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Conserved domains on  [gi|26350549|dbj|BAC38914|]
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unnamed protein product, partial [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DYN1 super family cl34955
Dynein, heavy chain [Cytoskeleton];
53-921 2.70e-54

Dynein, heavy chain [Cytoskeleton];


The actual alignment was detected with superfamily member COG5245:

Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 206.76  E-value: 2.70e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549   53 MKKALELYEQLRQRTGVVIVGPSGAGKSTLWRmlrAALCKIGKVVKQYTMNPKAMPRHQLLGHIDMDTREWSDGVLTNSA 132
Cdd:COG5245 1169 VAQFVSFLRSVDTGAFHAEYFRVFLCKIKHYT---DACDYLWHVKSPYVKKKYFDADMELRQFFLMFNREDMEARLADSK 1245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  133 RQVVREpqdvsswiicdgdidpEWIESLNSVLDDNRLLTMPSGERiqfgpnvNFVFETHDlscASPATISRMGMIFLSDE 212
Cdd:COG5245 1246 MEYEVE----------------RYVEKTKAEVSSLKLELSSVGEG-------QVVVSNLG---SIGDKVGRCLVEYDSIS 1299

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  213 ETDLNSLIKSWL--RNQPLEyrSNLENWIGDYFSK----ALQWVLKQNDYVVETSLVGTVmnGLSHLHGCKYHDQFIINL 286
Cdd:COG5245 1300 RLSTKGVFLDELgdTKRYLD--ECLDFFSCFEEVQkeidELSMVFCADALRFSADLYHIV--KERRFSGVLAGSDASESL 1375

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  287 I---RGLGGNLNMKSRLEFTKEVFN----WA------RETPPDSHRPMDTYYDCDRGQLASY--MLKKPESLTADDFSNG 351
Cdd:COG5245 1376 GgksIELAAILEHKDLIVEMKRGINdvlkLRifgdkcRESTPRFYLISDGDLIKDLNERSDYeeMLIMMFNISAVITNNG 1455

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  352 HI-----------LP---VIQTPDMQRGLDYFKPWLSsdTKQPFILVGPEGCGKGMLLRYAFSQLRSTEIATIHCSAQTT 417
Cdd:COG5245 1456 SIagfelrgervmLRkevVIPTSDTGFVDSFSNEALN--TLRSYIYCGPPGSGKEMLMCPSLRSELITEVKYFNFSTCTM 1533

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  418 SRHLLQKLSQTcMVISTNTG--RVYRPKDCERLVLYLKDINLPKLDKWGTSTLVAFLQQVLTYQGFYDE-NLEWVGLENI 494
Cdd:COG5245 1534 TPSKLSVLERE-TEYYPNTGvvRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSSiAVSWVTICGI 1612

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  495 QIVASMSAGGRLGRHKLTTRFTSIVRLCAIDYPEREQLQTIYGAYLEAVLHKNLKNHSIwgssskIYLLAGSMVQVYEQV 574
Cdd:COG5245 1613 ILYGACNPGTDEGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRL------SEETMSASVELYLSS 1686

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  575 RAKFTVDEYSHYFFTPCILTQWVLGLFRYDLEGGSSnhPLDYVLEIVAYEARRLFRDKIVGVKELHLFDNILTSVLQGDW 654
Cdd:COG5245 1687 KDKTKFFLQMNYGYKPRELTRSLRAIFGYAETRIDT--PDVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAI 1764

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  655 GSDILDNMADSFYVTWGAHHVSggktapgqplpphgkpLGKLTSADLKDVIKKGLIHYGRDNQNLDILLFQEVLEYMSRI 734
Cdd:COG5245 1765 REMIAGHIGEAEITFSMILFFG----------------MACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRS 1828

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  735 DRVLSFPGGSLLLAGRSGVGRRTVTSLVSHMHGAVLFSPKISRGYEPKQFRNDLKHVLKLAGIEAQQVVLLLEDYQFVHP 814
Cdd:COG5245 1829 RRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVES 1908

