|
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 ... |
5331-5601 |
1.19e-146 |
|
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: 457.58 E-value: 1.19e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5331 LSQQLCEQLRLILEPTQAAKLKGDYRTGKRLNMRKVIPYIASQFRKDKIWLRRTKPSKRQYQICLAIDDSSSMVDNHTKQ 5410
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5411 LAFESLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEQFSDYSGSQILRLCKFQQKKTKIAQFLESVANMFAAARQLSQ 5490
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDARTQSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5491 NVSPEtaQLLLVVSDGRGLFLEGKDRVLaaVQAARNANIFVIFVVLDNPNSRDSILDIKVPIFKGPGeMPEIRSYMEEFP 5570
Cdd:cd01460 161 SGSLW--QLLLIISDGRGEFSEGAQKVR--LREAREQNVFVVFIIIDNPDNKQSILDIKVVSFKNDK-SGVITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|.
gi 955495717 5571 FPFYIILRDVNALPETLSDALRQWFELVTAS 5601
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 |
1.18e-39 |
|
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: 144.26 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 915 DLQILIVDYLKGLSVNKSTVQGIINFYIAVRKDSGTKLVDGTGHKPHYSLRTLCRALRFAASN-PCSNIQRSLYEGFCLG 993
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLVRDIVKFYLEAKKLAEKSLVDGAGQRPHYSLRTLCRALSYARAIaPRYGLRRALYEGFCMS 80
|
90 100
....*....|....*....|....
gi 955495717 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 |
1.26e-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: 111.23 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1385 PVLLVGDTGCGKTTICQVFA-ALANQKLYSVNCHLHMETSDFLGGLRPVRQkpkdkeeidtskLFEWHDGPLVLAMKEDG 1463
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAaALSNRPVFYVQLTRDTTEEDLFGRRNIDPG------------GASWVDGPLVRAAREGE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 955495717 1464 FFLLDEISLADDSVLERLNSVLEvEKSLVLAEKGSLEDKDNevelltagKKFRILATMNPgGDFGKKELSPALRNRF 1540
Cdd:pfam07728 69 IAVLDEINRANPDVLNSLLSLLD-ERRLLLPDGGELVKAAP--------DGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1900-1998 |
1.84e-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: 100.84 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1900 DMEFIASTLFPaIDKNIVKKMVAFNNQIDHEVTVEKKWGQKGGPWEFNLRDLFRWCQLM-----LVDQSPGCYDPGQHVF 1974
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLssllpTLLSPTVREEIFLEAV 79
|
90 100
....*....|....*....|....
gi 955495717 1975 LVYGERMRTREDKEKVIAVFKDVF 1998
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVL 103
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1227-1328 |
2.03e-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: 95.06 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1227 ELETILHKRCSLPPSYCSKLVKVMLDLQSCRRSSSVFA--GKQGFITLRDLFRWAERYRLAEQTEKEYDWLQHLANNGFM 1304
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGssGSPREFNLRDLLRWCRRLSSLLPTLLSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....
gi 955495717 1305 LLAGRVRKQEEVDVIQEVLEKHFK 1328
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLG 104
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
1079-1215 |
6.82e-22 |
|
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: 94.67 E-value: 6.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1079 PVLIQGETSVGKTSLIRWLAAATGNHCVR-INNHEHTDIQEYIGCYTSDSSGKlVFKEGVLIDAMRKGYWIILDELNLAP 1157
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFyVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 955495717 1158 TDVLEALNRLLDDNRELFITETQEVVKAHPRFMLFATQNPPglYGGRKMLSRAFRNRF 1215
Cdd:pfam07728 80 PDVLNSLLSLLDERRLLLPDGGELVKAAPDGFRLIATMNPL--DRGLNELSPALRSRF 135
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
325-453 |
2.71e-20 |
|
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: 90.04 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 325 VLLEGPIGCGKTSLVEHLAAMTGRRKppqLLKVQLGDQTDSKMLLGMYRCTdvPGEFVWQPGTLTQAATKGHWILLEDID 404
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRP---VFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 955495717 405 YAPLDVVSVLIPLLENGELLIP-GRGDCLKVASGFQFFATRRLLSCGGNW 453
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLPdGGELVKAAPDGFRLIATMNPLDRGLNE 126
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
480-604 |
4.35e-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: 82.73 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 480 ELNEVLQNRYPSLLSATDHLLDIYLQLTAEKHRPQSDSSVGceqapeevsearrenkrlslEGRELSLRDLLNWCNRIAH 559
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSG--------------------SPREFNLRDLLRWCRRLSS 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 955495717 560 SFDSLSSSASL-NIFQEALDCFTAMLSKHTSKLKMAEVIGSKLNIS 604
Cdd:pfam17867 61 LLPTLLSPTVReEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
1748-1888 |
8.77e-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: 80.03 E-value: 8.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1748 PILLEGSPGVGKTSLVGALAKA-SGNTLVRINLSEQTDITDLFGADLPveggKGGEFAWRDGPLLAALKAGHWVVLDELN 1826
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNI----DPGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 955495717 1827 LASQSVLEGLNACFDHRgEIYVPELGMSFQVQHDKTKIFGCQNPfrQGGGRKGLPRSFLNRF 1888
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDGFRLIATMNP--LDRGLNELSPALRSRF 135
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4687-5280 |
7.04e-16 |
|
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: 85.84 E-value: 7.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4687 DVSDQIENEEQAEDTFQKGQEKDKEDPDSKSDIKGEDNAIEMSEDFDGKmhdgeleekEEDDEKSDSEGRDLDKQMGDLN 4766
Cdd:COG5271 360 DTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTS---------PTSDTDEEEEEADEDASAGETE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4767 GEEADKLDERLWGDDDEEEDEEEEDNKTEETGPGMDEEDCELVAKGDNLDAGksnrdknwqDKEEKKEAETDDDGQGQEK 4846
Cdd:COG5271 431 DESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDEAT---------DEDDASDDGDEEEAEEDAE 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4847 INEQIDEREYDENEVDPYHGNQEKLPEPEALDLPDDLNLDSEDKNSGEDTDHEEGEEENPLEiKEKPVDTEEAGPeaEEI 4926
Cdd:COG5271 502 AEADSDELTAEETSADDGADTDAAADPEDSDEDALEDETEGEENAPGSDQDADETDEPEATA-EEDEPDEAEAET--EDA 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4927 NEETEADQSEGQGHCEPEEGPSEDDDDKGEgeeemDTGADDQDKDTEHPEENSGEEQQSLEDKDKEASEESTEDggpvdq 5006
Cdd:COG5271 579 TENADADETEESADESEEAEASEDEAAEEE-----EADDDEADADADGAADEEETEEEAAEDEAAEPETDASEA------ 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5007 glQPQMQEKEEEGDNSD--TEEEVPEATERKEHDScgqtglesmqstqavELAGVAPEKEQGKEEHGSGAADANQAEG-H 5083
Cdd:COG5271 648 --ADEDADAETEAEASAdeSEEEAEDESETSSEDA---------------EEDADAAAAEASDDEEETEEADEDAETAsE 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5084 ESNFIARLASQKQTRKNTQSFKRKPGQADNERSmgdhsehvhkrLRTVDIDSHTEQGPAQPQAQAEDAEAFEHIKQGSDP 5163
Cdd:COG5271 711 EADAEEADTEADGTAEEAEEAAEEAESADEEAA-----------SLPDEADAEEEAEEAEEAEEDDADGLEEALEEEKAD 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5164 YDAQTYDvASKEQQQFAKDSSKDQEEEETEDVFMDLEEQEELTAGDPEqlkpEEVKSgtraspgfDEMEMEIETQTVKTE 5243
Cdd:COG5271 780 AEEAATD-EEAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGE----DEETA--------DEALEDIEAGIAEDD 846
|
570 580 590
....*....|....*....|....*....|....*..
gi 955495717 5244 EDQDPRTDKSRKETENEKPERSRDSTIHTAHQFLVDT 5280
Cdd:COG5271 847 EEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAET 883
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
672-902 |
6.64e-09 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.
The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 57.30 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 672 PVLLVGETGTGKTSAVQYLAH-ITGHRLRVVNMNQQSDTADLLGGYKPvdhkliwlplreafeelfaqtfskkqnftflg 750
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRNI-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 751 hiqtcyrqkrwhdllrlmqhvhksavnkdgkesetglllkekweafglrldhaqqqmkmteSALLFAFVEGTLAQAVKKG 830
Cdd:pfam07728 49 -------------------------------------------------------------DPGGASWVDGPLVRAAREG 67
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 955495717 831 EWILLDEINLAAPETLECLSGLLEGSSgslVLLDRGDTEPLVRHPDFRLFACMNPAtDVGKRNLPPGIRNRF 902
Cdd:pfam07728 68 EIAVLDEINRANPDVLNSLLSLLDERR---LLLPDGGELVKAAPDGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
2220-2306 |
3.74e-08 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.
The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 55.38 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 2220 GTFEWVDSMLVQALTSGDWLLMDNVNFCNPSVLDRLNALLEPGgvltvsERGMIDGSTPTITPNPNFRLFLSMDPVHG-- 2297
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDER------RLLLPDGGELVKAAPDGFRLIATMNPLDRgl 124
|
90
....*....|
gi 955495717 2298 -EISRAMRNR 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 ... |
643-693 |
1.65e-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 cd03223:
Pssm-ID: 476819 [Multi-domain] Cd Length: 166 Bit Score: 42.53 E-value: 1.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 955495717 643 IQREKLTFAaTRPSSVLIEQLAVCVSRGEPVLLVGETGTGKTSAVQYLAHI 693
Cdd:cd03223 1 IELENLSLA-TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL 50
|
|
| |
|
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 ... |
5331-5601 |
1.19e-146 |
|
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: 457.58 E-value: 1.19e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5331 LSQQLCEQLRLILEPTQAAKLKGDYRTGKRLNMRKVIPYIASQFRKDKIWLRRTKPSKRQYQICLAIDDSSSMVDNHTKQ 5410
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5411 LAFESLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEQFSDYSGSQILRLCKFQQKKTKIAQFLESVANMFAAARQLSQ 5490
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDARTQSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5491 NVSPEtaQLLLVVSDGRGLFLEGKDRVLaaVQAARNANIFVIFVVLDNPNSRDSILDIKVPIFKGPGeMPEIRSYMEEFP 5570
Cdd:cd01460 161 SGSLW--QLLLIISDGRGEFSEGAQKVR--LREAREQNVFVVFIIIDNPDNKQSILDIKVVSFKNDK-SGVITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|.
gi 955495717 5571 FPFYIILRDVNALPETLSDALRQWFELVTAS 5601
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 |
1.18e-39 |
|
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: 144.26 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 915 DLQILIVDYLKGLSVNKSTVQGIINFYIAVRKDSGTKLVDGTGHKPHYSLRTLCRALRFAASN-PCSNIQRSLYEGFCLG 993
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLVRDIVKFYLEAKKLAEKSLVDGAGQRPHYSLRTLCRALSYARAIaPRYGLRRALYEGFCMS 80
|
90 100
....*....|....*....|....
gi 955495717 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 |
1.26e-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: 111.23 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1385 PVLLVGDTGCGKTTICQVFA-ALANQKLYSVNCHLHMETSDFLGGLRPVRQkpkdkeeidtskLFEWHDGPLVLAMKEDG 1463
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAaALSNRPVFYVQLTRDTTEEDLFGRRNIDPG------------GASWVDGPLVRAAREGE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 955495717 1464 FFLLDEISLADDSVLERLNSVLEvEKSLVLAEKGSLEDKDNevelltagKKFRILATMNPgGDFGKKELSPALRNRF 1540
Cdd:pfam07728 69 IAVLDEINRANPDVLNSLLSLLD-ERRLLLPDGGELVKAAP--------DGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1900-1998 |
1.84e-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: 100.84 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1900 DMEFIASTLFPaIDKNIVKKMVAFNNQIDHEVTVEKKWGQKGGPWEFNLRDLFRWCQLM-----LVDQSPGCYDPGQHVF 1974
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLssllpTLLSPTVREEIFLEAV 79
|
90 100
....*....|....*....|....
gi 955495717 1975 LVYGERMRTREDKEKVIAVFKDVF 1998
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVL 103
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1227-1328 |
2.03e-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: 95.06 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1227 ELETILHKRCSLPPSYCSKLVKVMLDLQSCRRSSSVFA--GKQGFITLRDLFRWAERYRLAEQTEKEYDWLQHLANNGFM 1304
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGssGSPREFNLRDLLRWCRRLSSLLPTLLSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....
