:cd07776   290 VSLGTSDTVFLVLDEPKPGPEGHVFANPVDPGSYMAMLCYKNGSLARERVRDRYAGGSWEKFNELLESTPPGNNGNLGLY 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 150 FDVMEITPEIIGRHRFNTENHK-VAAFPGDVEVRALIEGQFMAKRIHAEGLGYRVmSKTKILATGGASHNREILQVLADV 228
Cdd:cd07776   370 FDEPEITPPVPGGGRRFFGDDGvDAFFDPAVEVRAVVESQFLSMRLHAERLGSDI-PPTRILATGGASANKAILQVLADV 448

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034636798 229 FDAPVYVIDTANSACVGSAYRAFHGLAGGTDVPFS--EVVKLAPNPRLAATPSPGASQR 285
Cdd:cd07776   449 FGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSpeFVVFSAEEPKLVAEPDPEAAEV 507
PLN02669 PLN02669
xylulokinase
 66-267 2.98e-58

xylulokinase


Pssm-ID: 178274 [Multi-domain]  Cd Length: 556  Bit Score: 204.23  E-value: 2.98e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798  66 GTTQVSLGTSDTLFLWLQEPMPALEGHIFCNPVDSQHYMALLCFKNGSLMREKIRNESVSRSWSDFSKALQSTEMGNGGN 145
Cdd:PLN02669  295 GDLAISLGTSDTVFGITREPQPSLEGHVFPNPVDPESYMVMLCYKNGSLTREDIRNRCADGSWDVFNKLLEQTPPLNGGK 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 146 LGFYFDVMEITPEI-IGRHRFNTEN-----------HKVAAFPGDVEVRALIEGQFMAKRIHAEGLGYRVMSKtKILATG 213
Cdd:PLN02669  375 LGFYYKEHEILPPLpVGFHRYILENfsgealdglveEEVGEFDPPSEVRAIIEGQFLSMRAHAERFGMPVPPK-RIIATG 453

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034636798 214 GASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGLA---GGTDVPFSEVVK 267
Cdd:PLN02669  454 GASANQSILKLIASIFGCDVYTVQRPDSASLGAALRAAHGWLcneQGSFVPISCLYE 510
HIV_retropepsin_like cd05482
Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family ...
 451-537 5.83e-29

Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133149  Cd Length: 87  Bit Score: 110.05  E-value: 5.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 451 CEITIQGKKFKGLGDTGADVSIISLQHWPSVWPIQSAQFNIVGVGKAPEVYQSiYILHCEGPHE-QSGTIQPIVTSVPIN 529
Cdd:cd05482     1 LTLYINGKLFEGLLDTGADVSIIAENDWPKNWPIQPAPSNLTGIGGAITPSQS-SVLLLEIDGEgHLGTILVYVLSLPVN 79


                  ....*...
gi 1034636798 530 LWGRDLLQ 537
Cdd:cd05482    80 LWGRDILS 87
RVP pfam00077
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ...
 445-542 3.26e-26

Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a single domain of the two-domain eukaryotic aspartyl proteases such as pepsins, cathepsins, and renins (pfam00026).


Pssm-ID: 425454  Cd Length: 101  Bit Score: 102.83  E-value: 3.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 445 TDKHPTCEITIQGKKFKGLGDTGADVSIISLQHWPSVWPIQSAQFNIVGVGKAPEVYQSIYILHCEGPHEQSGTIQPIVT 524
Cdd:pfam00077   1 AEQRPLLTVKIGGKYFTALLDTGADDTVISQNDWPTNWPKQKATTNIQGIGGGINVRQSDQILILIGEDKFRGTVSPLIL 80

                          90
                  ....*....|....*....
gi 1034636798 525 S-VPINLWGRDLLQQWGAQ 542
Cdd:pfam00077  81 PtCPVNIIGRDLLQQLGGR 99
FGGY_C pfam02782
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ...
 70-254 8.82e-18

