|
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 ... |
5325-5595 |
7.04e-145 |
|
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: 452.58 E-value: 7.04e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5325 LSQRLCEELRLILEPTQAAKLKGDYRTGKRLNIRKVIPYIASQFRKDKIWLRRTKPSKRQYQICLAIDDSSSMVDNHTKQ 5404
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5405 LAFESLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEQFSDYSGSQILRLCKFQQKKTKIAQFLESVASMFAAAQQlsQ 5484
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDART--Q 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5485 NISPEIAQLLLVVSDGRGLFLEGKERVLaaVQAARNANIFVIFVVLDNPSSRDSILDIKVPIFKGPGeMPEIRSYMEEFP 5564
Cdd:cd01460 159 SSSGSLWQLLLIISDGRGEFSEGAQKVR--LREAREQNVFVVFIIIDNPDNKQSILDIKVVSFKNDK-SGVITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|.
gi 1622932237 5565 FPYYIILRDVNALPETLSDALRQWFELVTAS 5595
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 |
3.43e-41 |
|
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: 148.50 E-value: 3.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 915 DLQVLIVDYLKGLSVNKNTVQGIINFYTALRKESGTKLVDGTGHRPHYSLRTLCRALRFAASN-PCGNIQRSLYEGFCLG 993
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLVRDIVKFYLEAKKLAEKSLVDGAGQRPHYSLRTLCRALSYARAIaPRYGLRRALYEGFCMS 80
|
90 100
....*....|....*....|....
gi 1622932237 994 FLTQLDRASHPIVQKLICQHIVSG 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 |
2.53e-27 |
|
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: 110.07 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1385 PVLLVGDTGCGKTTICQVFA-ALANQKLYSVSCHLHMETSDFLGGLrpvrqkpkdkeEIDTsRLFEWHDGPLVQAMKEDG 1463
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAaALSNRPVFYVQLTRDTTEEDLFGRR-----------NIDP-GGASWVDGPLVRAAREGE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622932237 1464 FFLLDEISLADDSVLERLNSVLEvEKSLVLAEKGSPEDKdsevelltAGKKFRILATMNPgGDFGKKELSPALRNRF 1540
Cdd:pfam07728 69 IAVLDEINRANPDVLNSLLSLLD-ERRLLLPDGGELVKA--------APDGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1900-1999 |
1.55e-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: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1900 DMEFIASTLFPaIEKNIVKKMVAFNNQIDHEVTVEKKWGQKGGPWEFNLRDLFRWCQLM-----LVDQSPGCYDPGQHVF 1974
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLssllpTLLSPTVREEIFLEAV 79
|
90 100
....*....|....*....|....*
gi 1622932237 1975 LVYGERMRTEEDKKKVIAVFKDVFG 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 |
8.73e-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: 97.36 E-value: 8.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1079 PVLIQGETSVGKTSLIQWLAAATGNHCVR-INNHEHTDIQEYIGCYTSDSSGKlVFKEGVLIDAMRKGYWIILDELNLAP 1157
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFyVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622932237 1158 TDVLEALNRLLDDNRELLVTETQEVVKAHPRFMLFATQNPPglYGGRKVLSRAFRNRF 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 |
1.06e-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: 95.83 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1227 ELETILHKRCSLPPSYCSKLVKVMLDLQSYRRSSSVFA--GKQGFITLRDLFRWAERYRLAEPTEKEYDWLQHLANDGYM 1304
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGssGSPREFNLRDLLRWCRRLSSLLPTLLSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....
gi 1622932237 1305 LLAGRVRKQEEVDVIQEVLEKHFK 1328
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLG 104
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
480-604 |
2.02e-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: 83.51 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 480 ELNEVLQSRYPSLLAVVDHLLEIYIQLTGEKHHSWSDRSVGceqapeevsearrenkrptlEGRELSLRDLLNWCNRIAH 559
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSG--------------------SPREFNLRDLLRWCRRLSS 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622932237 560 SFDSSSLSASL-NIFQEALDCFTAMLSEHTSKLKMAEVIGSKLNIS 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 ... |
325-453 |
2.79e-17 |
|
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: 81.57 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 325 VLLEGPIGCGKTSLVEYLAAMTGRTKppqLLKVQLGDQTDSKMLLGMYRCTdvPGEFVWQPGTLTQAATMGHWILLEDID 404
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRP---VFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622932237 405 YAPLDVVSVLIPLLENGDLLIP-GQGDCLKVAPGFQFFATRRLLSCGGNW 453
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLPdGGELVKAAPDGFRLIATMNPLDRGLNE 126
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
1748-1888 |
2.31e-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: 78.87 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1748 PILLEGSPGVGKTSLVGALAKA-SGNTLVRINLSEQTDITDLFGADLPveggKGGEFAWRDGPLLAALKAGHWVVLDELN 1826
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNI----DPGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622932237 1827 LASQSVLEGLNACFDHRgEIYVPELGMSFQVQHEKTKIFGCQNPfrQGGGRKGLPRSFLNRF 1888
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDGFRLIATMNP--LDRGLNELSPALRSRF 135
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4666-5259 |
4.19e-13 |
|
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: 76.59 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4666 SAGEGATEFHDYEGGGIGEGEGMKDVSDQIENEEQVEDTFQKGQEKDKEDPDSkSDIKGEDNAIEMSEDFDgkmhdgeLE 4745
Cdd:COG5271 257 SAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELTAAQAADPESDDDADD-STLAALEGAAEDTEIAT-------AD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4746 EQEEDDEKSDSEGGDLDKQMGDLNGEEADKLDERLWGDDDEEEDEEEEDNKTEETGPGMDEEDselvAKDDNLDSGNSNK 4825
Cdd:COG5271 329 ELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAA----ADDSADDEEASAD 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4826 DKSQKDKKEEKEESEADDGGEGEDKINEQID-EREYDENEVDpyhGNQEKLPEPEALDLPDDLNLDSEDKNG-------- 4896
Cdd:COG5271 405 GGTSPTSDTDEEEEEADEDASAGETEDESTDvTSAEDDIATD---EEADSLADEEEEAEAELDTEEDTESAEedadgdea 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4897 ----GEDTDNEEGEEENPLEIKEKPEEAGHEAEERETETDQNESQSPQEPEEGPSEDDKakgEEEMDTGADDQDGDAAQH 4972
Cdd:COG5271 482 tdedDASDDGDEEEAEEDAEAEADSDELTAEETSADDGADTDAAADPEDSDEDALEDET---EGEENAPGSDQDADETDE 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4973 PEEHSE-------EQQQSLEEKDKDADEEGGENGP-------ADQGFQPQKQEEEQEDSDTEEQVPEVLERKEHASCGQT 5038
Cdd:COG5271 559 PEATAEedepdeaEAETEDATENADADETEESADEseeaeasEDEAAEEEEADDDEADADADGAADEEETEEEAAEDEAA 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5039 GVENMQSTQAVELAGAAPEKEQGKEEHGSGAADANQAEGHESNFIAQLTSQKHTR--KNTQSFKRKPGQADNERSM---- 5112
Cdd:COG5271 639 EPETDASEAADEDADAETEAEASADESEEEAEDESETSSEDAEEDADAAAAEASDdeEETEEADEDAETASEEADAeead 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5113 ----GDHNERVHKRLRTVDTDSHAEQGPAQqpqaqvEDADAFEHIKQGSDAYDAQTYDVASKEQQQSAKDSGRDQEEEE- 5187
Cdd:COG5271 719 teadGTAEEAEEAAEEAESADEEAASLPDE------ADAEEEAEEAEEAEEDDADGLEEALEEEKADAEEAATDEEAEAa 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5188 ------IEDTLMDTEEQEELKAADVEQLKPEEIKSSTTAplgfDEM--EVEIQTVKTEEDQDPRTDRAHKETENEKPERS 5259
Cdd:COG5271 793 aeekekVADEDQDTDEDALLDEAEADEEEDLDGEDEETA----DEAleDIEAGIAEDDEEDDDAAAAKDVDADLDLDADL 868
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
672-902 |
7.12e-10 |
|
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: 60.38 E-value: 7.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 672 PVLLVGETGTGKTSTVQYLAH-ITGHRLRVVNMNQQSDTADLLGGYKPvdhkliwlplreafeelfaqtfskkqnftflg 750
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRNI-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 751 hiqtcyrqkrwhdllrlmqhvhksavnkdgkesetgllikekweafglrlnhaqqqmkmteNTLLFAFVEGTLAQAVKKG 830
Cdd:pfam07728 49 -------------------------------------------------------------DPGGASWVDGPLVRAAREG 67
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622932237 831 EWILLDEINLAAPEILECLSGLLEGSSgslVLLDRGDTEPLVRHPDFRLFACMNPAtDVGKRNLPPGIRNRF 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 ... |
2220-2306 |
2.52e-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: 55.76 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 2220 GTFEWVDSMLVQALKSGDWLLMDNVNFCNPSVLDRLNALLEPGgvltisERGMIDGSTPTITPNPNFRLFLSMDPVHGD- 2298
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDER------RLLLPDGGELVKAAPDGFRLIATMNPLDRGl 124
|
90
....*....|
gi 1622932237 2299 --ISRAMRNR 2306
Cdd:pfam07728 125 neLSPALRSR 134
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
659-780 |
1.47e-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: 42.52 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 659 LIEQL--AVCVSKGEPVLLVGETGTGKTSTVQYLAHITGHR-LRVVNMNqqsdTADLLGGYkpVDHKLIWLPLREAFEEL 735
Cdd:cd00009 6 AIEALreALELPPPKNLLLYGPPGTGKTTLARAIANELFRPgAPFLYLN----ASDLLEGL--VVAELFGHFLVRLLFEL 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622932237 736 FAqtfsKKQNFT-FLGHIQTCYRQKRWHdLLRLMQHVHKSAVNKDG 780
Cdd:cd00009 80 AE----KAKPGVlFIDEIDSLSRGAQNA-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 ... |
5325-5595 |
7.04e-145 |
|
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: 452.58 E-value: 7.04e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5325 LSQRLCEELRLILEPTQAAKLKGDYRTGKRLNIRKVIPYIASQFRKDKIWLRRTKPSKRQYQICLAIDDSSSMVDNHTKQ 5404
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5405 LAFESLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEQFSDYSGSQILRLCKFQQKKTKIAQFLESVASMFAAAQQlsQ 5484
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDART--Q 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5485 NISPEIAQLLLVVSDGRGLFLEGKERVLaaVQAARNANIFVIFVVLDNPSSRDSILDIKVPIFKGPGeMPEIRSYMEEFP 5564
Cdd:cd01460 159 SSSGSLWQLLLIISDGRGEFSEGAQKVR--LREAREQNVFVVFIIIDNPDNKQSILDIKVVSFKNDK-SGVITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|.
gi 1622932237 5565 FPYYIILRDVNALPETLSDALRQWFELVTAS 5595
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 |
3.43e-41 |
|
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: 148.50 E-value: 3.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 915 DLQVLIVDYLKGLSVNKNTVQGIINFYTALRKESGTKLVDGTGHRPHYSLRTLCRALRFAASN-PCGNIQRSLYEGFCLG 993
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLVRDIVKFYLEAKKLAEKSLVDGAGQRPHYSLRTLCRALSYARAIaPRYGLRRALYEGFCMS 80
|
90 100
....*....|....*....|....
