|
Name |
Accession |
Description |
Interval |
E-value |
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
40-815 |
0e+00 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 1303.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 40 LPSDLLILPLRNTVLFPGVVIPITAGRDKSIRLIDAANAGDKIIGVVSQKNEEDEDPTENDINKVGTVAKILRVLKMPDG 119
Cdd:COG0466 10 LPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDDLYEVGTVAKILQLLKLPDG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 120 NVTVILQGKKRFEIEQVTSTEPYMKASIKEVTEErpTKKDKEFSAIIESVRDLAIQIITESPNIPTEATFAIKNIDSSSF 199
Cdd:COG0466 90 TVKVLVEGLQRARIKEFVQEEPYLEAEVEPLEEE--EEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSNIEDPGR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 200 LVNFVSSNMNLSVVEKQDLLEINNLKERALATLKYMNIEFQKLELKNDIQSKVRFDLDQQQREYFLHQQMKTIQEELGGV 279
Cdd:COG0466 168 LADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELGEK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 280 S-QEEEIEEMRAKSKTKIWDEKTQKHFDKELSKMQRSNPNSPDFGIQRNYLELFLDLPWGKYSKDNFDLKRAQKILDKDH 358
Cdd:COG0466 248 DdGEDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDH 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 359 FGLEDVKKRMIEHLAVLKLRNDMKSPILCLTGPPGVGKTSIGRSIAEALGREYVRVSLGGLRDEAEIRGHRKTYIGALPG 438
Cdd:COG0466 328 YGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 439 RILQSLKKAGTSNPVFVLDEIDKLSNSNQGDPSSALLEVLDPEQNSEFYDNFLEIGYDLSKVMFIATSNNMATIQPALKD 518
Cdd:COG0466 408 RIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLD 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 519 RMEIIKMSGYTIEEKVEIAKQHLLPKQLAIHGLTSKHLQIGKKQLEKIVEGYTRESGVRGLENKMAQVIRNAAKCVAMDE 598
Cdd:COG0466 488 RMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGK 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 599 EYNIKVSDDDIVKILGVPRLERDKSENNEVAGVVTGLAWTSVGGDILFIESLISPGKGTMTITGNLGTVMKESATIALEY 678
Cdd:COG0466 568 KKKVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESAQAALSY 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 679 IKANAQLLGLNSEMLAKYNIHLHVPEGATPKDGPSAGIAMLTSLVSVFTQKKIKKSLAMTGEITLRGKVLPVGGIKEKIL 758
Cdd:COG0466 648 VRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLL 727
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 500641748 759 AAKRANIKEIILCHENKSDIDEIKPEYLTGLTFHYVKEMNEVLAIAITKDNVKNAKT 815
Cdd:COG0466 728 AAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKEPEPLPKK 784
|
|
| lon |
TIGR00763 |
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ... |
45-804 |
0e+00 |
|
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat shock and other stresses in E. coli, B. subtilis, and other species. The yeast member, designated PIM1, is located in the mitochondrial matrix, required for mitochondrial function, and also induced by heat shock. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273258 [Multi-domain] Cd Length: 775 Bit Score: 920.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 45 LILPLRNTVLFPGVVIPITAGRDKSIRLIDAANAGD-KIIGVVSQKNEEDEDPTENDINKVGTVAKILRVLKMPD---GN 120
Cdd:TIGR00763 1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKqPYLGLFLQKDDDNEEPEEDDIYSVGVVAQILEMLPLPSsgtAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 121 VTVILQGKKRFEIEQVTSTEPYMKASIKEVTEERPTKKDKEFSAIIESVRDLAIQIITESPN--IPTEATFAIKNIDSSS 198
Cdd:TIGR00763 81 YKVVVEGLRRIRIKELSDKGGYLVVRVDNLKEEPFDKDDEEIKALTREIKETFRELISLSKLfrEQPALLSALEDIDEPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 199 FLVNFVSSNMNLSVV-EKQDLLEINNLKERALATLKYMNIEFQKLELKNDIQSKVRFDLDQQQREYFLHQQMKTIQEELG 277
Cdd:TIGR00763 161 RLADFVAASLQLKEKdELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 278 GVSQ-EEEIEEMRAKSKTKIWDEKTQKHFDKELSKMQRSNPNSPDFGIQRNYLELFLDLPWGKYSKDNFDLKRAQKILDK 356
Cdd:TIGR00763 241 IEKDdKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 357 DHFGLEDVKKRMIEHLAVLKLRNDMKSPILCLTGPPGVGKTSIGRSIAEALGREYVRVSLGGLRDEAEIRGHRKTYIGAL 436
Cdd:TIGR00763 321 DHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 437 PGRILQSLKKAGTSNPVFVLDEIDKLSNSNQGDPSSALLEVLDPEQNSEFYDNFLEIGYDLSKVMFIATSNNMATIQPAL 516
Cdd:TIGR00763 401 PGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 517 KDRMEIIKMSGYTIEEKVEIAKQHLLPKQLAIHGLTSKHLQIGKKQLEKIVEGYTRESGVRGLENKMAQVIRNAAKCVAM 596
Cdd:TIGR00763 481 LDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 597 DEE------YNIKVSDDDIVKILGVPRLERDKSENNEVAGVVTGLAWTSVGGDILFIESLISPGKGTMTITGNLGTVMKE 670
Cdd:TIGR00763 561 QGEkkkseaESVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKE 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 671 SATIALEYIKANAQLLGLNSEMLAKYNIHLHVPEGATPKDGPSAGIAMLTSLVSVFTQKKIKKSLAMTGEITLRGKVLPV 750
Cdd:TIGR00763 641 SAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPI 720
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 500641748 751 GGIKEKILAAKRANIKEIILCHENKSDIDEIKPEYLTGLTFHYVKEMNEVLAIA 804
Cdd:TIGR00763 721 GGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKA 774
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
46-805 |
0e+00 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 711.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 46 ILPLRNTVLFPGVVIPITAGRDKSIRLIDAANAGDKIIGVVSQKNEEDEDPTENDINKVGTVAKILRVLKMPDGNVTVIL 125
Cdd:PRK10787 13 VLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQMLKLPDGTVKVLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 126 QGKKRFEIEQVTSTEPYMKASIKEVteERPTKKDKEFSAIIESVRDLAIQIITESPNIPTEATFAIKNIDSSSFLVNFVS 205
Cdd:PRK10787 93 EGLQRARISALSDNGEHFSAKAEYL--ESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSIDDPARLADTIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 206 SNMNLSVVEKQDLLEINNLKERALATLKYMNIEFQKLELKNDIQSKVRFDLDQQQREYFLHQQMKTIQEELGGVSQE-EE 284