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: 81.99  E-value: 8.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798  70 VSLGTSDTLFLWLQEPmpALEGHIFCNPVDSQH-----YMALLCFKNGSLM---------REKIRNESVSRSWSDFSKAL 135
Cdd:pfam02782   3 ISAGTSSFVLVETPEP--VLSVHGVWGPYTNEMlpgywGLEGGQSAAGSLLawllqfhglREELRDAGNVESLAELAALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 136 QSTEMGnggnlGFYFDvmeitPEIIGRHRFNTENHKVAAFPG-------DVEVRALIEGQFMAKRIHAEGL----GYRVM 204
Cdd:pfam02782  81 AVAPAG-----GLLFY-----PDFSGNRAPGADPGARGSITGlsspttlAHLYRAILESLALQLRQILEALtkqeGHPID 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034636798 205 SktkILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGL 254
Cdd:pfam02782 151 T---IHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVAA 197
XylB COG1070
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ...
 66-276 2.35e-14

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: 75.64  E-value: 2.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798  66 GTTQVSLGTSDTLFLWLQEPM--PALEGHIFCNPVDsQHYMALLCFKNGSLMREKIRNE---SVSRSWSDFSKALQSTEM 140
Cdd:COG1070   253 GDAAVSLGTSGVVFVVSDKPLpdPEGRVHTFCHAVP-GRWLPMGATNNGGSALRWFRDLfadGELDDYEELNALAAEVPP 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 141 GNGGnLGFY---------FDVMEITPEIIGRhrfnTENHKVAAFpgdveVRALIEGQFMAKRIHAE---GLGYRVmskTK 208
Cdd:COG1070   332 GADG-LLFLpylsgertpHWDPNARGAFFGL----TLSHTRAHL-----ARAVLEGVAFALRDGLEaleEAGVKI---DR 398

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034636798 209 ILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGLAGGTDVP--FSEVVKLA----PNPRLAA 276
Cdd:COG1070   399 IRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEeaAAAMVRVGetiePDPENVA 472
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 355-431 1.25e-12

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 65.00  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 355 ASGMAGSLLGRSNLHLKGVQVQTGVIDSDYSGEIQIVI--STSVPWKAEPGECIAQLLIVPYVEMGRSETK-------QT 425
Cdd:pfam00692  43 PDGTYGRIFPRSGLAAKGLIVVPGVIDSDYRGEVKVVLfnLGKSDFTIKKGDRIAQLIFEPILHPELEPVEtldntdrGD 122


                  ....*.
gi 1034636798 426 GGSGST 431
Cdd:pfam00692 123 GGFGSS 128
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 357-411 1.56e-10

Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common family of dUTPase, found in bacteria, eukaryotes, and archaea. They catalyze the hydrolysis of the dUTP-Mg complex (dUTP-Mg) into dUMP and pyrophosphate. This reaction is crucial for the preservation of chromosomal integrity as it removes dUTP and therefore reduces the cellular dUTP/dTTP ratio, and prevents dUTP from being incorporated into DNA. It also provides dUMP as the precursor for dTTP synthesis via the thymidylate synthase pathway. dUTPases are homotrimeric, except some monomeric viral dUTPases, which have been shown to mimic a trimer. Active sites are located at the subunit interface.


Pssm-ID: 143638 [Multi-domain]  Cd Length: 92  Bit Score: 57.89  E-value: 1.56e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034636798 357 GMAGSLLGRSNLHLKGVQVQT-GVIDSDYSGEIQIVIS--TSVPWKAEPGECIAQLLI 411
Cdd:cd07557    35 GYVGLVFPRSSLARKGITVHNaGVIDPGYRGEITLELYnlGPEPVVIKKGDRIAQLVF 92
dut PRK00601
dUTP diphosphatase;
355-434 2.06e-09

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 56.33  E-value: 2.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 355 ASGMAGSLLGRSNLHLK-GVQV--QTGVIDSDYSGEIQ-IVISTS-VPWKAEPGECIAQLLIVPYVEMGRSETKQ----- 424
Cdd:PRK00601   59 PDGYEAQILPRSGLAHKhGIVLgnLPGTIDSDYRGELKvSLWNRGqEPFTIEPGERIAQLVIVPVVQAEFEEVEEfdete 138

                          90
                  ....*....|..
gi 1034636798 425 --TGGSGSTNKQ 434
Cdd:PRK00601  139 rgAGGFGSTGRH 150
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 357-431 4.01e-08

dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP pyrophosphatase (dUTPase) is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 440519 [Multi-domain]  Cd Length: 143  Bit Score: 52.33  E-value: 4.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 357 GMAGSLLGRSNLHLK-G-VQVQT-GVIDSDYSGEIQ-IVISTS-VPWKAEPGECIAQLLIVPYVEMGRSETKQ------- 424
Cdd:COG0756    55 GYEAQVRPRSGLALKhGiTLLNSpGTIDSDYRGEIKvILINLGdEPFTIERGDRIAQLVIAPVVQAEFEEVEEldeterg 134


