|
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 ... |
4444-4717 |
9.23e-140 |
|
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: 437.55 E-value: 9.23e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4444 LSIELCEQLRLILEPTLATKMQGDFRTGKRLNMKRIIPYIASQFKKDKIWMRRVKPSKRTYQVMISIDDSKSMSESGSTV 4523
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4524 LALETLALVTKALSLLEVGQIAVMKFGEQPELLHPFDKQFSSESGVQMFSHFTFEQSNTNVLALADASMKCFNYANTASH 4603
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDARTQSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4604 HRSnsdIRQLEIIISDGICEDHDSIRKL-LRRAQEEKVMIVFVILDNVNtqKKSSILDIKKVYYDTKEDGtmdlKIQPYI 4682
Cdd:cd01460 161 SGS---LWQLLLIISDGRGEFSEGAQKVrLREAREQNVFVVFIIIDNPD--NKQSILDIKVVSFKNDKSG----VITPYL 231
|
250 260 270
....*....|....*....|....*....|....*
gi 1685823625 4683 DEFAFDYYLVVRNIEELPQLLSSALRQWFQQMSNT 4717
Cdd:cd01460 232 DEFPFPYYVIVRDLNQLPSVLSDALRQWFELVNSS 266
|
|
| AAA_lid_5 |
pfam17865 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
725-819 |
2.23e-30 |
|
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: 117.68 E-value: 2.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 725 DLLSIIQKYIGSLCIgNEHVIREVAELYQVAKSLSLdGSLVDGAGQRPHYTVRTLSRTLSYVTEIAPIYGLRRSLYEGFC 804
Cdd:pfam17865 1 DLELLVKAYLKGVSS-DDDLVRDIVKFYLEAKKLAE-KSLVDGAGQRPHYSLRTLCRALSYARAIAPRYGLRRALYEGFC 78
|
90
....*....|....*
gi 1685823625 805 MSFLTLLDHTSESLL 819
Cdd:pfam17865 79 MSFLTQLDAESRKIV 93
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
3899-4447 |
3.96e-27 |
|
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: 122.43 E-value: 3.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3899 QEGKSNSGELESGTGLGSGVGAEDITNTLNEDDDLEElANEEDTANQSDLDESEARELESDMNGVTKDSvvsenensDSE 3978
Cdd:COG5271 344 EDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGAD-TDAAADEADAAADDSADDEEASADGGTSPTS--------DTD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3979 EENQDLDE-----EVNDIPEDLSNSLNEKLWDEPNEEDLLETEQKSNEQSAANNESDLVSKEDDNKALEDKDRQEKEDEE 4053
Cdd:COG5271 415 EEEEEADEdasagETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDASDDGDEE 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4054 EM---------SDDVGIDDEIQPDIQENNSQPPPENEDhLDLPEDlKLDEKEGDVSKDSDLEDMDMEAADENKEEADAEK 4124
Cdd:COG5271 495 EAeedaeaeadSDELTAEETSADDGADTDAAADPEDSD-EDALED-ETEGEENAPGSDQDADETDEPEATAEEDEPDEAE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4125 DEPMQDfedplEENNTLDEDIQQDDFSDLAEDDEKMNEDGfEENVQENEESTEDGVKSDEELEQGEVPEDQAIDNhpkmD 4204
Cdd:COG5271 573 AETEDA-----TENADADETEESADESEEAEASEDEAAEE-EEADDDEADADADGAADEEETEEEAAEDEAAEPE----T 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4205 AKSTFASAEADEENTDKGIVGENEELGEEDGAAESgvrGNGTADGEFSSAEQVQKGEDTSTPKEAMSEADRQyqslGDHL 4284
Cdd:COG5271 643 DASEAADEDADAETEAEASADESEEEAEDESETSS---EDAEEDADAAAAEASDDEEETEEADEDAETASEE----ADAE 715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4285 REWQQANRIHEWEDLTESQSQAFD-DSEFMHVKEDEEEDLQALGNAEKDQIK----SIDRDESANQNPDSMNSTNIAEDE 4359
Cdd:COG5271 716 EADTEADGTAEEAEEAAEEAESADeEAASLPDEADAEEEAEEAEEAEEDDADgleeALEEEKADAEEAATDEEAEAAAEE 795
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4360 ADEVGDKQLQDGQDISDIKQTGEDTLPTEFGSINQSEKVFELSEDEDIEDELPDyNVKITNLPAAMPIDEARDLWNKHED 4439
Cdd:COG5271 796 KEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETADEALEDIEAGIAEDDEED-DDAAAAKDVDADLDLDADLAADEHE 874
|
....*...
gi 1685823625 4440 STKQLSIE 4447
Cdd:COG5271 875 AEEAQEAE 882
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
896-1032 |
2.48e-23 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.
