|
Name |
Accession |
Description |
Interval |
E-value |
| vWA_midasin |
cd01460 |
VWA_Midasin: Midasin is a member of the AAA ATPase family. The proteins of this family are ... |
5319-5589 |
7.19e-147 |
|
VWA_Midasin: Midasin is a member of the AAA ATPase family. The proteins of this family are unified by their common archetectural organization that is based upon a conserved ATPase domain. The AAA domain of midasin contains six tandem AAA protomers. The AAA domains in midasin is followed by a D/E rich domain that is following by a VWA domain. The members of this subgroup have a conserved MIDAS motif. The function of this domain is not exactly known although it has been speculated to play a crucial role in midasin function.
:
Pssm-ID: 238737 Cd Length: 266 Bit Score: 458.35 E-value: 7.19e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5319 LSQQLCEQLRLILEPTQAAKLKGDYRTGKRLNMRKVIPYIASQFRKDKIWLRRTKPSKRQYQICLAIDDSSSMVDNHTKQ 5398
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5399 LAFESLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEQFSDYSGSQILRLCKFQQKKTKIAQFLESVANMFAAAQQlsQ 5478
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDART--Q 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5479 NVSPEIAQLLLVVSDGRGLFLEGKDRVLaaVQAARNANIFVIFVVLDNPSSRDSILDIKVPIFKGPGeMPEIRSYMEEFP 5558
Cdd:cd01460 159 SSSGSLWQLLLIISDGRGEFSEGAQKVR--LREAREQNVFVVFIIIDNPDNKQSILDIKVVSFKNDK-SGVITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|.
gi 1131296855 5559 FPFYIILRDVNALPETLSDALRQWFELVTAS 5589
Cdd:cd01460 236 FPYYVIVRDLNQLPSVLSDALRQWFELVNSS 266
|
|
| AAA_lid_5 |
pfam17865 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
915-1017 |
2.41e-40 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
:
Pssm-ID: 407722 Cd Length: 104 Bit Score: 146.19 E-value: 2.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 915 DLQILIVDYLKGLSVNKNTVQGIITFYTAVRKESGTKLVDGTGHRPHYSLRTLCRALRFAASN-PCGNIQRSLYEGFCLG 993
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLVRDIVKFYLEAKKLAEKSLVDGAGQRPHYSLRTLCRALSYARAIaPRYGLRRALYEGFCMS 80
|
90 100
....*....|....*....|....
gi 1131296855 994 FLTQLDRASHPVVQKLICQHIVSG 1017
Cdd:pfam17865 81 FLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1385-1540 |
3.76e-29 |
|
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: 115.47 E-value: 3.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1385 PVLLVGDTGCGKTTICQVFA-ALANQKLYSVNCHLHMETSDFLGGLrpvrqkpndkeEIDTsRLFEWHDGPLVLAMKEDG 1463
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAaALSNRPVFYVQLTRDTTEEDLFGRR-----------NIDP-GGASWVDGPLVRAAREGE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131296855 1464 FFLLDEISLADDSVLERLNSVLEvEKTLLLAEKGNLEDKDNevelltagKKFRILATMNPgGDFGKKELSPALRNRF 1540
Cdd:pfam07728 69 IAVLDEINRANPDVLNSLLSLLD-ERRLLLPDGGELVKAAP--------DGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1900-1999 |
1.26e-24 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
:
Pssm-ID: 465540 Cd Length: 106 Bit Score: 101.22 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1900 DMEFIASTLFPaIDKNIVKKMVAFNNQIDHEVTVEKKWGQIGGPWEFNLRDLFRWCQLM-----LVDQSPGCYDPGQHVF 1974
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLssllpTLLSPTVREEIFLEAV 79
|
90 100
....*....|....*....|....*
gi 1131296855 1975 LVYGERMRTKEDKEKVIAVFKDVFN 1999
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVLG 104
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
1079-1215 |
5.81e-23 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.
The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 97.75 E-value: 5.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1079 PVLIQGETSVGKTSLIRWLAAATGNHCVR-INNHEHTDIQEYIGCYTSDSSGKlVFKEGVLIDAMRKGYWIILDELNLAP 1157
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFyVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1131296855 1158 TDVLEALNRLLDDNRELLITETQEVVKAHPRFMLFATQNPPglYGGRKVLSRAFRNRF 1215
Cdd:pfam07728 80 PDVLNSLLSLLDERRLLLPDGGELVKAAPDGFRLIATMNPL--DRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1227-1328 |
8.22e-22 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
:
Pssm-ID: 465540 Cd Length: 106 Bit Score: 93.52 E-value: 8.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1227 ELETILHKRCSLPPSYCSKLVKVMLDLQSYRRGSSVFA--GKQGFITLRDLFRWAERYRLAEQTEKEYDWLQHLANDGFM 1304
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGssGSPREFNLRDLLRWCRRLSSLLPTLLSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....
gi 1131296855 1305 LLAGRVRKQEEVVVIQEVLEKHFK 1328
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLG 104
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
325-453 |
6.03e-21 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.
The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 91.97 E-value: 6.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 325 VLLEGPIGCGKTSLVEHLAAMTGRRKpsqLLKVQLGDQTDSKMLLGMYRCTdvPGEFVWQPGTLTQAATKGHWILLEDID 404
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRP---VFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1131296855 405 YAPLDVVSVLIPLLENGELLIPGRGDCVKVAP-GFQFFATRRLLSCGGNW 453
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIATMNPLDRGLNE 126
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
480-604 |
1.30e-18 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
:
Pssm-ID: 465540 Cd Length: 106 Bit Score: 84.28 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 480 ELNEVLQNRYPSLSAATDHLLDIYFQLIGEKHHCLSESSVGGeqapgevpearqenkrlsleGRELSLRDLLNWCNRIAH 559
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGS--------------------PREFNLRDLLRWCRRLSS 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1131296855 560 SFDSLSSSASL-NIFQEALDCFTAMLSKQTSKLKMAEVIGSKLNIS 604
Cdd:pfam17867 61 LLPTLLSPTVReEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
1748-1888 |
1.71e-16 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.
The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 79.26 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1748 PILLEGSPGVGKTSLVGALARA-SGNTLVRINLSEQTDITDLFGADLPveggKGGEFAWRDGPLLAALKAGHWVVLDELN 1826
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNI----DPGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131296855 1827 LASQSVLEGLNACFDHRgEIYVPELGMSFQVQHEKTKIFGCQNPfrQGGGRKGLPRSFLNRF 1888
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDGFRLIATMNP--LDRGLNELSPALRSRF 135
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4678-5260 |
5.19e-15 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
:
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 82.76 E-value: 5.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4678 DVSDQIENEEQAEDTFQKGQEKDKEDPDSKSDIKGEDNAIEMSEDFDGKMHDGELEEQEEDDEKSDSETGDLDKQMGDLN 4757
Cdd:COG5271 244 ADETLLADDDDTESAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELTAAQAADPESDDDADDSTLAALEGAAEDTE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4758 GEEADKLDERLWGDDDDEEDEEEDSKTEETGPGMDEEDSELVAKDDNLDAGKSNRE-KTRQDKKEEKEEAEADDDGRGQD 4836
Cdd:COG5271 324 IATADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGAdTDAAADEADAAADDSADDEEASA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4837 KINEQID-EREYDENEVDPyhGNEEKLPEPEALDLPDDLNLDSEDKDGDGDTDHEDGEEENPLEIKEQPKDTEEAghe*e 4915
Cdd:COG5271 404 DGGTSPTsDTDEEEEEADE--DASAGETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDA----- 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4916 DINEETEADQDEGQAQPQPEGGHSEDDKGEEGEEEMDTGADDG-DQDAAEHPE*DTEEAplsSEDkDKDTSEESPEKDtp 4994
Cdd:COG5271 477 DGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSADDGaDTDAAADPEDSDEDA---LED-ETEGEENAPGSD-- 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4995 LDQGLQPQTQEKEEGESSDMEEpvPEPTERKEHESCGQTGLESVQSEQAVELAGAAPEKEQGREEH----GSGAADANQA 5070
Cdd:COG5271 551 QDADETDEPEATAEEDEPDEAE--AETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEadadADGAADEEET 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5071 EGHESSFMARMASQ---KHTRKNTQSFKRKPGQADNERSLG-DHSErvhkrlrTMDTESRAEQDpAQPQAQAEDAEAFEH 5146
Cdd:COG5271 629 EEEAAEDEAAEPETdasEAADEDADAETEAEASADESEEEAeDESE-------TSSEDAEEDAD-AAAAEASDDEEETEE 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5147 IKQgsepyDAQTYDVASTEQQQSAK--DSSKAHEEEEVEDTSVDPEEQEELRAVDTEPLKPEEVKSGSTAQPGSEEmEME 5224
Cdd:COG5271 701 ADE-----DAETASEEADAEEADTEadGTAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDADGLEE-ALE 774
|
570 580 590
....*....|....*....|....*....|....*.
gi 1131296855 5225 TQTVKTEEDQhprTDPSHEETENEKpERSRDSTIHT 5260
Cdd:COG5271 775 EEKADAEEAA---TDEEAEAAAEEK-EKVADEDQDT 806
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
672-902 |
2.12e-09 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.
The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 58.84 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 672 PVLLVGETGTGKTSTVQYLAH-ITGHRLRVVNMNQQSDTADLLGGYKPvdhkliwlplreafeelfvqtfskkqnftflg 750
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRNI-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 751 hiqtcyrqkrwqdllklmqhvhksavnkagaesepgsllkekweafglrlnhaqqqmkmteNALLFAFVEGTLAQAVKRG 830
Cdd:pfam07728 49 -------------------------------------------------------------DPGGASWVDGPLVRAAREG 67
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131296855 831 EWILLDEINLAAPETLECLSGLLEGSSgslVLLDRGDTEPLVRHPDFRLFACMNPAtDVGKRNLPPGIRNRF 902
Cdd:pfam07728 68 EIAVLDEINRANPDVLNSLLSLLDERR---LLLPDGGELVKAAPDGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
2218-2306 |
3.81e-08 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.
The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 55.38 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 2218 SRGTFEWVDSMLVQALKSGDWLLMDNVNFCNPSVLDRLNALLEPGgvltvsERGMIDGSTPTVTPHPNFRLFLSMDPVHG 2297
Cdd:pfam07728 49 DPGGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDER------RLLLPDGGELVKAAPDGFRLIATMNPLDR 122
|
90
....*....|..
gi 1131296855 2298 ---EISRAMRNR 2306
Cdd:pfam07728 123 glnELSPALRSR 134
|
|
| McrB super family |
cl34253 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1660-1828 |
1.85e-05 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
The actual alignment was detected with superfamily member COG1401:
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 50.92 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1660 ARRECLKFLIKKLSKIGRLTESQKNELKIYDRLKDKEFTGIDNLWGIHPFFIPRGPVLHRNNIADYALSAGTTAMNAQRL 1739
Cdd:COG1401 135 ARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKFEETLEAF 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1740 LRATKLNKPILLEGSPGVGKTSLVGALARA-SGNTLVRINLseqtdIT---DLFGADLpVEG----GKGGEFAWRDGPLL 1811
Cdd:COG1401 215 LAALKTKKNVILAGPPGTGKTYLARRLAEAlGGEDNGRIEF-----VQfhpSWSYEDF-LLGyrpsLDEGKYEPTPGIFL 288
|
170 180
....*....|....*....|....
gi 1131296855 1812 -AALKAG------HWVVLDELNLA 1828
Cdd:COG1401 289 rFCLKAEknpdkpYVLIIDEINRA 312
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
659-780 |
7.29e-03 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.
The actual alignment was detected with superfamily member cd00009:
Pssm-ID: 476819 [Multi-domain] Cd Length: 151 Bit Score: 40.59 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 659 LIEQL--AVCVSKGEPVLLVGETGTGKTSTVQYLAHITGHR-LRVVNMNqqsdTADLLGGYkpVDHKLIWLPLREAFEEL 735
Cdd:cd00009 6 AIEALreALELPPPKNLLLYGPPGTGKTTLARAIANELFRPgAPFLYLN----ASDLLEGL--VVAELFGHFLVRLLFEL 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1131296855 736 fvqtFSKKQNFT-FLGHIQTCYRQKRWQdLLKLMQHVHKSAVNKAG 780
Cdd:cd00009 80 ----AEKAKPGVlFIDEIDSLSRGAQNA-LLRVLETLNDLRIDREN 120
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| vWA_midasin |
cd01460 |
VWA_Midasin: Midasin is a member of the AAA ATPase family. The proteins of this family are ... |
5319-5589 |
7.19e-147 |
|
VWA_Midasin: Midasin is a member of the AAA ATPase family. The proteins of this family are unified by their common archetectural organization that is based upon a conserved ATPase domain. The AAA domain of midasin contains six tandem AAA protomers. The AAA domains in midasin is followed by a D/E rich domain that is following by a VWA domain. The members of this subgroup have a conserved MIDAS motif. The function of this domain is not exactly known although it has been speculated to play a crucial role in midasin function.