                  ....*..
gi 1034636798 425 TGGSGST 431
Cdd:COG0756   135 AGGFGST 141
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 357-431 4.62e-08

deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is in maintaining the levels of dUTP in the cell to prevent dUTP incorporation into DNA during DNA replication. Pol proteins in viruses are very similar to this protein family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Changed role from 132 to 123. RTD [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]


Pssm-ID: 273149 [Multi-domain]  Cd Length: 142  Bit Score: 52.24  E-value: 4.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 357 GMAGSLLGRSNLHLK-GVQVQT--GVIDSDYSGEIQIVI--STSVPWKAEPGECIAQLLIVPYV-EMGRSETKQ------ 424
Cdd:TIGR00576  53 GYYGRVAPRSGLALKhGVTIDNspGVIDADYRGEIKVILinLGKEDFTVKKGDRIAQLVVEKIVtEVEFEEVEEldeter 132


                  ....*...
gi 1034636798 425 -TGGSGST 431
Cdd:TIGR00576 133 gEGGFGST 140
G_patch smart00443
glycine rich nucleic binding domain; A predicted glycine rich nucleic binding domain found in ...
 562-595 3.33e-06

glycine rich nucleic binding domain; A predicted glycine rich nucleic binding domain found in the splicing factor 45, SON DNA binding protein and D-type Retrovirus- polyproteins.


Pssm-ID: 197727 [Multi-domain]  Cd Length: 47  Bit Score: 44.07  E-value: 3.33e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1034636798  562 MGYVPGMGLEKNLQGLKKPVQAEGKNSCQGLGYH 595
Cdd:smart00443  14 MGWKEGQGLGKNEQGIVEPISAEIKKDRKGLGAV 47
G-patch pfam01585
G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in ...
 560-594 5.00e-05

G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in proteins that contain RNA binding domains. This suggests that this domain may have an RNA binding function. This domain has seven highly conserved glycines.


Pssm-ID: 396249 [Multi-domain]  Cd Length: 45  Bit Score: 40.95  E-value: 5.00e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1034636798 560 QEMGYVPGMGLEKNLQGLKKPVQAEGKNSCQGLGY 594
Cdd:pfam01585  10 QKMGWKEGQGLGKNEQGIAEPIEAKIKKDRRGLGA 44
 
Name Accession Description Interval E-value
ASKHA_NBD_FGGY_SpXK-like cd07776
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ...
 70-285 5.38e-107

nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; 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. The subfamily includes XKs mainly from eukaryote. 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: 466795 [Multi-domain]  Cd Length: 514  Bit Score: 331.44  E-value: 5.38e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798  70 VSLGTSDTLFLWLQEPMPALEGHIFCNPVDSQHYMALLCFKNGSLMREKIRNESVSRSWSDFSKALQSTEMGNGGNLGFY 149
Cdd:cd07776   290 VSLGTSDTVFLVLDEPKPGPEGHVFANPVDPGSYMAMLCYKNGSLARERVRDRYAGGSWEKFNELLESTPPGNNGNLGLY 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 150 FDVMEITPEIIGRHRFNTENHK-VAAFPGDVEVRALIEGQFMAKRIHAEGLGYRVmSKTKILATGGASHNREILQVLADV 228
Cdd:cd07776   370 FDEPEITPPVPGGGRRFFGDDGvDAFFDPAVEVRAVVESQFLSMRLHAERLGSDI-PPTRILATGGASANKAILQVLADV 448