gi 955495717 1305 LLAGRVRKQEEVDVIQEVLEKHFK 1328
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1079-1215 |
6.82e-22 |
|
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: 94.67 E-value: 6.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1079 PVLIQGETSVGKTSLIRWLAAATGNHCVR-INNHEHTDIQEYIGCYTSDSSGKlVFKEGVLIDAMRKGYWIILDELNLAP 1157
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFyVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 955495717 1158 TDVLEALNRLLDDNRELFITETQEVVKAHPRFMLFATQNPPglYGGRKMLSRAFRNRF 1215
Cdd:pfam07728 80 PDVLNSLLSLLDERRLLLPDGGELVKAAPDGFRLIATMNPL--DRGLNELSPALRSRF 135
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
325-453 |
2.71e-20 |
|
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: 90.04 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 325 VLLEGPIGCGKTSLVEHLAAMTGRRKppqLLKVQLGDQTDSKMLLGMYRCTdvPGEFVWQPGTLTQAATKGHWILLEDID 404
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRP---VFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 955495717 405 YAPLDVVSVLIPLLENGELLIP-GRGDCLKVASGFQFFATRRLLSCGGNW 453
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLPdGGELVKAAPDGFRLIATMNPLDRGLNE 126
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
480-604 |
4.35e-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: 82.73 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 480 ELNEVLQNRYPSLLSATDHLLDIYLQLTAEKHRPQSDSSVGceqapeevsearrenkrlslEGRELSLRDLLNWCNRIAH 559
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSG--------------------SPREFNLRDLLRWCRRLSS 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 955495717 560 SFDSLSSSASL-NIFQEALDCFTAMLSKHTSKLKMAEVIGSKLNIS 604
Cdd:pfam17867 61 LLPTLLSPTVReEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1748-1888 |
8.77e-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: 80.03 E-value: 8.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1748 PILLEGSPGVGKTSLVGALAKA-SGNTLVRINLSEQTDITDLFGADLPveggKGGEFAWRDGPLLAALKAGHWVVLDELN 1826
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNI----DPGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 955495717 1827 LASQSVLEGLNACFDHRgEIYVPELGMSFQVQHDKTKIFGCQNPfrQGGGRKGLPRSFLNRF 1888
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDGFRLIATMNP--LDRGLNELSPALRSRF 135
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4687-5280 |
7.04e-16 |
|
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: 85.84 E-value: 7.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4687 DVSDQIENEEQAEDTFQKGQEKDKEDPDSKSDIKGEDNAIEMSEDFDGKmhdgeleekEEDDEKSDSEGRDLDKQMGDLN 4766
Cdd:COG5271 360 DTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTS---------PTSDTDEEEEEADEDASAGETE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4767 GEEADKLDERLWGDDDEEEDEEEEDNKTEETGPGMDEEDCELVAKGDNLDAGksnrdknwqDKEEKKEAETDDDGQGQEK 4846
Cdd:COG5271 431 DESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDEAT---------DEDDASDDGDEEEAEEDAE 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4847 INEQIDEREYDENEVDPYHGNQEKLPEPEALDLPDDLNLDSEDKNSGEDTDHEEGEEENPLEiKEKPVDTEEAGPeaEEI 4926
Cdd:COG5271 502 AEADSDELTAEETSADDGADTDAAADPEDSDEDALEDETEGEENAPGSDQDADETDEPEATA-EEDEPDEAEAET--EDA 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4927 NEETEADQSEGQGHCEPEEGPSEDDDDKGEgeeemDTGADDQDKDTEHPEENSGEEQQSLEDKDKEASEESTEDggpvdq 5006
Cdd:COG5271 579 TENADADETEESADESEEAEASEDEAAEEE-----EADDDEADADADGAADEEETEEEAAEDEAAEPETDASEA------ 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5007 glQPQMQEKEEEGDNSD--TEEEVPEATERKEHDScgqtglesmqstqavELAGVAPEKEQGKEEHGSGAADANQAEG-H 5083
Cdd:COG5271 648 --ADEDADAETEAEASAdeSEEEAEDESETSSEDA---------------EEDADAAAAEASDDEEETEEADEDAETAsE 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5084 ESNFIARLASQKQTRKNTQSFKRKPGQADNERSmgdhsehvhkrLRTVDIDSHTEQGPAQPQAQAEDAEAFEHIKQGSDP 5163
Cdd:COG5271 711 EADAEEADTEADGTAEEAEEAAEEAESADEEAA-----------SLPDEADAEEEAEEAEEAEEDDADGLEEALEEEKAD 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5164 YDAQTYDvASKEQQQFAKDSSKDQEEEETEDVFMDLEEQEELTAGDPEqlkpEEVKSgtraspgfDEMEMEIETQTVKTE 5243
Cdd:COG5271 780 AEEAATD-EEAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGE----DEETA--------DEALEDIEAGIAEDD 846
|
570 580 590
....*....|....*....|....*....|....*..
gi 955495717 5244 EDQDPRTDKSRKETENEKPERSRDSTIHTAHQFLVDT 5280
Cdd:COG5271 847 EEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAET 883
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4768-5327 |
1.09e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.48 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4768 EEADKLDERLWGDDDEEEDEEEEDNKTEETGPGMDEEDCELVAKGDNLDAGKSNR--DKNWQDKEEKKEAETDDDGQGQE 4845
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAeaAEKKKEEAKKKADAAKKKAEEKK 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4846 KINEQIDEREYDENEVDpyhgnqEKLPEPEALDLPDDLNLDSEDKNSGEdtdheegeeenplEIKEKpvdTEEAGPEAEE 4925
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKAD------ELKKAAAAKKKADEAKKKAEEKKKAD-------------EAKKK---AEEAKKADEA 1449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4926 INEETEADQSEGQGHCEPEEGPSEDDDDKGEGEEEmdtgADDQDKDTEHPEENSGEEQQSLEDKDKEASEESTEDGGPVD 5005
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK----ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD 1525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5006 QGLQPQMQEKEEEGDNSdteEEVPEATERKEhdscgqtgLESMQSTQAVELAGVAPEKEQGKEEHGSGAADANQAEGHES 5085
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKA---EEKKKADELKK--------AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5086 NFIARLASQKQTRKNTQSfkRKPGQADNERSMGDHSEHVHKRLRTVDIDSHTEQGPAQpqaQAEDAEAFEHIKQGSDPYD 5165
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEA--KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEEAKK 1669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5166 AQtydvaskEQQQFAKDSSKDQEEEETEDVFMDLEEQEELTAgdpEQLKPEEVKSGTRAspgfDEMEMEIETQTVKTEED 5245
Cdd:PTZ00121 1670 AE-------EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA---EELKKKEAEEKKKA----EELKKAEEENKIKAEEA 1735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5246 QDPRTDKSRKETENEKPERSRDSTIHTAHQflvdtifppLLKDVSELRQELERQLE--MWQPHESGNPEEEKAAADMWQN 5323
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEKKKIAHLKKE---------EEKKAEEIRKEKEAVIEeeLDEEDEKRRMEVDKKIKDIFDN 1806
|
....
gi 955495717 5324 YLVL 5327
Cdd:PTZ00121 1807 FANI 1810
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4933-5216 |
4.21e-11 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 70.02 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4933 DQSEGQGHCEPEEGPSE-----DDDDKGEGEEEMDTGADDQDKdtehpEENSGEEQQSLEDKDK---EASEESTEDGGPV 5004
Cdd:TIGR00927 636 AEAEHTGERTGEEGERPteaegENGEESGGEAEQEGETETKGE-----NESEGEIPAERKGEQEgegEIEAKEADHKGET 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5005 DQGLQPQMQEKEEEGDNSDTEEEVPEATErkehdSCGQTGLESMQSTQAVELAGVAPEKEQGKEEHGSGAADANQAEGHe 5084
Cdd:TIGR00927 711 EAEEVEHEGETEAEGTEDEGEIETGEEGE-----EVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQ- 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5085 snfiarlASQKQTRKNTQSFKRKpGQADNERSMGDHSEHVHKRlRTVDIDSHTEQGPAQPQAQAEDAEAFEHIKQGSDpy 5164
Cdd:TIGR00927 785 -------AGEDGEMKGDEGAEGK-VEHEGETEAGEKDEHEGQS-ETQADDTEVKDETGEQELNAENQGEAKQDEKGVD-- 853
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 955495717 5165 DAQTYDVASKEQQQFAKDSSKDQEEEETEdvfmdlEEQEELTAGDPEQLK-PE 5216
Cdd:TIGR00927 854 GGGGSDGGDSEEEEEEEEEEEEEEEEEEE------EEEEEEENEEPLSLEwPE 900
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1736-1888 |
2.11e-10 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 65.19 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1736 AQRLLRATKLNKPILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQTDITDLFGADLPVEggKGGEFAWRDGPLLAAlk 1815
Cdd:COG0714 21 IELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQ--QTGEFEFRPGPLFAN-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1816 aghwVVL-DELNLAS---QS----VLEglnacfdhRGEIYVP----ELGMSFQVqhdktkiFGCQNPFRQGGGRKgLPRS 1883
Cdd:COG0714 97 ----VLLaDEINRAPpktQSalleAME--------ERQVTIPggtyKLPEPFLV-------IATQNPIEQEGTYP-LPEA 156
|
....*
gi 955495717 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 |
4.67e-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: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1079 PVLIQGETSVGKTSLIRWLAAATGNHCVRINNHEHTDIQEyiGCYTSD---SSGKLVFKEG------VLIdamrkgywii 1149
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSD--ILGTYIydqQTGEFEFRPGplfanvLLA---------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1150 lDELNLAPTDVLEALNRLLDDNRelfITETQEVVKAHPRFMLFATQNPPGLYGGRkMLSRAFRNRF-VELHFDeLPSSEL 1228
Cdd:COG0714 101 -DEINRAPPKTQSALLEAMEERQ---VTIPGGTYKLPEPFLVIATQNPIEQEGTY-PLPEAQLDRFlLKLYIG-YPDAEE 174
|
....*...
gi 955495717 1229 ET-ILHKR 1235
Cdd:COG0714 175 EReILRRH 182
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
5393-5543 |
3.37e-09 |
|
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.
Pssm-ID: 214621 [Multi-domain] Cd Length: 175 Bit Score: 59.39 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5393 ICLAIDDSSSMVDNhTKQLAFESLAVIGNALTLLEVG-QIAVCSFGESVKLLHPFHeqfSDYSGSQILRLCKFQQKK--- 5468
Cdd:smart00327 2 VVFLLDGSGSMGGN-RFELAKEFVLKLVEQLDIGPDGdRVGLVTFSDDARVLFPLN---DSRSKDALLEALASLSYKlgg 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 955495717 5469 -TKIAQFLESVANMFAAARQLSQnvsPETAQLLLVVSDGRGLFleGKDRVLAAVQAARNANIFVIFVVLDNPNSRD 5543
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 ... |
672-902 |
6.64e-09 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 57.30 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 672 PVLLVGETGTGKTSAVQYLAH-ITGHRLRVVNMNQQSDTADLLGGYKPvdhkliwlplreafeelfaqtfskkqnftflg 750
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRNI-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 751 hiqtcyrqkrwhdllrlmqhvhksavnkdgkesetglllkekweafglrldhaqqqmkmteSALLFAFVEGTLAQAVKKG 830
Cdd:pfam07728 49 -------------------------------------------------------------DPGGASWVDGPLVRAAREG 67
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 955495717 831 EWILLDEINLAAPETLECLSGLLEGSSgslVLLDRGDTEPLVRHPDFRLFACMNPAtDVGKRNLPPGIRNRF 902
Cdd:pfam07728 68 EIAVLDEINRANPDVLNSLLSLLDERR---LLLPDGGELVKAAPDGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2220-2306 |
3.74e-08 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 55.38 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 2220 GTFEWVDSMLVQALTSGDWLLMDNVNFCNPSVLDRLNALLEPGgvltvsERGMIDGSTPTITPNPNFRLFLSMDPVHG-- 2297
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDER------RLLLPDGGELVKAAPDGFRLIATMNPLDRgl 124
|
90
....*....|
gi 955495717 2298 -EISRAMRNR 2306
Cdd:pfam07728 125 nELSPALRSR 134
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1383-1540 |
4.05e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.84 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1383 GEPVLLVGDTGCGKTTICQVFAALANQKLYSV---NCHLHMETSDFLGGLRPVRQKPKDKEEIDT-SKLFEwhdgplvLA 1458
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGViyiDGEDILEEVLDQLLLIIVGGKKASGSGELRlRLALA-------LA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1459 MKED-GFFLLDEISLADDSVLERLNSVLEVEKSLVLAEKgsledkdnevelltaGKKFRILATMNPGGDFGKKELSPALR 1537
Cdd:smart00382 75 RKLKpDVLILDEITSLLDAEQEALLLLLEELRLLLLLKS---------------EKNLTVILTTNDEKDLGPALLRRRFD 139
|
...