Cdd:PRK10787 171 AHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELGEMDDApDE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 285 IEEMRAKSKTKIWDEKTQKHFDKELSKMQRSNPNSPDFGIQRNYLELFLDLPWGKYSKDNFDLKRAQKILDKDHFGLEDV 364
Cdd:PRK10787 251 NEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 365 KKRMIEHLAVLKLRNDMKSPILCLTGPPGVGKTSIGRSIAEALGREYVRVSLGGLRDEAEIRGHRKTYIGALPGRILQSL 444
Cdd:PRK10787 331 KDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKM 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 445 KKAGTSNPVFVLDEIDKLSNSNQGDPSSALLEVLDPEQNSEFYDNFLEIGYDLSKVMFIATSNNMATIQPALkDRMEIIK 524
Cdd:PRK10787 411 AKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIPAPLL-DRMEVIR 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 525 MSGYTIEEKVEIAKQHLLPKQLAIHGLTSKHLQIGKKQLEKIVEGYTRESGVRGLENKMAQVIRNAAKCVAMDEEY-NIK 603
Cdd:PRK10787 490 LSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAVKQLLLDKSLkHIE 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 604 VSDDDIVKILGVPRLERDKSENNEVAGVVTGLAWTSVGGDILFIESLISPGKGTMTITGNLGTVMKESATIALEYIKANA 683
Cdd:PRK10787 570 INGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVVRARA 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 684 QLLGLNSEMLAKYNIHLHVPEGATPKDGPSAGIAMLTSLVSVFTQKKIKKSLAMTGEITLRGKVLPVGGIKEKILAAKRA 763
Cdd:PRK10787 650 EKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRG 729
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 500641748 764 NIKEIILCHENKSDIDEIKPEYLTGLTFHYVKEMNEVLAIAI 805
Cdd:PRK10787 730 GIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
347-528 |
2.09e-119 |
|
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410908 [Multi-domain] Cd Length: 182 Bit Score: 358.02 E-value: 2.09e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 347 LKRAQKILDKDHFGLEDVKKRMIEHLAVLKLRNDMKSPILCLTGPPGVGKTSIGRSIAEALGREYVRVSLGGLRDEAEIR 426
Cdd:cd19500 1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 427 GHRKTYIGALPGRILQSLKKAGTSNPVFVLDEIDKLSNSNQGDPSSALLEVLDPEQNSEFYDNFLEIGYDLSKVMFIATS 506
Cdd:cd19500 81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
|
170 180
....*....|....*....|..
gi 500641748 507 NNMATIQPALKDRMEIIKMSGY 528
Cdd:cd19500 161 NSLDTIPGPLLDRMEIIELSGY 182
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
603-807 |
3.19e-95 |
|
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops.
Pssm-ID: 428442 [Multi-domain] Cd Length: 205 Bit Score: 295.69 E-value: 3.19e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 603 KVSDDDIVKILGVPRLERDKSENNEVAGVVTGLAWTSVGGDILFIESLISPGKGTMTITGNLGTVMKESATIALEYIKAN 682
Cdd:pfam05362 1 KVTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 683 AQLLGLNSEMLAKYNIHLHVPEGATPKDGPSAGIAMLTSLVSVFTQKKIKKSLAMTGEITLRGKVLPVGGIKEKILAAKR 762
Cdd:pfam05362 81 AEELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 500641748 763 ANIKEIILCHENKSDIDEIKPEYLTGLTFHYVKEMNEVLAIAITK 807
Cdd:pfam05362 161 AGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALVG 205
|
|
| LON_substr_bdg |
pfam02190 |
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ... |
44-236 |
3.95e-47 |
|
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be part of the PUA superfamily. This domain represents a general protein and polypeptide interaction domain for the ATP-dependent serine peptidase, LON, Peptidase_S16, pfam05362. ATP-dependent Lon proteases are conserved in all living organizms and catalyze rapid turnover of short-lived regulatory proteins and many damaged or denatured proteins.
Pssm-ID: 426647 [Multi-domain] Cd Length: 195 Bit Score: 166.36 E-value: 3.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 44 LLILPLRNTVLFPGVVIPITAGRDKSIRLIDAANAGDKIIGV--VSQKNEEDEDPTENDINKVGTVAKILRVLKMPDGNV 121
Cdd:pfam02190 2 LPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKDKLYGVllVSQKDAEDEEPTPDDLYEVGTVAKIVQILKLPDGTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 122 TVILQGKKRFEIEQVTS-TEPYMKASIkEVTEERPTKKDKEFSAIIESVRDLAIQIITesPNIPTEATFAIKNIDSSSFL 200
Cdd:pfam02190 82 KVLVEGLERVRIVELVKkEEPYLRAEV-EDLPEDSDELSEALKALVKELIEKLRRLLK--LLLPLELLLKIKDIENPGRL 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 500641748 201 VNFVSSNMNLSVVEKQDLLEINNLKERALATLKYMN 236
Cdd:pfam02190 159 ADLVAAILPLSPEEKQELLETLDVKERLEKVLELLN 194
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
386-523 |
3.98e-27 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 106.91 E-value: 3.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 386 LCLTGPPGVGKTSIGRSIAEALGREYVRVSLGGLRDeaeirghrkTYIGALPGRILQSLKKAGTSNP-VFVLDEIDKLSN 464
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALAG 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500641748 465 SNQG-------DPSSALLEVLDPEQNSEfydnfleigydlSKVMFIATSNNMATIQPALKDRMEII 523
Cdd:pfam00004 72 SRGSggdsesrRVVNQLLTELDGFTSSN------------SKVIVIAATNRPDKLDPALLGRFDRI 125
|
|
| LON/PUA |
COG2802 |
Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function ... |
40-238 |
8.55e-24 |
|
Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function unknown];
Pssm-ID: 442054 [Multi-domain] Cd Length: 194 Bit Score: 99.57 E-value: 8.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 40 LPSDLLILPLrNTVLFPGVVIP--ITAGRDKsiRLIDAANAGDKIIGVVsQKNEEDEDPTENDINKVGTVAKILRVLKMP 117
Cdd:COG2802 3 LPMELPLFPL-GAVLFPGGRLPlhIFEPRYL--DMVRDCLAGDRPFGVV-LIREGREVGGPPPLYDVGTLARITDFEELE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 118 DGNVTVILQGKKRFEIEQVTSTE-PYMKASIKEVTEERPTKKDKEFSAIIESVRDLAIQIItESPNIPTEAtfaikNIDS 196
Cdd:COG2802 79 DGRLDITLRGVQRFRILEELQEDdPYRVAEVEWLPDEPDLPVPEELEALRERLLRLLRRYP-ELAGLEADP-----DLDD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 500641748 197 SSFLVNFVSSNMNLSVVEKQDLLEINNLKERALATLKYMNIE 238
Cdd:COG2802 153 PEWLSNRLAELLPLDPEEKQALLEAPDLLERLELLLALLERE 194