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034636798 229 FDAPVYVIDTANSACVGSAYRAFHGLAGGTDVPFS--EVVKLAPNPRLAATPSPGASQR 285
Cdd:cd07776   449 FGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSpeFVVFSAEEPKLVAEPDPEAAEV 507
PLN02669 PLN02669
xylulokinase
 66-267 2.98e-58

xylulokinase


Pssm-ID: 178274 [Multi-domain]  Cd Length: 556  Bit Score: 204.23  E-value: 2.98e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798  66 GTTQVSLGTSDTLFLWLQEPMPALEGHIFCNPVDSQHYMALLCFKNGSLMREKIRNESVSRSWSDFSKALQSTEMGNGGN 145
Cdd:PLN02669  295 GDLAISLGTSDTVFGITREPQPSLEGHVFPNPVDPESYMVMLCYKNGSLTREDIRNRCADGSWDVFNKLLEQTPPLNGGK 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 146 LGFYFDVMEITPEI-IGRHRFNTEN-----------HKVAAFPGDVEVRALIEGQFMAKRIHAEGLGYRVMSKtKILATG 213
Cdd:PLN02669  375 LGFYYKEHEILPPLpVGFHRYILENfsgealdglveEEVGEFDPPSEVRAIIEGQFLSMRAHAERFGMPVPPK-RIIATG 453

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034636798 214 GASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGLA---GGTDVPFSEVVK 267
Cdd:PLN02669  454 GASANQSILKLIASIFGCDVYTVQRPDSASLGAALRAAHGWLcneQGSFVPISCLYE 510
HIV_retropepsin_like cd05482
Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family ...
 451-537 5.83e-29

Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133149  Cd Length: 87  Bit Score: 110.05  E-value: 5.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 451 CEITIQGKKFKGLGDTGADVSIISLQHWPSVWPIQSAQFNIVGVGKAPEVYQSiYILHCEGPHE-QSGTIQPIVTSVPIN 529
Cdd:cd05482     1 LTLYINGKLFEGLLDTGADVSIIAENDWPKNWPIQPAPSNLTGIGGAITPSQS-SVLLLEIDGEgHLGTILVYVLSLPVN 79


                  ....*...
gi 1034636798 530 LWGRDLLQ 537
Cdd:cd05482    80 LWGRDILS 87
RVP pfam00077
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ...
 445-542 3.26e-26

Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a single domain of the two-domain eukaryotic aspartyl proteases such as pepsins, cathepsins, and renins (pfam00026).


Pssm-ID: 425454  Cd Length: 101  Bit Score: 102.83  E-value: 3.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 445 TDKHPTCEITIQGKKFKGLGDTGADVSIISLQHWPSVWPIQSAQFNIVGVGKAPEVYQSIYILHCEGPHEQSGTIQPIVT 524
Cdd:pfam00077   1 AEQRPLLTVKIGGKYFTALLDTGADDTVISQNDWPTNWPKQKATTNIQGIGGGINVRQSDQILILIGEDKFRGTVSPLIL 80

                          90
                  ....*....|....*....
gi 1034636798 525 S-VPINLWGRDLLQQWGAQ 542
Cdd:pfam00077  81 PtCPVNIIGRDLLQQLGGR 99
ASKHA_NBD_FGGY cd00366
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ...
 66-250 3.45e-23

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: 101.87  E-value: 3.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798  66 GTTQVSLGTSDTLFLWLQEPMPAlEGHIFCNP-VDSQHYMALLCFKNGSLMREKIRNESVSRSWSD-----FSKALQSTE 139
Cdd:cd00366   204 GDAVDSTGTSSVLSVCTDEPVPP-DPRLLNRChVVPGLWLLEGAINTGGASLRWFRDEFGEEEDSDaeyegLDELAAEVP 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 140 MGNGGNLGFYFDVMEITPEIIGRHR---FN-TENHKVAAFpgdveVRALIEGQFMAKRIHAEGLGYRVMSKTKILATGGA 215
Cdd:cd00366   283 PGSDGLIFLPYLSGERSPIWDPAARgvfFGlTLSHTRAHL-----IRAVLEGVAYALRDNLEILEELGVKIKEIRVTGGG 357

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1034636798 216 SHNREILQVLADVFDAPVYVIDTANSACVGSAYRA 250
Cdd:cd00366   358 AKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
FGGY_C pfam02782
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ...
 70-254 8.82e-18

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: 81.99  E-value: 8.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798  70 VSLGTSDTLFLWLQEPmpALEGHIFCNPVDSQH-----YMALLCFKNGSLM---------REKIRNESVSRSWSDFSKAL 135
Cdd:pfam02782   3 ISAGTSSFVLVETPEP--VLSVHGVWGPYTNEMlpgywGLEGGQSAAGSLLawllqfhglREELRDAGNVESLAELAALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 136 QSTEMGnggnlGFYFDvmeitPEIIGRHRFNTENHKVAAFPG-------DVEVRALIEGQFMAKRIHAEGL----GYRVM 204
Cdd:pfam02782  81 AVAPAG-----GLLFY-----PDFSGNRAPGADPGARGSITGlsspttlAHLYRAILESLALQLRQILEALtkqeGHPID 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034636798 205 SktkILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGL 254
Cdd:pfam02782 151 T---IHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVAA 197
XylB COG1070
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ...
 66-276 2.35e-14