gi 1622932237 994 FLTQLDRASHPIVQKLICQHIVSG 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 |
2.53e-27 |
|
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: 110.07 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1385 PVLLVGDTGCGKTTICQVFA-ALANQKLYSVSCHLHMETSDFLGGLrpvrqkpkdkeEIDTsRLFEWHDGPLVQAMKEDG 1463
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAaALSNRPVFYVQLTRDTTEEDLFGRR-----------NIDP-GGASWVDGPLVRAAREGE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622932237 1464 FFLLDEISLADDSVLERLNSVLEvEKSLVLAEKGSPEDKdsevelltAGKKFRILATMNPgGDFGKKELSPALRNRF 1540
Cdd:pfam07728 69 IAVLDEINRANPDVLNSLLSLLD-ERRLLLPDGGELVKA--------APDGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1900-1999 |
1.55e-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: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1900 DMEFIASTLFPaIEKNIVKKMVAFNNQIDHEVTVEKKWGQKGGPWEFNLRDLFRWCQLM-----LVDQSPGCYDPGQHVF 1974
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLssllpTLLSPTVREEIFLEAV 79
|
90 100
....*....|....*....|....*
gi 1622932237 1975 LVYGERMRTEEDKKKVIAVFKDVFG 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 |
8.73e-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: 97.36 E-value: 8.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1079 PVLIQGETSVGKTSLIQWLAAATGNHCVR-INNHEHTDIQEYIGCYTSDSSGKlVFKEGVLIDAMRKGYWIILDELNLAP 1157
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFyVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622932237 1158 TDVLEALNRLLDDNRELLVTETQEVVKAHPRFMLFATQNPPglYGGRKVLSRAFRNRF 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 |
1.06e-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: 95.83 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1227 ELETILHKRCSLPPSYCSKLVKVMLDLQSYRRSSSVFA--GKQGFITLRDLFRWAERYRLAEPTEKEYDWLQHLANDGYM 1304
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGssGSPREFNLRDLLRWCRRLSSLLPTLLSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....
gi 1622932237 1305 LLAGRVRKQEEVDVIQEVLEKHFK 1328
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLG 104
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
480-604 |
2.02e-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: 83.51 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 480 ELNEVLQSRYPSLLAVVDHLLEIYIQLTGEKHHSWSDRSVGceqapeevsearrenkrptlEGRELSLRDLLNWCNRIAH 559
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSG--------------------SPREFNLRDLLRWCRRLSS 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622932237 560 SFDSSSLSASL-NIFQEALDCFTAMLSEHTSKLKMAEVIGSKLNIS 604
Cdd:pfam17867 61 LLPTLLSPTVReEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
325-453 |
2.79e-17 |
|
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: 81.57 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 325 VLLEGPIGCGKTSLVEYLAAMTGRTKppqLLKVQLGDQTDSKMLLGMYRCTdvPGEFVWQPGTLTQAATMGHWILLEDID 404
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRP---VFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622932237 405 YAPLDVVSVLIPLLENGDLLIP-GQGDCLKVAPGFQFFATRRLLSCGGNW 453
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLPdGGELVKAAPDGFRLIATMNPLDRGLNE 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1748-1888 |
2.31e-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: 78.87 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1748 PILLEGSPGVGKTSLVGALAKA-SGNTLVRINLSEQTDITDLFGADLPveggKGGEFAWRDGPLLAALKAGHWVVLDELN 1826
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNI----DPGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622932237 1827 LASQSVLEGLNACFDHRgEIYVPELGMSFQVQHEKTKIFGCQNPfrQGGGRKGLPRSFLNRF 1888
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDGFRLIATMNP--LDRGLNELSPALRSRF 135
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4666-5259 |
4.19e-13 |
|
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: 76.59 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4666 SAGEGATEFHDYEGGGIGEGEGMKDVSDQIENEEQVEDTFQKGQEKDKEDPDSkSDIKGEDNAIEMSEDFDgkmhdgeLE 4745
Cdd:COG5271 257 SAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELTAAQAADPESDDDADD-STLAALEGAAEDTEIAT-------AD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4746 EQEEDDEKSDSEGGDLDKQMGDLNGEEADKLDERLWGDDDEEEDEEEEDNKTEETGPGMDEEDselvAKDDNLDSGNSNK 4825
Cdd:COG5271 329 ELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAA----ADDSADDEEASAD 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4826 DKSQKDKKEEKEESEADDGGEGEDKINEQID-EREYDENEVDpyhGNQEKLPEPEALDLPDDLNLDSEDKNG-------- 4896
Cdd:COG5271 405 GGTSPTSDTDEEEEEADEDASAGETEDESTDvTSAEDDIATD---EEADSLADEEEEAEAELDTEEDTESAEedadgdea 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4897 ----GEDTDNEEGEEENPLEIKEKPEEAGHEAEERETETDQNESQSPQEPEEGPSEDDKakgEEEMDTGADDQDGDAAQH 4972
Cdd:COG5271 482 tdedDASDDGDEEEAEEDAEAEADSDELTAEETSADDGADTDAAADPEDSDEDALEDET---EGEENAPGSDQDADETDE 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4973 PEEHSE-------EQQQSLEEKDKDADEEGGENGP-------ADQGFQPQKQEEEQEDSDTEEQVPEVLERKEHASCGQT 5038
Cdd:COG5271 559 PEATAEedepdeaEAETEDATENADADETEESADEseeaeasEDEAAEEEEADDDEADADADGAADEEETEEEAAEDEAA 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5039 GVENMQSTQAVELAGAAPEKEQGKEEHGSGAADANQAEGHESNFIAQLTSQKHTR--KNTQSFKRKPGQADNERSM---- 5112
Cdd:COG5271 639 EPETDASEAADEDADAETEAEASADESEEEAEDESETSSEDAEEDADAAAAEASDdeEETEEADEDAETASEEADAeead 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5113 ----GDHNERVHKRLRTVDTDSHAEQGPAQqpqaqvEDADAFEHIKQGSDAYDAQTYDVASKEQQQSAKDSGRDQEEEE- 5187
Cdd:COG5271 719 teadGTAEEAEEAAEEAESADEEAASLPDE------ADAEEEAEEAEEAEEDDADGLEEALEEEKADAEEAATDEEAEAa 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5188 ------IEDTLMDTEEQEELKAADVEQLKPEEIKSSTTAplgfDEM--EVEIQTVKTEEDQDPRTDRAHKETENEKPERS 5259
Cdd:COG5271 793 aeekekVADEDQDTDEDALLDEAEADEEEDLDGEDEETA----DEAleDIEAGIAEDDEEDDDAAAAKDVDADLDLDADL 868
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4914-5313 |
2.30e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.86 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4914 KEKPEEAGHEAEERETETDQNESQSpqepEEGPSEDDKAKGEEEmdtgaddQDGDAAQHPEEHSEEQQQSLEEKDKDADE 4993
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKA----EEAKKAAEAAKAEAE-------AAADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4994 ---EGGENGPADQgfqpqKQEEEQEDSDTEEQVPEVLERKEHASCGQTGVENMQstQAVELAGAAPEKEQGkEEHGSGAA 5070
Cdd:PTZ00121 1383 akkKAEEKKKADE-----AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK--KADEAKKKAEEAKKA-DEAKKKAE 1454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5071 DANQAE-----GHESNFIAQLTSQKHTRKNTQSFKRKpgqADNERSMGDHNERVHKRLRTVDTDSHAEQGPAQQPQAQVE 5145
Cdd:PTZ00121 1455 EAKKAEeakkkAEEAKKADEAKKKAEEAKKADEAKKK---AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5146 DADAFEHIKQGSDAYDAQtyDVASKEQQQSAKDSGR-DQEEEEIEDTLMDTEEQEELKaadveqlKPEEIKSSTTAPLGF 5224
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKAD--ELKKAEELKKAEEKKKaEEAKKAEEDKNMALRKAEEAK-------KAEEARIEEVMKLYE 1602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5225 DEMEVEIQTVKTEEDQDPRTDRAHKETENEKPERSRESTIHTAhqflmdtifqpfLKDVNELRQElERQLEMWQPHESEN 5304
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE------------KKKAEELKKA-EEENKIKAAEEAKK 1669
|
....*....
gi 1622932237 5305 PEEEKVAAE 5313
Cdd:PTZ00121 1670 AEEDKKKAE 1678
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1736-1888 |
3.39e-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: 64.80 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1736 AQRLLRATKLKKPILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQTDITDLFGADLPVEggKGGEFAWRDGPLLAAlk 1815
Cdd:COG0714 21 IELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQ--QTGEFEFRPGPLFAN-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1816 aghwVVL-DELNLAS---QS----VLEglnacfdhRGEIYVP----ELGMSFQVqhektkiFGCQNPFRQGGGRKgLPRS 1883
Cdd:COG0714 97 ----VLLaDEINRAPpktQSalleAME--------ERQVTIPggtyKLPEPFLV-------IATQNPIEQEGTYP-LPEA 156
|
....*
gi 1622932237 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 |
3.92e-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: 64.42 E-value: 3.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1079 PVLIQGETSVGKTSLIQWLAAATGNHCVRINNHEHTDIQEyiGCYTSD---SSGKLVFKEG------VLIdamrkgywii 1149
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSD--ILGTYIydqQTGEFEFRPGplfanvLLA---------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1150 lDELNLAPTDVLEALNRLLDDNRellVTETQEVVKAHPRFMLFATQNPPGLYGGRkVLSRAFRNRF-VELHFDeLPSSEL 1228
Cdd:COG0714 101 -DEINRAPPKTQSALLEAMEERQ---VTIPGGTYKLPEPFLVIATQNPIEQEGTY-PLPEAQLDRFlLKLYIG-YPDAEE 174
|
....*...
gi 1622932237 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 |
7.12e-10 |
|
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: 60.38 E-value: 7.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 672 PVLLVGETGTGKTSTVQYLAH-ITGHRLRVVNMNQQSDTADLLGGYKPvdhkliwlplreafeelfaqtfskkqnftflg 750
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRNI-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 751 hiqtcyrqkrwhdllrlmqhvhksavnkdgkesetgllikekweafglrlnhaqqqmkmteNTLLFAFVEGTLAQAVKKG 830
Cdd:pfam07728 49 -------------------------------------------------------------DPGGASWVDGPLVRAAREG 67
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622932237 831 EWILLDEINLAAPEILECLSGLLEGSSgslVLLDRGDTEPLVRHPDFRLFACMNPAtDVGKRNLPPGIRNRF 902
Cdd:pfam07728 68 EIAVLDEINRANPDVLNSLLSLLDERR---LLLPDGGELVKAAPDGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
5387-5537 |
6.94e-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: 58.62 E-value: 6.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5387 ICLAIDDSSSMVDNhTKQLAFESLAVIGNALTLLEVG-QIAVCSFGESVKLLHPFHeqfSDYSGSQILRLCKFQQKK--- 5462
Cdd:smart00327 2 VVFLLDGSGSMGGN-RFELAKEFVLKLVEQLDIGPDGdRVGLVTFSDDARVLFPLN---DSRSKDALLEALASLSYKlgg 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622932237 5463 -TKIAQFLESVASMFAAAQQLSQnisPEIAQLLLVVSDGRGLFleGKERVLAAVQAARNANIFVIFVVLDNPSSRD 5537
Cdd:smart00327 78 gTNLGAALQYALENLFSKSAGSR---RGAPKVVILITDGESND--GPKDLLKAAKELKRSGVKVFVVGVGNDVDEE 148
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2220-2306 |
2.52e-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: 55.76 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 2220 GTFEWVDSMLVQALKSGDWLLMDNVNFCNPSVLDRLNALLEPGgvltisERGMIDGSTPTITPNPNFRLFLSMDPVHGD- 2298
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDER------RLLLPDGGELVKAAPDGFRLIATMNPLDRGl 124
|
90
....*....|
gi 1622932237 2299 --ISRAMRNR 2306
Cdd:pfam07728 125 neLSPALRSR 134
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1383-1540 |
8.24e-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: 54.69 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1383 GEPVLLVGDTGCGKTTICQVFAALANQKLYSV---SCHLHMETSDFLGGLRPVRQKPKDKEEIDTSR-LFEwhdgpLVQA 1458
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGViyiDGEDILEEVLDQLLLIIVGGKKASGSGELRLRlALA-----LARK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1459 MKEDgFFLLDEISLADDSVLERLNSVLEVEKSLVLAEKgspedkdsevelltaGKKFRILATMNPGGDFGKKELSPALRN 1538
Cdd:smart00382 77 LKPD-VLILDEITSLLDAEQEALLLLLEELRLLLLLKS---------------EKNLTVILTTNDEKDLGPALLRRRFDR 140
|
..