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  815 TFLEMINSLLASGEVPGLYTLEELEPLLLPLKDQASQDG--FFGP--VFNYFTYRIQQNLHIVL-IMDSANLNFIVNCES 889
Cdd:COG5245 1909 SFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSleKDTEatLTRVFLVYMEENLPVVFsACCSQDTSVLAGIRS 1988

                        890       900       910
                 ....*....|....*....|....*....|..
gi 26350549  890 nPALHKKCQVLWMEGWSDSSMKKIPEMLFSET 921
Cdd:COG5245 1989 -PALKNRCFIDFKKLWDTEEMSQYANSVETLS 2019
AAA_6 super family cl37597
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ...
 1-80 2.25e-21

Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities: AAA1-AAA6). This is the first site (out of four nucleotide binding sites in the dynein motor) where the movement depends on ATP hydrolysis. When this site is nucleotide free or bound to ADP, the microtubule binding domain (MTBD) binds to the microtubule and the linker adopts the straight post-power-stroke conformation. Upon ATP binding and hydrolysis, the MTBD detaches from the microtubule and the linker is primed into the pre-power-stroke conformation. Dynein's AAA+ domains are each divided into an alpha/beta large subdomain designated with an L and and alpha small subdomains designated with an S. This is the AAA1 large (AAA1L) subdomain with the accompanying small subdomain (AAA1S). AAA1L, AAA1S and AAA2L enclose ADP.vanadate (ADP.Vi, ATP-hydrolysis transition state analogue). The AAA1L sensor-I loop, which varies in position depending on dynein's nucleotide state, swings in to contact AAA2L forming the important AAA1 nucleotide-binding site.


The actual alignment was detected with superfamily member pfam12774:

Pssm-ID: 463697 [Multi-domain]  Cd Length: 327  Bit Score: 96.40  E-value: 2.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549     1 MSKFTFADCTRFDALIKDVFPGIDFKEVEYDELSSALKQVFEEANYEVIPNQMKKALELYEQLRQRTGVVIVGPSGAGKS 80
Cdd:pfam12774 248 LPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVGPTGSGKT 327
 
Name Accession Description Interval E-value
DYN1 COG5245
Dynein, heavy chain [Cytoskeleton];
53-921 2.70e-54

Dynein, heavy chain [Cytoskeleton];


Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 206.76  E-value: 2.70e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549   53 MKKALELYEQLRQRTGVVIVGPSGAGKSTLWRmlrAALCKIGKVVKQYTMNPKAMPRHQLLGHIDMDTREWSDGVLTNSA 132
Cdd:COG5245 1169 VAQFVSFLRSVDTGAFHAEYFRVFLCKIKHYT---DACDYLWHVKSPYVKKKYFDADMELRQFFLMFNREDMEARLADSK 1245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  133 RQVVREpqdvsswiicdgdidpEWIESLNSVLDDNRLLTMPSGERiqfgpnvNFVFETHDlscASPATISRMGMIFLSDE 212
Cdd:COG5245 1246 MEYEVE----------------RYVEKTKAEVSSLKLELSSVGEG-------QVVVSNLG---SIGDKVGRCLVEYDSIS 1299

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  213 ETDLNSLIKSWL--RNQPLEyrSNLENWIGDYFSK----ALQWVLKQNDYVVETSLVGTVmnGLSHLHGCKYHDQFIINL 286
Cdd:COG5245 1300 RLSTKGVFLDELgdTKRYLD--ECLDFFSCFEEVQkeidELSMVFCADALRFSADLYHIV--KERRFSGVLAGSDASESL 1375

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  287 I---RGLGGNLNMKSRLEFTKEVFN----WA------RETPPDSHRPMDTYYDCDRGQLASY--MLKKPESLTADDFSNG 351
Cdd:COG5245 1376 GgksIELAAILEHKDLIVEMKRGINdvlkLRifgdkcRESTPRFYLISDGDLIKDLNERSDYeeMLIMMFNISAVITNNG 1455