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: 75.64  E-value: 2.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798  66 GTTQVSLGTSDTLFLWLQEPM--PALEGHIFCNPVDsQHYMALLCFKNGSLMREKIRNE---SVSRSWSDFSKALQSTEM 140
Cdd:COG1070   253 GDAAVSLGTSGVVFVVSDKPLpdPEGRVHTFCHAVP-GRWLPMGATNNGGSALRWFRDLfadGELDDYEELNALAAEVPP 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 141 GNGGnLGFY---------FDVMEITPEIIGRhrfnTENHKVAAFpgdveVRALIEGQFMAKRIHAE---GLGYRVmskTK 208
Cdd:COG1070   332 GADG-LLFLpylsgertpHWDPNARGAFFGL----TLSHTRAHL-----ARAVLEGVAFALRDGLEaleEAGVKI---DR 398

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034636798 209 ILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGLAGGTDVP--FSEVVKLA----PNPRLAA 276
Cdd:COG1070   399 IRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEeaAAAMVRVGetiePDPENVA 472
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 355-431 1.25e-12

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 65.00  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 355 ASGMAGSLLGRSNLHLKGVQVQTGVIDSDYSGEIQIVI--STSVPWKAEPGECIAQLLIVPYVEMGRSETK-------QT 425
Cdd:pfam00692  43 PDGTYGRIFPRSGLAAKGLIVVPGVIDSDYRGEVKVVLfnLGKSDFTIKKGDRIAQLIFEPILHPELEPVEtldntdrGD 122


                  ....*.
gi 1034636798 426 GGSGST 431
Cdd:pfam00692 123 GGFGSS 128
ASKHA_NBD_FGGY_BaXK-like cd07809
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ...
 66-250 3.71e-12

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: 68.73  E-value: 3.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798  66 GTTQVSLGTSDTLFLWLQEPMPALEGHI--FCNPVDsqHYMALLCFKNG--SLMrEKIRnESVSRSWSDFSKALQSTEMG 141
Cdd:cd07809   255 GTVAVSLGTSGTAYGVSDKPVSDPHGRVatFCDSTG--GMLPLINTTNCltAWT-ELFR-ELLGVSYEELDELAAQAPPG 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 142 NGGNLGF-YFDVMEIT--PEIIGR-HRFNTENHKVAAFpgdveVRALIEGQFMA-----KRIHAEGlgyrvMSKTKILAT 212
Cdd:cd07809   331 AGGLLLLpFLNGERTPnlPHGRASlVGLTLSNFTRANL-----ARAALEGATFGlryglDILRELG-----VEIDEIRLI 400

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1034636798 213 GGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRA 250
Cdd:cd07809   401 GGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQA 438
ASKHA_NBD_FGGY_GntK cd07770
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ...
 70-276 1.36e-10

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: 63.73  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798  70 VSLGTSDTLFLWLQEPMPALEGHIFCNPVDSQHY---MALlcfKNGSL----MREKIRNESVSrsWSDFSKALQSTEMGN 142
Cdd:cd07770   254 LTVGTSGAIRVVSDRPVLDPPGRLWCYRLDENRWlvgGAI---NNGGNvldwLRDTLLLSGDD--YEELDKLAEAVPPGS 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 143 GGNLGFYFdvmeITPE------------IIGRhrfnTENHKVAAFpgdveVRALIEGqfMAKRIH--AEGLGYRVMSKTK 208
Cdd:cd07770   329 HGLIFLPY----LAGErapgwnpdargaFFGL----TLNHTRADI-----LRAVLEG--VAFNLKsiYEALEELAGPVKE 393

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034636798 209 ILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGLAGGTDVPFSEVVKLA----PNPRLAA 276
Cdd:cd07770   394 IRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSLEADELVKIGkvvePDPENHA 465
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 357-411 1.56e-10

Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common family of dUTPase, found in bacteria, eukaryotes, and archaea. They catalyze the hydrolysis of the dUTP-Mg complex (dUTP-Mg) into dUMP and pyrophosphate. This reaction is crucial for the preservation of chromosomal integrity as it removes dUTP and therefore reduces the cellular dUTP/dTTP ratio, and prevents dUTP from being incorporated into DNA. It also provides dUMP as the precursor for dTTP synthesis via the thymidylate synthase pathway. dUTPases are homotrimeric, except some monomeric viral dUTPases, which have been shown to mimic a trimer. Active sites are located at the subunit interface.