gi 1622932237 1539 RF 1540
Cdd:smart00382 141 RI 142
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1372-1540 |
1.15e-07 |
|
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: 57.10 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1372 LAMLVGRalefgePVLLVGDTGCGKTTICQVFAALANQKLYSVSCHLHMETSDFLGglrpvrqkpkdkEEI---DTSRlF 1448
Cdd:COG0714 26 IALLAGG------HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILG------------TYIydqQTGE-F 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1449 EWHDGPLVQamkedGFFLLDEISLADDSVLerlNSVLEVekslvLAEKgspedkdsEV----ELLTAGKKFRILATMNPG 1524
Cdd:COG0714 87 EFRPGPLFA-----NVLLADEINRAPPKTQ---SALLEA-----MEER--------QVtipgGTYKLPEPFLVIATQNPI 145
|
170
....*....|....*.
gi 1622932237 1525 GDFGKKELSPALRNRF 1540
Cdd:COG0714 146 EQEGTYPLPEAQLDRF 161
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4918-5225 |
4.65e-07 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 56.93 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4918 EEAGHEAEERETETDQNESQSPQEPEEGP--SEDDKAKGEEEMDTGADDQDGDAaqhPEEHSEEQqqsleEKDKDADEEG 4995
Cdd:TIGR00927 632 KGDVAEAEHTGERTGEEGERPTEAEGENGeeSGGEAEQEGETETKGENESEGEI---PAERKGEQ-----EGEGEIEAKE 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4996 GENGPADQGFQPQKQEEEQEDSDTEEQVPEVLERKEhaSCGQTGVENMQSTQAVELAGAAPEKEQGKEEHGSGAADANQA 5075
Cdd:TIGR00927 704 ADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGE--EVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEG 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5076 EghesnfiaqltsqkhtrknTQSFKRKPGQADNERSMGDHNERVHKrlrTVDTDSHAEQGPAQQPQAQVEDadafehiKQ 5155
Cdd:TIGR00927 782 E-------------------IQAGEDGEMKGDEGAEGKVEHEGETE---AGEKDEHEGQSETQADDTEVKD-------ET 832
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622932237 5156 GSDAYDAQTYDVASKEQQ----QSAKDSGRDQEEEEIEDTLMDTEEQEElkaadveqlKPEEIKSSTTAPLGFD 5225
Cdd:TIGR00927 833 GEQELNAENQGEAKQDEKgvdgGGGSDGGDSEEEEEEEEEEEEEEEEEE---------EEEEEEEENEEPLSLE 897
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1746-1896 |
6.37e-07 |
|
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: 52.15 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1746 KKPILLEGSPGVGKTSLVGALAKAS---GNTLVRINLSeqtditDLFGADlpVEGGKGGEFAWRDGPLLAALKAGHWVVL 1822
Cdd:cd00009 19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNAS------DLLEGL--VVAELFGHFLVRLLFELAEKAKPGVLFI 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622932237 1823 DELNLASQSVLEGLNACFdhrgeiyvpELGMSFQVQHEKTKIFG-CQNPFRQgggrkGLPRSFLNRFTQVFVDPL 1896
Cdd:cd00009 91 DEIDSLSRGAQNALLRVL---------ETLNDLRIDRENVRVIGaTNRPLLG-----DLDRALYDRLDIRIVIPL 151
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1301-1618 |
1.60e-06 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 54.35 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1301 DGYMLLAGRVRKQEEVDVIQEVLEKHFKKKLcpqSLFSKENVVKLLGKLSTQISTLESNFGHIVWTEGMR--RLAMLVGR 1378
Cdd:PHA02244 42 DAIREKAETEGKEIAIDDIKKEIEDSPEEQF---FELPVKIELQQEGKPAGDISGIDTTKIASNPTFHYEtaDIAKIVNA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1379 ALefgePVLLVGDTGCGKTTICQVFAALANQKLYSvschlhmetsdflggLRPVRQKPKDKEEIDTSRLFewHDGPLVQA 1458
Cdd:PHA02244 119 NI----PVFLKGGAGSGKNHIAEQIAEALDLDFYF---------------MNAIMDEFELKGFIDANGKF--HETPFYEA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1459 MKEDGFFLLDEISLADDSVLERLNSVLevekslvlaekgSPEDKDSEVELLTAGKKFRILA---TMNPGGD---FGKKEL 1532
Cdd:PHA02244 178 FKKGGLFFIDEIDASIPEALIIINSAI------------ANKFFDFADERVTAHEDFRVISagnTLGKGADhiyVARNKI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1533 SPALRNRFTEIWCPQSTSREDLIQIINHNLrpglclgridpkgsdipevmLDFIDWLTHQ--EFGRKCVVSIRDILSWVN 1610
Cdd:PHA02244 246 DGATLDRFAPIEFDYDEKIEHLISNGDEDL--------------------VNFVALLRHEmaEKGLDHVFSMRAIIHGKK 305
|
....*...
gi 1622932237 1611 FMNKMGEE 1618
Cdd:PHA02244 306 FDGVFEAD 313
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1068-1221 |
3.83e-05 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 49.73 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1068 DIVRVVSAGTyPVLIQGETSVGKTSLIQWLAAAtgnhcVRINNHEHTDI-QEYIGCYTSDSSGKlvFKEGVLIDAMRKGY 1146
Cdd:PHA02244 111 DIAKIVNANI-PVFLKGGAGSGKNHIAEQIAEA-----LDLDFYFMNAImDEFELKGFIDANGK--FHETPFYEAFKKGG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1147 WIILDELNLAPTDVLEALNRLLDDNRELLVTETqevVKAHPRFMLFATQNPPG-----LYGGRKVLSRAFRNRFVELHFD 1221
Cdd:PHA02244 183 LFFIDEIDASIPEALIIINSAIANKFFDFADER---VTAHEDFRVISAGNTLGkgadhIYVARNKIDGATLDRFAPIEFD 259
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
1746-1782 |
2.23e-04 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 47.61 E-value: 2.23e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1622932237 1746 KKPILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQ 1782
Cdd:PRK04195 39 KKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQ 75
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1368-1543 |
2.25e-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: 44.83 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1368 GMRRLAMLVGRALEFGEP--VLLVGDTGCGKTTICQVFAALANQKLYSVschLHMETSDFLGGLRpvrqkpkdKEEIDTS 1445
Cdd:cd00009 2 GQEEAIEALREALELPPPknLLLYGPPGTGKTTLARAIANELFRPGAPF---LYLNASDLLEGLV--------VAELFGH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1446 RLFEWHDGPLVQAMKedGFFLLDEISLADDSVLERLNSVLEVekslvlaekgspedkdsEVELLTAGKKFRILATMNPGG 1525
Cdd:cd00009 71 FLVRLLFELAEKAKP--GVLFIDEIDSLSRGAQNALLRVLET-----------------LNDLRIDRENVRVIGATNRPL 131
|
170
....*....|....*...
gi 1622932237 1526 DFgkkELSPALRNRFTEI 1543
Cdd:cd00009 132 LG---DLDRALYDRLDIR 146
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1079-1221 |
3.83e-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: 44.29 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1079 PVLIQGETSVGKTSLIQ---WLAAATGNHCVRIN----NHEHTDIQEYIGCYTSDSSGKLVFKEGVLIDAMRKGYW--II 1149
Cdd:smart00382 4 VILIVGPPGSGKTTLARalaRELGPPGGGVIYIDgediLEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPdvLI 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622932237 1150 LDELNLAPTDVLEALNRLLDDNRELLVTEtqevvKAHPRFMLFATQNPPGLygGRKVLSRAFRNRFVELHFD 1221
Cdd:smart00382 84 LDEITSLLDAEQEALLLLLEELRLLLLLK-----SEKNLTVILTTNDEKDL--GPALLRRRFDRRIVLLLIL 148
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
669-737 |
7.90e-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: 43.13 E-value: 7.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622932237 669 KGEPVLLVGETGTGKTSTVQYLAHI---TGHRLRVVNMNQQSDTADLLGGYKPVDHKLIWLPLREAFEELFA 737
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALA 72
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1079-1215 |
1.16e-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: 42.90 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1079 PVLIQGETSVGKTSLIQ---WLAAATGNHCVRINNHEHTDIqeyigcyTSDSSGKLVFKEGVLIDAMRKGYW--IILDEL 1153
Cdd:cd00009 21 NLLLYGPPGTGKTTLARaiaNELFRPGAPFLYLNASDLLEG-------LVVAELFGHFLVRLLFELAEKAKPgvLFIDEI 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622932237 1154 NLAPTDVLEALNRLLDDnRELLVTETQEVvkahpRFMLFATQNPPGLyggrkvLSRAFRNRF 1215
Cdd:cd00009 94 DSLSRGAQNALLRVLET-LNDLRIDRENV-----RVIGATNRPLLGD------LDRALYDRL 143
|
|
| TFIIF_alpha |
pfam05793 |
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation ... |
4914-5045 |
1.28e-03 |
|
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation factor IIF, alpha subunit (TFIIF-alpha) or RNA polymerase II-associating protein 74 (RAP74) is the large subunit of transcription factor IIF (TFIIF), which is essential for accurate initiation and stimulates elongation by RNA polymerase II.
Pssm-ID: 310411 [Multi-domain] Cd Length: 528 Bit Score: 45.33 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4914 KEKPEEAGHEA----------EERETETDQNESQSPQEPEegpsEDDKAKGEEEMDTGADDQDGDAAQHPEEHSEEQQQs 4983
Cdd:pfam05793 258 KKKKRGGDDDAfeydsddgddEGREEDYISDSSASGNDPE----EREDKLSPEEPAKGEIEQSDDSEESEEEKNEEEGK- 332
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622932237 4984 LEEKDKDADEEGGENGPADQGFQPQKQEEEQEDSDTEEQVPEVLERKEHASCGQTGVENMQS 5045
Cdd:pfam05793 333 LSKKGKKAKKLKGKKNGKDKSESSDGDDSDDSDIDDEDSVPLFTAKKKKEPKKEEPVDSGPS 394
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
659-780 |
1.47e-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: 42.52 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 659 LIEQL--AVCVSKGEPVLLVGETGTGKTSTVQYLAHITGHR-LRVVNMNqqsdTADLLGGYkpVDHKLIWLPLREAFEEL 735
Cdd:cd00009 6 AIEALreALELPPPKNLLLYGPPGTGKTTLARAIANELFRPgAPFLYLN----ASDLLEGL--VVAELFGHFLVRLLFEL 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622932237 736 FAqtfsKKQNFT-FLGHIQTCYRQKRWHdLLRLMQHVHKSAVNKDG 780
Cdd:cd00009 80 AE----KAKPGVlFIDEIDSLSRGAQNA-LLRVLETLNDLRIDREN 120
|
|
| ChlD |
COG1240 |
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
5296-5540 |
1.69e-03 |
|
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];
Pssm-ID: 440853 [Multi-domain] Cd Length: 262 Bit Score: 43.77 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5296 MWQPHESENPEEEKVAAEMWQSYLILTAPLSQRLCEELRLILEPTQAAKLKGDYRTGKRLNIRKVIPYIASQFRKDKIWL 5375
Cdd:COG1240 1 DLALALLALLLLLALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5376 RRTKPSKRQ---YQICLAIDDSSSMVDNhtKQLAfeslAVIGNALTLLEVGQ----IAVCSFGESVKLLHPfheqfsdys 5448
Cdd:COG1240 81 LAPLALARPqrgRDVVLVVDASGSMAAE--NRLE----AAKGALLDFLDDYRprdrVGLVAFGGEAEVLLP--------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5449 gsqilrlckFQQKKTKIAQFLESV---------ASMFAAAQQLSQNiSPEIAQLLLVVSDGRGlfLEGKERVLAAVQAAR 5519
Cdd:COG1240 146 ---------LTRDREALKRALDELppgggtplgDALALALELLKRA-DPARRKVIVLLTDGRD--NAGRIDPLEAAELAA 213
|
250 260
....*....|....*....|.