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
360-613 |
2.14e-19 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 91.13 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 360 GLEDVKKRMIEHLAVL----KLRNDMKSPI---LCLTGPPGVGKTSIGRSIAEALGREYVRVSLGGLRDEaeirghrktY 432
Cdd:COG0464 161 GLEEVKEELRELVALPlkrpELREEYGLPPprgLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK---------Y 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 433 IGALPGRILQSLKKA-GTSNPVFVLDEIDKLSNSNQGDPSSALLEVLdpeqnsefyDNFL-EIGYDLSKVMFIATSNNMA 510
Cdd:COG0464 232 VGETEKNLREVFDKArGLAPCVLFIDEADALAGKRGEVGDGVGRRVV---------NTLLtEMEELRSDVVVIAATNRPD 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 511 TIQPALKDRM-EIIKMSGYTIEEKVEIAKQHLLPKQLAihglTSKHLQigkkQLEKIVEGYT-REsgvrglenkMAQVIR 588
Cdd:COG0464 303 LLDPALLRRFdEIIFFPLPDAEERLEIFRIHLRKRPLD----EDVDLE----ELAEATEGLSgAD---------IRNVVR 365
|
250 260
....*....|....*....|....*
gi 500641748 589 NAAKCVAMDEEynIKVSDDDIVKIL 613
Cdd:COG0464 366 RAALQALRLGR--EPVTTEDLLEAL 388
|
|
| COG1750 |
COG1750 |
Predicted archaeal serine protease, S18 family [General function prediction only]; |
649-801 |
1.04e-18 |
|
Predicted archaeal serine protease, S18 family [General function prediction only];
Pssm-ID: 441356 [Multi-domain] Cd Length: 213 Bit Score: 85.42 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 649 SLISPGKGTMTITGN--LGTVMKESATIALEYikaNAQLLGLNsemLAKYNIHLHVPEGATPKDGPSAGIAMLTSLVSVF 726
Cdd:COG1750 51 TVTYPGSGRVYVSTSplTGPDTQASARIAALV---ASLLAGVD---LSSYDVYISIESDSPIVGGPSAGGAMTVATYAAL 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500641748 727 TQKKIKKSLAMTGEITLRGKVLPVGGIKEKILAAKRANIKEIILCHENKSDIDEIKPEYLTGLTFHYVKEMNEVL 801
Cdd:COG1750 125 LGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPKGQAILTGYNTQVGETVDLVEYGKELGVKV 199
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
361-519 |
9.90e-17 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 78.09 E-value: 9.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 361 LEDVKKRMIEHLAVLKLR--NDMKSPILCLTGPPGVGKTSIGRSIAEALGREYVRVSLGGLRDEAeirghrKTYIGALPG 438
Cdd:cd19481 2 KASLREAVEAPRRGSRLRryGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 439 RILQSLKKagTSNPVFVLDEIDKL-----SNSNQGDPS---SALLEVLDPEQNsefydnfleigydLSKVMFIATSNNMA 510
Cdd:cd19481 76 KIFERARR--LAPCILFIDEIDAIgrkrdSSGESGELRrvlNQLLTELDGVNS-------------RSKVLVIAATNRPD 140
|
....*....
gi 500641748 511 TIQPALKDR 519
Cdd:cd19481 141 LLDPALLRP 149
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
386-520 |
7.15e-14 |
|
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: 69.24 E-value: 7.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 386 LCLTGPPGVGKTSIGRSIAEAL-GREYVRVSLGglRD--EAEIRGHRKtYIGALPGRILQSLKKAGTSNPVFVLDEIDKL 462
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALsNRPVFYVQLT--RDttEEDLFGRRN-IDPGGASWVDGPLVRAAREGEIAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500641748 463 SNSNQGdpssALLEVLDpeqNSEFY--DNFLEIGYDLSKVMFIATSNN----MATIQPALKDRM 520
Cdd:pfam07728 79 NPDVLN----SLLSLLD---ERRLLlpDGGELVKAAPDGFRLIATMNPldrgLNELSPALRSRF 135
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
367-523 |
3.54e-13 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 67.56 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 367 RMIEHLAVLKLRNDMKSPILCLTGPPGVGKTSIGRSIAEAL---GREYVRVSLGGLRDEAEIRGHRKTYIgalpgRILQS 443
Cdd:cd00009 3 QEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGHFL-----VRLLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 444 LKKAGTSNPVFVLDEIDKLSNSNQgdpsSALLEVLDPEqnsefydNFLEIGYDLSKVMFIATSNNMATIQPALKDRMEII 523
Cdd:cd00009 78 ELAEKAKPGVLFIDEIDSLSRGAQ----NALLRVLETL-------NDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIR 146
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
365-615 |
8.44e-08 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 54.40 E-value: 8.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 365 KKRMIEHL--AVLklrndMKSPILcLTGPPGVGKTSIGRSIAEALGREYVRVSlgglrdeaeirghrkTYIGALPGRILq 442
Cdd:COG0714 17 QEELIELVliALL-----AGGHLL-LEGVPGVGKTTLAKALARALGLPFIRIQ---------------FTPDLLPSDIL- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 443 slkkaGTSN-------------PVF---VL-DEIDKlsnsnqGDP--SSALLEVLdpeQNSEFYdnfleIG---YDLSKV 500
Cdd:COG0714 75 -----GTYIydqqtgefefrpgPLFanvLLaDEINR------APPktQSALLEAM---EERQVT-----IPggtYKLPEP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 501 MF-IATSNNMATIQ-----PALKDRMEI-IKMsGY-TIEEKVEIAKQHLLPKQLAIH-GLTSKHLQIGKKQLEKI----- 566
Cdd:COG0714 136 FLvIATQNPIEQEGtyplpEAQLDRFLLkLYI-GYpDAEEEREILRRHTGRHLAEVEpVLSPEELLALQELVRQVhvsea 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500641748 567 VEGY-------TRES-------GVRGLENkMAQVIRNAAkcvAMDEEYNikVSDDDIVKILGV 615
Cdd:COG0714 215 VLDYivdlvraTREHpdlrkgpSPRASIA-LLRAARALA---LLDGRDY--VTPDDVKAVAGP 271
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
356-613 |
2.54e-07 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 52.58 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 356 KDHFGLEDVKKR----MIEHLAVLKLRNDMKSP---ILcLTGPPGVGKTSIGRSIAEALGREYVRVSLGGLRDEaeirgh 428
Cdd:COG1223 2 DDVVGQEEAKKKlkliIKELRRRENLRKFGLWPprkIL-FYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGS------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 429 rktYIGALPGRILQSLKKAGTSNPVFVLDEIDKLSNSnQGDPS---------SALLevldpeqnsefydnfLEIGYDLSK 499
Cdd:COG1223 75 ---YLGETARNLRKLFDFARRAPCVIFFDEFDAIAKD-RGDQNdvgevkrvvNALL---------------QELDGLPSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 500 VMFIATSNNMATIQPALKDRM-EIIKMSGYTIEEKVEIAKQHLLPKQLAIhgltskhlqigKKQLEKIVEGYTRESGvRG 578
Cdd:COG1223 136 SVVIAATNHPELLDSALWRRFdEVIEFPLPDKEERKEILELNLKKFPLPF-----------ELDLKKLAKKLEGLSG-AD 203
|
250 260 270
....*....|....*....|....*....|....*.