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  352 HI-----------LP---VIQTPDMQRGLDYFKPWLSsdTKQPFILVGPEGCGKGMLLRYAFSQLRSTEIATIHCSAQTT 417
Cdd:COG5245 1456 SIagfelrgervmLRkevVIPTSDTGFVDSFSNEALN--TLRSYIYCGPPGSGKEMLMCPSLRSELITEVKYFNFSTCTM 1533

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  418 SRHLLQKLSQTcMVISTNTG--RVYRPKDCERLVLYLKDINLPKLDKWGTSTLVAFLQQVLTYQGFYDE-NLEWVGLENI 494
Cdd:COG5245 1534 TPSKLSVLERE-TEYYPNTGvvRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSSiAVSWVTICGI 1612

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  495 QIVASMSAGGRLGRHKLTTRFTSIVRLCAIDYPEREQLQTIYGAYLEAVLHKNLKNHSIwgssskIYLLAGSMVQVYEQV 574
Cdd:COG5245 1613 ILYGACNPGTDEGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRL------SEETMSASVELYLSS 1686

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  575 RAKFTVDEYSHYFFTPCILTQWVLGLFRYDLEGGSSnhPLDYVLEIVAYEARRLFRDKIVGVKELHLFDNILTSVLQGDW 654
Cdd:COG5245 1687 KDKTKFFLQMNYGYKPRELTRSLRAIFGYAETRIDT--PDVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAI 1764

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  655 GSDILDNMADSFYVTWGAHHVSggktapgqplpphgkpLGKLTSADLKDVIKKGLIHYGRDNQNLDILLFQEVLEYMSRI 734
Cdd:COG5245 1765 REMIAGHIGEAEITFSMILFFG----------------MACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRS 1828

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  735 DRVLSFPGGSLLLAGRSGVGRRTVTSLVSHMHGAVLFSPKISRGYEPKQFRNDLKHVLKLAGIEAQQVVLLLEDYQFVHP 814
Cdd:COG5245 1829 RRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVES 1908

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  815 TFLEMINSLLASGEVPGLYTLEELEPLLLPLKDQASQDG--FFGP--VFNYFTYRIQQNLHIVL-IMDSANLNFIVNCES 889
Cdd:COG5245 1909 SFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSleKDTEatLTRVFLVYMEENLPVVFsACCSQDTSVLAGIRS 1988

                        890       900       910
                 ....*....|....*....|....*....|..
gi 26350549  890 nPALHKKCQVLWMEGWSDSSMKKIPEMLFSET 921
Cdd:COG5245 1989 -PALKNRCFIDFKKLWDTEEMSQYANSVETLS 2019
AAA_8 pfam12780
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ...
 719-905 2.30e-45

P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This particular family is the D4 ATP-binding region of the motor.


Pssm-ID: 463701 [Multi-domain]  Cd Length: 259  Bit Score: 163.93  E-value: 2.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549   719 LDILLFQEVLEYMSRIDRVLSFPGGSLLLAGRSGVGRRTVTSLVSHMHGAVLFSPKISRGYEPKQFRNDLKHVLKLAGIE 798
Cdd:pfam12780   1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549   799 AQQVVLLLEDYQFVHPTFLEMINSLLASGEVPGLYTLEELEPLLLPLKDQASQDGFFGP---VFNYFTYRIQQNLHIVLI 875
Cdd:pfam12780  81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSreaVYNYFVKRCRNNLHIVLC 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 26350549   876 MDSANLNFIVNCESNPALHKKCQVLWMEGW 905
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEW 190
AAA_6 pfam12774
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ...
 1-80 2.25e-21

Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities: AAA1-AAA6). This is the first site (out of four nucleotide binding sites in the dynein motor) where the movement depends on ATP hydrolysis. When this site is nucleotide free or bound to ADP, the microtubule binding domain (MTBD) binds to the microtubule and the linker adopts the straight post-power-stroke conformation. Upon ATP binding and hydrolysis, the MTBD detaches from the microtubule and the linker is primed into the pre-power-stroke conformation. Dynein's AAA+ domains are each divided into an alpha/beta large subdomain designated with an L and and alpha small subdomains designated with an S. This is the AAA1 large (AAA1L) subdomain with the accompanying small subdomain (AAA1S). AAA1L, AAA1S and AAA2L enclose ADP.vanadate (ADP.Vi, ATP-hydrolysis transition state analogue). The AAA1L sensor-I loop, which varies in position depending on dynein's nucleotide state, swings in to contact AAA2L forming the important AAA1 nucleotide-binding site.


Pssm-ID: 463697 [Multi-domain]  Cd Length: 327  Bit Score: 96.40  E-value: 2.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549     1 MSKFTFADCTRFDALIKDVFPGIDFKEVEYDELSSALKQVFEEANYEVIPNQMKKALELYEQLRQRTGVVIVGPSGAGKS 80
Cdd:pfam12774 248 LPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVGPTGSGKT 327
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 31-82 1.53e-04

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 43.93  E-value: 1.53e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26350549  31 DELSSALKQVFEEANYEVIPNQMKKAL---ELYEQLRQRTgVVIVGPSGAGKSTL 82
Cdd:cd01854  48 DEELEELLEIYEKLGYPVLAVSAKTGEgldELRELLKGKT-SVLVGQSGVGKSTL 101
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
69-107 7.37e-04

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 42.91  E-value: 7.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 26350549   69 VVIVGPSGAGKSTLWRMLrAALCKI--------GKVVKQytMNPK----AM 107
Cdd:PRK11650  33 IVLVGPSGCGKSTLLRMV-AGLERItsgeiwigGRVVNE--LEPAdrdiAM 80
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 30-86 4.45e-03

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 40.69  E-value: 4.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26350549    30 YDELSSALKQVFEEANYEVIP------------NQMKKALE---LYEQLR---QRTGVV-IVGPSGAGKSTLWRML 86
Cdd:TIGR03719 293 YEELLSQEFQKRNETAEIYIPpgprlgdkvieaENLTKAFGdklLIDDLSfklPPGGIVgVIGPNGAGKSTLFRMI 368
 
Name Accession Description Interval E-value
DYN1 COG5245
Dynein, heavy chain [Cytoskeleton];
53-921 2.70e-54

Dynein, heavy chain [Cytoskeleton];


Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 206.76  E-value: 2.70e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549   53 MKKALELYEQLRQRTGVVIVGPSGAGKSTLWRmlrAALCKIGKVVKQYTMNPKAMPRHQLLGHIDMDTREWSDGVLTNSA 132
Cdd:COG5245 1169 VAQFVSFLRSVDTGAFHAEYFRVFLCKIKHYT---DACDYLWHVKSPYVKKKYFDADMELRQFFLMFNREDMEARLADSK 1245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  133 RQVVREpqdvsswiicdgdidpEWIESLNSVLDDNRLLTMPSGERiqfgpnvNFVFETHDlscASPATISRMGMIFLSDE 212
Cdd:COG5245 1246 MEYEVE----------------RYVEKTKAEVSSLKLELSSVGEG-------QVVVSNLG---SIGDKVGRCLVEYDSIS 1299

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  213 ETDLNSLIKSWL--RNQPLEyrSNLENWIGDYFSK----ALQWVLKQNDYVVETSLVGTVmnGLSHLHGCKYHDQFIINL 286
Cdd:COG5245 1300 RLSTKGVFLDELgdTKRYLD--ECLDFFSCFEEVQkeidELSMVFCADALRFSADLYHIV--KERRFSGVLAGSDASESL 1375