gi 1622932237 5520 NANIFVIFVVLDNPSSRDSIL 5540
Cdd:COG1240 214 AAGIRIYTIGVGTEAVDEGLL 234
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
4919-5220 |
3.70e-03 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 44.13 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4919 EAGHEAEERETETDQNESQSPQEPEEGPSEDDKAKGEE---EMDTGAD---DQDGDAAQHPEEHSEEQQQSLEEKDKDAD 4992
Cdd:NF033609 568 DSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDsasDSDSASDsdsASDSDSASDSDSASDSDSASDSDSDSDSD 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4993 EEGGENGPADQGFQPQKQEEEQEDSDTE---EQVPEVLERKEHASCGQTGVENMQSTQAVELAGAAPEKEQGKEEHGSGA 5069
Cdd:NF033609 648 SDSDSDSDSDSDSDSDSDSDSDSDSDSDsdsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5070 ADANQAEGHESNFIAQLTSQKHTRKNTQSFKRKPGQADNERSMGDHNERVHKRLRTVDTDSHAEQGPAQQPQAQVE-DAD 5148
Cdd:NF033609 728 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSD 807
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622932237 5149 AFEHIKQGSDAYDAQTYDVASKEQQQSAKDSGRDQEEEEIEDTLMDTEEQEElKAADVEQ------LKPEEIKSSTTA 5220
Cdd:NF033609 808 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESD-SNSDSESgsnnnvVPPNSPKNGTNA 884
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
312-432 |
9.25e-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: 40.21 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 312 LETLAMAV--ASQNAVLLEGPIGCGKTSLVEYLAAMTGRTKPPqLLKVQLGDqtdskMLLGMYRCTDVpGEFVWQPGTLT 389
Cdd:cd00009 7 IEALREALelPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-FLYLNASD-----LLEGLVVAELF-GHFLVRLLFEL 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1622932237 390 QAATMGHWILLEDIDYAPLDVVSVLIPLLENGDLLIPGQGDCL 432
Cdd:cd00009 80 AEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRENVR 122
|
|
| |
|
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 ... |
5325-5595 |
7.04e-145 |
|
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: 452.58 E-value: 7.04e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5325 LSQRLCEELRLILEPTQAAKLKGDYRTGKRLNIRKVIPYIASQFRKDKIWLRRTKPSKRQYQICLAIDDSSSMVDNHTKQ 5404
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5405 LAFESLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEQFSDYSGSQILRLCKFQQKKTKIAQFLESVASMFAAAQQlsQ 5484
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDART--Q 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5485 NISPEIAQLLLVVSDGRGLFLEGKERVLaaVQAARNANIFVIFVVLDNPSSRDSILDIKVPIFKGPGeMPEIRSYMEEFP 5564
Cdd:cd01460 159 SSSGSLWQLLLIISDGRGEFSEGAQKVR--LREAREQNVFVVFIIIDNPDNKQSILDIKVVSFKNDK-SGVITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|.
gi 1622932237 5565 FPYYIILRDVNALPETLSDALRQWFELVTAS 5595
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 |
3.43e-41 |
|
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: 148.50 E-value: 3.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 915 DLQVLIVDYLKGLSVNKNTVQGIINFYTALRKESGTKLVDGTGHRPHYSLRTLCRALRFAASN-PCGNIQRSLYEGFCLG 993
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLVRDIVKFYLEAKKLAEKSLVDGAGQRPHYSLRTLCRALSYARAIaPRYGLRRALYEGFCMS 80
|
90 100
....*....|....*....|....
gi 1622932237 994 FLTQLDRASHPIVQKLICQHIVSG 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 |
2.53e-27 |
|
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: 110.07 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1385 PVLLVGDTGCGKTTICQVFA-ALANQKLYSVSCHLHMETSDFLGGLrpvrqkpkdkeEIDTsRLFEWHDGPLVQAMKEDG 1463
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAaALSNRPVFYVQLTRDTTEEDLFGRR-----------NIDP-GGASWVDGPLVRAAREGE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622932237 1464 FFLLDEISLADDSVLERLNSVLEvEKSLVLAEKGSPEDKdsevelltAGKKFRILATMNPgGDFGKKELSPALRNRF 1540
Cdd:pfam07728 69 IAVLDEINRANPDVLNSLLSLLD-ERRLLLPDGGELVKA--------APDGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1900-1999 |
1.55e-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: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1900 DMEFIASTLFPaIEKNIVKKMVAFNNQIDHEVTVEKKWGQKGGPWEFNLRDLFRWCQLM-----LVDQSPGCYDPGQHVF 1974
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLssllpTLLSPTVREEIFLEAV 79
|
90 100
....*....|....*....|....*
gi 1622932237 1975 LVYGERMRTEEDKKKVIAVFKDVFG 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 |
8.73e-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: 97.36 E-value: 8.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1079 PVLIQGETSVGKTSLIQWLAAATGNHCVR-INNHEHTDIQEYIGCYTSDSSGKlVFKEGVLIDAMRKGYWIILDELNLAP 1157
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFyVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622932237 1158 TDVLEALNRLLDDNRELLVTETQEVVKAHPRFMLFATQNPPglYGGRKVLSRAFRNRF 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 |
1.06e-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: 95.83 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1227 ELETILHKRCSLPPSYCSKLVKVMLDLQSYRRSSSVFA--GKQGFITLRDLFRWAERYRLAEPTEKEYDWLQHLANDGYM 1304
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGssGSPREFNLRDLLRWCRRLSSLLPTLLSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....
gi 1622932237 1305 LLAGRVRKQEEVDVIQEVLEKHFK 1328
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLG 104
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
480-604 |
2.02e-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: 83.51 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 480 ELNEVLQSRYPSLLAVVDHLLEIYIQLTGEKHHSWSDRSVGceqapeevsearrenkrptlEGRELSLRDLLNWCNRIAH 559
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSG--------------------SPREFNLRDLLRWCRRLSS 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622932237 560 SFDSSSLSASL-NIFQEALDCFTAMLSEHTSKLKMAEVIGSKLNIS 604
Cdd:pfam17867 61 LLPTLLSPTVReEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
325-453 |
2.79e-17 |
|
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: 81.57 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 325 VLLEGPIGCGKTSLVEYLAAMTGRTKppqLLKVQLGDQTDSKMLLGMYRCTdvPGEFVWQPGTLTQAATMGHWILLEDID 404
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRP---VFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622932237 405 YAPLDVVSVLIPLLENGDLLIP-GQGDCLKVAPGFQFFATRRLLSCGGNW 453
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLPdGGELVKAAPDGFRLIATMNPLDRGLNE 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1748-1888 |
2.31e-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: 78.87 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1748 PILLEGSPGVGKTSLVGALAKA-SGNTLVRINLSEQTDITDLFGADLPveggKGGEFAWRDGPLLAALKAGHWVVLDELN 1826
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNI----DPGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622932237 1827 LASQSVLEGLNACFDHRgEIYVPELGMSFQVQHEKTKIFGCQNPfrQGGGRKGLPRSFLNRF 1888
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDGFRLIATMNP--LDRGLNELSPALRSRF 135
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4666-5259 |
4.19e-13 |
|
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: 76.59 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4666 SAGEGATEFHDYEGGGIGEGEGMKDVSDQIENEEQVEDTFQKGQEKDKEDPDSkSDIKGEDNAIEMSEDFDgkmhdgeLE 4745
Cdd:COG5271 257 SAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELTAAQAADPESDDDADD-STLAALEGAAEDTEIAT-------AD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4746 EQEEDDEKSDSEGGDLDKQMGDLNGEEADKLDERLWGDDDEEEDEEEEDNKTEETGPGMDEEDselvAKDDNLDSGNSNK 4825
Cdd:COG5271 329 ELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAA----ADDSADDEEASAD 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4826 DKSQKDKKEEKEESEADDGGEGEDKINEQID-EREYDENEVDpyhGNQEKLPEPEALDLPDDLNLDSEDKNG-------- 4896
Cdd:COG5271 405 GGTSPTSDTDEEEEEADEDASAGETEDESTDvTSAEDDIATD---EEADSLADEEEEAEAELDTEEDTESAEedadgdea 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4897 ----GEDTDNEEGEEENPLEIKEKPEEAGHEAEERETETDQNESQSPQEPEEGPSEDDKakgEEEMDTGADDQDGDAAQH 4972
Cdd:COG5271 482 tdedDASDDGDEEEAEEDAEAEADSDELTAEETSADDGADTDAAADPEDSDEDALEDET---EGEENAPGSDQDADETDE 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4973 PEEHSE-------EQQQSLEEKDKDADEEGGENGP-------ADQGFQPQKQEEEQEDSDTEEQVPEVLERKEHASCGQT 5038
Cdd:COG5271 559 PEATAEedepdeaEAETEDATENADADETEESADEseeaeasEDEAAEEEEADDDEADADADGAADEEETEEEAAEDEAA 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5039 GVENMQSTQAVELAGAAPEKEQGKEEHGSGAADANQAEGHESNFIAQLTSQKHTR--KNTQSFKRKPGQADNERSM---- 5112
Cdd:COG5271 639 EPETDASEAADEDADAETEAEASADESEEEAEDESETSSEDAEEDADAAAAEASDdeEETEEADEDAETASEEADAeead 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5113 ----GDHNERVHKRLRTVDTDSHAEQGPAQqpqaqvEDADAFEHIKQGSDAYDAQTYDVASKEQQQSAKDSGRDQEEEE- 5187
Cdd:COG5271 719 teadGTAEEAEEAAEEAESADEEAASLPDE------ADAEEEAEEAEEAEEDDADGLEEALEEEKADAEEAATDEEAEAa 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5188 ------IEDTLMDTEEQEELKAADVEQLKPEEIKSSTTAplgfDEM--EVEIQTVKTEEDQDPRTDRAHKETENEKPERS 5259
Cdd:COG5271 793 aeekekVADEDQDTDEDALLDEAEADEEEDLDGEDEETA----DEAleDIEAGIAEDDEEDDDAAAAKDVDADLDLDADL 868
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4690-5323 |
1.78e-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: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4690 DVSDQIENEEQVEDTFQKGQEKDKEDPDSKSDIKGEDNAIEMSEDFDGKmhDGELEEQEEDDEKSDSEGGDLDKQMGDLN 4769
Cdd:COG5271 360 DTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTS--PTSDTDEEEEEADEDASAGETEDESTDVT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4770 GEEADKLDerlwgdddeeedeeeedNKTEETGPGMDEEDSELVAKDDNLDSGNSNKDKSQKDKKEEKEESEADDGGEGED 4849
Cdd:COG5271 438 SAEDDIAT-----------------DEEADSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEEDA 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4850 KINEQIDEREYDE------NEVDPYHGNQEKLPEPEALDLPDDLNLDSEDKNGGEDTDNEEGEEENPLEIKEKPEEAGHE 4923
Cdd:COG5271 501 EAEADSDELTAEEtsaddgADTDAAADPEDSDEDALEDETEGEENAPGSDQDADETDEPEATAEEDEPDEAEAETEDATE 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4924 AEER-ETETDQNESQSPQEPEEGPSEDDKAKGEE---EMDTGADDQDGDAAQHPEEHSEEQQQSLEEKDKDADEEGGENG 4999
Cdd:COG5271 581 NADAdETEESADESEEAEASEDEAAEEEEADDDEadaDADGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEAEA 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5000 PADQgfqpqKQEEEQEDSDTEEQVPEVLERkehascGQTGVENMQSTQAVELAGAAPEKEQGKEEHGSGAADANQAEGHE 5079
Cdd:COG5271 661 SADE-----SEEEAEDESETSSEDAEEDAD------AAAAEASDDEEETEEADEDAETASEEADAEEADTEADGTAEEAE 729
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5080 SNFIAQLTS-QKHTRKNTQSFKRKPGQADNERSMGD------HNERVHKRLRTVDTDshAEQGPAQQPQAQVEDADAFEH 5152
Cdd:COG5271 730 EAAEEAESAdEEAASLPDEADAEEEAEEAEEAEEDDadgleeALEEEKADAEEAATD--EEAEAAAEEKEKVADEDQDTD 807
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5153 IKQGSDAYDAQ---TYDVASKEQQQSAKDSGRDQEEEEIEDTlmDTEEQEELKAADVEQLKPEEIKSSTTAPLGFDEMEV 5229
Cdd:COG5271 808 EDALLDEAEADeeeDLDGEDEETADEALEDIEAGIAEDDEED--DDAAAAKDVDADLDLDADLAADEHEAEEAQEAETDA 885
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5230 EIQTVKTEEDQDPRTDRAHKETENEKPERSRESTIHTAHQflMDTIFQPFLKDVNELRQELERQLEMWqpHESENPEEEK 5309
Cdd:COG5271 886 DADADAGEADSSGESSAAAEDDDAAEDADSDDGANDEDDD--DDAEEERKDAEEDELGAAEDDLDALA--LDEAGDEESD 961
|
650
....*....|....