Pssm-ID: 238737 Cd Length: 266 Bit Score: 458.35 E-value: 7.19e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5319 LSQQLCEQLRLILEPTQAAKLKGDYRTGKRLNMRKVIPYIASQFRKDKIWLRRTKPSKRQYQICLAIDDSSSMVDNHTKQ 5398
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5399 LAFESLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEQFSDYSGSQILRLCKFQQKKTKIAQFLESVANMFAAAQQlsQ 5478
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDART--Q 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5479 NVSPEIAQLLLVVSDGRGLFLEGKDRVLaaVQAARNANIFVIFVVLDNPSSRDSILDIKVPIFKGPGeMPEIRSYMEEFP 5558
Cdd:cd01460 159 SSSGSLWQLLLIISDGRGEFSEGAQKVR--LREAREQNVFVVFIIIDNPDNKQSILDIKVVSFKNDK-SGVITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|.
gi 1131296855 5559 FPFYIILRDVNALPETLSDALRQWFELVTAS 5589
Cdd:cd01460 236 FPYYVIVRDLNQLPSVLSDALRQWFELVNSS 266
|
|
| AAA_lid_5 |
pfam17865 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
915-1017 |
2.41e-40 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 407722 Cd Length: 104 Bit Score: 146.19 E-value: 2.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 915 DLQILIVDYLKGLSVNKNTVQGIITFYTAVRKESGTKLVDGTGHRPHYSLRTLCRALRFAASN-PCGNIQRSLYEGFCLG 993
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLVRDIVKFYLEAKKLAEKSLVDGAGQRPHYSLRTLCRALSYARAIaPRYGLRRALYEGFCMS 80
|
90 100
....*....|....*....|....
gi 1131296855 994 FLTQLDRASHPVVQKLICQHIVSG 1017
Cdd:pfam17865 81 FLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1385-1540 |
3.76e-29 |
|
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: 115.47 E-value: 3.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1385 PVLLVGDTGCGKTTICQVFA-ALANQKLYSVNCHLHMETSDFLGGLrpvrqkpndkeEIDTsRLFEWHDGPLVLAMKEDG 1463
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAaALSNRPVFYVQLTRDTTEEDLFGRR-----------NIDP-GGASWVDGPLVRAAREGE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131296855 1464 FFLLDEISLADDSVLERLNSVLEvEKTLLLAEKGNLEDKDNevelltagKKFRILATMNPgGDFGKKELSPALRNRF 1540
Cdd:pfam07728 69 IAVLDEINRANPDVLNSLLSLLD-ERRLLLPDGGELVKAAP--------DGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1900-1999 |
1.26e-24 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 101.22 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1900 DMEFIASTLFPaIDKNIVKKMVAFNNQIDHEVTVEKKWGQIGGPWEFNLRDLFRWCQLM-----LVDQSPGCYDPGQHVF 1974
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLssllpTLLSPTVREEIFLEAV 79
|
90 100
....*....|....*....|....*
gi 1131296855 1975 LVYGERMRTKEDKEKVIAVFKDVFN 1999
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVLG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1079-1215 |
5.81e-23 |
|
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: 97.75 E-value: 5.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1079 PVLIQGETSVGKTSLIRWLAAATGNHCVR-INNHEHTDIQEYIGCYTSDSSGKlVFKEGVLIDAMRKGYWIILDELNLAP 1157
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFyVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1131296855 1158 TDVLEALNRLLDDNRELLITETQEVVKAHPRFMLFATQNPPglYGGRKVLSRAFRNRF 1215
Cdd:pfam07728 80 PDVLNSLLSLLDERRLLLPDGGELVKAAPDGFRLIATMNPL--DRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1227-1328 |
8.22e-22 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 93.52 E-value: 8.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1227 ELETILHKRCSLPPSYCSKLVKVMLDLQSYRRGSSVFA--GKQGFITLRDLFRWAERYRLAEQTEKEYDWLQHLANDGFM 1304
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGssGSPREFNLRDLLRWCRRLSSLLPTLLSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....
gi 1131296855 1305 LLAGRVRKQEEVVVIQEVLEKHFK 1328
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
325-453 |
6.03e-21 |
|
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: 91.97 E-value: 6.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 325 VLLEGPIGCGKTSLVEHLAAMTGRRKpsqLLKVQLGDQTDSKMLLGMYRCTdvPGEFVWQPGTLTQAATKGHWILLEDID 404
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRP---VFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1131296855 405 YAPLDVVSVLIPLLENGELLIPGRGDCVKVAP-GFQFFATRRLLSCGGNW 453
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIATMNPLDRGLNE 126
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
480-604 |
1.30e-18 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 84.28 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 480 ELNEVLQNRYPSLSAATDHLLDIYFQLIGEKHHCLSESSVGGeqapgevpearqenkrlsleGRELSLRDLLNWCNRIAH 559
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGS--------------------PREFNLRDLLRWCRRLSS 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1131296855 560 SFDSLSSSASL-NIFQEALDCFTAMLSKQTSKLKMAEVIGSKLNIS 604
Cdd:pfam17867 61 LLPTLLSPTVReEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1748-1888 |
1.71e-16 |
|
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: 79.26 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1748 PILLEGSPGVGKTSLVGALARA-SGNTLVRINLSEQTDITDLFGADLPveggKGGEFAWRDGPLLAALKAGHWVVLDELN 1826
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNI----DPGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131296855 1827 LASQSVLEGLNACFDHRgEIYVPELGMSFQVQHEKTKIFGCQNPfrQGGGRKGLPRSFLNRF 1888
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDGFRLIATMNP--LDRGLNELSPALRSRF 135
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4678-5260 |
5.19e-15 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 82.76 E-value: 5.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4678 DVSDQIENEEQAEDTFQKGQEKDKEDPDSKSDIKGEDNAIEMSEDFDGKMHDGELEEQEEDDEKSDSETGDLDKQMGDLN 4757
Cdd:COG5271 244 ADETLLADDDDTESAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELTAAQAADPESDDDADDSTLAALEGAAEDTE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4758 GEEADKLDERLWGDDDDEEDEEEDSKTEETGPGMDEEDSELVAKDDNLDAGKSNRE-KTRQDKKEEKEEAEADDDGRGQD 4836
Cdd:COG5271 324 IATADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGAdTDAAADEADAAADDSADDEEASA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4837 KINEQID-EREYDENEVDPyhGNEEKLPEPEALDLPDDLNLDSEDKDGDGDTDHEDGEEENPLEIKEQPKDTEEAghe*e 4915
Cdd:COG5271 404 DGGTSPTsDTDEEEEEADE--DASAGETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDA----- 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4916 DINEETEADQDEGQAQPQPEGGHSEDDKGEEGEEEMDTGADDG-DQDAAEHPE*DTEEAplsSEDkDKDTSEESPEKDtp 4994
Cdd:COG5271 477 DGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSADDGaDTDAAADPEDSDEDA---LED-ETEGEENAPGSD-- 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4995 LDQGLQPQTQEKEEGESSDMEEpvPEPTERKEHESCGQTGLESVQSEQAVELAGAAPEKEQGREEH----GSGAADANQA 5070
Cdd:COG5271 551 QDADETDEPEATAEEDEPDEAE--AETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEadadADGAADEEET 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5071 EGHESSFMARMASQ---KHTRKNTQSFKRKPGQADNERSLG-DHSErvhkrlrTMDTESRAEQDpAQPQAQAEDAEAFEH 5146
Cdd:COG5271 629 EEEAAEDEAAEPETdasEAADEDADAETEAEASADESEEEAeDESE-------TSSEDAEEDAD-AAAAEASDDEEETEE 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5147 IKQgsepyDAQTYDVASTEQQQSAK--DSSKAHEEEEVEDTSVDPEEQEELRAVDTEPLKPEEVKSGSTAQPGSEEmEME 5224
Cdd:COG5271 701 ADE-----DAETASEEADAEEADTEadGTAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDADGLEE-ALE 774
|
570 580 590
....*....|....*....|....*....|....*.
gi 1131296855 5225 TQTVKTEEDQhprTDPSHEETENEKpERSRDSTIHT 5260
Cdd:COG5271 775 EEKADAEEAA---TDEEAEAAAEEK-EKVADEDQDT 806
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1736-1888 |
1.56e-10 |
|
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: 65.57 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1736 AQRLLRATKLNKPILLEGSPGVGKTSLVGALARASGNTLVRINLSEQTDITDLFGADLPVEggKGGEFAWRDGPLLAAlk 1815
Cdd:COG0714 21 IELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQ--QTGEFEFRPGPLFAN-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1816 aghwVVL-DELNLAS---QS----VLEglnacfdhRGEIYVP----ELGMSFQVqhektkiFGCQNPFRQGGGRKgLPRS 1883
Cdd:COG0714 97 ----VLLaDEINRAPpktQSalleAME--------ERQVTIPggtyKLPEPFLV-------IATQNPIEQEGTYP-LPEA 156
|
....*
gi 1131296855 1884 FLNRF 1888
Cdd:COG0714 157 QLDRF 161
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1079-1235 |
6.30e-10 |
|
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: 64.03 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1079 PVLIQGETSVGKTSLIRWLAAATGNHCVRINNHEHTDIQEyiGCYTSD---SSGKLVFKEG------VLIdamrkgywii 1149
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSD--ILGTYIydqQTGEFEFRPGplfanvLLA---------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1150 lDELNLAPTDVLEALNRLLDDNRellITETQEVVKAHPRFMLFATQNPPGLYGGRkVLSRAFRNRF-VELHFDeLPSSEL 1228
Cdd:COG0714 101 -DEINRAPPKTQSALLEAMEERQ---VTIPGGTYKLPEPFLVIATQNPIEQEGTY-PLPEAQLDRFlLKLYIG-YPDAEE 174
|
....*...
gi 1131296855 1229 ET-ILHKR 1235
Cdd:COG0714 175 EReILRRH 182
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
672-902 |
2.12e-09 |
|
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: 58.84 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 672 PVLLVGETGTGKTSTVQYLAH-ITGHRLRVVNMNQQSDTADLLGGYKPvdhkliwlplreafeelfvqtfskkqnftflg 750
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRNI-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 751 hiqtcyrqkrwqdllklmqhvhksavnkagaesepgsllkekweafglrlnhaqqqmkmteNALLFAFVEGTLAQAVKRG 830
Cdd:pfam07728 49 -------------------------------------------------------------DPGGASWVDGPLVRAAREG 67
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131296855 831 EWILLDEINLAAPETLECLSGLLEGSSgslVLLDRGDTEPLVRHPDFRLFACMNPAtDVGKRNLPPGIRNRF 902
Cdd:pfam07728 68 EIAVLDEINRANPDVLNSLLSLLDERR---LLLPDGGELVKAAPDGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
5381-5531 |
3.17e-09 |
|
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.
Pssm-ID: 214621 [Multi-domain] Cd Length: 175 Bit Score: 59.39 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5381 ICLAIDDSSSMVDNhTKQLAFESLAVIGNALTLLEVG-QIAVCSFGESVKLLHPFHeqfSDYSGSQILRLCKFQQKK--- 5456
Cdd:smart00327 2 VVFLLDGSGSMGGN-RFELAKEFVLKLVEQLDIGPDGdRVGLVTFSDDARVLFPLN---DSRSKDALLEALASLSYKlgg 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131296855 5457 -TKIAQFLESVANMFAAAQQLSQnvsPEIAQLLLVVSDGRGLFleGKDRVLAAVQAARNANIFVIFVVLDNPSSRD 5531
Cdd:smart00327 78 gTNLGAALQYALENLFSKSAGSR---RGAPKVVILITDGESND--GPKDLLKAAKELKRSGVKVFVVGVGNDVDEE 148
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4759-5249 |
6.35e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4759 EEADKLDE-RLWGDDDDEEDEEEDSKTEETGPGMDEEDSELVAKDDNLDAGKSNRE----KTRQDKKEEKEEAEADDDGR 4833
Cdd:PTZ00121 1312 EEAKKADEaKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaaekKKEEAKKKADAAKKKAEEKK 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4834 GQDKINEQIDEREYDENEVDpyHGNEEKLPEPEALDLPDDLNLDSEDKdgdgdTDHEDGEEENPLEIK-EQPKDTEEAGH 4912
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELK--KAAAAKKKADEAKKKAEEKKKADEAK-----KKAEEAKKADEAKKKaEEAKKAEEAKK 1464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4913 E*EDINEETEADQDEGQAQPQPEGghseddkgeegeeemdtgaddgdQDAAEHPE*DTEEAPLSSEDKDKDTSEESPEKD 4992
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEA-----------------------KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA 1521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4993 TPLDQGlqPQTQEKEEGESSDMEEPVPEPTERKEhescgqtgLESVQSEQAVELAGAAPEKEQGREEHGSGAADANQAEG 5072
Cdd:PTZ00121 1522 KKADEA--KKAEEAKKADEAKKAEEKKKADELKK--------AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE 1591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5073 HESSFMARMASQKHTRKNTQSfkRKPGQADNERSLGDHSERVHKRLRTMDTESRAEQDPAQpqaQAEDAEAFEHIKQGSE 5152
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEA--KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEE 1666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5153 PYDAQtydvastEQQQSAKDSSKAHEEEEVEDTSVDPEEQEELRAVDTEPLKPEEVKSGSTAQPGSEEMEMETQTVKTEE 5232
Cdd:PTZ00121 1667 AKKAE-------EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA 1739
|
490
....*....|....*..
gi 1131296855 5233 DQHPRTDPSHEETENEK 5249
Cdd:PTZ00121 1740 EEDKKKAEEAKKDEEEK 1756
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2218-2306 |
3.81e-08 |
|
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: 55.38 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 2218 SRGTFEWVDSMLVQALKSGDWLLMDNVNFCNPSVLDRLNALLEPGgvltvsERGMIDGSTPTVTPHPNFRLFLSMDPVHG 2297
Cdd:pfam07728 49 DPGGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDER------RLLLPDGGELVKAAPDGFRLIATMNPLDR 122
|
90
....*....|..
gi 1131296855 2298 ---EISRAMRNR 2306
Cdd:pfam07728 123 glnELSPALRSR 134
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1384-1540 |
5.24e-08 |
|
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: 55.46 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1384 EPVLLVGDTGCGKTTICQVFAALANQKLYSV---NCHLHMETSDFLGGLRPVRQKPNDKEEIDTSRLFewhdgpLVLAMK 1460
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGViyiDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLA------LALARK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1461 ED-GFFLLDEISLADDSVLERLNSVLEVEKTLLLAEKgnledkdnevelltaGKKFRILATMNPGGDFGKKELSPALRNR 1539
Cdd:smart00382 77 LKpDVLILDEITSLLDAEQEALLLLLEELRLLLLLKS---------------EKNLTVILTTNDEKDLGPALLRRRFDRR 141
|
.