gi 955495717 1538 NRF 1540
Cdd:smart00382 140 RRI 142
|
|
| Granin |
pfam01271 |
Granin (chromogranin or secretogranin); |
4910-5265 |
7.10e-08 |
|
Granin (chromogranin or secretogranin);
Pssm-ID: 279595 [Multi-domain] Cd Length: 584 Bit Score: 59.28 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4910 KEKPVDTEEAGPEAEEINEETEADQSEGQGHCEPEEGPSEDDDDKGEGEEEMDTGADDQDKDTEhPEENSGEEQQSLEDK 4989
Cdd:pfam01271 116 KEFKTDHSDDYETQQWEEEKLKHMRFPLRYEENSEEKHSEREGELSEVFENPRSQATLKKVFEE-VSRLDTPSKQKREKS 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4990 DKE--ASEESTEDGG-----PVDQGLQPQMQEKEEEGDNSDTEEEVPEATERKEHDSCGQTglESMQSTQA-VELAGVAP 5061
Cdd:pfam01271 195 DERekSSQESGEDTYrqeniPQEDQVGPEDQEPSEEGEEDATQEEVKRSRPRTHHGRSLPD--ESSRGGQLgLEEEASEE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5062 EKEQGKEEHGSGAADANQAEGHESNFIARLASQKQTRKNTQSFK--RKPGQADNE-RSMGDHSEHVHKRLRTVDIDSHTE 5138
Cdd:pfam01271 273 EEEYGEESRGLSAVQTYLLRLVNARGRGRSEKRAERERSEESEEeeLKRASPYEElEITANLQIPPSEEERMLKKAGRSP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5139 QGPAQPQAQAEDAEAFEHIKQGS-DPYDAQ-----TYDVASKEQQQFAKDSSKDQEEEETEDVFMDLEEQEeltagdPEQ 5212
Cdd:pfam01271 353 RGRVDEAGALEALEALEEKRKLDlDHSRVFessedGAPRAPQGAWVEALRNYLSYGEEGMEGKWNQQGPYF------PNE 426
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 955495717 5213 LKPEEVKSGTRASPGFDEMEMEIETQTVKT-EEDQDPRTDKSRKETENEKPERS 5265
Cdd:pfam01271 427 ENREEARFRLPQYLGELSNPWEDPKQWKPSdFERKELTADKFLEGEEENEYTLS 480
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1372-1571 |
2.26e-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: 55.94 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1372 LAMLVGRalefgePVLLVGDTGCGKTTICQVFAALANQKLYSVNCHLHMETSDFLGglrpvrqkpkdkEEI---DTSKlF 1448
Cdd:COG0714 26 IALLAGG------HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILG------------TYIydqQTGE-F 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1449 EWHDGPlVLAmkedGFFLLDEISLADDSVLerlNSVLEVekslvLAEKgsledkdnEV----ELLTAGKKFRILATMNPG 1524
Cdd:COG0714 87 EFRPGP-LFA----NVLLADEINRAPPKTQ---SALLEA-----MEER--------QVtipgGTYKLPEPFLVIATQNPI 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 955495717 1525 GDFGKKELSPALRNRFT-EIWC--PqstSREDLIQIISR-------NLRPGLSLGRI 1571
Cdd:COG0714 146 EQEGTYPLPEAQLDRFLlKLYIgyP---DAEEEREILRRhtgrhlaEVEPVLSPEEL 199
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1747-1896 |
1.12e-06 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 51.38 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1747 KPILLEGSPGVGKTSLVGALAKAS---GNTLVRINLSeqtditDLFGADlpVEGGKGGEFAWRDGPLLAALKAGHWVVLD 1823
Cdd:cd00009 20 KNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNAS------DLLEGL--VVAELFGHFLVRLLFELAEKAKPGVLFID 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 955495717 1824 ELNLASQSVLEGLNACFdhrgeiyvpELGMSFQVQHDKTKIFG-CQNPFRQgggrkGLPRSFLNRFTQVFVDPL 1896
Cdd:cd00009 92 EIDSLSRGAQNALLRVL---------ETLNDLRIDRENVRVIGaTNRPLLG-----DLDRALYDRLDIRIVIPL 151
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1385-1618 |
1.96e-06 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 53.97 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1385 PVLLVGDTGCGKTTICQVFAALANQKLYSVNchlhmetsdflgglrPVRQKPKDKEEIDTSKLFewHDGPLVLAMKEDGF 1464
Cdd:PHA02244 121 PVFLKGGAGSGKNHIAEQIAEALDLDFYFMN---------------AIMDEFELKGFIDANGKF--HETPFYEAFKKGGL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1465 FLLDEISLADDSVLERLNSvlevekslVLAEKGSledkDNEVELLTAGKKFRILA---TMNPGGD---FGKKELSPALRN 1538
Cdd:PHA02244 184 FFIDEIDASIPEALIIINS--------AIANKFF----DFADERVTAHEDFRVISagnTLGKGADhiyVARNKIDGATLD 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1539 RFTEIWCPQSTSREDLIQIISRNLRPGLSLGRIdhkgvDIAEVMLDFtdwlthqefgrrcVVSIRDILSWVNFMNTMGEE 1618
Cdd:PHA02244 252 RFAPIEFDYDEKIEHLISNGDEDLVNFVALLRH-----EMAEKGLDH-------------VFSMRAIIHGKKFDGVFEAD 313
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1068-1221 |
1.90e-05 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 50.89 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1068 DIVRVVSAGTyPVLIQGETSVGKTSLIRWLAAAtgnhcVRINNHEHTDI-QEYIGCYTSDSSGKlvFKEGVLIDAMRKGY 1146
Cdd:PHA02244 111 DIAKIVNANI-PVFLKGGAGSGKNHIAEQIAEA-----LDLDFYFMNAImDEFELKGFIDANGK--FHETPFYEAFKKGG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1147 WIILDELNLAPTDVLEALNRLLDDNRELFITETqevVKAHPRFMLFATQNPPG-----LYGGRKMLSRAFRNRFVELHFD 1221
Cdd:PHA02244 183 LFFIDEIDASIPEALIIINSAIANKFFDFADER---VTAHEDFRVISAGNTLGkgadhIYVARNKIDGATLDRFAPIEFD 259
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
320-432 |
8.69e-05 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 45.99 E-value: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 320 ASQNAVLLEGPIGCGKTSLVEHLAAMTGRRKPPqLLKVQLGDqtdskMLLGMYRCTDVpGEFVWQPGTLTQAATKGHWIL 399
Cdd:cd00009 17 PPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-FLYLNASD-----LLEGLVVAELF-GHFLVRLLFELAEKAKPGVLF 89
|
90 100 110
....*....|....*....|....*....|...
gi 955495717 400 LEDIDYAPLDVVSVLIPLLENGELLIPGRGDCL 432
Cdd:cd00009 90 IDEIDSLSRGAQNALLRVLETLNDLRIDRENVR 122
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1079-1221 |
2.75e-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: 44.67 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1079 PVLIQGETSVGKTSLIR---WLAAATGNHCVRIN----NHEHTDIQEYIGCYTSDSSGKLVFKEGVLIDAMRKGYW--II 1149
Cdd:smart00382 4 VILIVGPPGSGKTTLARalaRELGPPGGGVIYIDgediLEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPdvLI 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 955495717 1150 LDELNLAPTDVLEALNRLLDDNRELFITEtqevvKAHPRFMLFATQNPPGLygGRKMLSRAFRNRFVELHFD 1221
Cdd:smart00382 84 LDEITSLLDAEQEALLLLLEELRLLLLLK-----SEKNLTVILTTNDEKDL--GPALLRRRFDRRIVLLLIL 148
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1368-1543 |
2.81e-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: 44.44 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1368 GMRRLAMLVGRALEFGEP--VLLVGDTGCGKTTICQVFA---ALANQKLYSVNCHLHMETSDFLGglrpvrqkpkDKEEI 1442
Cdd:cd00009 2 GQEEAIEALREALELPPPknLLLYGPPGTGKTTLARAIAnelFRPGAPFLYLNASDLLEGLVVAE----------LFGHF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1443 DTSKLFEwhdgplVLAMKEDGFFLLDEISLADDSVLERLNSVLEVekslvlaekgsledkdnEVELLTAGKKFRILATMN 1522
Cdd:cd00009 72 LVRLLFE------LAEKAKPGVLFIDEIDSLSRGAQNALLRVLET-----------------LNDLRIDRENVRVIGATN 128
|
170 180
....*....|....*....|.
gi 955495717 1523 PGGDFgkkELSPALRNRFTEI 1543
Cdd:cd00009 129 RPLLG---DLDRALYDRLDIR 146
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1079-1215 |
4.19e-04 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 44.06 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1079 PVLIQGETSVGKTSLIR---WLAAATGNHCVRINNHEHTDIqeyigcyTSDSSGKLVFKEGVLIDAMRKGYW--IILDEL 1153
Cdd:cd00009 21 NLLLYGPPGTGKTTLARaiaNELFRPGAPFLYLNASDLLEG-------LVVAELFGHFLVRLLFELAEKAKPgvLFIDEI 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 955495717 1154 NLAPTDVLEALNRLLDdnrelfiTETQEVVKAHPRFMLFATQNPPGLyggrkMLSRAFRNRF 1215
Cdd:cd00009 94 DSLSRGAQNALLRVLE-------TLNDLRIDRENVRVIGATNRPLLG-----DLDRALYDRL 143
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
1747-1782 |
9.74e-04 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 45.68 E-value: 9.74e-04
10 20 30
....*....|....*....|....*....|....*.
gi 955495717 1747 KPILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQ 1782
Cdd:PRK04195 40 KALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQ 75
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
643-693 |
1.65e-03 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 42.53 E-value: 1.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 955495717 643 IQREKLTFAaTRPSSVLIEQLAVCVSRGEPVLLVGETGTGKTSAVQYLAHI 693
Cdd:cd03223 1 IELENLSLA-TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL 50
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
669-737 |
3.00e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.59 E-value: 3.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 955495717 669 RGEPVLLVGETGTGKTSAVQYLAHI---TGHRLRVVNMNQQSDTADLLGGYKPVDHKLIWLPLREAFEELFA 737
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALA 72
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
816-919 |
8.37e-03 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 42.08 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 816 FAFVEGTLAQAVkkgewILLDEINLAAPETLeclSGLLEgssgslVLLDR-----GDTEPLvRHPdFRLFACMNPATDVG 890
Cdd:COG0714 86 FEFRPGPLFANV-----LLADEINRAPPKTQ---SALLE------AMEERqvtipGGTYKL-PEP-FLVIATQNPIEQEG 149
|
90 100 110
....*....|....*....|....*....|
gi 955495717 891 KRNLPPGIRNRFT-ELYVEELESKEDLQIL 919
Cdd:COG0714 150 TYPLPEAQLDRFLlKLYIGYPDAEEEREIL 179
|
|
| |
|
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 ... |
5331-5601 |
1.19e-146 |
|
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: 457.58 E-value: 1.19e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5331 LSQQLCEQLRLILEPTQAAKLKGDYRTGKRLNMRKVIPYIASQFRKDKIWLRRTKPSKRQYQICLAIDDSSSMVDNHTKQ 5410
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5411 LAFESLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEQFSDYSGSQILRLCKFQQKKTKIAQFLESVANMFAAARQLSQ 5490
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDARTQSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5491 NVSPEtaQLLLVVSDGRGLFLEGKDRVLaaVQAARNANIFVIFVVLDNPNSRDSILDIKVPIFKGPGeMPEIRSYMEEFP 5570
Cdd:cd01460 161 SGSLW--QLLLIISDGRGEFSEGAQKVR--LREAREQNVFVVFIIIDNPDNKQSILDIKVVSFKNDK-SGVITPYLDEFP 235
|
250 260 270
....*....|....*....|....*....|.
gi 955495717 5571 FPFYIILRDVNALPETLSDALRQWFELVTAS 5601
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 |
1.18e-39 |
|
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: 144.26 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 915 DLQILIVDYLKGLSVNKSTVQGIINFYIAVRKDSGTKLVDGTGHKPHYSLRTLCRALRFAASN-PCSNIQRSLYEGFCLG 993
Cdd:pfam17865 1 DLELLVKAYLKGVSSDDDLVRDIVKFYLEAKKLAEKSLVDGAGQRPHYSLRTLCRALSYARAIaPRYGLRRALYEGFCMS 80
|
90 100
....*....|....*....|....
gi 955495717 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 |
1.26e-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: 111.23 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1385 PVLLVGDTGCGKTTICQVFA-ALANQKLYSVNCHLHMETSDFLGGLRPVRQkpkdkeeidtskLFEWHDGPLVLAMKEDG 1463
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAaALSNRPVFYVQLTRDTTEEDLFGRRNIDPG------------GASWVDGPLVRAAREGE 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 955495717 1464 FFLLDEISLADDSVLERLNSVLEvEKSLVLAEKGSLEDKDNevelltagKKFRILATMNPgGDFGKKELSPALRNRF 1540
Cdd:pfam07728 69 IAVLDEINRANPDVLNSLLSLLD-ERRLLLPDGGELVKAAP--------DGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1900-1998 |
1.84e-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: 100.84 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1900 DMEFIASTLFPaIDKNIVKKMVAFNNQIDHEVTVEKKWGQKGGPWEFNLRDLFRWCQLM-----LVDQSPGCYDPGQHVF 1974
Cdd:pfam17867 1 DLEQILSHRFP-LLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLssllpTLLSPTVREEIFLEAV 79
|
90 100
....*....|....*....|....
gi 955495717 1975 LVYGERMRTREDKEKVIAVFKDVF 1998
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVL 103
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1227-1328 |
2.03e-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: 95.06 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1227 ELETILHKRCSLPPSYCSKLVKVMLDLQSCRRSSSVFA--GKQGFITLRDLFRWAERYRLAEQTEKEYDWLQHLANNGFM 1304
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGssGSPREFNLRDLLRWCRRLSSLLPTLLSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....