The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 98.52 E-value: 2.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 896 PILIQGPTSSGKTSMIEYVAKKT-GHKFVRINNHEHTDLQEYIGTYVTDDNGSlSFREGVLVEALRNGYWIVLDELNLAP 974
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1685823625 975 TDVLEALNRLLDDNRELFIPETQVLVKPHPEFMLFATQNPPgvYAGRKHLSRAFRNRF 1032
Cdd:pfam07728 80 PDVLNSLLSLLDERRLLLPDGGELVKAAPDGFRLIATMNPL--DRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1712-1813 |
3.28e-20 |
|
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: 88.51 E-value: 3.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1712 DMIEIAaCNYHQVNEDWRLKIIKFMFRLQDNIEKDISFGSFGSPWEFNLRDTLRWLQLLNDA-----PKYTCVSPADYLE 1786
Cdd:pfam17867 1 DLEQIL-SHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLSSLlptllSPTVREEIFLEAV 79
|
90 100
....*....|....*....|....*..
gi 1685823625 1787 VMVLHRMRTVEDRVRTCELFKEVFDID 1813
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
1188-1382 |
3.59e-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: 89.66 E-value: 3.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1188 PVLLVGDTGCGKTTVCQILAECLH-KELHIINAHQDTENGDIIGaQRPVRNRsavnyslhsqlcekfnvqesldsiddli 1266
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTRDTTEEDLFG-RRNIDPG---------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1267 ekfeklsssekndnlsnlierqiikyrsLFEWHDGALVTAMKQGDFFLLDEISLADDSVLERLNSVLELSRTLTLvehSN 1346
Cdd:pfam07728 52 ----------------------------GASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDERRLLLP---DG 100
|
170 180 190
....*....|....*....|....*....|....*.
gi 1685823625 1347 AAVSLTAKDGFAFFATMNPgGDYGKKELSPALRNRF 1382
Cdd:pfam07728 101 GELVKAAPDGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
1561-1700 |
2.13e-17 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.
The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 81.57 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1561 PILLEGSPGVGKTSLITALARETGHQ-LVRINLSDQTDLMDLFGSDVPVEGGeggqFAWRDAPFLAAMRNGHWVLLDELN 1639
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRpVFYVQLTRDTTEEDLFGRRNIDPGG----ASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1685823625 1640 LASQSVLEGLNACLDHRnEAYIPELDKVFKAHP-NFRVFAAQNPQHQGGgrKGLPRSFINRF 1700
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPdGFRLIATMNPLDRGL--NELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1044-1138 |
1.27e-16 |
|
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: 78.50 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1044 ELETILHKRCKIAPSYAAKIVQVFRELSLRRQTTRIFEQKNS--FATLRDLFRWA---------FREAVGYQQLAENGYM 1112
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGSprEFNLRDLLRWCrrlssllptLLSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....*.
gi 1685823625 1113 LLAERARDQKDKLAVQEVIEKVMKVK 1138
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
154-269 |
2.08e-16 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.
The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 78.87 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 154 PILLAGPEGIGKKFLITQIAAKLGQQIIR-IHLSDSTDPKMLIGTYtSPKPGEFEWQPGVLTQAVITGKWILFTNIEHAP 232
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFyVQLTRDTTEEDLFGRR-NIDPGGASWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 1685823625 233 SEVLSVLLPLLEKRQLVIPSRGETIYAKG-SFQMFATS 269
Cdd:pfam07728 80 PDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIATM 117
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
294-405 |
7.47e-11 |
|
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: 61.93 E-value: 7.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 294 VEVVSTLYPVLSIICPTLYSVYKDIFDLFSQRSFLATSKIYRRLCLRDFYKFIKRVAFLYHKFmipsdhvvISQELQDAV 373
Cdd:pfam17867 3 EQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLSSLLPTL--------LSPTVREEI 74
|
90 100 110
....*....|....*....|....*....|..
gi 1685823625 374 FKEAIDMFGAFIPSRDGFDLVVRNVAIELNIP 405
Cdd:pfam17867 75 FLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
2012-2098 |
1.60e-09 |
|
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.