gi 1622932237 5310 VAAEMWQSYLILTA 5323
Cdd:COG5271 962 DAAADDAGDDSLAD 975
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4914-5313 |
2.30e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.86 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4914 KEKPEEAGHEAEERETETDQNESQSpqepEEGPSEDDKAKGEEEmdtgaddQDGDAAQHPEEHSEEQQQSLEEKDKDADE 4993
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKA----EEAKKAAEAAKAEAE-------AAADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4994 ---EGGENGPADQgfqpqKQEEEQEDSDTEEQVPEVLERKEHASCGQTGVENMQstQAVELAGAAPEKEQGkEEHGSGAA 5070
Cdd:PTZ00121 1383 akkKAEEKKKADE-----AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK--KADEAKKKAEEAKKA-DEAKKKAE 1454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5071 DANQAE-----GHESNFIAQLTSQKHTRKNTQSFKRKpgqADNERSMGDHNERVHKRLRTVDTDSHAEQGPAQQPQAQVE 5145
Cdd:PTZ00121 1455 EAKKAEeakkkAEEAKKADEAKKKAEEAKKADEAKKK---AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5146 DADAFEHIKQGSDAYDAQtyDVASKEQQQSAKDSGR-DQEEEEIEDTLMDTEEQEELKaadveqlKPEEIKSSTTAPLGF 5224
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKAD--ELKKAEELKKAEEKKKaEEAKKAEEDKNMALRKAEEAK-------KAEEARIEEVMKLYE 1602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5225 DEMEVEIQTVKTEEDQDPRTDRAHKETENEKPERSRESTIHTAhqflmdtifqpfLKDVNELRQElERQLEMWQPHESEN 5304
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE------------KKKAEELKKA-EEENKIKAAEEAKK 1669
|
....*....
gi 1622932237 5305 PEEEKVAAE 5313
Cdd:PTZ00121 1670 AEEDKKKAE 1678
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1736-1888 |
3.39e-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: 64.80 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1736 AQRLLRATKLKKPILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQTDITDLFGADLPVEggKGGEFAWRDGPLLAAlk 1815
Cdd:COG0714 21 IELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQ--QTGEFEFRPGPLFAN-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1816 aghwVVL-DELNLAS---QS----VLEglnacfdhRGEIYVP----ELGMSFQVqhektkiFGCQNPFRQGGGRKgLPRS 1883
Cdd:COG0714 97 ----VLLaDEINRAPpktQSalleAME--------ERQVTIPggtyKLPEPFLV-------IATQNPIEQEGTYP-LPEA 156
|
....*
gi 1622932237 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 |
3.92e-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: 64.42 E-value: 3.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1079 PVLIQGETSVGKTSLIQWLAAATGNHCVRINNHEHTDIQEyiGCYTSD---SSGKLVFKEG------VLIdamrkgywii 1149
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSD--ILGTYIydqQTGEFEFRPGplfanvLLA---------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1150 lDELNLAPTDVLEALNRLLDDNRellVTETQEVVKAHPRFMLFATQNPPGLYGGRkVLSRAFRNRF-VELHFDeLPSSEL 1228
Cdd:COG0714 101 -DEINRAPPKTQSALLEAMEERQ---VTIPGGTYKLPEPFLVIATQNPIEQEGTY-PLPEAQLDRFlLKLYIG-YPDAEE 174
|
....*...
gi 1622932237 1229 ET-ILHKR 1235
Cdd:COG0714 175 EReILRRH 182
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4914-5255 |
4.97e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.70 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4914 KEKPEEAGHEAEE-RETETDQNESQSPQEPEEGPSEDDKAKGEEEMDTGAD-----DQDGDAAQHPEEHSEEQQQSLEEK 4987
Cdd:PTZ00121 1430 KKKADEAKKKAEEaKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEeakkaDEAKKKAEEAKKKADEAKKAAEAK 1509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4988 DKdADE--EGGENGPADQgFQPQKQEEEQEDSDTEEQVPEVLERKEhascgqtgVENMQSTQAVELAGAAPEKEQGKEEH 5065
Cdd:PTZ00121 1510 KK-ADEakKAEEAKKADE-AKKAEEAKKADEAKKAEEKKKADELKK--------AEELKKAEEKKKAEEAKKAEEDKNMA 1579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5066 GSGAADANQAEGHESNFIAQLTSQKHTRKNTQSFKrkpgqADNERSMGDHNERVHKRLRTVDTDSHAEQgpaqqpqaqvE 5145
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK-----AEEAKIKAEELKKAEEEKKKVEQLKKKEA----------E 1644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5146 DADAFEHIKQGSDAYDAQTYDVASK--EQQQSAKDSGRDQEEEEIEDTLMDTEEQEELKAADVEQLKPEEIKSSTTAPLG 5223
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEAKKaeEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA 1724
|
330 340 350
....*....|....*....|....*....|..
gi 1622932237 5224 FDEMEVEIQTVKTEEDQDPRTDRAHKETENEK 5255
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
672-902 |
7.12e-10 |
|
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: 60.38 E-value: 7.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 672 PVLLVGETGTGKTSTVQYLAH-ITGHRLRVVNMNQQSDTADLLGGYKPvdhkliwlplreafeelfaqtfskkqnftflg 750
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRNI-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 751 hiqtcyrqkrwhdllrlmqhvhksavnkdgkesetgllikekweafglrlnhaqqqmkmteNTLLFAFVEGTLAQAVKKG 830
Cdd:pfam07728 49 -------------------------------------------------------------DPGGASWVDGPLVRAAREG 67
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622932237 831 EWILLDEINLAAPEILECLSGLLEGSSgslVLLDRGDTEPLVRHPDFRLFACMNPAtDVGKRNLPPGIRNRF 902
Cdd:pfam07728 68 EIAVLDEINRANPDVLNSLLSLLDERR---LLLPDGGELVKAAPDGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
5387-5537 |
6.94e-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: 58.62 E-value: 6.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5387 ICLAIDDSSSMVDNhTKQLAFESLAVIGNALTLLEVG-QIAVCSFGESVKLLHPFHeqfSDYSGSQILRLCKFQQKK--- 5462
Cdd:smart00327 2 VVFLLDGSGSMGGN-RFELAKEFVLKLVEQLDIGPDGdRVGLVTFSDDARVLFPLN---DSRSKDALLEALASLSYKlgg 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622932237 5463 -TKIAQFLESVASMFAAAQQLSQnisPEIAQLLLVVSDGRGLFleGKERVLAAVQAARNANIFVIFVVLDNPSSRD 5537
Cdd:smart00327 78 gTNLGAALQYALENLFSKSAGSR---RGAPKVVILITDGESND--GPKDLLKAAKELKRSGVKVFVVGVGNDVDEE 148
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2220-2306 |
2.52e-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: 55.76 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 2220 GTFEWVDSMLVQALKSGDWLLMDNVNFCNPSVLDRLNALLEPGgvltisERGMIDGSTPTITPNPNFRLFLSMDPVHGD- 2298
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDER------RLLLPDGGELVKAAPDGFRLIATMNPLDRGl 124
|
90
....*....|
gi 1622932237 2299 --ISRAMRNR 2306
Cdd:pfam07728 125 neLSPALRSR 134
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1383-1540 |
8.24e-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: 54.69 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1383 GEPVLLVGDTGCGKTTICQVFAALANQKLYSV---SCHLHMETSDFLGGLRPVRQKPKDKEEIDTSR-LFEwhdgpLVQA 1458
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGViyiDGEDILEEVLDQLLLIIVGGKKASGSGELRLRlALA-----LARK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1459 MKEDgFFLLDEISLADDSVLERLNSVLEVEKSLVLAEKgspedkdsevelltaGKKFRILATMNPGGDFGKKELSPALRN 1538
Cdd:smart00382 77 LKPD-VLILDEITSLLDAEQEALLLLLEELRLLLLLKS---------------EKNLTVILTTNDEKDLGPALLRRRFDR 140
|
..
gi 1622932237 1539 RF 1540
Cdd:smart00382 141 RI 142
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1372-1540 |
1.15e-07 |
|
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: 57.10 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1372 LAMLVGRalefgePVLLVGDTGCGKTTICQVFAALANQKLYSVSCHLHMETSDFLGglrpvrqkpkdkEEI---DTSRlF 1448
Cdd:COG0714 26 IALLAGG------HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILG------------TYIydqQTGE-F 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1449 EWHDGPLVQamkedGFFLLDEISLADDSVLerlNSVLEVekslvLAEKgspedkdsEV----ELLTAGKKFRILATMNPG 1524
Cdd:COG0714 87 EFRPGPLFA-----NVLLADEINRAPPKTQ---SALLEA-----MEER--------QVtipgGTYKLPEPFLVIATQNPI 145
|
170
....*....|....*.
gi 1622932237 1525 GDFGKKELSPALRNRF 1540
Cdd:COG0714 146 EQEGTYPLPEAQLDRF 161
|
|
| AAA_3 |
pfam07726 |
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ... |
1749-1888 |
3.34e-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: 52.56 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1749 ILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQTDITDLFGADLPVEggKGGEFAWRDGPLLAALkaghwVVLDELNLA 1828
Cdd:pfam07726 2 VLLEGVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGTEVFDQ--KTREFEFRPGPVFANV-----LLADEINRA 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622932237 1829 S---QSVLegLNACFDHR----GEIY-VPELGMsfqvqhektkIFGCQNPFRQGGGRKgLPRSFLNRF 1888
Cdd:pfam07726 75 PpktQSAL--LEAMQERQvtidGETHpLPEPFF----------VLATQNPIEQEGTYP-LPEAQLDRF 129
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4918-5225 |
4.65e-07 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 56.93 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4918 EEAGHEAEERETETDQNESQSPQEPEEGP--SEDDKAKGEEEMDTGADDQDGDAaqhPEEHSEEQqqsleEKDKDADEEG 4995
Cdd:TIGR00927 632 KGDVAEAEHTGERTGEEGERPTEAEGENGeeSGGEAEQEGETETKGENESEGEI---PAERKGEQ-----EGEGEIEAKE 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4996 GENGPADQGFQPQKQEEEQEDSDTEEQVPEVLERKEhaSCGQTGVENMQSTQAVELAGAAPEKEQGKEEHGSGAADANQA 5075
Cdd:TIGR00927 704 ADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGE--EVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEG 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5076 EghesnfiaqltsqkhtrknTQSFKRKPGQADNERSMGDHNERVHKrlrTVDTDSHAEQGPAQQPQAQVEDadafehiKQ 5155
Cdd:TIGR00927 782 E-------------------IQAGEDGEMKGDEGAEGKVEHEGETE---AGEKDEHEGQSETQADDTEVKD-------ET 832
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622932237 5156 GSDAYDAQTYDVASKEQQ----QSAKDSGRDQEEEEIEDTLMDTEEQEElkaadveqlKPEEIKSSTTAPLGFD 5225
Cdd:TIGR00927 833 GEQELNAENQGEAKQDEKgvdgGGGSDGGDSEEEEEEEEEEEEEEEEEE---------EEEEEEEENEEPLSLE 897
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1746-1896 |
6.37e-07 |
|
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: 52.15 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1746 KKPILLEGSPGVGKTSLVGALAKAS---GNTLVRINLSeqtditDLFGADlpVEGGKGGEFAWRDGPLLAALKAGHWVVL 1822
Cdd:cd00009 19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNAS------DLLEGL--VVAELFGHFLVRLLFELAEKAKPGVLFI 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622932237 1823 DELNLASQSVLEGLNACFdhrgeiyvpELGMSFQVQHEKTKIFG-CQNPFRQgggrkGLPRSFLNRFTQVFVDPL 1896
Cdd:cd00009 91 DEIDSLSRGAQNALLRVL---------ETLNDLRIDRENVRVIGaTNRPLLG-----DLDRALYDRLDIRIVIPL 151
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1301-1618 |
1.60e-06 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 54.35 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1301 DGYMLLAGRVRKQEEVDVIQEVLEKHFKKKLcpqSLFSKENVVKLLGKLSTQISTLESNFGHIVWTEGMR--RLAMLVGR 1378
Cdd:PHA02244 42 DAIREKAETEGKEIAIDDIKKEIEDSPEEQF---FELPVKIELQQEGKPAGDISGIDTTKIASNPTFHYEtaDIAKIVNA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1379 ALefgePVLLVGDTGCGKTTICQVFAALANQKLYSvschlhmetsdflggLRPVRQKPKDKEEIDTSRLFewHDGPLVQA 1458
Cdd:PHA02244 119 NI----PVFLKGGAGSGKNHIAEQIAEALDLDFYF---------------MNAIMDEFELKGFIDANGKF--HETPFYEA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1459 MKEDGFFLLDEISLADDSVLERLNSVLevekslvlaekgSPEDKDSEVELLTAGKKFRILA---TMNPGGD---FGKKEL 1532
Cdd:PHA02244 178 FKKGGLFFIDEIDASIPEALIIINSAI------------ANKFFDFADERVTAHEDFRVISagnTLGKGADhiyVARNKI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1533 SPALRNRFTEIWCPQSTSREDLIQIINHNLrpglclgridpkgsdipevmLDFIDWLTHQ--EFGRKCVVSIRDILSWVN 1610
Cdd:PHA02244 246 DGATLDRFAPIEFDYDEKIEHLISNGDEDL--------------------VNFVALLRHEmaEKGLDHVFSMRAIIHGKK 305
|
....*...