gi 1131296855 1540 F 1540
Cdd:smart00382 142 I 142
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1353-1540 |
6.91e-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: 57.87 E-value: 6.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1353 MSTLESKF---SHIVWTEGMRRL---AMLVGRalqfsePVLLVGDTGCGKTTICQVFAALANQKLYSVNCHLHMETSDFL 1426
Cdd:COG0714 1 MTEARLRAeigKVYVGQEELIELvliALLAGG------HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1427 GglrpvrqkpndkEEI---DTSRlFEWHDGPlVLAmkedGFFLLDEISLADDsvlerlnsvlEVEKTLLLAekgnLEDK- 1502
Cdd:COG0714 75 G------------TYIydqQTGE-FEFRPGP-LFA----NVLLADEINRAPP----------KTQSALLEA----MEERq 122
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1131296855 1503 ---DNEVelLTAGKKFRILATMNPGGDFGKKELSPALRNRF 1540
Cdd:COG0714 123 vtiPGGT--YKLPEPFLVIATQNPIEQEGTYPLPEAQLDRF 161
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1016-1316 |
2.22e-07 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 57.09 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1016 SGNIKSLLKQPIPEPKGGRLIQVEGYWISVGDKEPTIDETYILTSSVKLNLRDIVRVVSAGTYP--VLIQGETSVGKTSL 1093
Cdd:COG1401 158 LEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKFEETLEAFLAALKTKknVILAGPPGTGKTYL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1094 IRWLAAATG---NHCVRI-----NNHEHTDIQEYigcYTSDSSGKLVFKEGVLIDAMRKG-------YWIILDELNLAPT 1158
Cdd:COG1401 238 ARRLAEALGgedNGRIEFvqfhpSWSYEDFLLGY---RPSLDEGKYEPTPGIFLRFCLKAeknpdkpYVLIIDEINRANV 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1159 D--------VLEALNRLLDDNRELLITETQEVVKAHPRFMLFATQNPP--GLYGGRKVLSRAFRNRFVELHFDELPSSEL 1228
Cdd:COG1401 315 EkyfgellsLLESDKRGEELSIELPYSGEGEEFSIPPNLYIIGTMNTDdrSLALSDKALRRRFTFEFLDPDLDKLSNEEV 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1229 ETILHKrcslppsycsklVKVMLDLQSYRRGSSVFAGKQGFITLRDLFRWAERYRLAEQTEKEYDWLQHLANDGFMLLAG 1308
Cdd:COG1401 395 VDLLEE------------LNEILEKRDFQIGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLLDKLDLLGMAEFEDRLE 462
|
....*...
gi 1131296855 1309 RVRKQEEV 1316
Cdd:COG1401 463 LSEYLPLL 470
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1747-1896 |
1.24e-06 |
|
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: 51.38 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1747 KPILLEGSPGVGKTSLVGALARAS---GNTLVRINLSeqtditDLFGADlpVEGGKGGEFAWRDGPLLAALKAGHWVVLD 1823
Cdd:cd00009 20 KNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNAS------DLLEGL--VVAELFGHFLVRLLFELAEKAKPGVLFID 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131296855 1824 ELNLASQSVLEGLNACFdhrgeiyvpELGMSFQVQHEKTKIFG-CQNPFRQgggrkGLPRSFLNRFTQVFVDPL 1896
Cdd:cd00009 92 EIDSLSRGAQNALLRVL---------ETLNDLRIDRENVRVIGaTNRPLLG-----DLDRALYDRLDIRIVIPL 151
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4782-5028 |
1.50e-06 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 55.00 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4782 SKTEETGpgmDEEDSELVAKDDNLDAGKSNREKTRQDKKEEKEEAEADDDGRGQDkinEQIDEREYDENEVDpyHGNEEK 4861
Cdd:TIGR00927 640 HTGERTG---EEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKG---EQEGEGEIEAKEAD--HKGETE 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4862 LPEPEAldlpddlnldSEDKDGDGDTDHEDGEEENPLEIKEQPKDTE-EAGHE*E------------DINEETEADQDEG 4928
Cdd:TIGR00927 712 AEEVEH----------EGETEAEGTEDEGEIETGEEGEEVEDEGEGEaEGKHEVEtegdrketehegETEAEGKEDEDEG 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4929 QAQPQPEGGH---------SEDDKGEEGEEEMDTGADDGDQDAAEHPE*DTEEAPLSSEDKDKDTSEESPEKDTPLDQGL 4999
Cdd:TIGR00927 782 EIQAGEDGEMkgdegaegkVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDGG 861
|
250 260
....*....|....*....|....*....
gi 1131296855 5000 QPQTQEKEEGESSDMEEPVPEPTERKEHE 5028
Cdd:TIGR00927 862 DSEEEEEEEEEEEEEEEEEEEEEEEEEEN 890
|
|
| Granin |
pfam01271 |
Granin (chromogranin or secretogranin); |
4890-5363 |
4.98e-06 |
|
Granin (chromogranin or secretogranin);
Pssm-ID: 279595 [Multi-domain] Cd Length: 584 Bit Score: 53.11 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4890 EDGEEENP-LEIKE--QPKDTEEAGH--E*EDINEETEADQDEGQAQPQPE---GGHSEDDKGEEGEEEMDTGADDGDQD 4961
Cdd:pfam01271 47 ERSENYNPyFEVRLlrDLADQSEASHlsSRSRDGLSDEDMQIITEALRQAEnepGGHSRENQPYALQVEKEFKTDHSDDY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4962 AAEHPE*DtEEAPLSSEDKDKDTSEESPEKDTpldqGLQPQTQEKEEGESSdMEEPVPEPTERKEHESCGQTGLESVQ-S 5040
Cdd:pfam01271 127 ETQQWEEE-KLKHMRFPLRYEENSEEKHSERE----GELSEVFENPRSQAT-LKKVFEEVSRLDTPSKQKREKSDEREkS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5041 EQAVELAGAAPEKEQGrEEHGSGAADANQAEGHESsfmarmASQKHTRkntqsfkrkpgqadnerslgDHSERVHKRLRT 5120
Cdd:pfam01271 201 SQESGEDTYRQENIPQ-EDQVGPEDQEPSEEGEED------ATQEEVK--------------------RSRPRTHHGRSL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5121 MDTESRAEQDPAQPQAQAEDAEAFEHIK--QGSEPYDAQTYDVASTEQQQSAKDSSKAHEEEEVEDTSVDPEEQEELRAV 5198
Cdd:pfam01271 254 PDESSRGGQLGLEEEASEEEEEYGEESRglSAVQTYLLRLVNARGRGRSEKRAERERSEESEEEELKRASPYEELEITAN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5199 ----DTEPLKPEEVKSGSTAQPGSEEMEMETQTVKTE----EDQHPRTDPSHEETENEKPERSRDStihtahqllvdtif 5270
Cdd:pfam01271 334 lqipPSEEERMLKKAGRSPRGRVDEAGALEALEALEEkrklDLDHSRVFESSEDGAPRAPQGAWVE-------------- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5271 qpflKDVNELRQELERQLETWQ---PHESGNPEEEKA*AEMWQSYLVLTAPL--SQQLCEQLRLILEPTQAAKLKGDYRT 5345
Cdd:pfam01271 400 ----ALRNYLSYGEEGMEGKWNqqgPYFPNEENREEARFRLPQYLGELSNPWedPKQWKPSDFERKELTADKFLEGEEEN 475
|
490 500
....*....|....*....|.
gi 1131296855 5346 GKRLNMRKVIP---YIASQFR 5363
Cdd:pfam01271 476 EYTLSMKNSFPeynYDGYEKR 496
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1385-1618 |
6.01e-06 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 52.43 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1385 PVLLVGDTGCGKTTICQVFAALANQKLYSVNchlhmetsdflgglrPVRQKPNDKEEIDTSRLFewHDGPLVLAMKEDGF 1464
Cdd:PHA02244 121 PVFLKGGAGSGKNHIAEQIAEALDLDFYFMN---------------AIMDEFELKGFIDANGKF--HETPFYEAFKKGGL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1465 FLLDEISLADDSVLERLNSVlevektllLAEKGnledKDNEVELLTAGKKFRILA---TMNPGGD---FGKKELSPALRN 1538
Cdd:PHA02244 184 FFIDEIDASIPEALIIINSA--------IANKF----FDFADERVTAHEDFRVISagnTLGKGADhiyVARNKIDGATLD 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1539 RFTEIWCPQSTKREDLIQIISRNLhpglslgrtdhkgadiaevmLDFIDWLTHQ--EFGRRCVVSIRDILSWVNFMNTMG 1616
Cdd:PHA02244 252 RFAPIEFDYDEKIEHLISNGDEDL--------------------VNFVALLRHEmaEKGLDHVFSMRAIIHGKKFDGVFE 311
|
..
gi 1131296855 1617 EE 1618
Cdd:PHA02244 312 AD 313
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1660-1828 |
1.85e-05 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 50.92 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1660 ARRECLKFLIKKLSKIGRLTESQKNELKIYDRLKDKEFTGIDNLWGIHPFFIPRGPVLHRNNIADYALSAGTTAMNAQRL 1739
Cdd:COG1401 135 ARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKFEETLEAF 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1740 LRATKLNKPILLEGSPGVGKTSLVGALARA-SGNTLVRINLseqtdIT---DLFGADLpVEG----GKGGEFAWRDGPLL 1811
Cdd:COG1401 215 LAALKTKKNVILAGPPGTGKTYLARRLAEAlGGEDNGRIEF-----VQfhpSWSYEDF-LLGyrpsLDEGKYEPTPGIFL 288
|
170 180
....*....|....*....|....
gi 1131296855 1812 -AALKAG------HWVVLDELNLA 1828
Cdd:COG1401 289 rFCLKAEknpdkpYVLIIDEINRA 312
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1385-1543 |
1.61e-04 |
|
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: 45.21 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1385 PVLLVGDTGCGKTTICQVFA---ALANQKLYSVNCHLHMETSDFLGglrpvrqkpnDKEEIDTSRLFEwhdgplVLAMKE 1461
Cdd:cd00009 21 NLLLYGPPGTGKTTLARAIAnelFRPGAPFLYLNASDLLEGLVVAE----------LFGHFLVRLLFE------LAEKAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1462 DGFFLLDEISLADDSVLERLNSVLEVEKTLLLAEKGNledkdnevelltagkkFRILATMNPGGDfgkkELSPALRNRFT 1541
Cdd:cd00009 85 PGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRENV----------------RVIGATNRPLLG----DLDRALYDRLD 144
|
..
gi 1131296855 1542 EI 1543
Cdd:cd00009 145 IR 146
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1079-1221 |
1.84e-04 |
|
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: 45.06 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1079 PVLIQGETSVGKTSLIR---WLAAATGNHCVRIN----NHEHTDIQEYIGCYTSDSSGKLVFKEGVLIDAMRKGYW--II 1149
Cdd:smart00382 4 VILIVGPPGSGKTTLARalaRELGPPGGGVIYIDgediLEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPdvLI 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131296855 1150 LDELNLAPTDVLEALNRLLDDNRELLITEtqevvKAHPRFMLFATQNPPGLygGRKVLSRAFRNRFVELHFD 1221
Cdd:smart00382 84 LDEITSLLDAEQEALLLLLEELRLLLLLK-----SEKNLTVILTTNDEKDL--GPALLRRRFDRRIVLLLIL 148
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
320-432 |
1.86e-04 |
|
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: 45.21 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 320 ASQNAVLLEGPIGCGKTSLVEHLAAMTGRRKPSqLLKVQLGDqtdskMLLGMYRCTDVpGEFVWQPGTLTQAATKGHWIL 399
Cdd:cd00009 17 PPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-FLYLNASD-----LLEGLVVAELF-GHFLVRLLFELAEKAKPGVLF 89
|
90 100 110
....*....|....*....|....*....|...
gi 1131296855 400 LEDIDYAPLDVVSVLIPLLENGELLIPGRGDCV 432
Cdd:cd00009 90 IDEIDSLSRGAQNALLRVLETLNDLRIDRENVR 122
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1068-1221 |
1.88e-04 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 47.42 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1068 DIVRVVSAGTyPVLIQGETSVGKTSLIRWLAAAtgnhcVRINNHEHTDI-QEYIGCYTSDSSGKlvFKEGVLIDAMRKGY 1146
Cdd:PHA02244 111 DIAKIVNANI-PVFLKGGAGSGKNHIAEQIAEA-----LDLDFYFMNAImDEFELKGFIDANGK--FHETPFYEAFKKGG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1147 WIILDELNLAPTDVLEALNRLLDDNRELLITETqevVKAHPRFMLFATQNPPG-----LYGGRKVLSRAFRNRFVELHFD 1221
Cdd:PHA02244 183 LFFIDEIDASIPEALIIINSAIANKFFDFADER---VTAHEDFRVISAGNTLGkgadhIYVARNKIDGATLDRFAPIEFD 259
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
1747-1782 |
4.28e-04 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 46.84 E-value: 4.28e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1131296855 1747 KPILLEGSPGVGKTSLVGALARASGNTLVRINLSEQ 1782
Cdd:PRK04195 40 KALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQ 75
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1079-1215 |
4.82e-04 |
|
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: 44.06 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1079 PVLIQGETSVGKTSLIR---WLAAATGNHCVRINNHEHTDIqeyigcyTSDSSGKLVFKEGVLIDAMRKGYW--IILDEL 1153
Cdd:cd00009 21 NLLLYGPPGTGKTTLARaiaNELFRPGAPFLYLNASDLLEG-------LVVAELFGHFLVRLLFELAEKAKPgvLFIDEI 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131296855 1154 NLAPTDVLEALNRLLDDnRELLITETQEVvkahpRFMLFATQNPPGLyggrkvLSRAFRNRF 1215
Cdd:cd00009 94 DSLSRGAQNALLRVLET-LNDLRIDRENV-----RVIGATNRPLLGD------LDRALYDRL 143
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
669-736 |
2.34e-03 |
|
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: 41.98 E-value: 2.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131296855 669 KGEPVLLVGETGTGKTSTVQYLAHI---TGHRLRVVNMNQQSDTADLLGGYKPVDHKLIWLPLREAFEELF 736
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLAL 71
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
659-780 |
7.29e-03 |
|
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: 40.59 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 659 LIEQL--AVCVSKGEPVLLVGETGTGKTSTVQYLAHITGHR-LRVVNMNqqsdTADLLGGYkpVDHKLIWLPLREAFEEL 735
Cdd:cd00009 6 AIEALreALELPPPKNLLLYGPPGTGKTTLARAIANELFRPgAPFLYLN----ASDLLEGL--VVAELFGHFLVRLLFEL 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1131296855 736 fvqtFSKKQNFT-FLGHIQTCYRQKRWQdLLKLMQHVHKSAVNKAG 780
Cdd:cd00009 80 ----AEKAKPGVlFIDEIDSLSRGAQNA-LLRVLETLNDLRIDREN 120
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
312-501 |
7.99e-03 |
|
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: 42.08 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 312 LQTLAMAVASQNAVLLEGPIGCGKTSLVEHLAAMTGRR----------KPSQLLKVQLGDQTDskmllgmyrctdvpGEF 381
Cdd:COG0714 21 IELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPfiriqftpdlLPSDILGTYIYDQQT--------------GEF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 382 VWQPGTLTQAatkghwILLED-IDYAPLDVVSVLIPLLENGELLIPGRGdcVKVAPGFQFFATRRLLSCGGnwYRPLnsH 460
Cdd:COG0714 87 EFRPGPLFAN------VLLADeINRAPPKTQSALLEAMEERQVTIPGGT--YKLPEPFLVIATQNPIEQEG--TYPL--P 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1131296855 461 ATLLDKYWTKIHLDNMDKAELNEVLQNRYPSLSAATDHLLD 501
Cdd:COG0714 155 EAQLDRFLLKLYIGYPDAEEEREILRRHTGRHLAEVEPVLS 195
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| vWA_midasin |
cd01460 |
VWA_Midasin: Midasin is a member of the AAA ATPase family. The proteins of this family are ... |
5319-5589 |
7.19e-147 |
|
VWA_Midasin: Midasin is a member of the AAA ATPase family. The proteins of this family are unified by their common archetectural organization that is based upon a conserved ATPase domain. The AAA domain of midasin contains six tandem AAA protomers. The AAA domains in midasin is followed by a D/E rich domain that is following by a VWA domain. The members of this subgroup have a conserved MIDAS motif. The function of this domain is not exactly known although it has been speculated to play a crucial role in midasin function.