The actual alignment was detected with superfamily member pfam07728:
Pssm-ID: 476819 [Multi-domain] Cd Length: 135 Bit Score: 58.84 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 2012 GRFEWFDGYLLKAVEEGHWFVLDNANLCSPAVLDRLNSLLEHKgVLIVNEKTTEDGHPKtikphPNFRLFLTVNPVYG-- 2089
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDER-RLLLPDGGELVKAAP-----DGFRLIATMNPLDRgl 124
|
90
....*....|
gi 1685823625 2090 -ELSRAMRNR 2098
Cdd:pfam07728 125 nELSPALRSR 134
|
|
| P-loop_NTPase super family |
cl38936 |
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ... |
625-711 |
7.38e-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: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 625 FSFVEGALVKAVRSGHWVLLDEINLASLETLEPIGQLLSsyESGILLSERGDITPITPHkNFRLFGCMNPsTDVGKRELE 704
Cdd:pfam07728 53 ASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLD--ERRLLLPDGGELVKAAPD-GFRLIATMNP-LDRGLNELS 128
|
....*..
gi 1685823625 705 PSFRSRF 711
Cdd:pfam07728 129 PALRSRF 135
|
|
| PTZ00341 super family |
cl31759 |
Ring-infected erythrocyte surface antigen; Provisional |
3615-4143 |
2.30e-07 |
|
Ring-infected erythrocyte surface antigen; Provisional
The actual alignment was detected with superfamily member PTZ00341:
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 57.49 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3615 KNVYSEVGVNGSPLESFNNSS-FNEVSSLGYDHDFENRAQAVSMLcqiyAIVIQKHSSISptaSFQSIGHELSRF----- 3688
Cdd:PTZ00341 631 KKMYNKFGYDGIKGVNFIHPSiFYLLASLEKFADFTGSPQIVTLL----KFFFEKKLSMN---DLDNKSEHLLKFmeqyq 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3689 -------ADLLSNKLFPSsiplyasadkVSSIRDQQKGINDLIEYCRKKRTELP---ELSYCFKHlVSLQSLKSISRTQV 3758
Cdd:PTZ00341 704 kereahiSENLINILQPC----------IAGDRKWDVPIIDKIEELKGSPFDIAiidSIGWIFKH-VAKSHLKKPKKAAK 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3759 DL-----TNDEFL-----NLMNFVLNLFDSLlSSIETATKNMRTfkelaeTSSFIEMSSCFSKVLrafNLKFQSMKlsSL 3828
Cdd:PTZ00341 773 KLeqrskANKEELanennKLMNILKEYFGNN-EQINSITYNFEN------INLNEDNENGSKKIL---DLNHKDQK--EI 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3829 KEKLRSSSVDKMSCQLLMLFLPVCEQFINLaESVLDYFINVHNSNLDSLSKISTLFFMVANNGFCSPDlpQEGKSNSGEL 3908
Cdd:PTZ00341 841 FEEIISYIVDISLSDIENTAKNAAEQILSD-EGLDEKKLKKRAESLKKLANAIEKYAGGGKKDKKAKK--KDAKDLSGNI 917
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3909 ESGTGLgsgvgaedITNTL-NEDDDLEELANEEDTAN-QSDLDESEARELESDMNGVTKDSVvsenensdseeeNQDLDE 3986
Cdd:PTZ00341 918 AHEINL--------INKELkNQNENVPEHLKEHAEANiEEDAEENVEEDAEENVEENVEENV------------EENVEE 977
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3987 EVND-IPEDLSNSLNEKLwDEPNEEDLLETEQKSNEQSAANN--ESDLVSKEDDNKALEDKDRQEKEDEEEMSDDvGIDD 4063
Cdd:PTZ00341 978 NVEEnVEENVEENVEENV-EENVEENIEENVEENVEENIEENveEYDEENVEEVEENVEEYDEENVEEIEENAEE-NVEE 1055
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4064 EIQPDIQENNSQPPPENEDHLD--LPEDLKLDEKEGDVSKDSDLEDMDMEAADENKEEaDAEKDEPMQDFEDPLEENNTL 4141
Cdd:PTZ00341 1056 NIEENIEEYDEENVEEIEENIEenIEENVEENVEENVEEIEENVEENVEENAEENAEE-NAEENAEEYDDENPEEHNEEY 1134
|
..