Pssm-ID: 143638 [Multi-domain]  Cd Length: 92  Bit Score: 57.89  E-value: 1.56e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034636798 357 GMAGSLLGRSNLHLKGVQVQT-GVIDSDYSGEIQIVIS--TSVPWKAEPGECIAQLLI 411
Cdd:cd07557    35 GYVGLVFPRSSLARKGITVHNaGVIDPGYRGEITLELYnlGPEPVVIKKGDRIAQLVF 92
ASKHA_NBD_FGGY_FK cd07773
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ...
 64-256 6.58e-10

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: 61.45  E-value: 6.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798  64 SLGTTQVSLGTSDTLFLwlqEPMPALEGHIFCNPVDSQHYMALLCFKNGSLMrEKIRNESVSRSWSDFSKALQSTEMGNG 143
Cdd:cd07773   255 STGTAEALLAVVDEPPL---DEMLAEGGLSYGHHVPGGYYYLAGSLPGGALL-EWFRDLFGGDESDLAAADELAEAAPPG 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 144 GN-LGF--YFDVMEiTPEIIGRHRFNTENHKVAAFPGDVeVRALIEG-QFMAKRIHA--EGLGYRVmskTKILATGGASH 217
Cdd:cd07773   331 PTgLLFlpHLSGSG-TPDFDPDARGAFLGLTLGTTRADL-LRAILEGlAFELRLNLEalEKAGIPI---DEIRAVGGGAR 405

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034636798 218 NREILQVLADVFDAPVYVIDTANSACVGSAYrafhgLAG 256
Cdd:cd07773   406 SPLWLQLKADILGRPIEVPEVPEATALGAAL-----LAG 439
dut PRK00601
dUTP diphosphatase;
355-434 2.06e-09

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 56.33  E-value: 2.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 355 ASGMAGSLLGRSNLHLK-GVQV--QTGVIDSDYSGEIQ-IVISTS-VPWKAEPGECIAQLLIVPYVEMGRSETKQ----- 424
Cdd:PRK00601   59 PDGYEAQILPRSGLAHKhGIVLgnLPGTIDSDYRGELKvSLWNRGqEPFTIEPGERIAQLVIVPVVQAEFEEVEEfdete 138

                          90
                  ....*....|..
gi 1034636798 425 --TGGSGSTNKQ 434
Cdd:PRK00601  139 rgAGGFGSTGRH 150
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 357-431 4.01e-08

dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP pyrophosphatase (dUTPase) is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 440519 [Multi-domain]  Cd Length: 143  Bit Score: 52.33  E-value: 4.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 357 GMAGSLLGRSNLHLK-G-VQVQT-GVIDSDYSGEIQ-IVISTS-VPWKAEPGECIAQLLIVPYVEMGRSETKQ------- 424
Cdd:COG0756    55 GYEAQVRPRSGLALKhGiTLLNSpGTIDSDYRGEIKvILINLGdEPFTIERGDRIAQLVIAPVVQAEFEEVEEldeterg 134


                  ....*..
gi 1034636798 425 TGGSGST 431
Cdd:COG0756   135 AGGFGST 141
ASKHA_NBD_FGGY_EcXK-like cd07808
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ...
 66-276 4.13e-08

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: 56.01  E-value: 4.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798  66 GTTQVSLGTSDTLFLWLQEPMPALEG--HIFCNPVDSQHY-MALLCFKNGSL--MREKIRNESVSrsWSDFSKALQSTEM 140
Cdd:cd07808   251 GDALISLGTSGVVFAPTDKPVPDPKGrlHTFPHAVPGKWYaMGVTLSAGLSLrwLRDLFGPDRES--FDELDAEAAKVPP 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 141 GNGGnLGF----------YFDvmeitPEIigRHRFN--TENHKVAAFpgdveVRALIEGQFMA-----KRIHAEGLGYRv 203
Cdd:cd07808   329 GSEG-LLFlpylsgertpYWD-----PNA--RGSFFglSLSHTRAHL-----ARAVLEGVAFSlrdslEVLKELGIKVK- 394