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  287 I---RGLGGNLNMKSRLEFTKEVFN----WA------RETPPDSHRPMDTYYDCDRGQLASY--MLKKPESLTADDFSNG 351
Cdd:COG5245 1376 GgksIELAAILEHKDLIVEMKRGINdvlkLRifgdkcRESTPRFYLISDGDLIKDLNERSDYeeMLIMMFNISAVITNNG 1455

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  352 HI-----------LP---VIQTPDMQRGLDYFKPWLSsdTKQPFILVGPEGCGKGMLLRYAFSQLRSTEIATIHCSAQTT 417
Cdd:COG5245 1456 SIagfelrgervmLRkevVIPTSDTGFVDSFSNEALN--TLRSYIYCGPPGSGKEMLMCPSLRSELITEVKYFNFSTCTM 1533

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  418 SRHLLQKLSQTcMVISTNTG--RVYRPKDCERLVLYLKDINLPKLDKWGTSTLVAFLQQVLTYQGFYDE-NLEWVGLENI 494
Cdd:COG5245 1534 TPSKLSVLERE-TEYYPNTGvvRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSSiAVSWVTICGI 1612

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  495 QIVASMSAGGRLGRHKLTTRFTSIVRLCAIDYPEREQLQTIYGAYLEAVLHKNLKNHSIwgssskIYLLAGSMVQVYEQV 574
Cdd:COG5245 1613 ILYGACNPGTDEGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRL------SEETMSASVELYLSS 1686

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  575 RAKFTVDEYSHYFFTPCILTQWVLGLFRYDLEGGSSnhPLDYVLEIVAYEARRLFRDKIVGVKELHLFDNILTSVLQGDW 654
Cdd:COG5245 1687 KDKTKFFLQMNYGYKPRELTRSLRAIFGYAETRIDT--PDVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAI 1764

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  655 GSDILDNMADSFYVTWGAHHVSggktapgqplpphgkpLGKLTSADLKDVIKKGLIHYGRDNQNLDILLFQEVLEYMSRI 734
Cdd:COG5245 1765 REMIAGHIGEAEITFSMILFFG----------------MACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRS 1828

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  735 DRVLSFPGGSLLLAGRSGVGRRTVTSLVSHMHGAVLFSPKISRGYEPKQFRNDLKHVLKLAGIEAQQVVLLLEDYQFVHP 814
Cdd:COG5245 1829 RRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVES 1908

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  815 TFLEMINSLLASGEVPGLYTLEELEPLLLPLKDQASQDG--FFGP--VFNYFTYRIQQNLHIVL-IMDSANLNFIVNCES 889
Cdd:COG5245 1909 SFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSleKDTEatLTRVFLVYMEENLPVVFsACCSQDTSVLAGIRS 1988

                        890       900       910
                 ....*....|....*....|....*....|..
gi 26350549  890 nPALHKKCQVLWMEGWSDSSMKKIPEMLFSET 921
Cdd:COG5245 1989 -PALKNRCFIDFKKLWDTEEMSQYANSVETLS 2019
AAA_8 pfam12780
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ...
 719-905 2.30e-45

P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This particular family is the D4 ATP-binding region of the motor.


Pssm-ID: 463701 [Multi-domain]  Cd Length: 259  Bit Score: 163.93  E-value: 2.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549   719 LDILLFQEVLEYMSRIDRVLSFPGGSLLLAGRSGVGRRTVTSLVSHMHGAVLFSPKISRGYEPKQFRNDLKHVLKLAGIE 798
Cdd:pfam12780   1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549   799 AQQVVLLLEDYQFVHPTFLEMINSLLASGEVPGLYTLEELEPLLLPLKDQASQDGFFGP---VFNYFTYRIQQNLHIVLI 875
Cdd:pfam12780  81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSreaVYNYFVKRCRNNLHIVLC 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 26350549   876 MDSANLNFIVNCESNPALHKKCQVLWMEGW 905
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEW 190
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 68-204 1.83e-30