gi 500641748 579 LEnkmaQVIRNAAK-CVAMDEEyniKVSDDDIVKIL 613
Cdd:COG1223 204 IE----KVLKTALKkAILEDRE---KVTKEDLEEAL 232
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
360-547 |
7.94e-07 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 51.93 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 360 GLEDVKKRMIEHLaVLKLRN-------DMKSP--ILcLTGPPGVGKTSIGRSIAEALGREYVRVSLGGLRDEaeirghrk 430
Cdd:COG1222 82 GLDEQIEEIREAV-ELPLKNpelfrkyGIEPPkgVL-LYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK-------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 431 tYIGAlPGRILQSL-KKAGTSNPVFV-LDEIDKLSNSNQGDPSSA--------LLEVLDpeqnsefydnfleiGYD-LSK 499
Cdd:COG1222 152 -YIGE-GARNVREVfELAREKAPSIIfIDEIDAIAARRTDDGTSGevqrtvnqLLAELD--------------GFEsRGD 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500641748 500 VMFIATSNNMATIQPALK-----DRmeIIKMSGYTIEEKVEIAKQHLLPKQLA 547
Cdd:COG1222 216 VLIIAATNRPDLLDPALLrpgrfDR--VIEVPLPDEEAREEILKIHLRDMPLA 266
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
346-523 |
9.21e-07 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 49.87 E-value: 9.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 346 DLKRAQKILDKDHFGLEDVKKRMIEHL--AVLKLRNDMKSPI-LCLTGPPGVGKTSIGRSIAEAL---GREYVRVSLGgl 419
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIrrARAGLSDPNRPIGsFLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMS-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 420 rdeAEIRGHR-KTYIGALPG--------RILQSLKKAGTSnpVFVLDEIDKlsnsnqGDPS--SALLEVLDpeqnsefyD 488
Cdd:cd19499 79 ---EYMEKHSvSRLIGAPPGyvgyteggQLTEAVRRKPYS--VVLLDEIEK------AHPDvqNLLLQVLD--------D 139
|
170 180 190
....*....|....*....|....*....|....*....
gi 500641748 489 NFLEIGY----DLSKVMFIATSNNmatIQPALKDRMEII 523
Cdd:cd19499 140 GRLTDSHgrtvDFKNTIIIMTSNH---FRPEFLNRIDEI 175
|
|
| T7SS_EccA |
TIGR03922 |
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ... |
347-538 |
2.76e-06 |
|
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the actinobacterial flavor of type VII secretion systems. Species such as Mycobacterium tuberculosis have several instances of this system per genome, designated EccA1, EccA2, etc. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 188437 [Multi-domain] Cd Length: 557 Bit Score: 51.00 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 347 LKRAQKILDKdHFGLEDVK---KRMIEHLAVLKLRNDMKSPI------LCLTGPPGVGKTsigrSIAEALGREYvrVSLG 417
Cdd:TIGR03922 268 LAEAEAELAE-QIGLERVKrqvAALKSSTAMALARAERGLPVaqtsnhMLFAGPPGTGKT----TIARVVAKIY--CGLG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 418 GLRDEAEIRGHRKTYIGALPGrilQSLKKA-----GTSNPVFVLDEIDKLSNSNQGDPSSALLEVLDP----EQNSEfyD 488
Cdd:TIGR03922 341 VLRKPLVREVSRADLIGQYIG---ESEAKTneiidSALGGVLFLDEAYTLVETGYGQKDPFGLEAIDTllarMENDR--D 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500641748 489 NFLEIGYDLSKVMfiatsNNMATIQPALKDRM-EIIKMSGYTIEEKVEIAK 538
Cdd:TIGR03922 416 RLVVIGAGYRKDL-----DKFLEVNEGLRSRFtRVIEFPSYSPDELVEIAR 461
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
381-412 |
1.15e-05 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 46.34 E-value: 1.15e-05
10 20 30
....*....|....*....|....*....|..
gi 500641748 381 MKSPILCLTGPPGVGKTSIGRSIAEALGREYV 412
Cdd:PRK00131 2 LKGPNIVLIGFMGAGKSTIGRLLAKRLGYDFI 33
|
|
| LON |
smart00464 |
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ... |
44-95 |
1.50e-05 |
|
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La (LON), present also in other bacterial ORFs.
Pssm-ID: 197740 [Multi-domain] Cd Length: 92 Bit Score: 44.35 E-value: 1.50e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 500641748 44 LLILPLRNTVLFPGVVIPITAGRDKSIRLIDAA--NAGDKIIGVVSQKNEEDED 95
Cdd:smart00464 2 LPLLPIRRRPLFPGFVLPIPVKRPKSVAAIKEAlrRSQPYVIVFLLQDDPTETP 55
|
|
| LonB |
COG1067 |
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ... |
710-757 |
1.70e-05 |
|
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440686 [Multi-domain] Cd Length: 742 Bit Score: 48.40 E-value: 1.70e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 500641748 710 DGPSAGIAMLTSLVSVFTQKKIKKSLAMTGEITLRGKVLPVGGIKEKI 757
Cdd:COG1067 592 DGDSASSAELYALLSALSGVPIRQDIAVTGSVNQHGEVQPIGGVNEKI 639
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
385-463 |
1.74e-05 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 45.03 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 385 ILCLTGPPGVGKTSIGRSIAEAL---GREYVRVSLGGLRDEAEIR-------GHRKTYIG---ALPGRILQSLKKAGTSn 451
Cdd:pfam13401 7 ILVLTGESGTGKTTLLRRLLEQLpevRDSVVFVDLPSGTSPKDLLrallralGLPLSGRLskeELLAALQQLLLALAVA- 85
|
90
....*....|..