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034636798 204 msktKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGLAGGTDVPF--SEVVKLA----PNPRLAA 276
Cdd:cd07808   395 ----EIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEaaAACIKIEktiePDPERHE 469
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 357-431 4.62e-08

deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is in maintaining the levels of dUTP in the cell to prevent dUTP incorporation into DNA during DNA replication. Pol proteins in viruses are very similar to this protein family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Changed role from 132 to 123. RTD [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]


Pssm-ID: 273149 [Multi-domain]  Cd Length: 142  Bit Score: 52.24  E-value: 4.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 357 GMAGSLLGRSNLHLK-GVQVQT--GVIDSDYSGEIQIVI--STSVPWKAEPGECIAQLLIVPYV-EMGRSETKQ------ 424
Cdd:TIGR00576  53 GYYGRVAPRSGLALKhGVTIDNspGVIDADYRGEIKVILinLGKEDFTVKKGDRIAQLVVEKIVtEVEFEEVEEldeter 132


                  ....*...
gi 1034636798 425 -TGGSGST 431
Cdd:TIGR00576 133 gEGGFGST 140
ASKHA_NBD_FGGY_YgcE-like cd07779
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ...
 66-254 4.96e-07

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: 52.52  E-value: 4.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798  66 GTTQVSLGTSDTLFLWLQEPMPALEGHIFCNP--VDSQHYMALLCFKNGSLMR---------EKIRNESVSRSWSDFSKA 134
Cdd:cd07779   205 GTASLSLGTAAVVIAVSDKPVEDPERRIPCNPsaVPGKWVLEGSINTGGSAVRwfrdefgqdEVAEKELGVSPYELLNEE 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 135 LQSTEMGNGGnlgfyfdVMEItPEIIGRHRFNTENHKVAAF--------PGDVeVRALIEGQFMAKRIHAEGLGYRVMSK 206
Cdd:cd07779   285 AAKSPPGSDG-------LLFL-PYLAGAGTPYWNPEARGAFigltlshtRAHL-ARAILEGIAFELRDNLEAMEKAGVPI 355

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034636798 207 TKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFHGL 254
Cdd:cd07779   356 EEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGA 403
ASKHA_NBD_FGGY_RrXK-like cd07804
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ...
 182-257 6.19e-07

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: 52.14  E-value: 6.19e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034636798 182 RALIEGQFMAKRIHAEGLGYRVMSKTKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAfhGLAGG 257
Cdd:cd07804   378 RALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLA--GVGVG 451
ASKHA_NBD_FGGY_EcLyxK-like cd07802
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ...
 181-247 1.35e-06

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: 51.01  E-value: 1.35e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034636798 181 VRALIEGQFMAKRIHAEGLGYRVMSKTkILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSA 247
Cdd:cd07802   371 LRAVYEGIAFSHRDHLERLLVARKPET-IRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAA 436
G_patch smart00443
glycine rich nucleic binding domain; A predicted glycine rich nucleic binding domain found in ...
 562-595 3.33e-06

glycine rich nucleic binding domain; A predicted glycine rich nucleic binding domain found in the splicing factor 45, SON DNA binding protein and D-type Retrovirus- polyproteins.


Pssm-ID: 197727 [Multi-domain]  Cd Length: 47  Bit Score: 44.07  E-value: 3.33e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1034636798  562 MGYVPGMGLEKNLQGLKKPVQAEGKNSCQGLGYH 595
Cdd:smart00443  14 MGWKEGQGLGKNEQGIVEPISAEIKKDRKGLGAV 47
ASKHA_NBD_FGGY_L-RBK cd07781
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ...
 182-247 3.52e-06

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: 49.84  E-value: 3.52e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 182 RALIEG-QFMAKRI--HAEGLGYRVmskTKILATGG-ASHNREILQVLADVFDAPVYVIDTANSACVGSA 247
Cdd:cd07781   385 RALLEAtAFGTRAIieRFEEAGVPV---NRVVACGGiAEKNPLWMQIYADVLGRPIKVPKSDQAPALGAA 451
G-patch pfam01585
G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in ...
 560-594 5.00e-05

G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in proteins that contain RNA binding domains. This suggests that this domain may have an RNA binding function. This domain has seven highly conserved glycines.