gi 955495717 1305 LLAGRVRKQEEVDVIQEVLEKHFK 1328
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLG 104
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1079-1215 |
6.82e-22 |
|
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: 94.67 E-value: 6.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1079 PVLIQGETSVGKTSLIRWLAAATGNHCVR-INNHEHTDIQEYIGCYTSDSSGKlVFKEGVLIDAMRKGYWIILDELNLAP 1157
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFyVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 955495717 1158 TDVLEALNRLLDDNRELFITETQEVVKAHPRFMLFATQNPPglYGGRKMLSRAFRNRF 1215
Cdd:pfam07728 80 PDVLNSLLSLLDERRLLLPDGGELVKAAPDGFRLIATMNPL--DRGLNELSPALRSRF 135
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
325-453 |
2.71e-20 |
|
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: 90.04 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 325 VLLEGPIGCGKTSLVEHLAAMTGRRKppqLLKVQLGDQTDSKMLLGMYRCTdvPGEFVWQPGTLTQAATKGHWILLEDID 404
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRP---VFYVQLTRDTTEEDLFGRRNID--PGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 955495717 405 YAPLDVVSVLIPLLENGELLIP-GRGDCLKVASGFQFFATRRLLSCGGNW 453
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLPdGGELVKAAPDGFRLIATMNPLDRGLNE 126
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
480-604 |
4.35e-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: 82.73 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 480 ELNEVLQNRYPSLLSATDHLLDIYLQLTAEKHRPQSDSSVGceqapeevsearrenkrlslEGRELSLRDLLNWCNRIAH 559
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSG--------------------SPREFNLRDLLRWCRRLSS 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 955495717 560 SFDSLSSSASL-NIFQEALDCFTAMLSKHTSKLKMAEVIGSKLNIS 604
Cdd:pfam17867 61 LLPTLLSPTVReEIFLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1748-1888 |
8.77e-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: 80.03 E-value: 8.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1748 PILLEGSPGVGKTSLVGALAKA-SGNTLVRINLSEQTDITDLFGADLPveggKGGEFAWRDGPLLAALKAGHWVVLDELN 1826
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEDLFGRRNI----DPGGASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 955495717 1827 LASQSVLEGLNACFDHRgEIYVPELGMSFQVQHDKTKIFGCQNPfrQGGGRKGLPRSFLNRF 1888
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPDGFRLIATMNP--LDRGLNELSPALRSRF 135
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4687-5280 |
7.04e-16 |
|
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: 85.84 E-value: 7.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4687 DVSDQIENEEQAEDTFQKGQEKDKEDPDSKSDIKGEDNAIEMSEDFDGKmhdgeleekEEDDEKSDSEGRDLDKQMGDLN 4766
Cdd:COG5271 360 DTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTS---------PTSDTDEEEEEADEDASAGETE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4767 GEEADKLDERLWGDDDEEEDEEEEDNKTEETGPGMDEEDCELVAKGDNLDAGksnrdknwqDKEEKKEAETDDDGQGQEK 4846
Cdd:COG5271 431 DESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDEAT---------DEDDASDDGDEEEAEEDAE 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4847 INEQIDEREYDENEVDPYHGNQEKLPEPEALDLPDDLNLDSEDKNSGEDTDHEEGEEENPLEiKEKPVDTEEAGPeaEEI 4926
Cdd:COG5271 502 AEADSDELTAEETSADDGADTDAAADPEDSDEDALEDETEGEENAPGSDQDADETDEPEATA-EEDEPDEAEAET--EDA 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4927 NEETEADQSEGQGHCEPEEGPSEDDDDKGEgeeemDTGADDQDKDTEHPEENSGEEQQSLEDKDKEASEESTEDggpvdq 5006
Cdd:COG5271 579 TENADADETEESADESEEAEASEDEAAEEE-----EADDDEADADADGAADEEETEEEAAEDEAAEPETDASEA------ 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5007 glQPQMQEKEEEGDNSD--TEEEVPEATERKEHDScgqtglesmqstqavELAGVAPEKEQGKEEHGSGAADANQAEG-H 5083
Cdd:COG5271 648 --ADEDADAETEAEASAdeSEEEAEDESETSSEDA---------------EEDADAAAAEASDDEEETEEADEDAETAsE 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5084 ESNFIARLASQKQTRKNTQSFKRKPGQADNERSmgdhsehvhkrLRTVDIDSHTEQGPAQPQAQAEDAEAFEHIKQGSDP 5163
Cdd:COG5271 711 EADAEEADTEADGTAEEAEEAAEEAESADEEAA-----------SLPDEADAEEEAEEAEEAEEDDADGLEEALEEEKAD 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5164 YDAQTYDvASKEQQQFAKDSSKDQEEEETEDVFMDLEEQEELTAGDPEqlkpEEVKSgtraspgfDEMEMEIETQTVKTE 5243
Cdd:COG5271 780 AEEAATD-EEAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGE----DEETA--------DEALEDIEAGIAEDD 846
|
570 580 590
....*....|....*....|....*....|....*..
gi 955495717 5244 EDQDPRTDKSRKETENEKPERSRDSTIHTAHQFLVDT 5280
Cdd:COG5271 847 EEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAET 883
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4686-5269 |
2.87e-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: 77.36 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4686 KDVSDQIENEEQAEDTFQkGQEKDKEDPDSKSDIKGEDNAIEMSEDFDGKMHDGELEEKEEDDEKSDSEGRDLDKQMGDL 4765
Cdd:COG5271 175 ADGDDTLAVADAIEATPG-GTDAVELTATLGATVTTDPGDSVAADDDLAAEEGASAVVEEEDASEDAVAAADETLLADDD 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4766 NGEEADKLDERLWgdddeeeDEEEEDNKTEETGPGMDEEDCELVAK--------GDNLDAGKSNRDKNWQDKEEKKEAET 4837
Cdd:COG5271 254 DTESAGATAEVGG-------TPDTDDEATDDADGLEAAEDDALDAEltaaqaadPESDDDADDSTLAALEGAAEDTEIAT 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4838 DDDGQGQEK-INEQIDEREYDENEVDPYHGNQEKLPEPEALDLPDDLNldsEDKNSGEDTDHEEGEEENPLEIKEKPVDT 4916
Cdd:COG5271 327 ADELAAADDeDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAAD---ESEGADTDAAADEADAAADDSADDEEASA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4917 EEAG-PEAEEINEETEADQSEGQGHCEPE--------EGPSEDD------DDKGEGEEEMDTGADDQDKDTEHPEENSGE 4981
Cdd:COG5271 404 DGGTsPTSDTDEEEEEADEDASAGETEDEstdvtsaeDDIATDEeadslaDEEEEAEAELDTEEDTESAEEDADGDEATD 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4982 EQQSLEDKDKEASE----------ESTEDGGPVDQGLQPQMQEKEEEGDNSDTEEEVPEATERKEHDscgQTGLESMQST 5051
Cdd:COG5271 484 EDDASDDGDEEEAEedaeaeadsdELTAEETSADDGADTDAAADPEDSDEDALEDETEGEENAPGSD---QDADETDEPE 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5052 QAVELAGVAPEKEQGKEEHGSGAADANQAEGHESNFIARLASQKQTRKNTQSFKRKP---GQADNERSMGDHSEhvhkrl 5128
Cdd:COG5271 561 ATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEADAdadGAADEEETEEEAAE------ 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5129 rtvdiDSHTEQGPAQPQAQAEDAEAF--------EHIKQGSDPYDAQTyDVASKEQQQFAKDSSKDQEE-----EETEDV 5195
Cdd:COG5271 635 -----DEAAEPETDASEAADEDADAEteaeasadESEEEAEDESETSS-EDAEEDADAAAAEASDDEEEteeadEDAETA 708
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 955495717 5196 FMDLEEQEELTAGDPEQLKPEEVKSGTRAS-PGFDEMEMEIETQTVKTEEDQDPRTDKSRKETENEKPERSRDST 5269
Cdd:COG5271 709 SEEADAEEADTEADGTAEEAEEAAEEAESAdEEAASLPDEADAEEEAEEAEEAEEDDADGLEEALEEEKADAEEA 783
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4768-5327 |
1.09e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.48 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4768 EEADKLDERLWGDDDEEEDEEEEDNKTEETGPGMDEEDCELVAKGDNLDAGKSNR--DKNWQDKEEKKEAETDDDGQGQE 4845
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAeaAEKKKEEAKKKADAAKKKAEEKK 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4846 KINEQIDEREYDENEVDpyhgnqEKLPEPEALDLPDDLNLDSEDKNSGEdtdheegeeenplEIKEKpvdTEEAGPEAEE 4925
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKAD------ELKKAAAAKKKADEAKKKAEEKKKAD-------------EAKKK---AEEAKKADEA 1449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4926 INEETEADQSEGQGHCEPEEGPSEDDDDKGEGEEEmdtgADDQDKDTEHPEENSGEEQQSLEDKDKEASEESTEDGGPVD 5005
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK----ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD 1525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5006 QGLQPQMQEKEEEGDNSdteEEVPEATERKEhdscgqtgLESMQSTQAVELAGVAPEKEQGKEEHGSGAADANQAEGHES 5085
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKA---EEKKKADELKK--------AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5086 NFIARLASQKQTRKNTQSfkRKPGQADNERSMGDHSEHVHKRLRTVDIDSHTEQGPAQpqaQAEDAEAFEHIKQGSDPYD 5165
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEA--KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEEAKK 1669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5166 AQtydvaskEQQQFAKDSSKDQEEEETEDVFMDLEEQEELTAgdpEQLKPEEVKSGTRAspgfDEMEMEIETQTVKTEED 5245
Cdd:PTZ00121 1670 AE-------EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA---EELKKKEAEEKKKA----EELKKAEEENKIKAEEA 1735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5246 QDPRTDKSRKETENEKPERSRDSTIHTAHQflvdtifppLLKDVSELRQELERQLE--MWQPHESGNPEEEKAAADMWQN 5323
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEKKKIAHLKKE---------EEKKAEEIRKEKEAVIEeeLDEEDEKRRMEVDKKIKDIFDN 1806
|
....
gi 955495717 5324 YLVL 5327
Cdd:PTZ00121 1807 FANI 1810
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4686-5155 |
2.78e-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: 70.81 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4686 KDVSDQIENEEQAEDTFQKGQEKDKEDPDSKSD--IKGEDNAIEMSEDFDgkmhdgeleekeeddEKSDSEGRDLDKQMG 4763
Cdd:COG5271 588 EESADESEEAEASEDEAAEEEEADDDEADADADgaADEEETEEEAAEDEA---------------AEPETDASEAADEDA 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4764 DLNGEEADKLDErlwgdddeEEDEEEEDNKTEETGPGMDEEDCELVAKGDNLDAGKSNRDKNWQDKE-EKKEAETDDDGq 4842
Cdd:COG5271 653 DAETEAEASADE--------SEEEAEDESETSSEDAEEDADAAAAEASDDEEETEEADEDAETASEEaDAEEADTEADG- 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4843 gqekINEQIDEREYDENEVDPYHGNQEKLPEPEALDLPDDLNLDSEDKNSGEDTDheegeeENPLEIKEKPVDTEEAgpe 4922
Cdd:COG5271 724 ----TAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDADGLEEALE------EEKADAEEAATDEEAE--- 790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4923 AEEINEETEADQSEgqghcEPEEGPSEDDDDKGEGEEEMDTGADDQDKDTEHPEENSGEEQQSLEDKDKEASEESTEDGG 5002
Cdd:COG5271 791 AAAEEKEKVADEDQ-----DTDEDALLDEAEADEEEDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLD 865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5003 PVDQGLQPQMQEKEEEGDNSDTEEEVPEATERKEHDS----CGQTGLESMQSTQAVELAGVAPEKEQGKEEHGSGAADAN 5078
Cdd:COG5271 866 ADLAADEHEAEEAQEAETDADADADAGEADSSGESSAaaedDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAED 945
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 955495717 5079 QAEGHESNFIARLASQKQTRKNTQSFKRKPGQADNERSMGDHSEHVHKRL-RTVDIDSHTEQGPAQPQAQAEDAEAFE 5155
Cdd:COG5271 946 DLDALALDEAGDEESDDAAADDAGDDSLADDDEALADAADDAEADDSELDaSESTGEAEGDEDDDELEDGEAAAGEAT 1023
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4933-5216 |
4.21e-11 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 70.02 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4933 DQSEGQGHCEPEEGPSE-----DDDDKGEGEEEMDTGADDQDKdtehpEENSGEEQQSLEDKDK---EASEESTEDGGPV 5004
Cdd:TIGR00927 636 AEAEHTGERTGEEGERPteaegENGEESGGEAEQEGETETKGE-----NESEGEIPAERKGEQEgegEIEAKEADHKGET 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5005 DQGLQPQMQEKEEEGDNSDTEEEVPEATErkehdSCGQTGLESMQSTQAVELAGVAPEKEQGKEEHGSGAADANQAEGHe 5084
Cdd:TIGR00927 711 EAEEVEHEGETEAEGTEDEGEIETGEEGE-----EVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQ- 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5085 snfiarlASQKQTRKNTQSFKRKpGQADNERSMGDHSEHVHKRlRTVDIDSHTEQGPAQPQAQAEDAEAFEHIKQGSDpy 5164
Cdd:TIGR00927 785 -------AGEDGEMKGDEGAEGK-VEHEGETEAGEKDEHEGQS-ETQADDTEVKDETGEQELNAENQGEAKQDEKGVD-- 853
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 955495717 5165 DAQTYDVASKEQQQFAKDSSKDQEEEETEdvfmdlEEQEELTAGDPEQLK-PE 5216
Cdd:TIGR00927 854 GGGGSDGGDSEEEEEEEEEEEEEEEEEEE------EEEEEEENEEPLSLEwPE 900
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4792-5056 |
1.19e-10 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 68.48 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4792 NKTEETGpgmDEEDCELVAKGDNLDAGKSNRdKNWQDKEEKKEAETDDDGQGQEKiNEQIDEREYDENEVDpyHGNQEKL 4871
Cdd:TIGR00927 640 HTGERTG---EEGERPTEAEGENGEESGGEA-EQEGETETKGENESEGEIPAERK-GEQEGEGEIEAKEAD--HKGETEA 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4872 PEPEALDLPDDLNLDSE-DKNSGEDTDHEEGEEENPLEIKEKPVDTEEAGPEAEEINEETEADQSEGQGHCEPEEGPSE- 4949
Cdd:TIGR00927 713 EEVEHEGETEAEGTEDEgEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMk 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4950 -DDDDKGEGEEEMDTGADDQDK---------DTEHPEENSGEEQQSLEDKDKEAS-EESTEDGGPVDQGLQPQMQEKEEE 5018
Cdd:TIGR00927 793 gDEGAEGKVEHEGETEAGEKDEhegqsetqaDDTEVKDETGEQELNAENQGEAKQdEKGVDGGGGSDGGDSEEEEEEEEE 872
|
250 260 270
....*....|....*....|....*....|....*...