Pssm-ID: 238737 Cd Length: 266 Bit Score: 458.35 E-value: 7.19e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5319 LSQQLCEQLRLILEPTQAAKLKGDYRTGKRLNMRKVIPYIASQFRKDKIWLRRTKPSKRQYQICLAIDDSSSMVDNHTKQ 5398
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5399 LAFESLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEQFSDYSGSQILRLCKFQQKKTKIAQFLESVANMFAAAQQlsQ 5478
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDART--Q 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5479 NVSPEIAQLLLVVSDGRGLFLEGKDRVLaaVQAARNANIFVIFVVLDNPSSRDSILDIKVPIFKGPGeMPEIRSYMEEFP 5558
Cdd:cd01460 159 SSSGSLWQLLLIISDGRGEFSEGAQKVR--LREAREQNVFVVFIIIDNPDNKQSILDIKVVSFKNDK-SGVITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|.
gi 1131296855 5559 FPFYIILRDVNALPETLSDALRQWFELVTAS 5589
Cdd:cd01460 236 FPYYVIVRDLNQLPSVLSDALRQWFELVNSS 266
|
|
| AAA_lid_5 |
pfam17865 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
915-1017 |
2.41e-40 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 407722 Cd Length: 104 Bit Score: 146.19 E-value: 2.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 915 DLQILIVDYLKGLSVNKNTVQGIITFYTAVRKESGTKLVDGTGHRPHYSLRTLCRALRFAASN-PCGNIQRSLYEGFCLG 993
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLVRDIVKFYLEAKKLAEKSLVDGAGQRPHYSLRTLCRALSYARAIaPRYGLRRALYEGFCMS 80
|
90 100
....*....|....*....|....
gi 1131296855 994 FLTQLDRASHPVVQKLICQHIVSG 1017
Cdd:pfam17865 81 FLTQLDAESRKIVEKLIRKHLLKG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1385-1540 |
3.76e-29 |
|
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: 115.47 E-value: 3.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1385 PVLLVGDTGCGKTTICQVFA-ALANQKLYSVNCHLHMETSDFLGGLrpvrqkpndkeEIDTsRLFEWHDGPLVLAMKEDG 1463
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAaALSNRPVFYVQLTRDTTEEDLFGRR-----------NIDP-GGASWVDGPLVRAAREGE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131296855 1464 FFLLDEISLADDSVLERLNSVLEvEKTLLLAEKGNLEDKDNevelltagKKFRILATMNPgGDFGKKELSPALRNRF 1540
Cdd:pfam07728 69 IAVLDEINRANPDVLNSLLSLLD-ERRLLLPDGGELVKAAP--------DGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1900-1999 |
1.26e-24 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 101.22 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1900 DMEFIASTLFPaIDKNIVKKMVAFNNQIDHEVTVEKKWGQIGGPWEFNLRDLFRWCQLM-----LVDQSPGCYDPGQHVF 1974
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLssllpTLLSPTVREEIFLEAV 79
|
90 100
....*....|....*....|....*
gi 1131296855 1975 LVYGERMRTKEDKEKVIAVFKDVFN 1999
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVLG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1079-1215 |
5.81e-23 |
|
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: 97.75 E-value: 5.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1079 PVLIQGETSVGKTSLIRWLAAATGNHCVR-INNHEHTDIQEYIGCYTSDSSGKlVFKEGVLIDAMRKGYWIILDELNLAP 1157
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFyVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1131296855 1158 TDVLEALNRLLDDNRELLITETQEVVKAHPRFMLFATQNPPglYGGRKVLSRAFRNRF 1215
Cdd:pfam07728 80 PDVLNSLLSLLDERRLLLPDGGELVKAAPDGFRLIATMNPL--DRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1227-1328 |
8.22e-22 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 93.52 E-value: 8.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1227 ELETILHKRCSLPPSYCSKLVKVMLDLQSYRRGSSVFA--GKQGFITLRDLFRWAERYRLAEQTEKEYDWLQHLANDGFM 1304
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGssGSPREFNLRDLLRWCRRLSSLLPTLLSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....
gi 1131296855 1305 LLAGRVRKQEEVVVIQEVLEKHFK 1328
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
325-453 |
6.03e-21 |
|
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: 91.97 E-value: 6.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 325 VLLEGPIGCGKTSLVEHLAAMTGRRKpsqLLKVQLGDQTDSKMLLGMYRCTdvPGEFVWQPGTLTQAATKGHWILLEDID 404
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRP---VFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1131296855 405 YAPLDVVSVLIPLLENGELLIPGRGDCVKVAP-GFQFFATRRLLSCGGNW 453
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIATMNPLDRGLNE 126
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
480-604 |
1.30e-18 |
|
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. This lid domain is found in midasin proteins.
Pssm-ID: 465540 Cd Length: 106 Bit Score: 84.28 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 480 ELNEVLQNRYPSLSAATDHLLDIYFQLIGEKHHCLSESSVGGeqapgevpearqenkrlsleGRELSLRDLLNWCNRIAH 559
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGS--------------------PREFNLRDLLRWCRRLSS 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1131296855 560 SFDSLSSSASL-NIFQEALDCFTAMLSKQTSKLKMAEVIGSKLNIS 604
Cdd:pfam17867 61 LLPTLLSPTVReEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1748-1888 |
1.71e-16 |
|
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: 79.26 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1748 PILLEGSPGVGKTSLVGALARA-SGNTLVRINLSEQTDITDLFGADLPveggKGGEFAWRDGPLLAALKAGHWVVLDELN 1826
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNI----DPGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131296855 1827 LASQSVLEGLNACFDHRgEIYVPELGMSFQVQHEKTKIFGCQNPfrQGGGRKGLPRSFLNRF 1888
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDGFRLIATMNP--LDRGLNELSPALRSRF 135
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4678-5260 |
5.19e-15 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 82.76 E-value: 5.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4678 DVSDQIENEEQAEDTFQKGQEKDKEDPDSKSDIKGEDNAIEMSEDFDGKMHDGELEEQEEDDEKSDSETGDLDKQMGDLN 4757
Cdd:COG5271 244 ADETLLADDDDTESAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELTAAQAADPESDDDADDSTLAALEGAAEDTE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4758 GEEADKLDERLWGDDDDEEDEEEDSKTEETGPGMDEEDSELVAKDDNLDAGKSNRE-KTRQDKKEEKEEAEADDDGRGQD 4836
Cdd:COG5271 324 IATADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGAdTDAAADEADAAADDSADDEEASA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4837 KINEQID-EREYDENEVDPyhGNEEKLPEPEALDLPDDLNLDSEDKDGDGDTDHEDGEEENPLEIKEQPKDTEEAghe*e 4915
Cdd:COG5271 404 DGGTSPTsDTDEEEEEADE--DASAGETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDA----- 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4916 DINEETEADQDEGQAQPQPEGGHSEDDKGEEGEEEMDTGADDG-DQDAAEHPE*DTEEAplsSEDkDKDTSEESPEKDtp 4994
Cdd:COG5271 477 DGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSADDGaDTDAAADPEDSDEDA---LED-ETEGEENAPGSD-- 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4995 LDQGLQPQTQEKEEGESSDMEEpvPEPTERKEHESCGQTGLESVQSEQAVELAGAAPEKEQGREEH----GSGAADANQA 5070
Cdd:COG5271 551 QDADETDEPEATAEEDEPDEAE--AETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEadadADGAADEEET 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5071 EGHESSFMARMASQ---KHTRKNTQSFKRKPGQADNERSLG-DHSErvhkrlrTMDTESRAEQDpAQPQAQAEDAEAFEH 5146
Cdd:COG5271 629 EEEAAEDEAAEPETdasEAADEDADAETEAEASADESEEEAeDESE-------TSSEDAEEDAD-AAAAEASDDEEETEE 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5147 IKQgsepyDAQTYDVASTEQQQSAK--DSSKAHEEEEVEDTSVDPEEQEELRAVDTEPLKPEEVKSGSTAQPGSEEmEME 5224
Cdd:COG5271 701 ADE-----DAETASEEADAEEADTEadGTAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDADGLEE-ALE 774
|
570 580 590
....*....|....*....|....*....|....*.
gi 1131296855 5225 TQTVKTEEDQhprTDPSHEETENEKpERSRDSTIHT 5260
Cdd:COG5271 775 EEKADAEEAA---TDEEAEAAAEEK-EKVADEDQDT 806
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4678-5259 |
3.30e-14 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 80.44 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4678 DVSDQIENEEQAEDTFQKGQEKDKEDPDSKSDIKGEDNAIEMSEDFDGKmhDGELEEQEEDDEKSDSETGDLDKQMGDL- 4756
Cdd:COG5271 360 DTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTS--PTSDTDEEEEEADEDASAGETEDESTDVt 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4757 ---NGEEADKLDERLwgDDDDEEDEEEDSKTEETGPGMDEEDSELVAKDDNLDAGKSNREKTRQdkkeekeeaeadddgr 4833
Cdd:COG5271 438 saeDDIATDEEADSL--ADEEEEAEAELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEED---------------- 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4834 gqDKINEQIDEREYDENEVDPYHGNEEKLPEPEALDLPDDLNLDSEDKDGDGDTDHEDGEEENPLEiKEQPKDTEEAghE 4913
Cdd:COG5271 500 --AEAEADSDELTAEETSADDGADTDAAADPEDSDEDALEDETEGEENAPGSDQDADETDEPEATA-EEDEPDEAEA--E 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4914 *EDINEETEADQDEGQAQPQPEGGHSEDDkgeegeeemdtgADDGDQDAAEHPE*DTEEAPLSSEDKDKDTSEESPEKDT 4993
Cdd:COG5271 575 TEDATENADADETEESADESEEAEASEDE------------AAEEEEADDDEADADADGAADEEETEEEAAEDEAAEPET 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4994 PLDQGLQPQTQEKEEGESSDmEEPVPEPTErkehescgqtglESVQSEQAVELAGAAPEKEQGREEHGSGAADANQAEgh 5073
Cdd:COG5271 643 DASEAADEDADAETEAEASA-DESEEEAED------------ESETSSEDAEEDADAAAAEASDDEEETEEADEDAET-- 707
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5074 essfmarmasQKHTRKNTQSFKRKPGQADNERSLGDHSErvhkrlrTMDTEsraeqdpAQPQAQAEDAEAFEHIKQGSEP 5153
Cdd:COG5271 708 ----------ASEEADAEEADTEADGTAEEAEEAAEEAE-------SADEE-------AASLPDEADAEEEAEEAEEAEE 763
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5154 YDAQTYDvASTEQQQSAKDSSKAHEEEEVE----------------DTSVDPEEQEELRAVD-TEPLKPEEVKS-----G 5211
Cdd:COG5271 764 DDADGLE-EALEEEKADAEEAATDEEAEAAaeekekvadedqdtdeDALLDEAEADEEEDLDgEDEETADEALEdieagI 842
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1131296855 5212 STAQPGSEEMEMETQTVKTEEDQHPRTDPSHEETENEKPERSRDSTIH 5259
Cdd:COG5271 843 AEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAETDADADAD 890
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4676-5251 |
1.01e-11 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 71.97 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4676 MKDVSDQIENEEQAEDTFQKGQEKDKEDPDSKSDIKGEDNAIEmsEDFDGKMHDGELEEQEEDDEKSDSETGDLDKQMGD 4755
Cdd:COG5271 204 GATVTTDPGDSVAADDDLAAEEGASAVVEEEDASEDAVAAADE--TLLADDDDTESAGATAEVGGTPDTDDEATDDADGL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4756 LNGEEADKLDERLWGDDDDEEDEEEDSKTEETGPGMDEEDSELVAKDDNLDAGKSNREKTRQDKKEEKEEAEADDDGrgq 4835
Cdd:COG5271 282 EAAEDDALDAELTAAQAADPESDDDADDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAEDAAEEAATAEDSAA--- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4836 DKINEQIDEREYDENEVDPYHGNEEKLPEPEALDLPDDLNLDSEDKDGDGDTDHEDGEEENPleikEQPKDTEEAGHE*E 4915
Cdd:COG5271 359 EDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEA----DEDASAGETEDEST 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4916 DI-NEETEADQDEGQaqpqpegghseddkgeegeeemDTGADDGDQDAAEHPE*DTEEAPLSSEDKDKDTSEESPEKDTp 4994
Cdd:COG5271 435 DVtSAEDDIATDEEA----------------------DSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDASDDG- 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4995 LDQGLQPQTQEKEEGESSDMEEPVP-EPTERKEHESCGQTGLESVQSEQAVELAGAAPEKEQGREEHGSGAADANQAEGH 5073
Cdd:COG5271 492 DEEEAEEDAEAEADSDELTAEETSAdDGADTDAAADPEDSDEDALEDETEGEENAPGSDQDADETDEPEATAEEDEPDEA 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5074 ESsfmarMASQKHTRKNTQSFKRKPGQADNERSLGDhservhkrlrtmDTESRAEQDPAQPQAQAEDA--EAFEHIKQGS 5151
Cdd:COG5271 572 EA-----ETEDATENADADETEESADESEEAEASED------------EAAEEEEADDDEADADADGAadEEETEEEAAE 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5152 EPYDAQTYDVASTEQQQS--------AKDSSKAHEEEEVEDTSVDPEE------------QEELRAVDTEPLKPEEVK-- 5209
Cdd:COG5271 635 DEAAEPETDASEAADEDAdaeteaeaSADESEEEAEDESETSSEDAEEdadaaaaeasddEEETEEADEDAETASEEAda 714
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1131296855 5210 -SGSTAQPGSEEMEMETQTVKTEEDQHprTDPSHEETENEKPE 5251
Cdd:COG5271 715 eEADTEADGTAEEAEEAAEEAESADEE--AASLPDEADAEEEA 755
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4677-5261 |
2.15e-11 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 71.20 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4677 KDVSDQIENEEQAEDTFQkGQEKDKEDPDSKSDIKGEDNAIEMSEDFDGKMHDGELEEQEEDDEKSDSETGDLDKQMGDL 4756
Cdd:COG5271 175 ADGDDTLAVADAIEATPG-GTDAVELTATLGATVTTDPGDSVAADDDLAAEEGASAVVEEEDASEDAVAAADETLLADDD 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4757 NGEEADKLDERLWgddddeEDEEEDSKTEETGPGMDEEDSELVAKDDN-LDAGKSNREKTRQDKKEEKEEAEADDDGRGQ 4835
Cdd:COG5271 254 DTESAGATAEVGG------TPDTDDEATDDADGLEAAEDDALDAELTAaQAADPESDDDADDSTLAALEGAAEDTEIATA 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4836 DKINEQIDEREYDENEVDpYHGNEEKLPEPEALDLPDDLNLDSEDKDGDGDTDHEDGEEENPLEIKEQPKDTEEAGHE-- 4913
Cdd:COG5271 328 DELAAADDEDDDDSAAED-AAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADgg 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4914 ----*EDINEETEADQDEGQAQPQPEGGHSEDDKGEEGE-EEMDTGADDGDQDAAEHPE*DTEEAPLSSEDKDKDTSEES 4988
Cdd:COG5271 407 tsptSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATdEEADSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDD 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4989 PEKDTpLDQGLQPQTQEKEEGESSDMEEPVPEPTERKEhescgqtglesvQSEQAVELAGAAPEKEQGREEHGSGAaDAN 5068
Cdd:COG5271 487 ASDDG-DEEEAEEDAEAEADSDELTAEETSADDGADTD------------AAADPEDSDEDALEDETEGEENAPGS-DQD 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5069 QAEGHEssfmarmasqkhtrkntqsfkrkpGQADNERSLGDhservhkrlrtmdtESRAEQDPAQPQAQAEDAEAFEHIK 5148
Cdd:COG5271 553 ADETDE------------------------PEATAEEDEPD--------------EAEAETEDATENADADETEESADES 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5149 QGSEPydaqTYDvASTEQQQSAKDSSKAHEEEEVEDTSVDPEEQE-ELRAVDTEPLKPEEVKSGSTaqpgseememetQT 5227
Cdd:COG5271 595 EEAEA----SED-EAAEEEEADDDEADADADGAADEEETEEEAAEdEAAEPETDASEAADEDADAE------------TE 657
|
570 580 590
....*....|....*....|....*....|....