Pssm-ID: 396249 [Multi-domain]  Cd Length: 45  Bit Score: 40.95  E-value: 5.00e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1034636798 560 QEMGYVPGMGLEKNLQGLKKPVQAEGKNSCQGLGY 594
Cdd:pfam01585  10 QKMGWKEGQGLGKNEQGIAEPIEAKIKKDRRGLGA 44
ASKHA_NBD_FGGY_CvXK-like cd07805
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ...
 181-276 6.18e-05

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: 45.97  E-value: 6.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 181 VRALIEGQFMAKRIHAEGLGYRVMSKTKILATGGASHNREILQVLADVFDAPVYVIDTA-NSACVGSAYRAFHGLagGTD 259
Cdd:cd07805   374 ARAVLEGVAFNLRWLLEALEKLTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPENPqEAGALGAALLAAVGL--GLL 451

                          90       100
                  ....*....|....*....|....
gi 1034636798 260 VPFSEVVKL-------APNPRLAA 276
Cdd:cd07805   452 KSFDEAKALvkvekvfEPDPENRA 475
ASKHA_NBD_FGGY_GK5-like cd07793
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ...
 181-257 3.23e-03

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: 40.24  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 181 VRALIEGqfMAKRIHA--EGLGYRVMSK-TKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAfhGLAGG 257
Cdd:cd07793   387 VRAILES--IAFRVKQllETMEKETSIKiSSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLA--GLASG 462
PRK04123 PRK04123
ribulokinase; Provisional
 182-261 6.05e-03

ribulokinase; Provisional


Pssm-ID: 235221 [Multi-domain]  Cd Length: 548  Bit Score: 39.44  E-value: 6.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 182 RALIEGQ-FMAKRI----HAEGLgyRVmskTKILATGG-ASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAFhgLA 255
Cdd:PRK04123  415 RALIEATaFGTRAImecfEDQGV--PV---EEVIAAGGiARKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAA--VA 487


                  ....*...
gi 1034636798 256 GGT--DVP 261
Cdd:PRK04123  488 AGAypDIP 495
PTZ00294 PTZ00294
glycerol kinase-like protein; Provisional
 145-286 6.72e-03

glycerol kinase-like protein; Provisional


Pssm-ID: 240348 [Multi-domain]  Cd Length: 504  Bit Score: 39.19  E-value: 6.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 145 NLGFYFDVMEItpEIIGRHRFNTEN-HKVAAFPG------DVEVRALIEG-QFMAKRIHA-----EGLGYRV------MS 205
Cdd:PTZ00294  323 NMGLISHPSEI--EKLARSVKDTGGvVFVPAFSGlfapywRPDARGTIVGmTLKTTRAHIvraalEAIALQTndviesME 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 206 K------TKILATGGASHNREILQVLADVFDAPVYVIDTANSACVGSAYRAfhGLAGG--TDVpfSEVVKLAPNPRLAAT 277
Cdd:PTZ00294  401 KdagielNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLA--GLAVGvwKSL--EEVKKLIRRSNSTFS 476


                  ....*....
gi 1034636798 278 PSPGASQRR 286
Cdd:PTZ00294  477 PQMSAEERK 485
RP_RTVL_H_like cd06095
Retropepsin of the RTVL_H family of human endogenous retrovirus-like elements; This family ...
 453-537 7.17e-03

Retropepsin of the RTVL_H family of human endogenous retrovirus-like elements; This family includes aspartate proteases from retroelements with LTR (long terminal repeats) including the RTVL_H family of human endogenous retrovirus-like elements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.


Pssm-ID: 133159  Cd Length: 86  Bit Score: 36.16  E-value: 7.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034636798 453 ITIQGKKFKGLGDTGADVSIISLQHWPSvwPIQSAQF-NIVGVGKAPEVYQSIYILHCE-GPHEQSGTIQpIVTSVPINL 530
Cdd:cd06095     3 ITVEGVPIVFLVDTGATHSVLKSDLGPK--QELSTTSvLIRGVSGQSQQPVTTYRTLVDlGGHTVSHSFL-VVPNCPDPL 79


                  ....*..
gi 1034636798 531 WGRDLLQ 537
Cdd:cd06095    80 LGRDLLS 86
 
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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