gi 955495717 5019 GDNSDTEEEVPEATERKEHDSCGQTGLESMQStQAVEL 5056
Cdd:TIGR00927 873 EEEEEEEEEEEEEEEEENEEPLSLEWPETRQK-QAIYL 909
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4889-5149 |
1.71e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 66.92 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4889 DKNSGEDTDHEEGEEENPLEIKEKPVDTEEAGPEAEEINEETEADQSEGQGHCEPEEGPSEDDDDKGEGEEEMDTGADDQ 4968
Cdd:PHA03169 51 PTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPES 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4969 DKDTEHPEENSGEEQQSlEDKDKEASEESTEDGGpvDQGLQPQMQEKEEEGDNSDTEEEvPEATERKEHDSCGQTGLESM 5048
Cdd:PHA03169 131 PASHSPPPSPPSHPGPH-EPAPPESHNPSPNQQP--SSFLQPSHEDSPEEPEPPTSEPE-PDSPGPPQSETPTSSPPPQS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5049 QSTQAVELAGVAPEKEQGKEEHGSGAADANQAEGHESNfiarlASQKQTRknTQSFK----RKPGQADNERSMgdhsehv 5124
Cdd:PHA03169 207 PPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREG-----PPFPGHR--SHSYTvvgwKPSTRPGGVPKL------- 272
|
250 260
....*....|....*....|....*
gi 955495717 5125 hkRLRTVDIDSHTEQGPAQPQAQAE 5149
Cdd:PHA03169 273 --CLRCTSHPSHRSRLPEGQQSEDK 295
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1736-1888 |
2.11e-10 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 65.19 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1736 AQRLLRATKLNKPILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQTDITDLFGADLPVEggKGGEFAWRDGPLLAAlk 1815
Cdd:COG0714 21 IELVLIALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQ--QTGEFEFRPGPLFAN-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1816 aghwVVL-DELNLAS---QS----VLEglnacfdhRGEIYVP----ELGMSFQVqhdktkiFGCQNPFRQGGGRKgLPRS 1883
Cdd:COG0714 97 ----VLLaDEINRAPpktQSalleAME--------ERQVTIPggtyKLPEPFLV-------IATQNPIEQEGTYP-LPEA 156
|
....*
gi 955495717 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 |
4.67e-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: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1079 PVLIQGETSVGKTSLIRWLAAATGNHCVRINNHEHTDIQEyiGCYTSD---SSGKLVFKEG------VLIdamrkgywii 1149
Cdd:COG0714 33 HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSD--ILGTYIydqQTGEFEFRPGplfanvLLA---------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1150 lDELNLAPTDVLEALNRLLDDNRelfITETQEVVKAHPRFMLFATQNPPGLYGGRkMLSRAFRNRF-VELHFDeLPSSEL 1228
Cdd:COG0714 101 -DEINRAPPKTQSALLEAMEERQ---VTIPGGTYKLPEPFLVIATQNPIEQEGTY-PLPEAQLDRFlLKLYIG-YPDAEE 174
|
....*...
gi 955495717 1229 ET-ILHKR 1235
Cdd:COG0714 175 EReILRRH 182
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4816-5036 |
2.89e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 63.07 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4816 DAGKSNRdKNWQDKEEKKEAETDDDGQGQEKINE-QIDEREYDENEVDPYHGNQEKLPE--PEALDLPDDLNLDSEDKNS 4892
Cdd:PHA03169 32 QAGRRRG-TAARAAKPAPPAPTTSGPQVRAVAEQgHRQTESDTETAEESRHGEKEERGQggPSGSGSESVGSPTPSPSGS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4893 GEDtdheegeeenpLEIKEKPVDTEEAGPEAEEINEETEADQSEGQGHCEPEE---GPSEDDDDKGEGEEEMDTGADDQD 4969
Cdd:PHA03169 111 AEE-----------LASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPeshNPSPNQQPSSFLQPSHEDSPEEPE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 955495717 4970 KDTEHPEENSGEEQQSLEDKDKEASEESTEDGGPvDQGLQPQMQEKEEEGDNSDTEEEvPEATERKE 5036
Cdd:PHA03169 180 PPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGE-PQSPTPQQAPSPNTQQAVEHEDE-PTEPEREG 244
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
5393-5543 |
3.37e-09 |
|
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.
Pssm-ID: 214621 [Multi-domain] Cd Length: 175 Bit Score: 59.39 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5393 ICLAIDDSSSMVDNhTKQLAFESLAVIGNALTLLEVG-QIAVCSFGESVKLLHPFHeqfSDYSGSQILRLCKFQQKK--- 5468
Cdd:smart00327 2 VVFLLDGSGSMGGN-RFELAKEFVLKLVEQLDIGPDGdRVGLVTFSDDARVLFPLN---DSRSKDALLEALASLSYKlgg 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 955495717 5469 -TKIAQFLESVANMFAAARQLSQnvsPETAQLLLVVSDGRGLFleGKDRVLAAVQAARNANIFVIFVVLDNPNSRD 5543
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 ... |
672-902 |
6.64e-09 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 57.30 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 672 PVLLVGETGTGKTSAVQYLAH-ITGHRLRVVNMNQQSDTADLLGGYKPvdhkliwlplreafeelfaqtfskkqnftflg 750
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRNI-------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 751 hiqtcyrqkrwhdllrlmqhvhksavnkdgkesetglllkekweafglrldhaqqqmkmteSALLFAFVEGTLAQAVKKG 830
Cdd:pfam07728 49 -------------------------------------------------------------DPGGASWVDGPLVRAAREG 67
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 955495717 831 EWILLDEINLAAPETLECLSGLLEGSSgslVLLDRGDTEPLVRHPDFRLFACMNPAtDVGKRNLPPGIRNRF 902
Cdd:pfam07728 68 EIAVLDEINRANPDVLNSLLSLLDERR---LLLPDGGELVKAAPDGFRLIATMNPL-DRGLNELSPALRSRF 135
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2220-2306 |
3.74e-08 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 55.38 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 2220 GTFEWVDSMLVQALTSGDWLLMDNVNFCNPSVLDRLNALLEPGgvltvsERGMIDGSTPTITPNPNFRLFLSMDPVHG-- 2297
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDER------RLLLPDGGELVKAAPDGFRLIATMNPLDRgl 124
|
90
....*....|
gi 955495717 2298 -EISRAMRNR 2306
Cdd:pfam07728 125 nELSPALRSR 134
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1383-1540 |
4.05e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.84 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1383 GEPVLLVGDTGCGKTTICQVFAALANQKLYSV---NCHLHMETSDFLGGLRPVRQKPKDKEEIDT-SKLFEwhdgplvLA 1458
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGViyiDGEDILEEVLDQLLLIIVGGKKASGSGELRlRLALA-------LA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1459 MKED-GFFLLDEISLADDSVLERLNSVLEVEKSLVLAEKgsledkdnevelltaGKKFRILATMNPGGDFGKKELSPALR 1537
Cdd:smart00382 75 RKLKpDVLILDEITSLLDAEQEALLLLLEELRLLLLLKS---------------EKNLTVILTTNDEKDLGPALLRRRFD 139
|
...
gi 955495717 1538 NRF 1540
Cdd:smart00382 140 RRI 142
|
|
| Granin |
pfam01271 |
Granin (chromogranin or secretogranin); |
4910-5265 |
7.10e-08 |
|
Granin (chromogranin or secretogranin);
Pssm-ID: 279595 [Multi-domain] Cd Length: 584 Bit Score: 59.28 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4910 KEKPVDTEEAGPEAEEINEETEADQSEGQGHCEPEEGPSEDDDDKGEGEEEMDTGADDQDKDTEhPEENSGEEQQSLEDK 4989
Cdd:pfam01271 116 KEFKTDHSDDYETQQWEEEKLKHMRFPLRYEENSEEKHSEREGELSEVFENPRSQATLKKVFEE-VSRLDTPSKQKREKS 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4990 DKE--ASEESTEDGG-----PVDQGLQPQMQEKEEEGDNSDTEEEVPEATERKEHDSCGQTglESMQSTQA-VELAGVAP 5061
Cdd:pfam01271 195 DERekSSQESGEDTYrqeniPQEDQVGPEDQEPSEEGEEDATQEEVKRSRPRTHHGRSLPD--ESSRGGQLgLEEEASEE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5062 EKEQGKEEHGSGAADANQAEGHESNFIARLASQKQTRKNTQSFK--RKPGQADNE-RSMGDHSEHVHKRLRTVDIDSHTE 5138
Cdd:pfam01271 273 EEEYGEESRGLSAVQTYLLRLVNARGRGRSEKRAERERSEESEEeeLKRASPYEElEITANLQIPPSEEERMLKKAGRSP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5139 QGPAQPQAQAEDAEAFEHIKQGS-DPYDAQ-----TYDVASKEQQQFAKDSSKDQEEEETEDVFMDLEEQEeltagdPEQ 5212
Cdd:pfam01271 353 RGRVDEAGALEALEALEEKRKLDlDHSRVFessedGAPRAPQGAWVEALRNYLSYGEEGMEGKWNQQGPYF------PNE 426
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 955495717 5213 LKPEEVKSGTRASPGFDEMEMEIETQTVKT-EEDQDPRTDKSRKETENEKPERS 5265
Cdd:pfam01271 427 ENREEARFRLPQYLGELSNPWEDPKQWKPSdFERKELTADKFLEGEEENEYTLS 480
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4827-5037 |
2.08e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 57.29 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4827 QDKEEKKEAETDDDGQGQEKINEQIDEREYDENEVDPyhgnqeklPEPEALDLPDDLNLDSEDKNSGEDTDHEEGEEENP 4906
Cdd:PHA03169 66 HRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGS--------PTPSPSGSAEELASGLSPENTSGSSPESPASHSPP 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4907 LEIKEKPVDTEEAGPEAeeineeteADQSEGQGHCEPEEGPSEDDDDKGEGEEEMDtgADDQDKDTEHPEENSGEEQQSL 4986
Cdd:PHA03169 138 PSPPSHPGPHEPAPPES--------HNPSPNQQPSSFLQPSHEDSPEEPEPPTSEP--EPDSPGPPQSETPTSSPPPQSP 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 955495717 4987 EDKDKEASEEsTEDGGPVDQGLQPQMQEKEEEGdnsDTEEEVPEATERKEH 5037
Cdd:PHA03169 208 PDEPGEPQSP-TPQQAPSPNTQQAVEHEDEPTE---PEREGPPFPGHRSHS 254
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1372-1571 |
2.26e-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: 55.94 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1372 LAMLVGRalefgePVLLVGDTGCGKTTICQVFAALANQKLYSVNCHLHMETSDFLGglrpvrqkpkdkEEI---DTSKlF 1448
Cdd:COG0714 26 IALLAGG------HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILG------------TYIydqQTGE-F 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1449 EWHDGPlVLAmkedGFFLLDEISLADDSVLerlNSVLEVekslvLAEKgsledkdnEV----ELLTAGKKFRILATMNPG 1524
Cdd:COG0714 87 EFRPGP-LFA----NVLLADEINRAPPKTQ---SALLEA-----MEER--------QVtipgGTYKLPEPFLVIATQNPI 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 955495717 1525 GDFGKKELSPALRNRFT-EIWC--PqstSREDLIQIISR-------NLRPGLSLGRI 1571
Cdd:COG0714 146 EQEGTYPLPEAQLDRFLlKLYIgyP---DAEEEREILRRhtgrhlaEVEPVLSPEEL 199
|
|
| AAA_3 |
pfam07726 |
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ... |
1749-1888 |
3.83e-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: 52.17 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1749 ILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQTDITDLFGADLPVEggKGGEFAWRDGPLLAALkaghwVVLDELNLA 1828
Cdd:pfam07726 2 VLLEGVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGTEVFDQ--KTREFEFRPGPVFANV-----LLADEINRA 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 955495717 1829 S---QSVLegLNACFDHR----GEIY-VPELGMsfqvqhdktkIFGCQNPFRQGGGRKgLPRSFLNRF 1888
Cdd:pfam07726 75 PpktQSAL--LEAMQERQvtidGETHpLPEPFF----------VLATQNPIEQEGTYP-LPEAQLDRF 129
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1747-1896 |
1.12e-06 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 51.38 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1747 KPILLEGSPGVGKTSLVGALAKAS---GNTLVRINLSeqtditDLFGADlpVEGGKGGEFAWRDGPLLAALKAGHWVVLD 1823
Cdd:cd00009 20 KNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNAS------DLLEGL--VVAELFGHFLVRLLFELAEKAKPGVLFID 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 955495717 1824 ELNLASQSVLEGLNACFdhrgeiyvpELGMSFQVQHDKTKIFG-CQNPFRQgggrkGLPRSFLNRFTQVFVDPL 1896
Cdd:cd00009 92 EIDSLSRGAQNALLRVL---------ETLNDLRIDRENVRVIGaTNRPLLG-----DLDRALYDRLDIRIVIPL 151
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1385-1618 |
1.96e-06 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 53.97 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1385 PVLLVGDTGCGKTTICQVFAALANQKLYSVNchlhmetsdflgglrPVRQKPKDKEEIDTSKLFewHDGPLVLAMKEDGF 1464
Cdd:PHA02244 121 PVFLKGGAGSGKNHIAEQIAEALDLDFYFMN---------------AIMDEFELKGFIDANGKF--HETPFYEAFKKGGL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1465 FLLDEISLADDSVLERLNSvlevekslVLAEKGSledkDNEVELLTAGKKFRILA---TMNPGGD---FGKKELSPALRN 1538
Cdd:PHA02244 184 FFIDEIDASIPEALIIINS--------AIANKFF----DFADERVTAHEDFRVISagnTLGKGADhiyVARNKIDGATLD 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1539 RFTEIWCPQSTSREDLIQIISRNLRPGLSLGRIdhkgvDIAEVMLDFtdwlthqefgrrcVVSIRDILSWVNFMNTMGEE 1618
Cdd:PHA02244 252 RFAPIEFDYDEKIEHLISNGDEDLVNFVALLRH-----EMAEKGLDH-------------VFSMRAIIHGKKFDGVFEAD 313
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4763-4992 |
2.08e-06 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 54.62 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4763 GDLNGEEADKLDERLWGDDDEEEDEEEEDNKTEETGPGMDEEDCELVAKGDNLDAG---------KSNRDKNWQDKEEKK 4833
Cdd:TIGR00927 642 GERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGeieakeadhKGETEAEEVEHEGET 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4834 EAE-TDDDGQGQEKINEQIDEREyDENEVDPYHGNQEKLPEPEALDLPDDLNLDSEDKNSGE---DTDHEEGEEENPLEI 4909
Cdd:TIGR00927 722 EAEgTEDEGEIETGEEGEEVEDE-GEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEiqaGEDGEMKGDEGAEGK 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4910 KEKPVDTEEAGPEAEEINEETEADQSEGQGHCEPEEGPSED-----DDDKG-EGEEEMDTG---ADDQDKDTEHPEENSG 4980
Cdd:TIGR00927 801 VEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENqgeakQDEKGvDGGGGSDGGdseEEEEEEEEEEEEEEEE 880
|
250
....*....|..