gi 1131296855 5228 VKTEEDQHPRTDPSHEETENEKPERSRDSTIHTA 5261
Cdd:COG5271 658 AEASADESEEEAEDESETSSEDAEEDADAAAAEA 691
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1736-1888 |
1.56e-10 |
|
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: 65.57 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1736 AQRLLRATKLNKPILLEGSPGVGKTSLVGALARASGNTLVRINLSEQTDITDLFGADLPVEggKGGEFAWRDGPLLAAlk 1815
Cdd:COG0714 21 IELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQ--QTGEFEFRPGPLFAN-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1816 aghwVVL-DELNLAS---QS----VLEglnacfdhRGEIYVP----ELGMSFQVqhektkiFGCQNPFRQGGGRKgLPRS 1883
Cdd:COG0714 97 ----VLLaDEINRAPpktQSalleAME--------ERQVTIPggtyKLPEPFLV-------IATQNPIEQEGTYP-LPEA 156
|
....*
gi 1131296855 1884 FLNRF 1888
Cdd:COG0714 157 QLDRF 161
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1079-1235 |
6.30e-10 |
|
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: 64.03 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1079 PVLIQGETSVGKTSLIRWLAAATGNHCVRINNHEHTDIQEyiGCYTSD---SSGKLVFKEG------VLIdamrkgywii 1149
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSD--ILGTYIydqQTGEFEFRPGplfanvLLA---------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1150 lDELNLAPTDVLEALNRLLDDNRellITETQEVVKAHPRFMLFATQNPPGLYGGRkVLSRAFRNRF-VELHFDeLPSSEL 1228
Cdd:COG0714 101 -DEINRAPPKTQSALLEAMEERQ---VTIPGGTYKLPEPFLVIATQNPIEQEGTY-PLPEAQLDRFlLKLYIG-YPDAEE 174
|
....*...
gi 1131296855 1229 ET-ILHKR 1235
Cdd:COG0714 175 EReILRRH 182
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
672-902 |
2.12e-09 |
|
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: 58.84 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 672 PVLLVGETGTGKTSTVQYLAH-ITGHRLRVVNMNQQSDTADLLGGYKPvdhkliwlplreafeelfvqtfskkqnftflg 750
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRNI-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 751 hiqtcyrqkrwqdllklmqhvhksavnkagaesepgsllkekweafglrlnhaqqqmkmteNALLFAFVEGTLAQAVKRG 830
Cdd:pfam07728 49 -------------------------------------------------------------DPGGASWVDGPLVRAAREG 67
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131296855 831 EWILLDEINLAAPETLECLSGLLEGSSgslVLLDRGDTEPLVRHPDFRLFACMNPAtDVGKRNLPPGIRNRF 902
Cdd:pfam07728 68 EIAVLDEINRANPDVLNSLLSLLDERR---LLLPDGGELVKAAPDGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
5381-5531 |
3.17e-09 |
|
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.
Pssm-ID: 214621 [Multi-domain] Cd Length: 175 Bit Score: 59.39 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5381 ICLAIDDSSSMVDNhTKQLAFESLAVIGNALTLLEVG-QIAVCSFGESVKLLHPFHeqfSDYSGSQILRLCKFQQKK--- 5456
Cdd:smart00327 2 VVFLLDGSGSMGGN-RFELAKEFVLKLVEQLDIGPDGdRVGLVTFSDDARVLFPLN---DSRSKDALLEALASLSYKlgg 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131296855 5457 -TKIAQFLESVANMFAAAQQLSQnvsPEIAQLLLVVSDGRGLFleGKDRVLAAVQAARNANIFVIFVVLDNPSSRD 5531
Cdd:smart00327 78 gTNLGAALQYALENLFSKSAGSR---RGAPKVVILITDGESND--GPKDLLKAAKELKRSGVKVFVVGVGNDVDEE 148
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4759-5249 |
6.35e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4759 EEADKLDE-RLWGDDDDEEDEEEDSKTEETGPGMDEEDSELVAKDDNLDAGKSNRE----KTRQDKKEEKEEAEADDDGR 4833
Cdd:PTZ00121 1312 EEAKKADEaKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaaekKKEEAKKKADAAKKKAEEKK 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4834 GQDKINEQIDEREYDENEVDpyHGNEEKLPEPEALDLPDDLNLDSEDKdgdgdTDHEDGEEENPLEIK-EQPKDTEEAGH 4912
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELK--KAAAAKKKADEAKKKAEEKKKADEAK-----KKAEEAKKADEAKKKaEEAKKAEEAKK 1464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4913 E*EDINEETEADQDEGQAQPQPEGghseddkgeegeeemdtgaddgdQDAAEHPE*DTEEAPLSSEDKDKDTSEESPEKD 4992
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEA-----------------------KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA 1521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4993 TPLDQGlqPQTQEKEEGESSDMEEPVPEPTERKEhescgqtgLESVQSEQAVELAGAAPEKEQGREEHGSGAADANQAEG 5072
Cdd:PTZ00121 1522 KKADEA--KKAEEAKKADEAKKAEEKKKADELKK--------AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE 1591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5073 HESSFMARMASQKHTRKNTQSfkRKPGQADNERSLGDHSERVHKRLRTMDTESRAEQDPAQpqaQAEDAEAFEHIKQGSE 5152
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEA--KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEE 1666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5153 PYDAQtydvastEQQQSAKDSSKAHEEEEVEDTSVDPEEQEELRAVDTEPLKPEEVKSGSTAQPGSEEMEMETQTVKTEE 5232
Cdd:PTZ00121 1667 AKKAE-------EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA 1739
|
490
....*....|....*..
gi 1131296855 5233 DQHPRTDPSHEETENEK 5249
Cdd:PTZ00121 1740 EEDKKKAEEAKKDEEEK 1756
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4840-5028 |
1.80e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 60.37 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4840 EQIDEREYDENEVDPYHGNEEKLPE--PEAldlpddlnldsEDKDGDGDTDHEDGEEENPLEIKEQPKDTEEAGHE*EDI 4917
Cdd:PHA03169 65 GHRQTESDTETAEESRHGEKEERGQggPSG-----------SGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPAS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4918 NEETEADQ-DEGQAQPQPEGGHSEDdkgeEGEEEMDTGADDGdQDAAEHPE*DTEEAPLSSED-KDKDTSEESPEKDTPL 4995
Cdd:PHA03169 134 HSPPPSPPsHPGPHEPAPPESHNPS----PNQQPSSFLQPSH-EDSPEEPEPPTSEPEPDSPGpPQSETPTSSPPPQSPP 208
|
170 180 190
....*....|....*....|....*....|...
gi 1131296855 4996 DQGLQPQTQEKEEGESSDMEEPVPEPTERKEHE 5028
Cdd:PHA03169 209 DEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPE 241
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4971-5250 |
2.00e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 60.37 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4971 EEAPLSSEDKDKDTSEESPEKDTPLDQGLQPQTQEKEEGESSDMEEPVPEPTERKEHESCGQ-----TGLESVQSEQAVE 5045
Cdd:PHA03169 28 GTREQAGRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQggpsgSGSESVGSPTPSP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5046 lAGAAPEK-EQGREEHGSGAADANQAEGHESsfmarmasqkhtrkntqsfkrkPGQADNErslGDHSErvhkrlrtmDTE 5124
Cdd:PHA03169 108 -SGSAEELaSGLSPENTSGSSPESPASHSPP----------------------PSPPSHP---GPHEP---------APP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5125 SRAEQDPAQpqaqAEDAEAFEHIKQGSEPYDAqtydvASTEQQQSAKDSSKAHEEEEVEDTSVDPEEQEElravDTEPlK 5204
Cdd:PHA03169 153 ESHNPSPNQ----QPSSFLQPSHEDSPEEPEP-----PTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGE----PQSP-T 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1131296855 5205 PEEVKSGSTAQPGSEEMEMETQtvKTEEDQHPRTDPSHEETENEKP 5250
Cdd:PHA03169 219 PQQAPSPNTQQAVEHEDEPTEP--EREGPPFPGHRSHSYTVVGWKP 262
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2218-2306 |
3.81e-08 |
|
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: 55.38 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 2218 SRGTFEWVDSMLVQALKSGDWLLMDNVNFCNPSVLDRLNALLEPGgvltvsERGMIDGSTPTVTPHPNFRLFLSMDPVHG 2297
Cdd:pfam07728 49 DPGGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDER------RLLLPDGGELVKAAPDGFRLIATMNPLDR 122
|
90
....*....|..
gi 1131296855 2298 ---EISRAMRNR 2306
Cdd:pfam07728 123 glnELSPALRSR 134
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1384-1540 |
5.24e-08 |
|
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: 55.46 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1384 EPVLLVGDTGCGKTTICQVFAALANQKLYSV---NCHLHMETSDFLGGLRPVRQKPNDKEEIDTSRLFewhdgpLVLAMK 1460
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGViyiDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLA------LALARK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1461 ED-GFFLLDEISLADDSVLERLNSVLEVEKTLLLAEKgnledkdnevelltaGKKFRILATMNPGGDFGKKELSPALRNR 1539
Cdd:smart00382 77 LKpDVLILDEITSLLDAEQEALLLLLEELRLLLLLKS---------------EKNLTVILTTNDEKDLGPALLRRRFDRR 141
|
.