gi 1622932237 1611 FMNKMGEE 1618
Cdd:PHA02244 306 FDGVFEAD 313
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1016-1234 |
1.83e-06 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 54.39 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1016 SGNVKSLLKQPIPEPKGGRLIQVEGYWIAVGDKEPTIDETYILTSSVKLNLRDIVRVVSAGTYP--VLIQGETSVGKTSL 1093
Cdd:COG1401 158 LEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKFEETLEAFLAALKTKknVILAGPPGTGKTYL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1094 IQWLAAATG---NHCVRI-----NNHEHTDIQEYigcYTSDSSGKLVFKEGVLIDAMRKG-------YWIILDELNLAPT 1158
Cdd:COG1401 238 ARRLAEALGgedNGRIEFvqfhpSWSYEDFLLGY---RPSLDEGKYEPTPGIFLRFCLKAeknpdkpYVLIIDEINRANV 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1159 D--------VLEALNRLLDDNRELLVTETQEVVKAHPRFMLFATQNPP--GLYGGRKVLSRAFRNRFVELHFDELPSSEL 1228
Cdd:COG1401 315 EkyfgellsLLESDKRGEELSIELPYSGEGEEFSIPPNLYIIGTMNTDdrSLALSDKALRRRFTFEFLDPDLDKLSNEEV 394
|
....*.
gi 1622932237 1229 ETILHK 1234
Cdd:COG1401 395 VDLLEE 400
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4914-5251 |
3.92e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4914 KEKPEEAGHEAEE-RETETDQNESQSPQEPEEGP--SEDDKAKGEEEMDTGADDQDGDAAQHPEEHSEEQQQSLEEKDKD 4990
Cdd:PTZ00121 1456 AKKAEEAKKKAEEaKKADEAKKKAEEAKKADEAKkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK 1535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4991 ADE--EGGENGPADQgfqpqkqEEEQEDSDTEEQVPEVLERKEHASCGQTGVENMQSTQAVELAGAAPEKEQGKEEHGSG 5068
Cdd:PTZ00121 1536 ADEakKAEEKKKADE-------LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5069 AADANQAEgHESNFIAQLTSQKHTRKNTQSFKRKPGQ------------------ADNERSMGDHNERVHKRLRTVDTDs 5130
Cdd:PTZ00121 1609 AEEAKKAE-EAKIKAEELKKAEEEKKKVEQLKKKEAEekkkaeelkkaeeenkikAAEEAKKAEEDKKKAEEAKKAEED- 1686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5131 haEQGPAQQPQAQVEDADAFEHIKQGS--DAYDAQTYDVASKEQQQSAKDSGRDQEEEEIEDTLMDTEEQEELKaadVEQ 5208
Cdd:PTZ00121 1687 --EKKAAEALKKEAEEAKKAEELKKKEaeEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK---IAH 1761
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1622932237 5209 LKPEEIKSsttAPLGFDEMEVEIQTVKTEEDQDPR--TDRAHKET 5251
Cdd:PTZ00121 1762 LKKEEEKK---AEEIRKEKEAVIEEELDEEDEKRRmeVDKKIKDI 1803
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1738-1828 |
4.46e-06 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 53.23 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1738 RLLRATKLKKPILLEGSPGVGKTSLVGALAKA-SGNTLVRINLseqtdIT---DLFGADLpVEG----GKGGEFAWRDGP 1809
Cdd:COG1401 213 AFLAALKTKKNVILAGPPGTGKTYLARRLAEAlGGEDNGRIEF-----VQfhpSWSYEDF-LLGyrpsLDEGKYEPTPGI 286
|
90 100
....*....|....*....|....*.
gi 1622932237 1810 LL-AALKAG------HWVVLDELNLA 1828
Cdd:COG1401 287 FLrFCLKAEknpdkpYVLIIDEINRA 312
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4915-5080 |
5.89e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 52.67 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4915 EKPEEAGHEAEERETET----DQNESQSPQEPEEGPSEDDKAKGEEEMDTGADDQDGDAAQHPEEHSEEQQQSLEEKDKD 4990
Cdd:PHA03169 74 ETAEESRHGEKEERGQGgpsgSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4991 ADEEGGENGPA--DQGfqpqkqeeEQEDSDTEEQVPEVLERKEhascGQTGVENMQSTQAVELAGAAPEKEQGKEEHGSG 5068
Cdd:PHA03169 154 SHNPSPNQQPSsfLQP--------SHEDSPEEPEPPTSEPEPD----SPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQ 221
|
170
....*....|..
gi 1622932237 5069 AADANQAEGHES 5080
Cdd:PHA03169 222 APSPNTQQAVEH 233
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1749-1784 |
7.20e-06 |
|
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: 48.74 E-value: 7.20e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1622932237 1749 ILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQTD 1784
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS 36
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4692-5313 |
8.63e-06 |
|
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: 52.71 E-value: 8.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4692 SDQIENEEQVEDTFQKGQEKDKEDPDSKSDIKGEDNAIEMseDFDGKMHDGELEEQEEDDEKSDSEGGDLDKQMGDLNGE 4771
Cdd:COG5271 150 KDGDELLPSLADNDEAAADEGDELAADGDDTLAVADAIEA--TPGGTDAVELTATLGATVTTDPGDSVAADDDLAAEEGA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4772 EADKLDERLWGDDDEEEDEEEEDNKTE-ETGPGMDEEDSELVAKDDNLDSGNSNKDKSQKDKKEEKEESEADDGGEGEDK 4850
Cdd:COG5271 228 SAVVEEEDASEDAVAAADETLLADDDDtESAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELTAAQAADPESDDDA 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4851 INEQIDEREYDENEVDPYHGNQEKLPEPEALDLPDDLNLDSEDKNGGEDtdneegeeenpleIKEKPEEAGHEAEERETE 4930
Cdd:COG5271 308 DDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAEDAAEEAATAEDS-------------AAEDTQDAEDEAAGEAAD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4931 TDQNESQSPQEPEEGPSEDDKAKGEEeMDTGADDQDGDAAQHPEEHSEEQQQSLEEKDKDADEEGGENG-PADQGFQPQK 5009
Cdd:COG5271 375 ESEGADTDAAADEADAAADDSADDEE-ASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDDiATDEEADSLA 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5010 QEEEQEDSDTEEQVPEVLErkehascgQTGVENMQSTQAVELAGAAPEKEQGKEEHGSGAADANQAEGHESNFIAQLTSQ 5089
Cdd:COG5271 454 DEEEEAEAELDTEEDTESA--------EEDADGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSADDGADTDAA 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5090 KHTRKNTqsfkrkpgqadnERSMGDHNErVHKRLRTVDTDSHAEQGPAQQPQAQVEDADAFE-HIKQGSDAYDAQTYDVA 5168
Cdd:COG5271 526 ADPEDSD------------EDALEDETE-GEENAPGSDQDADETDEPEATAEEDEPDEAEAEtEDATENADADETEESAD 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5169 SKEQQQSAKDSGRDQEEEEIEDTLMDTEEQEELKAADVEQLKPEEIKSSTTAPLGFDEMEVEIQTVKTEEDQDPRTDRAH 5248
Cdd:COG5271 593 ESEEAEASEDEAAEEEEADDDEADADADGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEAEASADESEEEAEDE 672
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622932237 5249 KETENEKPERSRESTIHTAhqfLMDTifqpflKDVNELRQELERQlemwqpheSENPEEEKVAAE 5313
Cdd:COG5271 673 SETSSEDAEEDADAAAAEA---SDDE------EETEEADEDAETA--------SEEADAEEADTE 720
|
|
| vWFA |
cd00198 |
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
5385-5542 |
9.52e-06 |
|
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: 49.10 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5385 YQICLAIDDSSSMVD---NHTKQLAfesLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEqfsDYSGSQILRlcKFQQK 5461
Cdd:cd00198 1 ADIVFLLDVSGSMGGeklDKAKEAL---KALVSSLSASPPGDRVGLVTFGSNARVVLPLTT---DTDKADLLE--AIDAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5462 KTKIAQFLESVASMFAAAQQLSQNISPEIAQLLLVVSDGRglFLEGKERVLAAVQAARNANIFVIFVVLDNPSSRDSILD 5541
Cdd:cd00198 73 KKGLGGGTNIGAALRLALELLKSAKRPNARRVIILLTDGE--PNDGPELLAEAARELRKLGITVYTIGIGDDANEDELKE 150
|
.
gi 1622932237 5542 I 5542
Cdd:cd00198 151 I 151
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4914-5314 |
1.12e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4914 KEKPEEAGHEAEE--------RETETDQNESQSPQEPEEGPSEDDKAKGEEEMDTGADDQDGDAAQhpEEHSEEQQQSLE 4985
Cdd:PTZ00121 1377 KKKADAAKKKAEEkkkadeakKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE--AKKADEAKKKAE 1454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4986 EKDK--DADEEGGENGPADQgfqpqKQEEEQEDSDTEEQVPEVLERKEHASCGQTGVEnmQSTQAVELAGAAPEK---EQ 5060
Cdd:PTZ00121 1455 EAKKaeEAKKKAEEAKKADE-----AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE--AKKKADEAKKAEEAKkadEA 1527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5061 GKEEHGSGAADANQAE----GHESNFIAQLTSQKHTRKNTQSFKRKPGQADNERSMGDHNERVHKRLRTVDTDSHAEQGP 5136
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEekkkADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5137 AQQPQAQVEDA--DAFEHIKQGSDAYDAQTYDVASKEQQQSAKDSGRDQEEEEIEDTLMDTEEQEELKAAD--------- 5205
Cdd:PTZ00121 1608 KAEEAKKAEEAkiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEeakkaeede 1687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5206 ---VEQLKPEEIKSSTTAPLGFDEMEvEI----QTVKTEEDQDPRTDRAHKETENEKpERSRESTIHTAHQFLMDTIFQP 5278
Cdd:PTZ00121 1688 kkaAEALKKEAEEAKKAEELKKKEAE-EKkkaeELKKAEEENKIKAEEAKKEAEEDK-KKAEEAKKDEEEKKKIAHLKKE 1765
|
410 420 430
....*....|....*....|....*....|....*.