gi 500641748 452 PVFVLDEIDKLS 463
Cdd:pfam13401 86 VVLIIDEAQHLS 97
|
|
| RecA-like_KTNA1 |
cd19522 |
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ... |
357-521 |
1.88e-05 |
|
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410930 [Multi-domain] Cd Length: 170 Bit Score: 45.75 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 357 DHFGLEDVKkRMIEHLAVLKL---------RNDMKSpiLCLTGPPGVGKTSIGRSIAEALGREYVRVSLGGLrdEAEIRG 427
Cdd:cd19522 1 DIADLEEAK-KLLEEAVVLPMwmpeffkgiRRPWKG--VLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTL--TSKYRG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 428 HRKTYIgalpgRILQSLKKAGTSNPVFVlDEIDKLSNSNQGDPS--------SALLEVLDPEQNSEFYDnfleigyDLSK 499
Cdd:cd19522 76 ESEKLV-----RLLFEMARFYAPTTIFI-DEIDSICSRRGTSEEheasrrvkSELLVQMDGVGGASEND-------DPSK 142
|
170 180
....*....|....*....|...
gi 500641748 500 -VMFIATSNNMATIQPALKDRME 521
Cdd:cd19522 143 mVMVLAATNFPWDIDEALRRRLE 165
|
|
| SdrC |
COG3480 |
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms]; |
711-766 |
2.43e-05 |
|
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
Pssm-ID: 442703 [Multi-domain] Cd Length: 344 Bit Score: 47.11 E-value: 2.43e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 500641748 711 GPSAGIaMLT-SLVSVFTQKKIKKSL--AMTGEITLRGKVLPVGGIKEKILAAKRANIK 766
Cdd:COG3480 240 GPSAGL-MFAlGIYDQLTPGDLTGGKkiAGTGTIDADGTVGPIGGIDQKVVAARRAGAT 297
|
|
| CDC6 |
COG1474 |
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair]; |
369-539 |
2.45e-05 |
|
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
Pssm-ID: 441083 [Multi-domain] Cd Length: 389 Bit Score: 47.54 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 369 IEHLA-VLK--LRNDMKSPILcLTGPPGVGKTSIGRSIAEALGRE---------YVRVS--------------LGGLRDE 422
Cdd:COG1474 35 IEELAsALRpaLRGERPSNVL-IYGPTGTGKTAVAKYVLEELEEEaeergvdvrVVYVNcrqastryrvlsriLEELGSG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 423 AEI--RGH-RKTYIGalpgRILQSLKKAGTSnPVFVLDEIDKLSNSNQGDpssaLLEVLdpeqnSEFYDNfleigYDLSK 499
Cdd:COG1474 114 EDIpsTGLsTDELFD----RLYEALDERDGV-LVVVLDEIDYLVDDEGDD----LLYQL-----LRANEE-----LEGAR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 500641748 500 VMFIATSNN---MATIQPALKDRM--EIIKMSGYTIEEKVEIAKQ 539
Cdd:COG1474 175 VGVIGISNDlefLENLDPRVKSSLgeEEIVFPPYDADELRDILED 219
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
386-412 |
5.26e-05 |
|
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440467 [Multi-domain] Cd Length: 165 Bit Score: 44.35 E-value: 5.26e-05
10 20
....*....|....*....|....*..
gi 500641748 386 LCLTGPPGVGKTSIGRSIAEALGREYV 412
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPFV 27
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
388-568 |
5.92e-05 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 46.23 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 388 LTGPPGVGKTSIGRSIAEALGREYVRVS--LGGLrdeAEIRghrktyigalpgRILQSLKKAGTS--NPVFVLDEIDKLs 463
Cdd:PRK13342 41 LWGPPGTGKTTLARIIAGATDAPFEALSavTSGV---KDLR------------EVIEEARQRRSAgrRTILFIDEIHRF- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 464 NSNQGDpssALLEvldpeqnsefydnFLEIGydlsKVMFIA--TSNNMATIQPALKDRMEIIKMSGYTIEEKVEIAKQhl 541
Cdd:PRK13342 105 NKAQQD---ALLP-------------HVEDG----TITLIGatTENPSFEVNPALLSRAQVFELKPLSEEDIEQLLKR-- 162
|
170 180
....*....|....*....|....*..
gi 500641748 542 lpkqlAIHGLTSKHLQIGKKQLEKIVE 568
Cdd:PRK13342 163 -----ALEDKERGLVELDDEALDALAR 184
|
|
| 44 |
PHA02544 |
clamp loader, small subunit; Provisional |
384-539 |
8.24e-05 |
|
clamp loader, small subunit; Provisional
Pssm-ID: 222866 [Multi-domain] Cd Length: 316 Bit Score: 45.37 E-value: 8.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 384 PILCL-TGPPGVGKTSIGRSIAEALGREYVRVSLGGLRDEAeIRGHRKTYIGALpgrilqSLKKAGTsnpVFVLDEIDKL 462
Cdd:PHA02544 43 PNMLLhSPSPGTGKTTVAKALCNEVGAEVLFVNGSDCRIDF-VRNRLTRFASTV------SLTGGGK---VIIIDEFDRL 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500641748 463 SNSNQGDPSSALLEvldpeqnsEFYDNfleigydlskVMFIATSNNMATIQPALKDRMEIIKMSGYTIEEKVEIAKQ 539
Cdd:PHA02544 113 GLADAQRHLRSFME--------AYSKN----------CSFIITANNKNGIIEPLRSRCRVIDFGVPTKEEQIEMMKQ 171
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
382-516 |
8.88e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.52 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 382 KSPILCLTGPPGVGKTSIGRSIAEALGREYVRV--------SLGGLRDEAEIRGHRKTYIGALPGRILQSLKKA-GTSNP 452
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgediLEEVLDQLLLIIVGGKKASGSGELRLRLALALArKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500641748 453 VFVLDEIDKLSNSNQGDPSSALLEVLDPEQNSEFYDnfleigydlskVMFIATSNNMATIQPAL 516
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKN-----------LTVILTTNDEKDLGPAL 133
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
390-568 |
1.41e-04 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 45.05 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 390 GPPGVGKTSIGRSIAEALGREYVRVS--LGG---LR---DEAEIR--GHRKTyigalpgrILqslkkagtsnpvFVlDEI 459
Cdd:COG2256 56 GPPGTGKTTLARLIANATDAEFVALSavTSGvkdIReviEEARERraYGRRT--------IL------------FV-DEI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 460 DKLSNSNQgDpssALLEvldpeqnsefydnFLEIGYdlskVMFIA--TSNNMATIQPALKDRMEIIKMSGYTIEEKVEIA 537
Cdd:COG2256 115 HRFNKAQQ-D---ALLP-------------HVEDGT----ITLIGatTENPSFEVNSALLSRCRVFVLKPLSEEDLEQLL 173
|
170 180 190
....*....|....*....|....*....|.