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 117.01  E-value: 1.83e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549    68 GVVIVGPSGAGKSTLWRMLRAALCKigkVVKQYTMNPKAMPRHQLLGHIDMDTR--EWSDGVLTNSARqvvrepqdvSSW 145
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSN---RPVFYVQLTRDTTEEDLFGRRNIDPGgaSWVDGPLVRAAR---------EGE 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26350549   146 IICDGDID---PEWIESLNSVLDDNRLLTMPSGERIQFGP-NVNFVFETHDL----SCASPATISRM 204
Cdd:pfam07728  69 IAVLDEINranPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIATMNPLdrglNELSPALRSRF 135
AAA_6 pfam12774
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ...
 1-80 2.25e-21

Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities: AAA1-AAA6). This is the first site (out of four nucleotide binding sites in the dynein motor) where the movement depends on ATP hydrolysis. When this site is nucleotide free or bound to ADP, the microtubule binding domain (MTBD) binds to the microtubule and the linker adopts the straight post-power-stroke conformation. Upon ATP binding and hydrolysis, the MTBD detaches from the microtubule and the linker is primed into the pre-power-stroke conformation. Dynein's AAA+ domains are each divided into an alpha/beta large subdomain designated with an L and and alpha small subdomains designated with an S. This is the AAA1 large (AAA1L) subdomain with the accompanying small subdomain (AAA1S). AAA1L, AAA1S and AAA2L enclose ADP.vanadate (ADP.Vi, ATP-hydrolysis transition state analogue). The AAA1L sensor-I loop, which varies in position depending on dynein's nucleotide state, swings in to contact AAA2L forming the important AAA1 nucleotide-binding site.


Pssm-ID: 463697 [Multi-domain]  Cd Length: 327  Bit Score: 96.40  E-value: 2.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549     1 MSKFTFADCTRFDALIKDVFPGIDFKEVEYDELSSALKQVFEEANYEVIPNQMKKALELYEQLRQRTGVVIVGPSGAGKS 80
Cdd:pfam12774 248 LPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVGPTGSGKT 327
AAA_7 pfam12775
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ...
 378-517 6.58e-21

P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).


Pssm-ID: 463698 [Multi-domain]  Cd Length: 179  Bit Score: 90.91  E-value: 6.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549   378 KQPFILVGPEGCGKGMLLRYAFSQLRSTE--IATIHCSAQTTSrhllqklSQTCMVISTN----TGRVYRPKDCERLVLY 451
Cdd:pfam12775  31 GKPVLLVGPTGTGKTVIIQNLLRKLDKEKylPLFINFSAQTTS-------NQTQDIIESKlekrRKGVYGPPGGKKLVVF 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26350549   452 LKDINLPKLDKWGTSTLVAFLQQVLTYQGFYD-ENLEWVGLENIQIVASMS-AGGrlGRHKLTTRFTS 517
Cdd:pfam12775 104 IDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDrKKLTFKEIVDVQFVAAMGpPGG--GRNDITPRLLR 169
DYN1 COG5245
Dynein, heavy chain [Cytoskeleton];
24-219 1.37e-08

Dynein, heavy chain [Cytoskeleton];


Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 59.23  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549   24 DFKEVEYDELSSALKQVFEEANYEVIPNQMKKALELYEQ-LRQRTGVVIVGPSGAGKSTLwrmlRAALCKIGKVVKQYtm 102
Cdd:COG5245 1786 GMACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHiLRSRRGLLVVGGHGVLKGVL----IRGACDAREFVCWL-- 1859

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  103 NPKAMprHQLLGHIDMDTREWSDGVLTNSARQVVREPQdvSSWIICDGDI-DPEWIESLNSVLDDNRLLTMPSG-ERIQF 180
Cdd:COG5245 1860 NPRNM--REIFGHRDELTGDFRDSLKVQDLRRNIHGGR--ECLFIFESIPvESSFLEDFNPLLDNNRFLCLFSGnERIRI 1935