gi 1622932237 5279 FLKDVNELRQELERQLEmwqphESENPEEEKVAAEM 5314
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAVIE-----EELDEEDEKRRMEV 1796
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
1744-1781 |
1.47e-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: 48.43 E-value: 1.47e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1622932237 1744 KLKKPILLEGSPGVGKTSLVGALAKASGNTLVRINLSE 1781
Cdd:cd19481 24 GLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSS 61
|
|
| CobT2 |
COG4547 |
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ... |
4926-5004 |
3.82e-05 |
|
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 443611 [Multi-domain] Cd Length: 608 Bit Score: 50.18 E-value: 3.82e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622932237 4926 ERETETDQNESQSPQEPEEGPSEDDKAKGEEEMDTGADDQDGDAAQHPEEHSEEQQQSLEEKDKDADEEGGENGPADQG 5004
Cdd:COG4547 208 AEELGEDEDEEDEDDEDDSGEQEEDEEDGEDEDEESDEGAEAEDAEASGDDAEEGESEAAEAESDEMAEEAEGEDSEEP 286
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1068-1221 |
3.83e-05 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 49.73 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1068 DIVRVVSAGTyPVLIQGETSVGKTSLIQWLAAAtgnhcVRINNHEHTDI-QEYIGCYTSDSSGKlvFKEGVLIDAMRKGY 1146
Cdd:PHA02244 111 DIAKIVNANI-PVFLKGGAGSGKNHIAEQIAEA-----LDLDFYFMNAImDEFELKGFIDANGK--FHETPFYEAFKKGG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1147 WIILDELNLAPTDVLEALNRLLDDNRELLVTETqevVKAHPRFMLFATQNPPG-----LYGGRKVLSRAFRNRFVELHFD 1221
Cdd:PHA02244 183 LFFIDEIDASIPEALIIINSAIANKFFDFADER---VTAHEDFRVISAGNTLGkgadhIYVARNKIDGATLDRFAPIEFD 259
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4915-5255 |
5.28e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4915 EKPEEAGHEAEE-RETETDQNESQSPQEPEEGPSED----------DKAKGEEEMDTGADDQDGDAAQHPEE--HSEEQQ 4981
Cdd:PTZ00121 1091 EATEEAFGKAEEaKKTETGKAEEARKAEEAKKKAEDarkaeearkaEDARKAEEARKAEDAKRVEIARKAEDarKAEEAR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4982 QSLEEKDKDADEEGGENGPADqgfqpqkqeeeqedsdtEEQVPEVLERKEHAScgqtGVENMQSTQAVELAGAAPEKEQG 5061
Cdd:PTZ00121 1171 KAEDAKKAEAARKAEEVRKAE-----------------ELRKAEDARKAEAAR----KAEEERKAEEARKAEDAKKAEAV 1229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5062 K--EEHGSGAADANQAEGHESNfiAQLTSQKHTRKNTQSFKRKPGQADNERSmGDHNERVHKRLRTVDTDSHAEQGPAQQ 5139
Cdd:PTZ00121 1230 KkaEEAKKDAEEAKKAEEERNN--EEIRKFEEARMAHFARRQAAIKAEEARK-ADELKKAEEKKKADEAKKAEEKKKADE 1306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5140 PQAQVEDADAFEHIKQGSDAYDAQTYDVASKEQQQSAKDSGRDQEEEEIEDTLMDTEEQ---------EELKAADVEQLK 5210
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKaeaaekkkeEAKKKADAAKKK 1386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1622932237 5211 PEEIKSSTTAPLGFDEMEVEIQTVKTEEDQDPRTDRAHKETENEK 5255
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK 1431
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4759-5034 |
1.81e-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: 48.45 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4759 GDLDK-------QMGDLNGEEADKLDERLWGDDDEEEDEEEEDNKTEETGPGMDEEDSELVAKDDNLDSGNSNKDKSQKD 4831
Cdd:TIGR00927 628 GDLSKgdvaeaeHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHK 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4832 KKEEKEESEADDGGEgedkineqiDEREYDENEVDPYHGNQEKLPEPEALDLPDDLNLDSEDKNGGEDTDNEEGEeenpl 4911
Cdd:TIGR00927 708 GETEAEEVEHEGETE---------AEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAE----- 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4912 eIKEKPEEAGHEAEERETETDQNESQSPQEPEEGPSEDDKAKGEEEMDTGADDQDGDAAQHPEEHSEEQQQSLEEKDKDA 4991
Cdd:TIGR00927 774 -GKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGV 852
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1622932237 4992 DEEGGENGPADQGFQPQKQEEEQEDSDTEEQVPEVLERKEHAS 5034
Cdd:TIGR00927 853 DGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLS 895
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
1746-1782 |
2.23e-04 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 47.61 E-value: 2.23e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1622932237 1746 KKPILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQ 1782
Cdd:PRK04195 39 KKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQ 75
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1368-1543 |
2.25e-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: 44.83 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1368 GMRRLAMLVGRALEFGEP--VLLVGDTGCGKTTICQVFAALANQKLYSVschLHMETSDFLGGLRpvrqkpkdKEEIDTS 1445
Cdd:cd00009 2 GQEEAIEALREALELPPPknLLLYGPPGTGKTTLARAIANELFRPGAPF---LYLNASDLLEGLV--------VAELFGH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1446 RLFEWHDGPLVQAMKedGFFLLDEISLADDSVLERLNSVLEVekslvlaekgspedkdsEVELLTAGKKFRILATMNPGG 1525
Cdd:cd00009 71 FLVRLLFELAEKAKP--GVLFIDEIDSLSRGAQNALLRVLET-----------------LNDLRIDRENVRVIGATNRPL 131
|
170
....*....|....*...
gi 1622932237 1526 DFgkkELSPALRNRFTEI 1543
Cdd:cd00009 132 LG---DLDRALYDRLDIR 146
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4806-4979 |
3.46e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 46.89 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4806 EEDSELVAKDDNLDSGNSNKDKSQKDKKEEKEESEADDGGEGEDKINEQIDEREYDENEVDPyhGNQEKLPEPEALDLPD 4885
Cdd:PHA03169 76 AEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPP--PSPPSHPGPHEPAPPE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4886 DLNLDSEDKNGGEDTDNEEGEEENPLEIKEKPEEAGHEAEERETETDQNESQSPQEpEEGPSEDDKAKGEEEMDTGaddQ 4965
Cdd:PHA03169 154 SHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPD-EPGEPQSPTPQQAPSPNTQ---Q 229
|
170
....*....|....
gi 1622932237 4966 DGDAAQHPEEHSEE 4979
Cdd:PHA03169 230 AVEHEDEPTEPERE 243
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
1736-1790 |
3.52e-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: 44.86 E-value: 3.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622932237 1736 AQRLLRAtKLKKPIL-LEGSPGVGKTSLVGALAKASGNTLVRINLSEQTDITDLFG 1790
Cdd:cd19500 27 AVRKLKG-SMKGPILcLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRG 81
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
663-712 |
3.79e-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: 3.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1622932237 663 LAVCVSKGEPVLLVGETGTGKTSTVQ-YLAHI--TGHRLRVVNMNQQSDTADL 712
Cdd:pfam12775 24 LDLLLKNGKPVLLVGPTGTGKTVIIQnLLRKLdkEKYLPLFINFSAQTTSNQT 76
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1079-1221 |
3.83e-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: 44.29 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1079 PVLIQGETSVGKTSLIQ---WLAAATGNHCVRIN----NHEHTDIQEYIGCYTSDSSGKLVFKEGVLIDAMRKGYW--II 1149
Cdd:smart00382 4 VILIVGPPGSGKTTLARalaRELGPPGGGVIYIDgediLEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPdvLI 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622932237 1150 LDELNLAPTDVLEALNRLLDDNRELLVTEtqevvKAHPRFMLFATQNPPGLygGRKVLSRAFRNRFVELHFD 1221
Cdd:smart00382 84 LDEITSLLDAEQEALLLLLEELRLLLLLK-----SEKNLTVILTTNDEKDL--GPALLRRRFDRRIVLLLIL 148
|
|
| Taf7 |
COG5414 |
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation ... |
5168-5296 |
7.90e-04 |
|
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation complex [Transcription];
Pssm-ID: 227701 Cd Length: 392 Bit Score: 45.46 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5168 ASKEQQQSAKDSGRDQEEEEIEDTLMDTEEQEELKAADVEQLKPEEIKSSTTAPLGFDEMEVEIQtvkTEEDQDPRTDRA 5247
Cdd:COG5414 256 ALKKEKQGAEEEGEEGMSEEDLDVGAAEIENKEVSEGDKEQQQEEVENAEAHKEEVQSDRPDEIG---EEKEEDDENEEN 332
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622932237 5248 HKETENEKPERSR-ESTI-HTAHQflMDTIFQP-----FLKDVNELRQELE---RQLEM 5296
Cdd:COG5414 333 ERHTELLADELNElEKGIeEKRRQ--MESATNPilqkrFESQLNVLLKELElkrKQLEM 389
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
669-737 |
7.90e-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: 43.13 E-value: 7.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622932237 669 KGEPVLLVGETGTGKTSTVQYLAHI---TGHRLRVVNMNQQSDTADLLGGYKPVDHKLIWLPLREAFEELFA 737
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALA 72
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
1741-1790 |
9.82e-04 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 45.70 E-value: 9.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1622932237 1741 RATKLKKPIL-LEGSPGVGKTSLVGALAKASGNTLVRINLSEQTDITDLFG 1790
Cdd:PRK10787 343 RVNKIKGPILcLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRG 393
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1079-1215 |
1.16e-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: 42.90 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1079 PVLIQGETSVGKTSLIQ---WLAAATGNHCVRINNHEHTDIqeyigcyTSDSSGKLVFKEGVLIDAMRKGYW--IILDEL 1153
Cdd:cd00009 21 NLLLYGPPGTGKTTLARaiaNELFRPGAPFLYLNASDLLEG-------LVVAELFGHFLVRLLFELAEKAKPgvLFIDEI 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622932237 1154 NLAPTDVLEALNRLLDDnRELLVTETQEVvkahpRFMLFATQNPPGLyggrkvLSRAFRNRF 1215
Cdd:cd00009 94 DSLSRGAQNALLRVLET-LNDLRIDRENV-----RVIGATNRPLLGD------LDRALYDRL 143
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
1724-1800 |
1.22e-03 |
|
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: 43.32 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1724 DYALSAGTTAMNAQRLLRATKLKKPI--LLEGSPGVGKTSLVGALAKA---SGNTLVRINLSEQT---DITDLFGADlPV 1795
Cdd:cd19499 17 DEAVKAVSDAIRRARAGLSDPNRPIGsfLFLGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYMekhSVSRLIGAP-PG 95
|
....*
gi 1622932237 1796 EGGKG 1800
Cdd:cd19499 96 YVGYT 100
|
|
| TFIIF_alpha |
pfam05793 |
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation ... |
4914-5045 |
1.28e-03 |
|
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation factor IIF, alpha subunit (TFIIF-alpha) or RNA polymerase II-associating protein 74 (RAP74) is the large subunit of transcription factor IIF (TFIIF), which is essential for accurate initiation and stimulates elongation by RNA polymerase II.