gi 500641748 538 KQHLlpkQLAIHGLTSKHLQIGKKQLEKIVE 568
Cdd:COG2256 174 ERAL---ADDERGLGGYKLELDDEALEALAR 201
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
241-478 |
1.49e-04 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 45.15 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 241 KLELKNDIQSKVRFDLDQQQREYFLHQQMKTIQEELGGVSQEEEIEEMRAKSKTKIWDEKTQKHFDKELSKMQRSN-PNS 319
Cdd:COG1401 88 LNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEALERARLLLELADLEERAALETEVLEALEAELEeLLA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 320 PDFGIQRNYLELFLDLPWGKYSKDNFDLKRAQKILdkdhfgLEDVKKRMIEHLaVLKLRNdmkSPILCLTGPPGVGKTSI 399
Cdd:COG1401 168 APEDLSADALAAELSAAEELYSEDLESEDDYLKDL------LREKFEETLEAF-LAALKT---KKNVILAGPPGTGKTYL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 400 GRSIAEALGRE----YVRVS----------LGGLRDeaeiRGHRKTYIgALPGRILQSLKKA--GTSNP-VFVLDEIdkl 462
Cdd:COG1401 238 ARRLAEALGGEdngrIEFVQfhpswsyedfLLGYRP----SLDEGKYE-PTPGIFLRFCLKAekNPDKPyVLIIDEI--- 309
|
250
....*....|....*.
gi 500641748 463 snsNQGDPSSALLEVL 478
Cdd:COG1401 310 ---NRANVEKYFGELL 322
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
388-412 |
2.26e-04 |
|
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.
Pssm-ID: 238260 [Multi-domain] Cd Length: 154 Bit Score: 42.16 E-value: 2.26e-04
10 20
....*....|....*....|....*
gi 500641748 388 LTGPPGVGKTSIGRSIAEALGREYV 412
Cdd:cd00464 4 LIGMMGAGKTTVGRLLAKALGLPFV 28
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
341-459 |
2.62e-04 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 44.58 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 341 SKDNFDLKRAQKILD----KDHFGLEDVKKRMIEHLAvlklrndMKSPILCLTGPPGVGKTSIGRSIAEALGREYVRVSL 416
Cdd:COG0507 101 ARPALDEADVEAALAalepRAGITLSDEQREAVALAL-------TTRRVSVLTGGAGTGKTTTLRALLAALEALGLRVAL 173
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 500641748 417 G--------GLRDEAEIRG---HRKTYIGALPGRILQSLKKAGTSNPVFVLDEI 459
Cdd:COG0507 174 AaptgkaakRLSESTGIEArtiHRLLGLRPDSGRFRHNRDNPLTPADLLVVDEA 227
|
|
| RecA-like_VCP_r2 |
cd19529 |
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ... |
388-516 |
3.02e-04 |
|
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410937 [Multi-domain] Cd Length: 159 Bit Score: 42.10 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 388 LTGPPGVGKTSIGRSIAEALGREYVRVslgglrdeaeiRGHR--KTYIGALPGRILQSLKKAGTSNP-VFVLDEIDKLSN 464
Cdd:cd19529 32 LYGPPGTGKTLLAKAVATESNANFISV-----------KGPEllSKWVGESEKAIREIFRKARQVAPcVIFFDEIDSIAP 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 500641748 465 SNQGDPSSALLEVLDPEQNSEFyDNFLEIGydlsKVMFIATSNNMATIQPAL 516
Cdd:cd19529 101 RRGTTGDSGVTERVVNQLLTEL-DGLEEMN----GVVVIAATNRPDIIDPAL 147
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
386-523 |
4.10e-04 |
|
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410915 [Multi-domain] Cd Length: 161 Bit Score: 41.59 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 386 LCLTGPPGVGKTSIGRSIAEALGREYVRVSLGGLRDEaeirghrktYIGALPGRILQSLKKAGTSNP-VFVLDEIDK-LS 463
Cdd:cd19507 34 LLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGG---------LVGESESRLRQMIQTAEAIAPcVLWIDEIEKgFS 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500641748 464 NSNQGDpssallevlDPEQNSEFYDNFLE-IGYDLSKVMFIATSNNMATIQPAL--KDRMEII 523
Cdd:cd19507 105 NADSKG---------DSGTSSRVLGTFLTwLQEKKKPVFVVATANNVQSLPPELlrKGRFDEI 158
|
|
| Kti12 |
COG4088 |
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ... |
381-416 |
5.06e-04 |
|
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];
Pssm-ID: 443264 [Multi-domain] Cd Length: 179 Bit Score: 41.64 E-value: 5.06e-04
10 20 30
....*....|....*....|....*....|....*..