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 26350549  181 GPNVNFVFETHDLSCASPATISRmgmIFLSDEETDLNSL 219
Cdd:COG5245 1936 PENLRFVFESTSLEKDTEATLTR---VFLVYMEENLPVV 1971
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 31-82 1.53e-04

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 43.93  E-value: 1.53e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26350549  31 DELSSALKQVFEEANYEVIPNQMKKAL---ELYEQLRQRTgVVIVGPSGAGKSTL 82
Cdd:cd01854  48 DEELEELLEIYEKLGYPVLAVSAKTGEgldELRELLKGKT-SVLVGQSGVGKSTL 101
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 38-90 5.72e-04

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 42.25  E-value: 5.72e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 26350549  38 KQVFEEANYEVIPNQMkkalelyeqlrqrtgVVIVGPSGAGKSTLWRMLRAAL 90
Cdd:COG2401  43 RYVLRDLNLEIEPGEI---------------VLIVGASGSGKSTLLRLLAGAL 80
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
69-107 7.37e-04

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 42.91  E-value: 7.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 26350549   69 VVIVGPSGAGKSTLWRMLrAALCKI--------GKVVKQytMNPK----AM 107
Cdd:PRK11650  33 IVLVGPSGCGKSTLLRMV-AGLERItsgeiwigGRVVNE--LEPAdrdiAM 80
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 69-86 9.76e-04

ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 42.37  E-value: 9.76e-04
                        10
                ....*....|....*...
gi 26350549  69 VVIVGPSGAGKSTLWRML 86
Cdd:COG3839  32 LVLLGPSGCGKSTLLRMI 49
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 380-423 2.08e-03

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 39.20  E-value: 2.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 26350549   380 PFILVGPEGCGKGMLLRYAFSQLRSTEIATIHCSAQTTSRHLLQ 423
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLTRDTTEEDLFG 44
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 69-86 2.55e-03

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 40.50  E-value: 2.55e-03
                        10
                ....*....|....*...
gi 26350549  69 VVIVGPSGAGKSTLWRML 86
Cdd:COG4778  40 VALTGPSGAGKSTLLKCI 57
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 52-90 2.67e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 40.54  E-value: 2.67e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 26350549  52 QMKKALE-LYEQLRQRTG-VVIVGPSGAGKSTLWRMLRAAL 90
Cdd:COG3267  27 SHREALArLEYALAQGGGfVVLTGEVGTGKTTLLRRLLERL 67
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 69-86 3.02e-03

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 40.36  E-value: 3.02e-03
                        10
                ....*....|....*...
gi 26350549  69 VVIVGPSGAGKSTLWRML 86
Cdd:COG1126  30 VVIIGPSGSGKSTLLRCI 47
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 69-86 3.58e-03

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 40.07  E-value: 3.58e-03
                        10
                ....*....|....*...
gi 26350549  69 VVIVGPSGAGKSTLWRML 86
Cdd:COG1116  40 VALVGPSGCGKSTLLRLI 57
AAA_22 pfam13401
AAA domain;
376-425 3.89e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.48  E-value: 3.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 26350549   376 DTKQPFILVGPEGCGKGMLLRYAFSQL--RSTEIATIHCSAQTTSRHLLQKL 425
Cdd:pfam13401   3 FGAGILVLTGESGTGKTTLLRRLLEQLpeVRDSVVFVDLPSGTSPKDLLRAL 54
PRK13764 PRK13764
ATPase; Provisional
 54-102 4.10e-03