Pssm-ID: 310411 [Multi-domain] Cd Length: 528 Bit Score: 45.33 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4914 KEKPEEAGHEA----------EERETETDQNESQSPQEPEegpsEDDKAKGEEEMDTGADDQDGDAAQHPEEHSEEQQQs 4983
Cdd:pfam05793 258 KKKKRGGDDDAfeydsddgddEGREEDYISDSSASGNDPE----EREDKLSPEEPAKGEIEQSDDSEESEEEKNEEEGK- 332
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622932237 4984 LEEKDKDADEEGGENGPADQGFQPQKQEEEQEDSDTEEQVPEVLERKEHASCGQTGVENMQS 5045
Cdd:pfam05793 333 LSKKGKKAKKLKGKKNGKDKSESSDGDDSDDSDIDDEDSVPLFTAKKKKEPKKEEPVDSGPS 394
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
659-780 |
1.47e-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: 42.52 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 659 LIEQL--AVCVSKGEPVLLVGETGTGKTSTVQYLAHITGHR-LRVVNMNqqsdTADLLGGYkpVDHKLIWLPLREAFEEL 735
Cdd:cd00009 6 AIEALreALELPPPKNLLLYGPPGTGKTTLARAIANELFRPgAPFLYLN----ASDLLEGL--VVAELFGHFLVRLLFEL 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622932237 736 FAqtfsKKQNFT-FLGHIQTCYRQKRWHdLLRLMQHVHKSAVNKDG 780
Cdd:cd00009 80 AE----KAKPGVlFIDEIDSLSRGAQNA-LLRVLETLNDLRIDREN 120
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4914-5080 |
1.47e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 44.96 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4914 KEKPEEAGHEAEERETETdqnesQSPQEPEEGPSEDDKAKGEEEMDTGADDQDG-DAAQHPE-EHSEEQQQSLEEKDKDA 4991
Cdd:PHA03169 48 PPAPTTSGPQVRAVAEQG-----HRQTESDTETAEESRHGEKEERGQGGPSGSGsESVGSPTpSPSGSAEELASGLSPEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4992 DEEGGENGPADQGfqpqkqeeeqeDSDTEEQVPEVLERKEHASCGQTGVENMQSTQAVELAGAAPEKEQGKEEHGSGAAD 5071
Cdd:PHA03169 123 TSGSSPESPASHS-----------PPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPG 191
|
....*....
gi 1622932237 5072 ANQAEGHES 5080
Cdd:PHA03169 192 PPQSETPTS 200
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4915-5079 |
1.61e-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: 45.37 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4915 EKPEEAGHEAE-ERETETDQNESQSPQEPEEGPSEDDkakGEEEMDTGADDQDGDAAQHPEEHSEEQQQ--SLEEKDKDA 4991
Cdd:TIGR00927 658 ENGEESGGEAEqEGETETKGENESEGEIPAERKGEQE---GEGEIEAKEADHKGETEAEEVEHEGETEAegTEDEGEIET 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4992 DEEGGENGPADQGFQPQKQEEEQE--DSDTEEQVPEVLERKEHASCGQTGVE---NMQSTQAVELAGAAPEKEQ--GKEE 5064
Cdd:TIGR00927 735 GEEGEEVEDEGEGEAEGKHEVETEgdRKETEHEGETEAEGKEDEDEGEIQAGedgEMKGDEGAEGKVEHEGETEagEKDE 814
|
170
....*....|....*
gi 1622932237 5065 HGSGAADANQAEGHE 5079
Cdd:TIGR00927 815 HEGQSETQADDTEVK 829
|
|
| ChlD |
COG1240 |
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
5296-5540 |
1.69e-03 |
|
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];
Pssm-ID: 440853 [Multi-domain] Cd Length: 262 Bit Score: 43.77 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5296 MWQPHESENPEEEKVAAEMWQSYLILTAPLSQRLCEELRLILEPTQAAKLKGDYRTGKRLNIRKVIPYIASQFRKDKIWL 5375
Cdd:COG1240 1 DLALALLALLLLLALALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5376 RRTKPSKRQ---YQICLAIDDSSSMVDNhtKQLAfeslAVIGNALTLLEVGQ----IAVCSFGESVKLLHPfheqfsdys 5448
Cdd:COG1240 81 LAPLALARPqrgRDVVLVVDASGSMAAE--NRLE----AAKGALLDFLDDYRprdrVGLVAFGGEAEVLLP--------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5449 gsqilrlckFQQKKTKIAQFLESV---------ASMFAAAQQLSQNiSPEIAQLLLVVSDGRGlfLEGKERVLAAVQAAR 5519
Cdd:COG1240 146 ---------LTRDREALKRALDELppgggtplgDALALALELLKRA-DPARRKVIVLLTDGRD--NAGRIDPLEAAELAA 213
|
250 260
....*....|....*....|.
gi 1622932237 5520 NANIFVIFVVLDNPSSRDSIL 5540
Cdd:COG1240 214 AAGIRIYTIGVGTEAVDEGLL 234
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4843-5076 |
1.82e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 44.58 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4843 DGGEGEdkinEQIDEREYDENEVDPYHGNQEklpEPEALDLPDDLNLDSEDKNGgedtdneegeeENPLeiKEKPEEAGH 4922
Cdd:PHA03169 92 PSGSGS----ESVGSPTPSPSGSAEELASGL---SPENTSGSSPESPASHSPPP-----------SPPS--HPGPHEPAP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4923 EAEERETETDQNESQSPQEPEEGPSEDDKAKGEEEmdtgadDQDGDAAQHPEEHSEEQQQSLEEKDKDADEEGGENGPAD 5002
Cdd:PHA03169 152 PESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPE------PDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSP 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622932237 5003 QGfqpqKQEEEQEDSDTEEQVPEVlERKEHASCGQTGVENMQSTQavelAGAAPE---KEQGKEEHGSGAADANQAE 5076
Cdd:PHA03169 226 NT----QQAVEHEDEPTEPEREGP-PFPGHRSHSYTVVGWKPSTR----PGGVPKlclRCTSHPSHRSRLPEGQQSE 293
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1080-1215 |
3.10e-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: 41.04 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 1080 VLIQGETSVGKTSLIQWLAAATGNHCVRINNHEHTDiqEYIGcytsDSSGKLvfkEGVLIDAMRKGYWII-LDELNLAPT 1158
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS--KYVG----ESEKRL---RELFEAAKKLAPCVIfIDEIDALAG 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622932237 1159 DVLEALNRLLDDNRELLVTETQEVVKAHPRFMLFATQNPPGLyggrkvLSRAFRNRF 1215
Cdd:pfam00004 72 SRGSGGDSESRRVVNQLLTELDGFTSSNSKVIVIAATNRPDK------LDPALLGRF 122
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
4919-5220 |
3.70e-03 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 44.13 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4919 EAGHEAEERETETDQNESQSPQEPEEGPSEDDKAKGEE---EMDTGAD---DQDGDAAQHPEEHSEEQQQSLEEKDKDAD 4992
Cdd:NF033609 568 DSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDsasDSDSASDsdsASDSDSASDSDSASDSDSASDSDSDSDSD 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4993 EEGGENGPADQGFQPQKQEEEQEDSDTE---EQVPEVLERKEHASCGQTGVENMQSTQAVELAGAAPEKEQGKEEHGSGA 5069
Cdd:NF033609 648 SDSDSDSDSDSDSDSDSDSDSDSDSDSDsdsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5070 ADANQAEGHESNFIAQLTSQKHTRKNTQSFKRKPGQADNERSMGDHNERVHKRLRTVDTDSHAEQGPAQQPQAQVE-DAD 5148
Cdd:NF033609 728 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSD 807
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622932237 5149 AFEHIKQGSDAYDAQTYDVASKEQQQSAKDSGRDQEEEEIEDTLMDTEEQEElKAADVEQ------LKPEEIKSSTTA 5220
Cdd:NF033609 808 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESD-SNSDSESgsnnnvVPPNSPKNGTNA 884
|
|
| Sigma54_activ_2 |
pfam14532 |
Sigma-54 interaction domain; |
650-708 |
4.55e-03 |
|
Sigma-54 interaction domain;
Pssm-ID: 434021 [Multi-domain] Cd Length: 138 Bit Score: 40.79 E-value: 4.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622932237 650 FAATRPSSVLIEQLAVCVSKGEPVLLVGETGTGKTSTVQYLAHITGHRLRVVNMNQQSD 708
Cdd:pfam14532 1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAH 59
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
2228-2294 |
4.56e-03 |
|
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: 40.12 E-value: 4.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622932237 2228 MLVQALKSGDWLLMDNVNFCnPSVLDRLNALLEpggvltisergmidgSTPTITPNPNFRLFLSMDP 2294
Cdd:pfam03028 49 LIEEAAKEGGWVLLQNCHLA-LSWMPELEKILE---------------ELPEETLHPDFRLWLTSEP 99
|
|
| CobT2 |
COG4547 |
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ... |
4934-5022 |
4.72e-03 |
|
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 443611 [Multi-domain] Cd Length: 608 Bit Score: 43.24 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4934 NESQSPQEPEEGPSEDDKAKGEEEMDTGADDQDGDAAQHPEEHSEEQQQSLEEKDKDADEEGGENGPADQgfqpqkqeee 5013
Cdd:COG4547 209 EELGEDEDEEDEDDEDDSGEQEEDEEDGEDEDEESDEGAEAEDAEASGDDAEEGESEAAEAESDEMAEEA---------- 278
|
....*....
gi 1622932237 5014 qeDSDTEEQ 5022
Cdd:COG4547 279 --EGEDSEE 285
|
|
| RecA-like_ATAD1 |
cd19520 |
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ... |
1738-1784 |
6.10e-03 |
|
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410928 [Multi-domain] Cd Length: 166 Bit Score: 40.87 E-value: 6.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1622932237 1738 RLLRATKlkkPILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQTD 1784
Cdd:cd19520 30 RLLQPPK---GVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTD 73
|
|
| COG5137 |
COG5137 |
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics] ... |
4915-5004 |
6.11e-03 |
|
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics];
Pssm-ID: 227466 [Multi-domain] Cd Length: 279 Bit Score: 42.29 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4915 EKPEEAGHEAEEREteTDQNESQSPQEPEEGPSEDDKAKGEEEMDTGADDQDGDaaqHPEEHSEEQQQSLEEKDKDAD-- 4992
Cdd:COG5137 176 NEEEERLEESDGRE--EEEDEEVGSDSYGEGNRELNEEEEEEAEGSDDGEDVVD---YEGERIDKKQGEEEEMEEEVInl 250
|
90
....*....|....
gi 1622932237 4993 --EEGGENGPADQG 5004
Cdd:COG5137 251 feIEWEEESPSEEV 264
|
|
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
1741-1779 |
7.33e-03 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 43.08 E-value: 7.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1622932237 1741 RATKLKKPIL-LEGSPGVGKTSLVGALAKASGNTLVRINL 1779
Cdd:COG0466 346 LKKKLKGPILcLVGPPGVGKTSLGKSIARALGRKFVRISL 385
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4843-5079 |
8.98e-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: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4843 DGGEGE---DKINEQIDEREYDENEVDPYHGNQEKLPEPEALDLPDDLNLDSEDKNGGEDTDNEEGEEENPLEIKEKPEE 4919
Cdd:TIGR00927 634 DVAEAEhtgERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAE 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 4920 AGHEAEERETETDQNESQSpQEPEEGPSEDDKAKGEEEmdtGADDQDGDAAQHPEEHSEEQQQSLEEKDKDADEEGGENG 4999
Cdd:TIGR00927 714 EVEHEGETEAEGTEDEGEI-ETGEEGEEVEDEGEGEAE---GKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDG 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 5000 --PADQGFQPQKQEEEQEDSDTEEQVPEVLERKEHASCGQTGVENMQSTqaVELAGAAPEKEQGKEehGSGAADANQAEG 5077
Cdd:TIGR00927 790 emKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELN--AENQGEAKQDEKGVD--GGGGSDGGDSEE 865
|
..
gi 1622932237 5078 HE 5079
Cdd:TIGR00927 866 EE 867
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
312-432 |
9.25e-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: 40.21 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622932237 312 LETLAMAV--ASQNAVLLEGPIGCGKTSLVEYLAAMTGRTKPPqLLKVQLGDqtdskMLLGMYRCTDVpGEFVWQPGTLT 389
Cdd:cd00009 7 IEALREALelPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-FLYLNASD-----LLEGLVVAELF-GHFLVRLLFEL 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1622932237 390 QAATMGHWILLEDIDYAPLDVVSVLIPLLENGDLLIPGQGDCL 432
Cdd:cd00009 80 AEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRENVR 122
|
|
| |