gi 500641748 381 MKSP-ILCLTGPPGVGKTSIGRSIAEALGREYVRVSL 416
Cdd:COG4088 1 MDSPmLLILTGPPGSGKTTFAKALAQRLYAEGIAVAL 37
|
|
| RecA-like_Figl-1 |
cd19525 |
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ... |
357-473 |
7.80e-04 |
|
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410933 [Multi-domain] Cd Length: 186 Bit Score: 41.51 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 357 DHFGLEDVKKRMIEHLAVLKLRNDMKSPI------LCLTGPPGVGKTSIGRSIAEALGREYVRVSLGGLRDEAEIRGHRK 430
Cdd:cd19525 23 DIAGLEFAKKTIKEIVVWPMLRPDIFTGLrgppkgILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKM 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 500641748 431 TyigalpgRILQSLKKAGTSNPVFVlDEIDK-LSNSNQGDPSSA 473
Cdd:cd19525 103 V-------RALFSVARCKQPAVIFI-DEIDSlLSQRGEGEHESS 138
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
388-517 |
7.92e-04 |
|
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410911 [Multi-domain] Cd Length: 165 Bit Score: 41.12 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 388 LTGPPGVGKTSIGRSIAEALGREYVRVSlgglrdeaeirGHrkTYIGALPG-------RILQSLKKAGTSnpVFVLDEID 460
Cdd:cd19503 39 LHGPPGTGKTLLARAVANEAGANFLSIS-----------GP--SIVSKYLGeseknlrEIFEEARSHAPS--IIFIDEID 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500641748 461 KLS---NSNQGDPS----SALLEVLDPEQNSefydnfleigydlSKVMFIATSNNMATIQPALK 517
Cdd:cd19503 104 ALApkrEEDQREVErrvvAQLLTLMDGMSSR-------------GKVVVIAATNRPDAIDPALR 154
|
|
| RecA-like_NVL_r2-like |
cd19530 |
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
388-516 |
1.04e-03 |
|
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410938 [Multi-domain] Cd Length: 161 Bit Score: 40.55 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 388 LTGPPGVGKTSIGRSIAEALGREYVRVSLGGLRDEaeirghrktYIGALPGRILQSLKKAGTSNP-VFVLDEIDKLSNSN 466
Cdd:cd19530 35 LYGPPGCGKTLLAKAVANESGANFISVKGPELLNK---------YVGESERAVRQVFQRARASAPcVIFFDEVDALVPKR 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 500641748 467 QGDPSSALLEVLdpeqNSEFYDnfLEIGYDLSKVMFIATSNNMATIQPAL 516
Cdd:cd19530 106 GDGGSWASERVV----NQLLTE--MDGLEERSNVFVIAATNRPDIIDPAM 149
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
383-444 |
1.05e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 42.70 E-value: 1.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500641748 383 SPILCLTGPPGVGKTSIGRSIAEALGREY---VR-VSLGGLRDEAEirghrktyigaLPGRILQSL 444
Cdd:COG3903 176 ARLVTLTGPGGVGKTRLALEVAHRLADRFpdgVWfVDLAGVTDPAL-----------VLAAVARAL 230
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
382-459 |
1.27e-03 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350691 [Multi-domain] Cd Length: 155 Bit Score: 40.23 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 382 KSPILCLTGPPGVGKTSIGRSIAEALGREYVRVSL--------GGLRDEAEIRG---HRktYIGALPGRILQSLKKAG-T 449
Cdd:cd17933 11 RNRVSVLTGGAGTGKTTTLKALLAALEAEGKRVVLaaptgkaaKRLSESTGIEAstiHR--LLGINPGGGGFYYNEENpL 88
|
90
....*....|
gi 500641748 450 SNPVFVLDEI 459
Cdd:cd17933 89 DADLLIVDEA 98
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
384-421 |
1.40e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 40.18 E-value: 1.40e-03
10 20 30
....*....|....*....|....*....|....*...
gi 500641748 384 PILCLTGPPGVGKTSIGRSIAEALGREYVRVSLGGLRD 421
Cdd:pfam13191 25 PSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDE 62
|
|
| COG1373 |
COG1373 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
367-459 |
1.70e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440984 [Multi-domain] Cd Length: 405 Bit Score: 41.47 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 367 RMIEHLAVLKLRNDMKS-PILCLTGPPGVGKTSIGRSIAEALgREYVRVSLgglrDEAEIRGhrktYIGALPGRILQSLK 445
Cdd:COG1373 3 IMIKRKILDKLLKLLDNrKAVVITGPRQVGKTTLLKQLAKEL-ENILYINL----DDPRLRA----LAEEDPDDLLEALK 73
|
90
....*....|....
gi 500641748 446 KAGTSNPVFVLDEI 459
Cdd:COG1373 74 ELYPGKTYLFLDEI 87
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
390-423 |
2.33e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 39.39 E-value: 2.33e-03
10 20 30
....*....|....*....|....*....|....
gi 500641748 390 GPPGVGKTSIGRSIAEALGREYvrVSLGGLRDEA 423
Cdd:cd02020 6 GPAGSGKSTVAKLLAKKLGLPY--LDTGGIRTEE 37
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
385-524 |
3.43e-03 |
|
ATP-binding cassette transporter nucleotide-binding domain; 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: 213179 [Multi-domain] Cd Length: 157 Bit Score: 38.77 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 385 ILCLTGPPGVGKTSIGRSIAEALGREYVRVSLGGLRDEAEIRGHRKTYIGALPG-------RIlqSLKKAGTSNP-VFVL 456
Cdd:cd00267 27 IVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQlsggqrqRV--ALARALLLNPdLLLL 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500641748 457 DEidklsnsnqgdPSSAllevLDPEQNSEFYDNFLEIGydLSKVMFIATSNNMATIQPAlKDRMEIIK 524
Cdd:cd00267 105 DE-----------PTSG----LDPASRERLLELLRELA--EEGRTVIIVTHDPELAELA-ADRVIVLK 154
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
385-413 |
3.95e-03 |
|
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.
Pssm-ID: 238979 [Multi-domain] Cd Length: 150 Bit Score: 38.77 E-value: 3.95e-03
10 20
....*....|....*....|....*....
gi 500641748 385 ILCLTGPPGVGKTSIGRSIAEALGREYVR 413
Cdd:cd02021 1 IIVVMGVSGSGKSTVGKALAERLGAPFID 29
|
|
| Sigma54_activat |
pfam00158 |
Sigma-54 interaction domain; |
366-487 |
4.32e-03 |
|
Sigma-54 interaction domain;
Pssm-ID: 425491 [Multi-domain] Cd Length: 168 Bit Score: 38.92 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 366 KRMIEHLAvlklrnDMKSPILcLTGPPGVGKTSIGRSIAEALGRE---YVRVSLGGLRD---EAEIRGHRK-TYIGALPG 438
Cdd:pfam00158 12 LEQAKRVA------PTDAPVL-ITGESGTGKELFARAIHQLSPRAdgpFVAVNCAAIPEellESELFGHEKgAFTGADSD 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 500641748 439 RI-LqsLKKA--GTsnpVFvLDEIDKLSNSNQgdpsSALLEVLdpeQNSEFY 487
Cdd:pfam00158 85 RKgL--FELAdgGT---LF-LDEIGELPLELQ----AKLLRVL---QEGEFE 123
|
|
| AAA_14 |
pfam13173 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
382-532 |
4.40e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 463799 [Multi-domain] Cd Length: 128 Bit Score: 37.95 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 382 KSPILCLTGPPGVGKTSIGRSIAEAL--GREYVRVSLgglrDEAEIRGHRKTyigALPGRILQSLKKAGTsnpVFVLDEI 459
Cdd:pfam13173 1 SRKILVITGPRQVGKTTLLLQLIKELlpPENILYINL----DDPRLLKLADF---ELLELFLELLYPGKT---YLFLDEI 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500641748 460 DKLSNsnqgdpssaLLEVLDpeqnsEFYDNFLEIgydlskvMFIAT-SNN---MATIQPALKDRMEIIKMSGYTIEE 532
Cdd:pfam13173 71 QRVPD---------WELALK-----RLYDDGPNG-------RVILTgSSAlllSKEIAESLAGRVVVIELYPLSFRE 126
|
|
| ruvB |
TIGR00635 |
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ... |
356-463 |
4.44e-03 |
|
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129721 [Multi-domain] Cd Length: 305 Bit Score: 39.98 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 356 KDHFGLEDVKKRMIEHLAVLKLRNDMKSPILcLTGPPGVGKTSIGRSIAEALGREYVRVSLGGLRDEAEIRGhrktyiga 435
Cdd:TIGR00635 4 AEFIGQEKVKEQLQLFIEAAKMRQEALDHLL-LYGPPGLGKTTLAHIIANEMGVNLKITSGPALEKPGDLAA-------- 74
|
90 100
....*....|....*....|....*...