ATPase; Provisional


Pssm-ID: 184311 [Multi-domain]  Cd Length: 602  Bit Score: 40.98  E-value: 4.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 26350549   54 KKALELY---EQLRQR-----TGVVIVGPSGAGKSTLWRMLRAALCKIGKVVKqyTM 102
Cdd:PRK13764 237 KLSLEDYnlsEKLKERleeraEGILIAGAPGAGKSTFAQALAEFYADMGKIVK--TM 291
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 67-86 4.26e-03

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 40.89  E-value: 4.26e-03
                        10        20
                ....*....|....*....|
gi 26350549  67 TGVVIVGPSGAGKSTLWRML 86
Cdd:COG4618 359 EVLGVIGPSGSGKSTLARLL 378
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 30-86 4.45e-03

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 40.69  E-value: 4.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26350549    30 YDELSSALKQVFEEANYEVIP------------NQMKKALE---LYEQLR---QRTGVV-IVGPSGAGKSTLWRML 86
Cdd:TIGR03719 293 YEELLSQEFQKRNETAEIYIPpgprlgdkvieaENLTKAFGdklLIDDLSfklPPGGIVgVIGPNGAGKSTLFRMI 368
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 36-82 5.75e-03

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 38.68  E-value: 5.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 26350549    36 ALKQVFEEANYEVIP---NQMKKALELYEQLRQRTgVVIVGPSGAGKSTL 82
Cdd:pfam03193  74 ELLKIYRAIGYPVLFvsaKTGEGIEALKELLKGKT-TVLAGQSGVGKSTL 122
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
69-90 5.98e-03

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 39.27  E-value: 5.98e-03
                        10        20
                ....*....|....*....|..
gi 26350549  69 VVIVGPSGAGKSTLWRMLRAAL 90
Cdd:COG2884  31 VFLTGPSGAGKSTLLKLLYGEE 52
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
 69-162 6.89e-03

Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP).


Pssm-ID: 238835  Cd Length: 200  Bit Score: 38.79  E-value: 6.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26350549  69 VVIVGPSGAGKSTLWRMLRAALCKIGKVVKQyTMNPKAMPR----HQLLGHIDMDTREWSDGVLTNSA--RQVVRE---- 138
Cdd:cd01672   3 IVFEGIDGAGKTTLIELLAERLEARGYEVVL-TREPGGTPIgeaiRELLLDPEDEKMDPRAELLLFAAdrAQHVEEvikp 81

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 26350549 139 --PQDvsSWIICD-------------GDIDPEWIESLNS 162
Cdd:cd01672  82 alARG--KIVLSDrfvdsslayqgagRGLGEALIEALND 118
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 69-86 7.13e-03

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 40.19  E-value: 7.13e-03
                        10
                ....*....|....*...
gi 26350549  69 VVIVGPSGAGKSTLWRML 86
Cdd:COG5265 387 VAIVGPSGAGKSTLARLL 404
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
69-86 7.64e-03

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 38.64  E-value: 7.64e-03
                        10
                ....*....|....*...
gi 26350549  69 VVIVGPSGAGKSTLWRML 86
Cdd:COG4619  29 VAITGPSGSGKSTLLRAL 46
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 69-86 7.82e-03

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 39.09  E-value: 7.82e-03
                        10
                ....*....|....*...
gi 26350549  69 VVIVGPSGAGKSTLWRML 86
Cdd:cd03256  30 VALIGPSGAGKSTLLRCL 47
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 69-86 9.85e-03

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213260 [Multi-domain]  Cd Length: 220  Bit Score: 38.61  E-value: 9.85e-03
                        10
                ....*....|....*...
gi 26350549  69 VVIVGPSGAGKSTLWRML 86
Cdd:cd03293  33 VALVGPSGCGKSTLLRII 50
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
69-97 9.93e-03

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 38.13  E-value: 9.93e-03
                        10        20
                ....*....|....*....|....*....
gi 26350549  69 VVIVGPSGAGKSTLWRMLRAALCKIGKVV 97
Cdd:COG0194   5 IVLSGPSGAGKTTLVKALLERDPDLRFSV 33
 
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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