gi 1131296855 1540 F 1540
Cdd:smart00382 142 I 142
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1353-1540 |
6.91e-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: 57.87 E-value: 6.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1353 MSTLESKF---SHIVWTEGMRRL---AMLVGRalqfsePVLLVGDTGCGKTTICQVFAALANQKLYSVNCHLHMETSDFL 1426
Cdd:COG0714 1 MTEARLRAeigKVYVGQEELIELvliALLAGG------HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1427 GglrpvrqkpndkEEI---DTSRlFEWHDGPlVLAmkedGFFLLDEISLADDsvlerlnsvlEVEKTLLLAekgnLEDK- 1502
Cdd:COG0714 75 G------------TYIydqQTGE-FEFRPGP-LFA----NVLLADEINRAPP----------KTQSALLEA----MEERq 122
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1131296855 1503 ---DNEVelLTAGKKFRILATMNPGGDFGKKELSPALRNRF 1540
Cdd:COG0714 123 vtiPGGT--YKLPEPFLVIATQNPIEQEGTYPLPEAQLDRF 161
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4783-5307 |
7.36e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4783 KTEETGPGMDEEDSELVAKDDnlDAGKSNREKTRQDKKEEKEEAEADDDGRGQDKINEQIDEREYDENEVDPYHGNEEKL 4862
Cdd:PTZ00121 1213 KAEEARKAEDAKKAEAVKKAE--EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKK 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4863 PEPEALDlpddlnldSEDKDgDGDTDHEDGEEENPLEikEQPKDTEEAGHE*EDINEETEADQDEGQAQPQPEGGHSEDD 4942
Cdd:PTZ00121 1291 KADEAKK--------AEEKK-KADEAKKKAEEAKKAD--EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEA 1359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4943 KGEEGEEEMDTGADDGDQDAAEHPE*DTEEAPLSSEDKDKdtSEESPEKDTPLdqglqpqtqEKEEGESSDMEEPVPEPT 5022
Cdd:PTZ00121 1360 EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK--AEEDKKKADEL---------KKAAAAKKKADEAKKKAE 1428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5023 ERKEHESCGQTGLESVQSEqavELAGAAPEKEQGrEEHGSGAADANQAEghessfmaRMASQKHTRKNTQSFKRKpgqAD 5102
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKAD---EAKKKAEEAKKA-EEAKKKAEEAKKAD--------EAKKKAEEAKKADEAKKK---AE 1493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5103 NERSLGDHSERVHKRLRTMDTESRAEQ-DPAQPQAQAEDAEAFEHIKQGSEPYDAQtyDVASTEQQQSAKDSSKAHE-EE 5180
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEaKKADEAKKAEEAKKADEAKKAEEKKKAD--ELKKAEELKKAEEKKKAEEaKK 1571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5181 EVEDTSVDPEEQEELRAVD-------------TEPLKPEEVKSGSTAQPGSEEMEMETQTVKTEEDQHPRtdpshEETEN 5247
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEearieevmklyeeEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK-----EAEEK 1646
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5248 EKPERSRDStihtahqllvdtifqpflKDVNELRQELERQLEtwqphesgnpEEEKA*AE 5307
Cdd:PTZ00121 1647 KKAEELKKA------------------EEENKIKAAEEAKKA----------EEDKKKAE 1678
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4878-5053 |
2.06e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 57.29 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4878 SEDKDGDGdTDHEDGEEENPLEIKEQPKDTEEAGHE*EDINEETEADQ-DEGQAQPQPEGGHSEDDKGEEGEEEMDTGAD 4956
Cdd:PHA03169 83 EKEERGQG-GPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPEsPASHSPPPSPPSHPGPHEPAPPESHNPSPNQ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4957 DGDQDAAEHPE*DTEEAPLSSEDKDKDTSEESPEKDTPLDQGlqpqtqekEEGESSDMEEPVPEPTERKEHESCGQTGLE 5036
Cdd:PHA03169 162 QPSSFLQPSHE-DSPEEPEPPTSEPEPDSPGPPQSETPTSSP--------PPQSPPDEPGEPQSPTPQQAPSPNTQQAVE 232
|
170
....*....|....*..
gi 1131296855 5037 SVQSEQAVELAGAAPEK 5053
Cdd:PHA03169 233 HEDEPTEPEREGPPFPG 249
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1016-1316 |
2.22e-07 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 57.09 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1016 SGNIKSLLKQPIPEPKGGRLIQVEGYWISVGDKEPTIDETYILTSSVKLNLRDIVRVVSAGTYP--VLIQGETSVGKTSL 1093
Cdd:COG1401 158 LEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKFEETLEAFLAALKTKknVILAGPPGTGKTYL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1094 IRWLAAATG---NHCVRI-----NNHEHTDIQEYigcYTSDSSGKLVFKEGVLIDAMRKG-------YWIILDELNLAPT 1158
Cdd:COG1401 238 ARRLAEALGgedNGRIEFvqfhpSWSYEDFLLGY---RPSLDEGKYEPTPGIFLRFCLKAeknpdkpYVLIIDEINRANV 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1159 D--------VLEALNRLLDDNRELLITETQEVVKAHPRFMLFATQNPP--GLYGGRKVLSRAFRNRFVELHFDELPSSEL 1228
Cdd:COG1401 315 EkyfgellsLLESDKRGEELSIELPYSGEGEEFSIPPNLYIIGTMNTDdrSLALSDKALRRRFTFEFLDPDLDKLSNEEV 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1229 ETILHKrcslppsycsklVKVMLDLQSYRRGSSVFAGKQGFITLRDLFRWAERYRLAEQTEKEYDWLQHLANDGFMLLAG 1308
Cdd:COG1401 395 VDLLEE------------LNEILEKRDFQIGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLLDKLDLLGMAEFEDRLE 462
|
....*...
gi 1131296855 1309 RVRKQEEV 1316
Cdd:COG1401 463 LSEYLPLL 470
|
|
| AAA_3 |
pfam07726 |
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ... |
1749-1888 |
2.34e-07 |
|
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 429622 [Multi-domain] Cd Length: 131 Bit Score: 52.95 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1749 ILLEGSPGVGKTSLVGALARASGNTLVRINLSEQTDITDLFGADLPVEggKGGEFAWRDGPLLAALkaghwVVLDELNLA 1828
Cdd:pfam07726 2 VLLEGVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGTEVFDQ--KTREFEFRPGPVFANV-----LLADEINRA 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131296855 1829 S---QSVLegLNACFDHR----GEIY-VPELGMsfqvqhektkIFGCQNPFRQGGGRKgLPRSFLNRF 1888
Cdd:pfam07726 75 PpktQSAL--LEAMQERQvtidGETHpLPEPFF----------VLATQNPIEQEGTYP-LPEAQLDRF 129
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4677-5233 |
3.09e-07 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 57.33 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4677 KDVSDQIENEEQAEDTFQKGQEKDKEDPDSKSDIKGEDNAIEMSEDFDgkmhdgeleeqeeddeksdsETGDLDKQMGDL 4756
Cdd:COG5271 588 EESADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEEEAAED--------------------EAAEPETDASEA 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4757 NGEEADklderlwgddddeeDEEEDSKTEETGPGMDEEDSELVAKDDNLDAGKSNREKTRqdkkeekeeaeadddgrgqd 4836
Cdd:COG5271 648 ADEDAD--------------AETEAEASADESEEEAEDESETSSEDAEEDADAAAAEASD-------------------- 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4837 kineqiDEREYDENEVDPYHGNEEKLPEpealdlpddlnldSEDKDGDGDTDHEDGEEENPLEIKEQPKDTEEAGHE*ED 4916
Cdd:COG5271 694 ------DEEETEEADEDAETASEEADAE-------------EADTEADGTAEEAEEAAEEAESADEEAASLPDEADAEEE 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4917 INEETEADQDEGQAQPQpegghseddkgeegeeemdtgADDGDQDAAEHPE*DTEEAPLSSEDKDKDTSEESPEKDTPLD 4996
Cdd:COG5271 755 AEEAEEAEEDDADGLEE---------------------ALEEEKADAEEAATDEEAEAAAEEKEKVADEDQDTDEDALLD 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4997 QglqpqtQEKEEGESSDMEEPvpepterKEHESCGQTgLESVQSEQAVELAGAAPEKEQGREEhgsGAADANQAEGHESS 5076
Cdd:COG5271 814 E------AEADEEEDLDGEDE-------ETADEALED-IEAGIAEDDEEDDDAAAAKDVDADL---DLDADLAADEHEAE 876
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5077 fmarmasqkHTRKNTQSfkrkpGQADNERSLGDHSERVHKRLRTMDTESRAEQDPAQPQAQA------EDAEAFEHIKQG 5150
Cdd:COG5271 877 ---------EAQEAETD-----ADADADAGEADSSGESSAAAEDDDAAEDADSDDGANDEDDdddaeeERKDAEEDELGA 942
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5151 SEPYDAQTYDVASTEQQQSAKDSSKAHEEE-EVEDTSVDPEEQEELRAVDTEPLKPEEVKSGSTAQPGSEEMEMETQTVK 5229
Cdd:COG5271 943 AEDDLDALALDEAGDEESDDAAADDAGDDSlADDDEALADAADDAEADDSELDASESTGEAEGDEDDDELEDGEAAAGEA 1022
|
....
gi 1131296855 5230 TEED 5233
Cdd:COG5271 1023 TADL 1026
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4684-5308 |
3.78e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4684 ENEEQAEDTFQKGQEKDKEDPDSKSDIKGEDNAIEMSEDfdgkmhdgeLEEQEEDDEKSDSETGDLDKQMGDLNGEEADK 4763
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEE---------ERNNEEIRKFEEARMAHFARRQAAIKAEEARK 1279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4764 LDErlwgddddeedeeeDSKTEETGPGMDEEDSELVAKDDNL-----DAGKSN--REKTRQDKKEEKEEAEADDDGRGQD 4836
Cdd:PTZ00121 1280 ADE--------------LKKAEEKKKADEAKKAEEKKKADEAkkkaeEAKKADeaKKKAEEAKKKADAAKKKAEEAKKAA 1345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4837 KINEQIDEREYDENEVDPYHGNEEKLPEPEALDLPDDLNLDSEDKDgDGDTDHEDGEEENplEIKEQPKDTEEAGHE*ED 4916
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK-KADEAKKKAEEDK--KKADELKKAAAAKKKADE 1422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4917 INEETEADQDEGQAQPQPEgghseddkgeegeeeMDTGADDGDQDAAEhpE*DTEEAPLSSEDKDKdtSEESPEKdtpld 4996
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAE---------------EAKKADEAKKKAEE--AKKAEEAKKKAEEAKK--ADEAKKK----- 1478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4997 qglqPQTQEKEEGESSDMEEPVPEPTERKEHESCGQTGLESVQSEQA--VELAGAAPEKEQGRE----EHGSGAADANQA 5070
Cdd:PTZ00121 1479 ----AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAkkADEAKKAEEAKKADEakkaEEKKKADELKKA 1554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5071 EGHESSFMARMASQK---HTRKNTQSFK----RKPGQADNERSLGDHSERVHKRLRTMDTESRAEQDPAQPQAQAEDAEA 5143
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAkkaEEDKNMALRKaeeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5144 FEHIKQGSEPYDAQTYDVASTEQQQSAKDSSKAHEEEEVEDTS--VDPEEQEELRAVDTEPLKPEEV-KSGSTAQPGSEE 5220
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAEEAkKAEELKKKEAEE 1714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5221 MEMETQTVKTEEDQHPRTDPSHEETENEKpERSRDSTIHTAHQLLVDTIFQPFLKDVNELRQELERQLEtwqphESGNPE 5300
Cdd:PTZ00121 1715 KKKAEELKKAEEENKIKAEEAKKEAEEDK-KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE-----EELDEE 1788
|
....*...
gi 1131296855 5301 EEKA*AEM 5308
Cdd:PTZ00121 1789 DEKRRMEV 1796
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4897-5075 |
8.18e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 55.36 E-value: 8.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4897 PLEIKEQPKDTEEAGHE*EDINEETEADQDEGQAQPQPEGGHS----------EDDKGEEGEEemdtGADDGDQDAAEH- 4965
Cdd:PHA03169 51 PTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSgsgsesvgspTPSPSGSAEE----LASGLSPENTSGs 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4966 -PE*DTEEAPLSSEDKDKDTSEESPEKDTPLDQGLQPQTQEKEEGESSDmeEPVPEPTERKEHESCGqtGLESVQSEQAV 5044
Cdd:PHA03169 127 sPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSP--EEPEPPTSEPEPDSPG--PPQSETPTSSP 202
|
170 180 190
....*....|....*....|....*....|.
gi 1131296855 5045 ELAGAAPEKEQGREEHGSGAADANQAEGHES 5075
Cdd:PHA03169 203 PPQSPPDEPGEPQSPTPQQAPSPNTQQAVEH 233
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1747-1896 |
1.24e-06 |
|
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: 51.38 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1747 KPILLEGSPGVGKTSLVGALARAS---GNTLVRINLSeqtditDLFGADlpVEGGKGGEFAWRDGPLLAALKAGHWVVLD 1823
Cdd:cd00009 20 KNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNAS------DLLEGL--VVAELFGHFLVRLLFELAEKAKPGVLFID 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131296855 1824 ELNLASQSVLEGLNACFdhrgeiyvpELGMSFQVQHEKTKIFG-CQNPFRQgggrkGLPRSFLNRFTQVFVDPL 1896
Cdd:cd00009 92 EIDSLSRGAQNALLRVL---------ETLNDLRIDRENVRVIGaTNRPLLG-----DLDRALYDRLDIRIVIPL 151
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4782-5028 |
1.50e-06 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 55.00 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4782 SKTEETGpgmDEEDSELVAKDDNLDAGKSNREKTRQDKKEEKEEAEADDDGRGQDkinEQIDEREYDENEVDpyHGNEEK 4861
Cdd:TIGR00927 640 HTGERTG---EEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKG---EQEGEGEIEAKEAD--HKGETE 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4862 LPEPEAldlpddlnldSEDKDGDGDTDHEDGEEENPLEIKEQPKDTE-EAGHE*E------------DINEETEADQDEG 4928
Cdd:TIGR00927 712 AEEVEH----------EGETEAEGTEDEGEIETGEEGEEVEDEGEGEaEGKHEVEtegdrketehegETEAEGKEDEDEG 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4929 QAQPQPEGGH---------SEDDKGEEGEEEMDTGADDGDQDAAEHPE*DTEEAPLSSEDKDKDTSEESPEKDTPLDQGL 4999
Cdd:TIGR00927 782 EIQAGEDGEMkgdegaegkVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDGG 861
|
250 260
....*....|....*....|....*....