gi 955495717 4981 EEQQSLEDKDKE 4992
Cdd:TIGR00927 881 EEEEEEEEENEE 892
|
|
| TFIIF_alpha |
pfam05793 |
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation ... |
4798-5148 |
6.30e-06 |
|
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: 52.64 E-value: 6.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4798 GPGMDEEDCELvAKGDNLDAGKSnRDKNWQDKEEKKEAETDDDGQGQEKineqiDEREYDENEVDPYHGNQEKLPEPEAL 4877
Cdd:pfam05793 188 GPAAFGEHDEE-TEGEKGGGGRG-KDLKIKDLEGDDEDDGDESDKGGED-----GDEEKKKKKKKKLAKNKKKLDDDKKK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4878 DLPDDLNLDSEDKNSGEDTDHEEGEEENpleikekpvdteeagpeaeeineeteaDQSEGQGHCEPEEGPSEDDDDKGEg 4957
Cdd:pfam05793 261 KRGGDDDAFEYDSDDGDDEGREEDYISD---------------------------SSASGNDPEEREDKLSPEEPAKGE- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4958 eeemdtgaDDQDKDTEHPEENSGEEQQSLEDKDKEAseestedggpvdqglqPQMQEKEEEGDNSDTEEEvpeaTERKEH 5037
Cdd:pfam05793 313 --------IEQSDDSEESEEEKNEEEGKLSKKGKKA----------------KKLKGKKNGKDKSESSDG----DDSDDS 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5038 DSCGQTGLESMQSTQAVElagvaPEKEQGKEEHGSGAADANQAEGHESNFiarlaSQKQTRKNTQSFKRKPgqadnersm 5117
Cdd:pfam05793 365 DIDDEDSVPLFTAKKKKE-----PKKEEPVDSGPSSPGNSGPARPSPESG-----STSSKRKAAAEVSKSP--------- 425
|
330 340 350
....*....|....*....|....*....|.
gi 955495717 5118 gdhSEHVHKRLRTvDIDSHTEQGPAQPQAQA 5148
Cdd:pfam05793 426 ---ASVPAKKLKT-ENGPKSSSGKSTPQTFS 452
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1749-1784 |
7.42e-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: 7.42e-06
10 20 30
....*....|....*....|....*....|....*.
gi 955495717 1749 ILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQTD 1784
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS 36
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4795-5029 |
1.58e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 51.12 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4795 EETGPGMDEEDCELVAKGDNLDAGKSNRDKNWQDKEEKKEAETDDDGQGQEKINEQIDE--REYDENEVDPYHGNQEKLP 4872
Cdd:PHA03169 71 SDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPEspASHSPPPSPPSHPGPHEPA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4873 EPEALDLPDDLNLDSEDKNSGEDTDHEEGEEEN-PLEIKEKPVDTEEA--GPEAEEINEETEADQSEGqghcePEEGPSE 4949
Cdd:PHA03169 151 PPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSePEPDSPGPPQSETPtsSPPPQSPPDEPGEPQSPT-----PQQAPSP 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4950 DDDDKGEGEEEmdtgaddqdkDTEHPEENSGEEQQSLEDKDKEASEESTEDGGPVDQGL----QPQMQEKEEEGDNSdtE 5025
Cdd:PHA03169 226 NTQQAVEHEDE----------PTEPEREGPPFPGHRSHSYTVVGWKPSTRPGGVPKLCLrctsHPSHRSRLPEGQQS--E 293
|
....
gi 955495717 5026 EEVP 5029
Cdd:PHA03169 294 DKVP 297
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1068-1221 |
1.90e-05 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 50.89 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1068 DIVRVVSAGTyPVLIQGETSVGKTSLIRWLAAAtgnhcVRINNHEHTDI-QEYIGCYTSDSSGKlvFKEGVLIDAMRKGY 1146
Cdd:PHA02244 111 DIAKIVNANI-PVFLKGGAGSGKNHIAEQIAEA-----LDLDFYFMNAImDEFELKGFIDANGK--FHETPFYEAFKKGG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1147 WIILDELNLAPTDVLEALNRLLDDNRELFITETqevVKAHPRFMLFATQNPPG-----LYGGRKMLSRAFRNRFVELHFD 1221
Cdd:PHA02244 183 LFFIDEIDASIPEALIIINSAIANKFFDFADER---VTAHEDFRVISAGNTLGkgadhIYVARNKIDGATLDRFAPIEFD 259
|
|
| vWFA |
cd00198 |
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
5391-5548 |
1.98e-05 |
|
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.
Pssm-ID: 238119 [Multi-domain] Cd Length: 161 Bit Score: 48.33 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5391 YQICLAIDDSSSMVD---NHTKQLAfesLAVIGNALTLLEVGQIAVCSFGESVKLLHPFHEQFSDYSGSQILRLCKFQQK 5467
Cdd:cd00198 1 ADIVFLLDVSGSMGGeklDKAKEAL---KALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5468 -KTKIAQFLESVANMFAAARQLSQNvspetaQLLLVVSDGRglFLEGKDRVLAAVQAARNANIFVIFVVLDNPNSRDSIL 5546
Cdd:cd00198 78 gGTNIGAALRLALELLKSAKRPNAR------RVIILLTDGE--PNDGPELLAEAARELRKLGITVYTIGIGDDANEDELK 149
|
..
gi 955495717 5547 DI 5548
Cdd:cd00198 150 EI 151
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1738-1828 |
3.26e-05 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 50.15 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1738 RLLRATKLNKPILLEGSPGVGKTSLVGALAKA-SGNTLVRINLseqtdIT---DLFGADLpVEG----GKGGEFAWRDGP 1809
Cdd:COG1401 213 AFLAALKTKKNVILAGPPGTGKTYLARRLAEAlGGEDNGRIEF-----VQfhpSWSYEDF-LLGyrpsLDEGKYEPTPGI 286
|
90 100
....*....|....*....|....*.
gi 955495717 1810 LL-AALKAG------HWVVLDELNLA 1828
Cdd:COG1401 287 FLrFCLKAEknpdkpYVLIIDEINRA 312
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
1744-1781 |
3.85e-05 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 47.28 E-value: 3.85e-05
10 20 30
....*....|....*....|....*....|....*...
gi 955495717 1744 KLNKPILLEGSPGVGKTSLVGALAKASGNTLVRINLSE 1781
Cdd:cd19481 24 GLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSS 61
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4693-5234 |
7.39e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4693 ENEEQAEDTFQKGQEKDKEDPDSK--SDIKGEDNAIEMSEDFDGKMHDGEleekeeDDEKSDSEGRDLDKqmgdlnGEEA 4770
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEAKKADEAKKkaEEAKKADEAKKKAEEAKKKADEAK------KAAEAKKKADEAKK------AEEA 1521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4771 DKLDErlwgdddeeedeeeeDNKTEETGPGMDEEDCELVAKGDNLDAGKSNRDKNWQDK-EEKKEAETDDDGQGQE-KIN 4848
Cdd:PTZ00121 1522 KKADE---------------AKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKaEEAKKAEEDKNMALRKaEEA 1586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4849 EQIDEREYDEnevdpyhgnQEKLPEPEALDLPDDLNLDSEDKNSGEDTDHEEgeeenplEIKEKPVDTEEAGPEAEEINE 4928
Cdd:PTZ00121 1587 KKAEEARIEE---------VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE-------EEKKKVEQLKKKEAEEKKKAE 1650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4929 ETEADQSEGQGHCEPEEGPSEDDDDKGE---GEEEMDTGADDQDKDTEHPEENSGEEQQSLEDKDKEASEESTEDGgpvD 5005
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEeakKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE---E 1727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5006 QGLQPQMQEKEEEGDNSDTEEEVPEATERKehdscgqtglesmqstqavELAGVAPEKEQGKEEHGSGAADANQAEGHES 5085
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKKDEEEKK-------------------KIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5086 NFIARLASQKQTRKNTQSFKR-KPGQADNERSMGDHSEHVHKRLRTVDIDSHTeqgpaqpqaQAEDAEAFEHIKQGSDpy 5164
Cdd:PTZ00121 1789 DEKRRMEVDKKIKDIFDNFANiIEGGKEGNLVINDSKEMEDSAIKEVADSKNM---------QLEEADAFEKHKFNKN-- 1857
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5165 daqtyDVASKEQQQFAKDSSKDQEEEETEDVFMDLEEQEELTAGDPEQLKPEEVKSGTRASPGFDEMEME 5234
Cdd:PTZ00121 1858 -----NENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKD 1922
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1016-1156 |
8.36e-05 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 49.00 E-value: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1016 SGNVKSLLKQPIPEPKGGRLIQVEGYWISVGDKEPTIDETYILTSSVKLNLRDIVRVVSAGTYP--VLIQGETSVGKTSL 1093
Cdd:COG1401 158 LEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKFEETLEAFLAALKTKknVILAGPPGTGKTYL 237
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 955495717 1094 IRWLAAATG---NHCVRI-----NNHEHTDIQEYigcYTSDSSGKLVFKEGVLIDAMRKG-------YWIILDELNLA 1156
Cdd:COG1401 238 ARRLAEALGgedNGRIEFvqfhpSWSYEDFLLGY---RPSLDEGKYEPTPGIFLRFCLKAeknpdkpYVLIIDEINRA 312
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
320-432 |
8.69e-05 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 45.99 E-value: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 320 ASQNAVLLEGPIGCGKTSLVEHLAAMTGRRKPPqLLKVQLGDqtdskMLLGMYRCTDVpGEFVWQPGTLTQAATKGHWIL 399
Cdd:cd00009 17 PPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-FLYLNASD-----LLEGLVVAELF-GHFLVRLLFELAEKAKPGVLF 89
|
90 100 110
....*....|....*....|....*....|...
gi 955495717 400 LEDIDYAPLDVVSVLIPLLENGELLIPGRGDCL 432
Cdd:cd00009 90 IDEIDSLSRGAQNALLRVLETLNDLRIDRENVR 122
|
|
| COG5137 |
COG5137 |
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics] ... |
4911-5038 |
1.11e-04 |
|
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics];
Pssm-ID: 227466 [Multi-domain] Cd Length: 279 Bit Score: 47.68 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4911 EKPVDTEEAGPEAEEINEETEADQSEGQGHcEPEEGPSEDDDDKGEGEEEMDTGADDQDKDTEHPEENSGEEQQSLEDKD 4990
Cdd:COG5137 159 DNDEDNDEAPPAQPDVDNEEEERLEESDGR-EEEEDEEVGSDSYGEGNRELNEEEEEEAEGSDDGEDVVDYEGERIDKKQ 237
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 955495717 4991 KEASEESTEDGgpvdqglqpqmQEKEEEGDNSDTEEEVPEATERKEHD 5038
Cdd:COG5137 238 GEEEEMEEEVI-----------NLFEIEWEEESPSEEVPRNNEESPAK 274
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4873-5084 |
1.57e-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: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4873 EPEALDLPDDLNLDSEDKNSGEDTDHEEGEEENPLEIKEKPVDTEEAgpeaeeINEETEADQSEGQGHCEPEEGPSEDDD 4952
Cdd:TIGR00927 637 EAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEG------EIPAERKGEQEGEGEIEAKEADHKGET 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4953 DKGE-------------GEEEMDTGADDQDKDTE--------HPEENSGEEQQSLEDKDKEASEESTEDGGPVDQGLQPQ 5011
Cdd:TIGR00927 711 EAEEvehegeteaegteDEGEIETGEEGEEVEDEgegeaegkHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGE 790
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 955495717 5012 MQ--EKEEEGDNSDTEEEVPEATERKEHDSCGQTGLESMQSTQAVELA----GVAPEKEQGKEehGSGAADANQAEGHE 5084
Cdd:TIGR00927 791 MKgdEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNaenqGEAKQDEKGVD--GGGGSDGGDSEEEE 867
|
|
| CobT2 |
COG4547 |
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ... |
4940-5026 |
2.24e-04 |
|
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: 47.87 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4940 HCEPEEGPSEDDDDkGEGEEEMDTGADDQDKDTEHPEENSGEEQQSLEdkDKEASEESTEDgGPVDQGLQPQmQEKEEEG 5019
Cdd:COG4547 204 DLDLAEELGEDEDE-EDEDDEDDSGEQEEDEEDGEDEDEESDEGAEAE--DAEASGDDAEE-GESEAAEAES-DEMAEEA 278
|
....*..