gi 500641748 436 lpgrILQSLKKAGtsnpVFVLDEIDKLS 463
Cdd:TIGR00635 75 ----ILTNLEEGD----VLFIDEIHRLS 94
|
|
| DnaC |
COG1484 |
DNA replication protein DnaC [Replication, recombination and repair]; |
349-479 |
4.50e-03 |
|
DNA replication protein DnaC [Replication, recombination and repair];
Pssm-ID: 441093 [Multi-domain] Cd Length: 242 Bit Score: 39.76 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 349 RAQKILDK-DHFGLEDVKKRMIEHLAVL----KLRNdmkspiLCLTGPPGVGKTsigrSIAEALGREYVRvslgglrdea 423
Cdd:COG1484 66 PAAKTLEDfDFDAQPGLDRRQILELATLdfieRGEN------LILLGPPGTGKT----HLAIALGHEACR---------- 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500641748 424 eiRGHRKTYI---------------GALpGRILQSLKKAgtsnPVFVLDEIDKLSNSNQGdpSSALLEVLD 479
Cdd:COG1484 126 --AGYRVRFTtapdlvnelkearadGRL-ERLLKRLAKV----DLLILDELGYLPLDAEG--AELLFELIS 187
|
|
| aroL |
PRK03731 |
shikimate kinase AroL; |
381-412 |
5.44e-03 |
|
shikimate kinase AroL;
Pssm-ID: 235153 [Multi-domain] Cd Length: 171 Bit Score: 38.38 E-value: 5.44e-03
10 20 30
....*....|....*....|....*....|..
gi 500641748 381 MKSPILcLTGPPGVGKTSIGRSIAEALGREYV 412
Cdd:PRK03731 1 MTQPLF-LVGARGCGKTTVGMALAQALGYRFV 31
|
|
| Fap7 |
COG1936 |
Broad-specificity NMP kinase [Nucleotide transport and metabolism]; |
385-415 |
5.85e-03 |
|
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
Pssm-ID: 441539 [Multi-domain] Cd Length: 173 Bit Score: 38.64 E-value: 5.85e-03
10 20 30
....*....|....*....|....*....|.
gi 500641748 385 ILCLTGPPGVGKTSIGRSIAEALGREYVRVS 415
Cdd:COG1936 2 RIAITGTPGTGKTTVAKLLAERLGLEVIHLN 32
|
|
| THEP1 |
COG1618 |
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism]; |
388-462 |
8.57e-03 |
|
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];
Pssm-ID: 441225 [Multi-domain] Cd Length: 175 Bit Score: 37.96 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 388 LTGPPGVGKTSIGRSIAEALGREYVRVslGGLRDEAEIRGHRKT-------------------------------YIGAL 436
Cdd:COG1618 5 ITGRPGVGKTTLLLKVVEELRDEGLRV--GGFITPEVREGGRRVgfklvdlatgeeailasvdidsgprvgkygvDPEAL 82
|
90 100
....*....|....*....|....*.
gi 500641748 437 PGRILQSLKKAGTSNPVFVLDEIDKL 462
Cdd:COG1618 83 EAIAVEALERALEEADLIVIDEIGKM 108
|
|
| NTPase_1 |
pfam03266 |
NTPase; This domain is found across all species from bacteria to human, and the function was ... |
388-481 |
8.66e-03 |
|
NTPase; This domain is found across all species from bacteria to human, and the function was determined first in a hyperthermophilic bacterium to be an NTPase. The structure of one member-sequence represents a variation of the RecA fold, and implies that the function might be that of a DNA/RNA modifying enzyme. The sequence carries both a Walker A and Walker B motif which together are characteriztic of ATPases or GTPases. The protein exhibits an increased expression profile in human liver cholangiocarcinoma when compared to normal tissue.
Pssm-ID: 460869 Cd Length: 168 Bit Score: 37.99 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 388 LTGPPGVGKTSIGRSIAEALGREYVRVslGGLRDEaEIR--GHR------------------------------KTYIGA 435
Cdd:pfam03266 4 ITGPPGVGKTTLVLKVAELLKSSGVKV--GGFYTP-EVRegGRRigfkivdlasgeegwlarvgavsgprvgkyVVNVES 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 500641748 436 LPGRILQSLKKAGTSNPVFVLDEIDKLSNSNQGdPSSALLEVLDPE 481
Cdd:pfam03266 81 FEEIAVPALRRALEEADLIIIDEIGPMELKSKK-FREAVREVLDSG 125
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
388-613 |
9.07e-03 |
|
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.
Pssm-ID: 273521 [Multi-domain] Cd Length: 733 Bit Score: 39.51 E-value: 9.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 388 LTGPPGVGKTSIGRSIAEALGREYVRVslgglrdeaeiRGHR--KTYIGALPGRILQSLKKAGTSNPVFV-LDEIDKLSN 464
Cdd:TIGR01243 492 LFGPPGTGKTLLAKAVATESGANFIAV-----------RGPEilSKWVGESEKAIREIFRKARQAAPAIIfFDEIDAIAP 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 465 SNQGDPSSALLEVLDPEQNSEFyDNFLEigydLSKVMFIATSNNMATIQPALK-----DRmeIIKMSGYTIEEKVEIAKQ 539
Cdd:TIGR01243 561 ARGARFDTSVTDRIVNQLLTEM-DGIQE----LSNVVVIAATNRPDILDPALLrpgrfDR--LILVPPPDEEARKEIFKI 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641748 540 HLLPKQLAihgltskhLQIGKKQLEKIVEGYT--------RESGVRGLENKMAQVIRNAAKCVAMDEEYNIKVSDDDIVK 611
Cdd:TIGR01243 634 HTRSMPLA--------EDVDLEELAEMTEGYTgadieavcREAAMAALRESIGSPAKEKLEVGEEEFLKDLKVEMRHFLE 705
|
..
gi 500641748 612 IL 613
Cdd:TIGR01243 706 AL 707
|
|
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