gi 1131296855 5000 QPQTQEKEEGESSDMEEPVPEPTERKEHE 5028
Cdd:TIGR00927 862 DSEEEEEEEEEEEEEEEEEEEEEEEEEEN 890
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4958-5250 |
2.26e-06 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 54.62 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4958 GDQDAAEHPE*DT---EEAPLSSEDKDKDTSEESPEKDTPLDQGLQPQTQEKEEGESSDMEEPVPEpTERKEHESCGQTG 5034
Cdd:TIGR00927 633 GDVAEAEHTGERTgeeGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGE-IEAKEADHKGETE 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5035 LESVQSEQAVELAGAAPEKEQGREEHGS--GAADANQAEGHESsfmarmasqkhtrkntqsfkrkpGQADNERSLGDHse 5112
Cdd:TIGR00927 712 AEEVEHEGETEAEGTEDEGEIETGEEGEevEDEGEGEAEGKHE-----------------------VETEGDRKETEH-- 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5113 rvhkrlrtmDTESRAEQDPAQPQAQAEDAEAFEHikQGSEpyDAQTYDVASTEQQQSAKDSSKAHEEEEVEDTSVDPEEQ 5192
Cdd:TIGR00927 767 ---------EGETEAEGKEDEDEGEIQAGEDGEM--KGDE--GAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETG 833
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5193 E-ELRAVDT-EPLKPEEVKSGSTAQPGSEEMEMETQTVKTEEDQHPRTDPSHEETENEKP 5250
Cdd:TIGR00927 834 EqELNAENQgEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEP 893
|
|
| Granin |
pfam01271 |
Granin (chromogranin or secretogranin); |
4890-5363 |
4.98e-06 |
|
Granin (chromogranin or secretogranin);
Pssm-ID: 279595 [Multi-domain] Cd Length: 584 Bit Score: 53.11 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4890 EDGEEENP-LEIKE--QPKDTEEAGH--E*EDINEETEADQDEGQAQPQPE---GGHSEDDKGEEGEEEMDTGADDGDQD 4961
Cdd:pfam01271 47 ERSENYNPyFEVRLlrDLADQSEASHlsSRSRDGLSDEDMQIITEALRQAEnepGGHSRENQPYALQVEKEFKTDHSDDY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4962 AAEHPE*DtEEAPLSSEDKDKDTSEESPEKDTpldqGLQPQTQEKEEGESSdMEEPVPEPTERKEHESCGQTGLESVQ-S 5040
Cdd:pfam01271 127 ETQQWEEE-KLKHMRFPLRYEENSEEKHSERE----GELSEVFENPRSQAT-LKKVFEEVSRLDTPSKQKREKSDEREkS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5041 EQAVELAGAAPEKEQGrEEHGSGAADANQAEGHESsfmarmASQKHTRkntqsfkrkpgqadnerslgDHSERVHKRLRT 5120
Cdd:pfam01271 201 SQESGEDTYRQENIPQ-EDQVGPEDQEPSEEGEED------ATQEEVK--------------------RSRPRTHHGRSL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5121 MDTESRAEQDPAQPQAQAEDAEAFEHIK--QGSEPYDAQTYDVASTEQQQSAKDSSKAHEEEEVEDTSVDPEEQEELRAV 5198
Cdd:pfam01271 254 PDESSRGGQLGLEEEASEEEEEYGEESRglSAVQTYLLRLVNARGRGRSEKRAERERSEESEEEELKRASPYEELEITAN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5199 ----DTEPLKPEEVKSGSTAQPGSEEMEMETQTVKTE----EDQHPRTDPSHEETENEKPERSRDStihtahqllvdtif 5270
Cdd:pfam01271 334 lqipPSEEERMLKKAGRSPRGRVDEAGALEALEALEEkrklDLDHSRVFESSEDGAPRAPQGAWVE-------------- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5271 qpflKDVNELRQELERQLETWQ---PHESGNPEEEKA*AEMWQSYLVLTAPL--SQQLCEQLRLILEPTQAAKLKGDYRT 5345
Cdd:pfam01271 400 ----ALRNYLSYGEEGMEGKWNqqgPYFPNEENREEARFRLPQYLGELSNPWedPKQWKPSDFERKELTADKFLEGEEEN 475
|
490 500
....*....|....*....|.
gi 1131296855 5346 GKRLNMRKVIP---YIASQFR 5363
Cdd:pfam01271 476 EYTLSMKNSFPeynYDGYEKR 496
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1385-1618 |
6.01e-06 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 52.43 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1385 PVLLVGDTGCGKTTICQVFAALANQKLYSVNchlhmetsdflgglrPVRQKPNDKEEIDTSRLFewHDGPLVLAMKEDGF 1464
Cdd:PHA02244 121 PVFLKGGAGSGKNHIAEQIAEALDLDFYFMN---------------AIMDEFELKGFIDANGKF--HETPFYEAFKKGGL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1465 FLLDEISLADDSVLERLNSVlevektllLAEKGnledKDNEVELLTAGKKFRILA---TMNPGGD---FGKKELSPALRN 1538
Cdd:PHA02244 184 FFIDEIDASIPEALIIINSA--------IANKF----FDFADERVTAHEDFRVISagnTLGKGADhiyVARNKIDGATLD 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1539 RFTEIWCPQSTKREDLIQIISRNLhpglslgrtdhkgadiaevmLDFIDWLTHQ--EFGRRCVVSIRDILSWVNFMNTMG 1616
Cdd:PHA02244 252 RFAPIEFDYDEKIEHLISNGDEDL--------------------VNFVALLRHEmaEKGLDHVFSMRAIIHGKKFDGVFE 311
|
..
gi 1131296855 1617 EE 1618
Cdd:PHA02244 312 AD 313
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1749-1784 |
1.04e-05 |
|
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: 47.97 E-value: 1.04e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1131296855 1749 ILLEGSPGVGKTSLVGALARASGNTLVRINLSEQTD 1784
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS 36
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1660-1828 |
1.85e-05 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 50.92 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1660 ARRECLKFLIKKLSKIGRLTESQKNELKIYDRLKDKEFTGIDNLWGIHPFFIPRGPVLHRNNIADYALSAGTTAMNAQRL 1739
Cdd:COG1401 135 ARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKFEETLEAF 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1740 LRATKLNKPILLEGSPGVGKTSLVGALARA-SGNTLVRINLseqtdIT---DLFGADLpVEG----GKGGEFAWRDGPLL 1811
Cdd:COG1401 215 LAALKTKKNVILAGPPGTGKTYLARRLAEAlGGEDNGRIEF-----VQfhpSWSYEDF-LLGyrpsLDEGKYEPTPGIFL 288
|
170 180
....*....|....*....|....
gi 1131296855 1812 -AALKAG------HWVVLDELNLA 1828
Cdd:COG1401 289 rFCLKAEknpdkpYVLIIDEINRA 312
|
|
| vWFA |
cd00198 |
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
5379-5536 |
1.98e-05 |
|
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.
Pssm-ID: 238119 [Multi-domain] Cd Length: 161 Bit Score: 48.33 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5379 YQICLAIDDSSSMVD---NHTKQLAfesLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEQFSDYSGSQILRLCKFQQK 5455
Cdd:cd00198 1 ADIVFLLDVSGSMGGeklDKAKEAL---KALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5456 -KTKIAQFLEsvanmfAAAQQLSQNVSPEIAQLLLVVSDGRglFLEGKDRVLAAVQAARNANIFVIFVVLDNPSSRDSIL 5534
Cdd:cd00198 78 gGTNIGAALR------LALELLKSAKRPNARRVIILLTDGE--PNDGPELLAEAARELRKLGITVYTIGIGDDANEDELK 149
|
..
gi 1131296855 5535 DI 5536
Cdd:cd00198 150 EI 151
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
1386-1626 |
2.66e-05 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 49.11 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1386 VLLVGDTGCGKTTICQVFAALANQKLYSVNCHLHMetSDFLGglrpvrqkpndkeeiDTSR----LFEwhdgplvLAMKE 1461
Cdd:COG1223 38 ILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLI--GSYLG---------------ETARnlrkLFD-------FARRA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1462 DGFFLLDEIsladDSV-LER--LNSVLEVEKTL--LLAEkgnLEDKDNEVELltagkkfrILATMNPggdfgkKELSPAL 1536
Cdd:COG1223 94 PCVIFFDEF----DAIaKDRgdQNDVGEVKRVVnaLLQE---LDGLPSGSVV--------IAATNHP------ELLDSAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1537 RNRFTEIWCPQSTKREDLIQIISRNLHP-GLSLGRTDHK---------GADIAEVMLDFIdwlthqefgRRCVVSIRDIL 1606
Cdd:COG1223 153 WRRFDEVIEFPLPDKEERKEILELNLKKfPLPFELDLKKlakkleglsGADIEKVLKTAL---------KKAILEDREKV 223
|
250 260
....*....|....*....|
gi 1131296855 1607 SWVNFMNTMGEEAALKRQET 1626
Cdd:COG1223 224 TKEDLEEALKQRKERKKEPK 243
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
1744-1781 |
4.27e-05 |
|
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: 47.28 E-value: 4.27e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1131296855 1744 KLNKPILLEGSPGVGKTSLVGALARASGNTLVRINLSE 1781
Cdd:cd19481 24 GLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSS 61
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1385-1543 |
1.61e-04 |
|
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: 45.21 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1385 PVLLVGDTGCGKTTICQVFA---ALANQKLYSVNCHLHMETSDFLGglrpvrqkpnDKEEIDTSRLFEwhdgplVLAMKE 1461
Cdd:cd00009 21 NLLLYGPPGTGKTTLARAIAnelFRPGAPFLYLNASDLLEGLVVAE----------LFGHFLVRLLFE------LAEKAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1462 DGFFLLDEISLADDSVLERLNSVLEVEKTLLLAEKGNledkdnevelltagkkFRILATMNPGGDfgkkELSPALRNRFT 1541
Cdd:cd00009 85 PGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRENV----------------RVIGATNRPLLG----DLDRALYDRLD 144
|
..
gi 1131296855 1542 EI 1543
Cdd:cd00009 145 IR 146
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1080-1215 |
1.76e-04 |
|
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: 44.51 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1080 VLIQGETSVGKTSLIRWLAAATGNHCVRINNHEHTDiqEYIGcytsDSSGKLvfkEGVLIDAMRKGYWII-LDELNLAPT 1158
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS--KYVG----ESEKRL---RELFEAAKKLAPCVIfIDEIDALAG 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1131296855 1159 DVLEALNRLLDDNRELLITETQEVVKAHPRFMLFATQNPPGLyggrkvLSRAFRNRF 1215
Cdd:pfam00004 72 SRGSGGDSESRRVVNQLLTELDGFTSSNSKVIVIAATNRPDK------LDPALLGRF 122
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1079-1221 |
1.84e-04 |
|
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: 45.06 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1079 PVLIQGETSVGKTSLIR---WLAAATGNHCVRIN----NHEHTDIQEYIGCYTSDSSGKLVFKEGVLIDAMRKGYW--II 1149
Cdd:smart00382 4 VILIVGPPGSGKTTLARalaRELGPPGGGVIYIDgediLEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPdvLI 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131296855 1150 LDELNLAPTDVLEALNRLLDDNRELLITEtqevvKAHPRFMLFATQNPPGLygGRKVLSRAFRNRFVELHFD 1221
Cdd:smart00382 84 LDEITSLLDAEQEALLLLLEELRLLLLLK-----SEKNLTVILTTNDEKDL--GPALLRRRFDRRIVLLLIL 148
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
320-432 |
1.86e-04 |
|
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: 45.21 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 320 ASQNAVLLEGPIGCGKTSLVEHLAAMTGRRKPSqLLKVQLGDqtdskMLLGMYRCTDVpGEFVWQPGTLTQAATKGHWIL 399
Cdd:cd00009 17 PPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-FLYLNASD-----LLEGLVVAELF-GHFLVRLLFELAEKAKPGVLF 89
|
90 100 110
....*....|....*....|....*....|...
gi 1131296855 400 LEDIDYAPLDVVSVLIPLLENGELLIPGRGDCV 432
Cdd:cd00009 90 IDEIDSLSRGAQNALLRVLETLNDLRIDRENVR 122
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1068-1221 |
1.88e-04 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 47.42 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1068 DIVRVVSAGTyPVLIQGETSVGKTSLIRWLAAAtgnhcVRINNHEHTDI-QEYIGCYTSDSSGKlvFKEGVLIDAMRKGY 1146
Cdd:PHA02244 111 DIAKIVNANI-PVFLKGGAGSGKNHIAEQIAEA-----LDLDFYFMNAImDEFELKGFIDANGK--FHETPFYEAFKKGG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1147 WIILDELNLAPTDVLEALNRLLDDNRELLITETqevVKAHPRFMLFATQNPPG-----LYGGRKVLSRAFRNRFVELHFD 1221
Cdd:PHA02244 183 LFFIDEIDASIPEALIIINSAIANKFFDFADER---VTAHEDFRVISAGNTLGkgadhIYVARNKIDGATLDRFAPIEFD 259
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4857-5076 |
2.44e-04 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 48.07 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4857 GNEEKLPEPEALDLPDDLNLDSEDKDGDGDTDHEDGEEENPLEIKEQPKDTEEAGHE*EDINEETEADQDEGQAQPQPEG 4936
Cdd:TIGR00927 646 GEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEG 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4937 GHSEDDKGEEGEEEMDTGADDGDQDAAEHPE*DTEEaplsseDKDKDTSEESPEKDTPLDQGlqpQTQEKEEGESSDMEE 5016
Cdd:TIGR00927 726 TEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDR------KETEHEGETEAEGKEDEDEG---EIQAGEDGEMKGDEG 796
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131296855 5017 PVPEPTERKEHESCGQTGLESVQSEQAVELAGAAPEKEQ--GREEHGSGAADANQAEGHESS 5076
Cdd:TIGR00927 797 AEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQelNAENQGEAKQDEKGVDGGGGS 858
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
1724-1800 |
2.90e-04 |
|
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: 45.25 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1724 DYALSAGTTAMNAQRLLrATKLNKPI---LLEGSPGVGKTSLVGALARA---SGNTLVRINLSEQT---DITDLFGADlP 1794
Cdd:cd19499 17 DEAVKAVSDAIRRARAG-LSDPNRPIgsfLFLGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYMekhSVSRLIGAP-P 94
|
....*.