gi 955495717 5020 DNSDTEE 5026
Cdd:COG4547 279 EGEDSEE 285
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
4686-5027 |
2.27e-04 |
|
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: 48.09 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4686 KDVSDQIENEEQAEDTFQKGQEKDKEDpDSKSDIKGEDNAIEMSEDFDGKMHDGELEEKEEDDEKSDSEGRDLDKQMGDL 4765
Cdd:COG5271 667 EEAEDESETSSEDAEEDADAAAAEASD-DEEETEEADEDAETASEEADAEEADTEADGTAEEAEEAAEEAESADEEAASL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4766 N-----GEEADKLDERLWGDDDEEEDEEEEDNKTEETGPGmDEE------------DCELVAKGDNLDAGKSNRDKNWQD 4828
Cdd:COG5271 746 PdeadaEEEAEEAEEAEEDDADGLEEALEEEKADAEEAAT-DEEaeaaaeekekvaDEDQDTDEDALLDEAEADEEEDLD 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4829 KEEkkEAETDDDGQGQEKINEQIDEREYDENEVDPYHGNQEKLPEPEALDLPDDLNLDSEDKNSGEDTDHEEGEEENPLE 4908
Cdd:COG5271 825 GED--EETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAETDADADADAGEADSSGESSA 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4909 IKEKPVDTE-EAGPEAEEINEETEADQSEGQGHCEPEEGPSEDDDDKGEGEEEMDTGADDQDKDTEHpEENSGEEQQSLE 4987
Cdd:COG5271 903 AAEDDDAAEdADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALALDEAGDEESDDAAADDAG-DDSLADDDEALA 981
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 955495717 4988 DKDKEASE------ESTEDGGPVDQGLQPQMQEKEEEGDNSDTEEE 5027
Cdd:COG5271 982 DAADDAEAddseldASESTGEAEGDEDDDELEDGEAAAGEATADLA 1027
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1079-1221 |
2.75e-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: 44.67 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1079 PVLIQGETSVGKTSLIR---WLAAATGNHCVRIN----NHEHTDIQEYIGCYTSDSSGKLVFKEGVLIDAMRKGYW--II 1149
Cdd:smart00382 4 VILIVGPPGSGKTTLARalaRELGPPGGGVIYIDgediLEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPdvLI 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 955495717 1150 LDELNLAPTDVLEALNRLLDDNRELFITEtqevvKAHPRFMLFATQNPPGLygGRKMLSRAFRNRFVELHFD 1221
Cdd:smart00382 84 LDEITSLLDAEQEALLLLLEELRLLLLLK-----SEKNLTVILTTNDEKDL--GPALLRRRFDRRIVLLLIL 148
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1368-1543 |
2.81e-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: 44.44 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1368 GMRRLAMLVGRALEFGEP--VLLVGDTGCGKTTICQVFA---ALANQKLYSVNCHLHMETSDFLGglrpvrqkpkDKEEI 1442
Cdd:cd00009 2 GQEEAIEALREALELPPPknLLLYGPPGTGKTTLARAIAnelFRPGAPFLYLNASDLLEGLVVAE----------LFGHF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1443 DTSKLFEwhdgplVLAMKEDGFFLLDEISLADDSVLERLNSVLEVekslvlaekgsledkdnEVELLTAGKKFRILATMN 1522
Cdd:cd00009 72 LVRLLFE------LAEKAKPGVLFIDEIDSLSRGAQNALLRVLET-----------------LNDLRIDRENVRVIGATN 128
|
170 180
....*....|....*....|.
gi 955495717 1523 PGGDFgkkELSPALRNRFTEI 1543
Cdd:cd00009 129 RPLLG---DLDRALYDRLDIR 146
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1080-1215 |
3.18e-04 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 43.74 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1080 VLIQGETSVGKTSLIRWLAAATGNHCVRINNHEHTDiqEYIGcytsDSSGKLvfkEGVLIDAMRKGYWII-LDELNLAPT 1158
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS--KYVG----ESEKRL---RELFEAAKKLAPCVIfIDEIDALAG 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 955495717 1159 DVLEALNRLLDDNRELFITETQEVVKAHPRFMLFATQNPPGlyggrkMLSRAFRNRF 1215
Cdd:pfam00004 72 SRGSGGDSESRRVVNQLLTELDGFTSSNSKVIVIAATNRPD------KLDPALLGRF 122
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
1724-1800 |
3.64e-04 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 44.86 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1724 DYALSAGTTAMNAQRLLrATKLNKPI---LLEGSPGVGKTSLVGALAKA---SGNTLVRINLSEQT---DITDLFGADlP 1794
Cdd:cd19499 17 DEAVKAVSDAIRRARAG-LSDPNRPIgsfLFLGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYMekhSVSRLIGAP-P 94
|
....*.
gi 955495717 1795 VEGGKG 1800
Cdd:cd19499 95 GYVGYT 100
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
1381-1584 |
3.91e-04 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 45.65 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1381 EFGEP----VLLVGDTGCGKTTICQVFAALANQKLYSVNCHLHMetSDFLGglrpvrqkpkdkeeiDTS----KLFEwhd 1452
Cdd:COG1223 29 KFGLWpprkILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLI--GSYLG---------------ETArnlrKLFD--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1453 gplvLAMKEDGFFLLDEIsladDSV-LER--LNSVLEVeKSLVLAEKGSLEDKDNEVELltagkkfrILATMNPggdfgk 1529
Cdd:COG1223 89 ----FARRAPCVIFFDEF----DAIaKDRgdQNDVGEV-KRVVNALLQELDGLPSGSVV--------IAATNHP------ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 955495717 1530 KELSPALRNRFTEIWCPQSTSREDLIQIISRNLRP-----GLSLGRI-----DHKGVDIAEVMLD 1584
Cdd:COG1223 146 ELLDSALWRRFDEVIEFPLPDKEERKEILELNLKKfplpfELDLKKLakkleGLSGADIEKVLKT 210
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1079-1215 |
4.19e-04 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 44.06 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1079 PVLIQGETSVGKTSLIR---WLAAATGNHCVRINNHEHTDIqeyigcyTSDSSGKLVFKEGVLIDAMRKGYW--IILDEL 1153
Cdd:cd00009 21 NLLLYGPPGTGKTTLARaiaNELFRPGAPFLYLNASDLLEG-------LVVAELFGHFLVRLLFELAEKAKPgvLFIDEI 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 955495717 1154 NLAPTDVLEALNRLLDdnrelfiTETQEVVKAHPRFMLFATQNPPGLyggrkMLSRAFRNRF 1215
Cdd:cd00009 94 DSLSRGAQNALLRVLE-------TLNDLRIDRENVRVIGATNRPLLG-----DLDRALYDRL 143
|
|
| PHA00435 |
PHA00435 |
capsid assembly protein |
4942-5163 |
4.28e-04 |
|
capsid assembly protein
Pssm-ID: 222792 Cd Length: 306 Bit Score: 45.98 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4942 EPEEGPSEDDDDKGEGEEEMDTGADDQDKDTEHPeensGEEQQSLEDKDKEASEEST-----------------EDGgpV 5004
Cdd:PHA00435 65 EDDEGRIEVRISEDGEEEEVEEGEEDEEEEGEEE----SEEFEPLGDTPEELTEASEqleeheegfqamveqavERG--L 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5005 DQGLQPQMQ-EKEEEGDNSD-TEEEVPEATERKEH-DSC--GQTGLESMQSTQAVELAGvAPEKEQGKEEH-----GSGA 5074
Cdd:PHA00435 139 SAETITRIQaEYEEEGGLSEeSYAELAAAGYSKAFvDSYirGQEALVEQYVESVVEYAG-GRERFQAIYSHleatnPSAA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5075 ADANQAegHESNFIAR----LASQKQTRknTQSFKRKPgqadnERSmgdhsehVHKRLRtvdidshteqgPAQPQAQaeD 5150
Cdd:PHA00435 218 ESLEAA--IENRDLATvkaiINLAGASR--AKKFGKKP-----KRS-------VTKRAK-----------PAKPVAP--K 268
|
250
....*....|....*..
gi 955495717 5151 AEAF----EHIKQGSDP 5163
Cdd:PHA00435 269 VEGFasqaEMIKAMSDP 285
|
|
| Granin |
pfam01271 |
Granin (chromogranin or secretogranin); |
4803-5224 |
4.53e-04 |
|
Granin (chromogranin or secretogranin);
Pssm-ID: 279595 [Multi-domain] Cd Length: 584 Bit Score: 46.56 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4803 EEDCELVAKGDnldaGKSNRDKNWQDKEEKKEAETDDDGQGQEKINEQIDEREYDENEVDPyhGNQEKLPEpealdlpdd 4882
Cdd:pfam01271 174 KKVFEEVSRLD----TPSKQKREKSDEREKSSQESGEDTYRQENIPQEDQVGPEDQEPSEE--GEEDATQE--------- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4883 lnldsEDKNSGEDTDH------EEGEEENPLEIKEKPVDTEEAG----------PEAEEINEETEADQSEGQGHCEPEEG 4946
Cdd:pfam01271 239 -----EVKRSRPRTHHgrslpdESSRGGQLGLEEEASEEEEEYGeesrglsavqTYLLRLVNARGRGRSEKRAERERSEE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4947 PSEDDDDKGEGEEEMDTGADDQDKDTEHPE--ENSGEEQQSLEDKDKEAS-EESTEDGGPVDQGlQPQMQEKEEEGDNSD 5023
Cdd:pfam01271 314 SEEEELKRASPYEELEITANLQIPPSEEERmlKKAGRSPRGRVDEAGALEaLEALEEKRKLDLD-HSRVFESSEDGAPRA 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5024 TEEEVPEATerKEHDSCGQTGLESMQSTQAvELAGVAP--EKEQGKEEHGSGAADANQAEGhesnfiARLASQKQTRKNT 5101
Cdd:pfam01271 393 PQGAWVEAL--RNYLSYGEEGMEGKWNQQG-PYFPNEEnrEEARFRLPQYLGELSNPWEDP------KQWKPSDFERKEL 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5102 QSFKRKPGQADNERsmgDHSEHVHKRLRTVDIDSHTEQGPA------QPQAQAEDaeAFEHIKQGSDPYDAQTYDVASKE 5175
Cdd:pfam01271 464 TADKFLEGEEENEY---TLSMKNSFPEYNYDGYEKRVPSPGldlkrqYDPVARED--QLLHYRKKSSEFPDFYDSEEKKE 538
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 955495717 5176 QQQFAKDsSKDQEEEETEDVFMDLeeqEELTAGDPEQLKPEEVKSGTRA 5224
Cdd:pfam01271 539 PPVGAEK-EEDSANRQTRDEDKEL---ENLAAMDLELQKIAEKFSALRR 583
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4944-5335 |
5.17e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4944 EEGPSEDDDDKGEGEEEMDTGADDQDKDTEHPEENSGEEQQSLEDKdKEASEESTEDGGPVDQGLQPQMQEKEEEGDNSD 5023
Cdd:PTZ00121 1215 EEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEA-RMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5024 teeEVPEATERKEHDSCGQTGLESMQSTQAVELAGVAPEKEQG---KEEHGSGAADANQAEGHESNFIARLASQK----- 5095
Cdd:PTZ00121 1294 ---EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAakkKAEEAKKAAEAAKAEAEAAADEAEAAEEKaeaae 1370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5096 ----QTRKNTQSFKRKPGQADNERSMGDHSEHVHKRLRTVDIDSHTEQGPAQPQAQAEDAEAFEHIKQGSDpyDAQTYDV 5171
Cdd:PTZ00121 1371 kkkeEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE--EAKKADE 1448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5172 ASK--EQQQFAKDSSKDQEEEETEDVFMDLEEQ----EELTAGDPE-QLKPEEVKSGTRASPGFDEMEMEIETQtvKTEE 5244
Cdd:PTZ00121 1449 AKKkaEEAKKAEEAKKKAEEAKKADEAKKKAEEakkaDEAKKKAEEaKKKADEAKKAAEAKKKADEAKKAEEAK--KADE 1526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5245 ----DQDPRTDKSRKETENEKPERSRDS-TIHTAHQflvdtifpplLKDVSELRQELERQLEMWQPHESGNPEEEKAAAD 5319
Cdd:PTZ00121 1527 akkaEEAKKADEAKKAEEKKKADELKKAeELKKAEE----------KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
|
410
....*....|....*.
gi 955495717 5320 MWQNYLVLTAPLSQQL 5335
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEA 1612
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
1736-1790 |
9.33e-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: 43.70 E-value: 9.33e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 955495717 1736 AQRLLRATKLNKPILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQTDITDLFG 1790
Cdd:cd19500 27 AVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRG 81
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
1747-1782 |
9.74e-04 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 45.68 E-value: 9.74e-04
10 20 30
....*....|....*....|....*....|....*.