gi 1131296855 1795 VEGGKG 1800
Cdd:cd19499 95 GYVGYT 100
|
|
| COG5644 |
COG5644 |
U3 small nucleolar RNA-associated protein 14 [Function unknown]; |
4786-5307 |
3.01e-04 |
|
U3 small nucleolar RNA-associated protein 14 [Function unknown];
Pssm-ID: 227931 [Multi-domain] Cd Length: 869 Bit Score: 47.39 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4786 ETGPGMDEEDSELVAkDDNLDA---GKSNREktrqdkkeekeeaEADDDGRGQDKINEQIDEREYDENEVDpyhGNEEKL 4862
Cdd:COG5644 57 DSDEAFDEEDEKRFA-DWSFNAsksGKSNKD-------------HKNLNNTKEISLNDSDDSVNSDKLENE---GSVSSI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4863 PEPEALDLPDDLNLDSEDKDGDGDTDHeDGEEENPLE---IKEQPKDTEEAGHE*EDINEETEADQDEGQAQPQPEGGHS 4939
Cdd:COG5644 120 DENELVDLDTLLDNDQPEKNESGNNDH-ATDKENLLEsdaSSSNDSESEESDSESEIESSDSDHDDENSDSKLDNLRNYI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4940 EDDKGEEGEEEMDTGADDGDQ-DAAEHPE*DTEEAPLSSEDKD-----------------KDTSEESPEKDTPLDQGLQP 5001
Cdd:COG5644 199 VSLKKDEADAESVLSSDDNDSiEEIKYDPHETNKESGSSETIDitdlldsipmeqlkvslKPLVSESSKLDAPLAKSIQD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5002 QTQEKEEGESSDME-------------------------EPVP---------EP---TERKEHESCGQTGLESVQSEQAV 5044
Cdd:COG5644 279 RLERQAAYEQTKNDlekwkpivadnrksdqlifpmnetaRPVPsnnglassfEPrteSERKMHQALLDAGLENESALKKQ 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5045 E---LAGAAPEKEQGREEHGSGAADANQAEGHESSFMARMASQ--KHTRKNTQSFKR----KPGQADNERS-LGDHSERV 5114
Cdd:COG5644 359 EelaLNKLSVEEVAERTRQLRFMRELMFREERKAKRVAKIKSKtyRKIRKNRKEKEMalipKSEDLENEKSeEARALERM 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5115 HKRLRTMDTESRAEQDPAQPQAQAEDaEAFEHIKQGSEpydaqtydvasTEQQQSAKDSSKAHEEEEVEDTSVDPEEQEe 5194
Cdd:COG5644 439 TQRHKNTSSWTRKMLERASHGEGTRE-AVNEQIRKGDE-----------LMQRIHGKEIMDGEDVSEFSDSDYDTNEQV- 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5195 lrAVDTEPLKPEEVKSG---------STAQPGSEEMEMETQTVKTEE----DQHPRTDPSHEETENEKPERSRDSTIHTA 5261
Cdd:COG5644 506 --STAFEKIRNEEELKGvlgmkfmrdASNRQMAASKISVADLVKVENgddiDVGELDEVGGDAIYANAGRREVFPVVEQR 583
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1131296855 5262 HQLLVDTIFQPFLKDVNELRQELERQLETWQPHESGNPEEEKA*AE 5307
Cdd:COG5644 584 RKLAPRKRKEDFVTPSTSLEKSMDRILHGQKKRAEGAVVFEKPLEA 629
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
2228-2294 |
3.03e-04 |
|
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of dynein heavy chain. The chain also contains ATPase activity and microtubule binding ability and acts as a motor for the movement of organelles and vesicles along microtubules. Dynein is also involved in cilia and flagella movement. The dynein subunit consists of at least two heavy chains and a number of intermediate and light chains. 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 C-terminal domain carries the D6 region of the dynein motor where the P-loop has been lost in evolution but the general structure of a potential ATP binding site appears to be retained.
Pssm-ID: 460782 Cd Length: 115 Bit Score: 43.59 E-value: 3.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131296855 2228 MLVQALKSGDWLLMDNVNFCnPSVLDRLNALLEpggvltvsergmidgSTPTVTPHPNFRLFLSMDP 2294
Cdd:pfam03028 49 LIEEAAKEGGWVLLQNCHLA-LSWMPELEKILE---------------ELPEETLHPDFRLWLTSEP 99
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
663-712 |
3.78e-04 |
|
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: 44.69 E-value: 3.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1131296855 663 LAVCVSKGEPVLLVGETGTGKTSTVQ-YLAHI--TGHRLRVVNMNQQSDTADL 712
Cdd:pfam12775 24 LDLLLKNGKPVLLVGPTGTGKTVIIQnLLRKLdkEKYLPLFINFSAQTTSNQT 76
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
1747-1782 |
4.28e-04 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 46.84 E-value: 4.28e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1131296855 1747 KPILLEGSPGVGKTSLVGALARASGNTLVRINLSEQ 1782
Cdd:PRK04195 40 KALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQ 75
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1079-1215 |
4.82e-04 |
|
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: 44.06 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1079 PVLIQGETSVGKTSLIR---WLAAATGNHCVRINNHEHTDIqeyigcyTSDSSGKLVFKEGVLIDAMRKGYW--IILDEL 1153
Cdd:cd00009 21 NLLLYGPPGTGKTTLARaiaNELFRPGAPFLYLNASDLLEG-------LVVAELFGHFLVRLLFELAEKAKPgvLFIDEI 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131296855 1154 NLAPTDVLEALNRLLDDnRELLITETQEVvkahpRFMLFATQNPPGLyggrkvLSRAFRNRF 1215
Cdd:cd00009 94 DSLSRGAQNALLRVLET-LNDLRIDRENV-----RVIGATNRPLLGD------LDRALYDRL 143
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
1736-1790 |
6.90e-04 |
|
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: 44.09 E-value: 6.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1131296855 1736 AQRLLRATKLNKPILLEGSPGVGKTSLVGALARASGNTLVRINLSEQTDITDLFG 1790
Cdd:cd19500 27 AVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRG 81
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
669-736 |
2.34e-03 |
|
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: 41.98 E-value: 2.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131296855 669 KGEPVLLVGETGTGKTSTVQYLAHI---TGHRLRVVNMNQQSDTADLLGGYKPVDHKLIWLPLREAFEELF 736
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLAL 71
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
4855-5023 |
2.47e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 44.20 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4855 YHGNEEKLPEPEALDlpddlnldSEDKDGD-GDTDHEDGEEEN-PLEIKEQPKDTEEAGHE*EDINEETEADQDEGQAQP 4932
Cdd:PRK13108 290 YVVDEALEREPAELA--------AAAVASAaSAVGPVGPGEPNqPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTP 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4933 QPEGGHSEDDKGEEGEEEMDTGADDGDQDAAEHPE*DTEEAPLSSEDKDkDTSEESPEKDTPLDQGLQPqtqekeegESS 5012
Cdd:PRK13108 362 AVEETSEADIEREQPGDLAGQAPAAHQVDAEAASAAPEEPAALASEAHD-ETEPEVPEKAAPIPDPAKP--------DEL 432
|
170
....*....|.
gi 1131296855 5013 DMEEPVPEPTE 5023
Cdd:PRK13108 433 AVAGPGDDPAE 443
|
|
| Granin |
pfam01271 |
Granin (chromogranin or secretogranin); |
4840-5186 |
2.72e-03 |
|
Granin (chromogranin or secretogranin);
Pssm-ID: 279595 [Multi-domain] Cd Length: 584 Bit Score: 44.25 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4840 EQIDEREYDenevdpYHGNEEKLPEPEALDLpddlnldsEDKDGDGDTDH-EDGEEEnplEIKEQPKDTEEAGHE*EDIN 4918
Cdd:pfam01271 192 EKSDEREKS------SQESGEDTYRQENIPQ--------EDQVGPEDQEPsEEGEED---ATQEEVKRSRPRTHHGRSLP 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4919 EET---------EADQDEGQAQPQPEGGHSEDDKGEEGEEEMDTGADDGDQdaaehpe*dtEEAPLSSEDKDKDTSEESP 4989
Cdd:pfam01271 255 DESsrggqlgleEEASEEEEEYGEESRGLSAVQTYLLRLVNARGRGRSEKR----------AERERSEESEEEELKRASP 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4990 EKDTPLDQGLQPQTQEKEEGessdmeepvPEPTERKEHEScgqtglesVQSEQAVELAGAAPEKEQGREEHgsgaadanq 5069
Cdd:pfam01271 325 YEELEITANLQIPPSEEERM---------LKKAGRSPRGR--------VDEAGALEALEALEEKRKLDLDH--------- 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 5070 aeghessfmarmASQKHTRKNTqsFKRKPGQADNErslgdhSERVHKRLRTMDTESRAEQDPAQPQAQAEDAEAFEHIKQ 5149
Cdd:pfam01271 379 ------------SRVFESSEDG--APRAPQGAWVE------ALRNYLSYGEEGMEGKWNQQGPYFPNEENREEARFRLPQ 438
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1131296855 5150 GSEPYDAQTYDVA----STEQQQSAKDSSKAHEEEEVEDTS 5186
Cdd:pfam01271 439 YLGELSNPWEDPKqwkpSDFERKELTADKFLEGEEENEYTL 479
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1386-1543 |
4.38e-03 |
|
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: 40.65 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1386 VLLVGDTGCGKTTICQVFAALANQKLYSVNChlhmetSDFLGGLRPVRQKpndkeeiDTSRLFEW--HDGPLVLamkedg 1463
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISG------SELVSKYVGESEK-------RLRELFEAakKLAPCVI------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 1464 ffLLDEIsladDSVL----ERLNSVLEVEKTLLLAEKGNLEDKDNEVELltagkkfrILATMNPGgdfgkkELSPALRNR 1539
Cdd:pfam00004 62 --FIDEI----DALAgsrgSGGDSESRRVVNQLLTELDGFTSSNSKVIV--------IAATNRPD------KLDPALLGR 121
|
....
gi 1131296855 1540 FTEI 1543
Cdd:pfam00004 122 FDRI 125
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4681-4935 |
4.42e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 43.83 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4681 DQIENEEQAEDTFQKGQEKD-----KEDPDSKSDIKGEDNAIEMSEDfDGKMHDGELEEQEEDDEKSDSETGDLDKQMGD 4755
Cdd:TIGR00927 665 GEAEQEGETETKGENESEGEipaerKGEQEGEGEIEAKEADHKGETE-AEEVEHEGETEAEGTEDEGEIETGEEGEEVED 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4756 LNGEEADKLDErlwGDDDDEEDEEEDSKTEETGPGMDEEDSELVAKDDNLDAGKSNREKTRQDKKEEKEEAEADDDGRGQ 4835
Cdd:TIGR00927 744 EGEGEAEGKHE---VETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSE 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4836 DKINEQIDEREYDENEVDPYHGNEEKLPEpealdlpddlnldsEDKDGDGDTDHEDGEEEnpleikEQPKDTEEAGHE*E 4915
Cdd:TIGR00927 821 TQADDTEVKDETGEQELNAENQGEAKQDE--------------KGVDGGGGSDGGDSEEE------EEEEEEEEEEEEEE 880
|
250 260
....*....|....*....|
gi 1131296855 4916 DINEETEADQDEGQAQPQPE 4935
Cdd:TIGR00927 881 EEEEEEEEENEEPLSLEWPE 900
|
|
| Sigma54_activ_2 |
pfam14532 |
Sigma-54 interaction domain; |
650-708 |
4.59e-03 |
|
Sigma-54 interaction domain;
Pssm-ID: 434021 [Multi-domain] Cd Length: 138 Bit Score: 40.79 E-value: 4.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1131296855 650 FAATRPSSVLIEQLAVCVSKGEPVLLVGETGTGKTSTVQYLAHITGHRLRVVNMNQQSD 708
Cdd:pfam14532 1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAH 59
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
1741-1790 |
5.23e-03 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 43.39 E-value: 5.23e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1131296855 1741 RATKLNKPIL-LEGSPGVGKTSLVGALARASGNTLVRINLSEQTDITDLFG 1790
Cdd:PRK10787 343 RVNKIKGPILcLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRG 393
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
659-780 |
7.29e-03 |
|
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: 40.59 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 659 LIEQL--AVCVSKGEPVLLVGETGTGKTSTVQYLAHITGHR-LRVVNMNqqsdTADLLGGYkpVDHKLIWLPLREAFEEL 735
Cdd:cd00009 6 AIEALreALELPPPKNLLLYGPPGTGKTTLARAIANELFRPgAPFLYLN----ASDLLEGL--VVAELFGHFLVRLLFEL 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1131296855 736 fvqtFSKKQNFT-FLGHIQTCYRQKRWQdLLKLMQHVHKSAVNKAG 780
Cdd:cd00009 80 ----AEKAKPGVlFIDEIDSLSRGAQNA-LLRVLETLNDLRIDREN 120
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
312-501 |
7.99e-03 |
|
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: 42.08 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 312 LQTLAMAVASQNAVLLEGPIGCGKTSLVEHLAAMTGRR----------KPSQLLKVQLGDQTDskmllgmyrctdvpGEF 381
Cdd:COG0714 21 IELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPfiriqftpdlLPSDILGTYIYDQQT--------------GEF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 382 VWQPGTLTQAatkghwILLED-IDYAPLDVVSVLIPLLENGELLIPGRGdcVKVAPGFQFFATRRLLSCGGnwYRPLnsH 460
Cdd:COG0714 87 EFRPGPLFAN------VLLADeINRAPPKTQSALLEAMEERQVTIPGGT--YKLPEPFLVIATQNPIEQEG--TYPL--P 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1131296855 461 ATLLDKYWTKIHLDNMDKAELNEVLQNRYPSLSAATDHLLD 501
Cdd:COG0714 155 EAQLDRFLLKLYIGYPDAEEEREILRRHTGRHLAEVEPVLS 195
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4830-5074 |
8.97e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 42.68 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4830 DDGRGQDkineqiDEREYDENEvdPYHGNEEKlpePEALDLPDDLNLDSEDKDGDGDTDHEDGEEENpleikeqPKDTEE 4909
Cdd:TIGR00927 653 TEAEGEN------GEESGGEAE--QEGETETK---GENESEGEIPAERKGEQEGEGEIEAKEADHKG-------ETEAEE 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4910 AGHE*EDineETEADQDEGQAQPQpEGGHSEDDKGEEGEEEMDTGADDGDQDAAEHpE*DTEEAPLSSEDKDKDTSEESP 4989
Cdd:TIGR00927 715 VEHEGET---EAEGTEDEGEIETG-EEGEEVEDEGEGEAEGKHEVETEGDRKETEH-EGETEAEGKEDEDEGEIQAGEDG 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131296855 4990 EKDTPlDQGLQPQTQEKEEGESSDMEEPVPEPTERKEHESCGQTGlesvQSEQAVELAGAAPEKEQGREehGSGAADANQ 5069
Cdd:TIGR00927 790 EMKGD-EGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETG----EQELNAENQGEAKQDEKGVD--GGGGSDGGD 862
|
....*
gi 1131296855 5070 AEGHE 5074
Cdd:TIGR00927 863 SEEEE 867
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
643-693 |
9.65e-03 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 40.21 E-value: 9.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1131296855 643 IQREKFTFAaTRPSSVLIEQLAVCVSKGEPVLLVGETGTGKTSTVQYLAHI 693
Cdd:cd03223 1 IELENLSLA-TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL 50
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
325-361 |
9.84e-03 |
|
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: 40.34 E-value: 9.84e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1131296855 325 VLLEGPIGCGKTSLVEHLAAMTGrrkpSQLLKVQLGD 361
Cdd:cd19481 29 ILLYGPPGTGKTLLAKALAGELG----LPLIVVKLSS 61
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