gi 955495717 1747 KPILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQ 1782
Cdd:PRK04195 40 KALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQ 75
|
|
| Sigma54_activ_2 |
pfam14532 |
Sigma-54 interaction domain; |
650-708 |
1.46e-03 |
|
Sigma-54 interaction domain;
Pssm-ID: 434021 [Multi-domain] Cd Length: 138 Bit Score: 42.33 E-value: 1.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 955495717 650 FAATRPSSVLIEQLAVCVSRGEPVLLVGETGTGKTSAVQYLAHITGHRLRVVNMNQQSD 708
Cdd:pfam14532 1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAH 59
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
643-693 |
1.65e-03 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 42.53 E-value: 1.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 955495717 643 IQREKLTFAaTRPSSVLIEQLAVCVSRGEPVLLVGETGTGKTSAVQYLAHI 693
Cdd:cd03223 1 IELENLSLA-TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL 50
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
659-780 |
1.99e-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: 42.13 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 659 LIEQL--AVCVSRGEPVLLVGETGTGKTSAVQYLAHITGHR-LRVVNMNqqsdTADLLGGYkpVDHKLIWLPLREAFEEL 735
Cdd:cd00009 6 AIEALreALELPPPKNLLLYGPPGTGKTTLARAIANELFRPgAPFLYLN----ASDLLEGL--VVAELFGHFLVRLLFEL 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 955495717 736 FAqtfsKKQNFT-FLGHIQTCYRQKRWHdLLRLMQHVHKSAVNKDG 780
Cdd:cd00009 80 AE----KAKPGVlFIDEIDSLSRGAQNA-LLRVLETLNDLRIDREN 120
|
|
| CobT2 |
COG4547 |
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ... |
4958-5031 |
2.20e-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: 44.40 E-value: 2.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 955495717 4958 EEEMDTGADDQDKDTEHPEENSGEEQQSLEDKDKEASEESTEDGgpvDQGLQPQMQEKEEEGDNSDTEEEVPEA 5031
Cdd:COG4547 208 AEELGEDEDEEDEDDEDDSGEQEEDEEDGEDEDEESDEGAEAED---AEASGDDAEEGESEAAEAESDEMAEEA 278
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4695-5270 |
2.72e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4695 EEQAEDTFQKGQEKDKEDPDSKSDIKGEdnAIEMSEDFDGKMHDGELEEKEEDD----------EKSDSEGRDLDKQMGD 4764
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKK--ADAAKKKAEEKKKADEAKKKAEEDkkkadelkkaAAAKKKADEAKKKAEE 1429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4765 L--------NGEEADKLDErLWGDDDEEEDEEEEDNKTEETGPGMD-EEDCELVAKGDNL----DAGKSNRDKNWQDKEE 4831
Cdd:PTZ00121 1430 KkkadeakkKAEEAKKADE-AKKKAEEAKKAEEAKKKAEEAKKADEaKKKAEEAKKADEAkkkaEEAKKKADEAKKAAEA 1508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4832 KKEAETDDDGQGQEKINE---QIDEREYDENEVDPYHGNQEKLPEPEALDLPDDLNLDSEDKNSGEDTDHEEGEEENPLE 4908
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEakkAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK 1588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4909 IKEKPVDTEEAGPEAEEINEETEADQSEgQGHCEPEEGPSEDDDDKG----EGEEEMDTGADDQDKDTEHPEENSGEEQQ 4984
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAE-EAKIKAEELKKAEEEKKKveqlKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4985 SLEDKDKEASEEStedggpvdqglqpqmqEKEEEGDNSDTEEEVPEATERKEHDSCGQTGLESMQSTQAV----ELAGVA 5060
Cdd:PTZ00121 1668 KKAEEDKKKAEEA----------------KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELkkaeEENKIK 1731
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5061 PEKEQGKEEHGSGAADANQAEGHESNFIARLASQKQtRKNTQSFKRKPGQADNERSMGDHSEHVHKRLRTVDIDSHTE-- 5138
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE-KKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFAni 1810
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5139 -QGPAQPQAQAEDAEAFE--HIKQGSDPYDAQTYDVASKEQQQFAKD--SSKDQEEEETEDVFMDLEEQEEltagdPEQL 5213
Cdd:PTZ00121 1811 iEGGKEGNLVINDSKEMEdsAIKEVADSKNMQLEEADAFEKHKFNKNneNGEDGNKEADFNKEKDLKEDDE-----EEIE 1885
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 955495717 5214 KPEEVKSGTRaspgfDEMEMEIETQTVKTEEDQDPRTDKSRKETENEKPERSRDSTI 5270
Cdd:PTZ00121 1886 EADEIEKIDK-----DDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEII 1937
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
663-712 |
2.79e-03 |
|
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: 41.99 E-value: 2.79e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 955495717 663 LAVCVSRGEPVLLVGETGTGKTSAVQ-YLAHI--TGHRLRVVNMNQQSDTADL 712
Cdd:pfam12775 24 LDLLLKNGKPVLLVGPTGTGKTVIIQnLLRKLdkEKYLPLFINFSAQTTSNQT 76
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4690-4987 |
2.79e-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: 44.22 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4690 DQIENEEQAEDTFQKGqEKDKEDPDSKSDIKGEDNAIE-MSEDFDGKMHDGELEEKeeddeksdseGRDLDKQMGDLNGE 4768
Cdd:TIGR00927 634 DVAEAEHTGERTGEEG-ERPTEAEGENGEESGGEAEQEgETETKGENESEGEIPAE----------RKGEQEGEGEIEAK 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4769 EADKLDERLWGDDDEEEDEEEEDNKTE---ETGPG--MDEEDCELVAKGDNLDAGKSNRDKNWQDKEEKKEAETDDDgQG 4843
Cdd:TIGR00927 703 EADHKGETEAEEVEHEGETEAEGTEDEgeiETGEEgeEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDED-EG 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4844 QEKINEQIDEREYDENEVDPYHGnqeklpEPEALDLPDDLNLDSEDKNSGEDTDHEEGEEENPLEIKEKPVDTEEAgpea 4923
Cdd:TIGR00927 782 EIQAGEDGEMKGDEGAEGKVEHE------GETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKG---- 851
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 955495717 4924 eeineeteadqSEGQGhcEPEEGPSEDDDDKGEGEEEmdtgaDDQDKDTEHPEENSGEEQQSLE 4987
Cdd:TIGR00927 852 -----------VDGGG--GSDGGDSEEEEEEEEEEEE-----EEEEEEEEEEEEEENEEPLSLE 897
|
|
| Taf7 |
COG5414 |
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation ... |
5119-5302 |
2.93e-03 |
|
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation complex [Transcription];
Pssm-ID: 227701 Cd Length: 392 Bit Score: 43.92 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5119 DHSEHVHKRLRTVDIDSHTEQGPAQPQAQAEDAEAFEHIKQGSDPYDAQTYDVASKEQQQFAKDSSKDQEEEETEDVFMD 5198
Cdd:COG5414 203 EEVEKKVDDLLEKDMKAESVSVVLKDEKELARQERVSSWENFKEEPGEPLSRPALKKEKQGAEEEGEEGMSEEDLDVGAA 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 5199 LEEQEELTAGDPEQLKPEEVKSGTRASPGFDEMEMEIEtqtvkTEEDQDPRTDKSRKETENEKPERSR-DSTI-HTAHQf 5276
Cdd:COG5414 283 EIENKEVSEGDKEQQQEEVENAEAHKEEVQSDRPDEIG-----EEKEEDDENEENERHTELLADELNElEKGIeEKRRQ- 356
|
170 180 190
....*....|....*....|....*....|....
gi 955495717 5277 lVDTIFPPLLK-----DVSELRQELE---RQLEM 5302
Cdd:COG5414 357 -MESATNPILQkrfesQLNVLLKELElkrKQLEM 389
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
669-737 |
3.00e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.59 E-value: 3.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 955495717 669 RGEPVLLVGETGTGKTSAVQYLAHI---TGHRLRVVNMNQQSDTADLLGGYKPVDHKLIWLPLREAFEELFA 737
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALA 72
|
|
| DNA_pol_phi |
pfam04931 |
DNA polymerase phi; This family includes the fifth essential DNA polymerase in yeast EC:2.7.7. ... |
4949-5025 |
3.33e-03 |
|
DNA polymerase phi; This family includes the fifth essential DNA polymerase in yeast EC:2.7.7.7. Pol5p is localized exclusively to the nucleolus and binds near or at the enhancer region of rRNA-encoding DNA repeating units.
Pssm-ID: 461488 Cd Length: 765 Bit Score: 44.15 E-value: 3.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 955495717 4949 EDDDDKGEGEEEMDTGADDQDKDTEHPEENSGEEQQSLEDKDKEASEESTEDggpVDQGLQPQMQEKEEEGDNSDTE 5025
Cdd:pfam04931 639 EDEDEEDDDEEEDDDDEDDEDSEEDDDEDDDDEDEEDDDDEDVDEIDELRAK---LAEALGEHGDDADDDDSDSDED 712
|
|
| Taf7 |
COG5414 |
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation ... |
4942-5051 |
4.21e-03 |
|
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation complex [Transcription];
Pssm-ID: 227701 Cd Length: 392 Bit Score: 43.15 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4942 EPEEGPSEDDDDKGeGEEEMDTGADDQDKDTEHPEEnsGEEQQSLEDKdkeaseESTEDGGPVDQGLQPQMQEKEEEGDN 5021
Cdd:COG5414 250 EPLSRPALKKEKQG-AEEEGEEGMSEEDLDVGAAEI--ENKEVSEGDK------EQQQEEVENAEAHKEEVQSDRPDEIG 320
|
90 100 110
....*....|....*....|....*....|
gi 955495717 5022 SDTEEEvPEATERKEHDSCGQTGLESMQST 5051
Cdd:COG5414 321 EEKEED-DENEENERHTELLADELNELEKG 349
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1386-1543 |
4.22e-03 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 40.65 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1386 VLLVGDTGCGKTTICQVFAALANQKLYSVNChlhmetSDFLGGLRPVRQKpkdkeeiDTSKLFEW--HDGPLVLamkedg 1463
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISG------SELVSKYVGESEK-------RLRELFEAakKLAPCVI------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 1464 ffLLDEIsladDSVLERLNSVLEVEKSLVLAekgsledkdnevELLTA-------GKKFRILATMN-PGgdfgkkELSPA 1535
Cdd:pfam00004 62 --FIDEI----DALAGSRGSGGDSESRRVVN------------QLLTEldgftssNSKVIVIAATNrPD------KLDPA 117
|
....*...
gi 955495717 1536 LRNRFTEI 1543
Cdd:pfam00004 118 LLGRFDRI 125
|
|
| CobT2 |
COG4547 |
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ... |
4942-5053 |
4.97e-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: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4942 EPEEGPSEDDDDKGEGEEEMDTGADDQDKDTEhpEENSGEEQQSledkdkEASEESTEDggpvdqglqpqmqekEEEGDN 5021
Cdd:COG4547 208 AEELGEDEDEEDEDDEDDSGEQEEDEEDGEDE--DEESDEGAEA------EDAEASGDD---------------AEEGES 264
|
90 100 110
....*....|....*....|....*....|..
gi 955495717 5022 SDTEEEVPEATERKEHDSCGQTGLESMQSTQA 5053
Cdd:COG4547 265 EAAEAESDEMAEEAEGEDSEEPGEPWRPNAPP 296
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
1741-1790 |
5.38e-03 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 43.39 E-value: 5.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 955495717 1741 RATKLNKPIL-LEGSPGVGKTSLVGALAKASGNTLVRINLSEQTDITDLFG 1790
Cdd:PRK10787 343 RVNKIKGPILcLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRG 393
|
|
| RecA-like_ATAD1 |
cd19520 |
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ... |
1738-1784 |
6.40e-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: 6.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 955495717 1738 RLLRATKlnkPILLEGSPGVGKTSLVGALAKASGNTLVRINLSEQTD 1784
Cdd:cd19520 30 RLLQPPK---GVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTD 73
|
|
| Taf7 |
COG5414 |
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation ... |
4915-4999 |
6.71e-03 |
|
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation complex [Transcription];
Pssm-ID: 227701 Cd Length: 392 Bit Score: 42.77 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 4915 DTEEAGPEAEEINEETEADQSEGQghcEPEEGPSEDDDDKGEGEEEMDTGADDQDKDTEHP----EENSGEEQQSLEDKD 4990
Cdd:COG5414 243 NFKEEPGEPLSRPALKKEKQGAEE---EGEEGMSEEDLDVGAAEIENKEVSEGDKEQQQEEvenaEAHKEEVQSDRPDEI 319
|
....*....
gi 955495717 4991 KEASEESTE 4999
Cdd:COG5414 320 GEEKEEDDE 328
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
816-919 |
8.37e-03 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 42.08 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955495717 816 FAFVEGTLAQAVkkgewILLDEINLAAPETLeclSGLLEgssgslVLLDR-----GDTEPLvRHPdFRLFACMNPATDVG 890
Cdd:COG0714 86 FEFRPGPLFANV-----LLADEINRAPPKTQ---SALLE------AMEERqvtipGGTYKL-PEP-FLVIATQNPIEQEG 149
|
90 100 110
....*....|....*....|....*....|
gi 955495717 891 KRNLPPGIRNRFT-ELYVEELESKEDLQIL 919
Cdd:COG0714 150 TYPLPEAQLDRFLlKLYIGYPDAEEEREIL 179
|
|
| |