gi 1685823625 4142 DE 4143
Cdd:PTZ00341 1135 DE 1136
|
|
| McrB super family |
cl34253 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1381-1641 |
5.01e-04 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
The actual alignment was detected with superfamily member COG1401:
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 46.30 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1381 RFTEIWVPPMVDTEDILKIVEGKLHNNKIELARPLVEYAKWHANEYLYTDVISIRDVLSAVEFINACEILDLNLVLFNAV 1460
Cdd:COG1401 45 RLAERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1461 SMVFIDALGSFTTFSLSNNLASLHAERQRCFAKLNELAGSNIMASKSADISIKFSDSSFFIGDFGIPLGDsvESDSTYSL 1540
Cdd:COG1401 125 RSDALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLES--EDDYLKDL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1541 HTDTTLMNASKVLRALQVLKPILLEGSPGVGKTSLITALARETG------HQLV--RINLSDQTDLMDLfgsdVPVEGGe 1612
Cdd:COG1401 203 LREKFEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGgedngrIEFVqfHPSWSYEDFLLGY----RPSLDE- 277
|
250 260 270
....*....|....*....|....*....|....*.
gi 1685823625 1613 gGQFAWRDAPFL----AAMRNG---HWVLLDELNLA 1641
Cdd:COG1401 278 -GKYEPTPGIFLrfclKAEKNPdkpYVLIIDEINRA 312
|
|
| |
|
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 ... |
4444-4717 |
9.23e-140 |
|
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: 437.55 E-value: 9.23e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4444 LSIELCEQLRLILEPTLATKMQGDFRTGKRLNMKRIIPYIASQFKKDKIWMRRVKPSKRTYQVMISIDDSKSMSESGSTV 4523
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4524 LALETLALVTKALSLLEVGQIAVMKFGEQPELLHPFDKQFSSESGVQMFSHFTFEQSNTNVLALADASMKCFNYANTASH 4603
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDARTQSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4604 HRSnsdIRQLEIIISDGICEDHDSIRKL-LRRAQEEKVMIVFVILDNVNtqKKSSILDIKKVYYDTKEDGtmdlKIQPYI 4682
Cdd:cd01460 161 SGS---LWQLLLIISDGRGEFSEGAQKVrLREAREQNVFVVFIIIDNPD--NKQSILDIKVVSFKNDKSG----VITPYL 231
|
250 260 270
....*....|....*....|....*....|....*
gi 1685823625 4683 DEFAFDYYLVVRNIEELPQLLSSALRQWFQQMSNT 4717
Cdd:cd01460 232 DEFPFPYYVIVRDLNQLPSVLSDALRQWFELVNSS 266
|
|
| AAA_lid_5 |
pfam17865 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
725-819 |
2.23e-30 |
|
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: 117.68 E-value: 2.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 725 DLLSIIQKYIGSLCIgNEHVIREVAELYQVAKSLSLdGSLVDGAGQRPHYTVRTLSRTLSYVTEIAPIYGLRRSLYEGFC 804
Cdd:pfam17865 1 DLELLVKAYLKGVSS-DDDLVRDIVKFYLEAKKLAE-KSLVDGAGQRPHYSLRTLCRALSYARAIAPRYGLRRALYEGFC 78
|
90
....*....|....*
gi 1685823625 805 MSFLTLLDHTSESLL 819
Cdd:pfam17865 79 MSFLTQLDAESRKIV 93
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
3899-4447 |
3.96e-27 |
|
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: 122.43 E-value: 3.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3899 QEGKSNSGELESGTGLGSGVGAEDITNTLNEDDDLEElANEEDTANQSDLDESEARELESDMNGVTKDSvvsenensDSE 3978
Cdd:COG5271 344 EDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGAD-TDAAADEADAAADDSADDEEASADGGTSPTS--------DTD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3979 EENQDLDE-----EVNDIPEDLSNSLNEKLWDEPNEEDLLETEQKSNEQSAANNESDLVSKEDDNKALEDKDRQEKEDEE 4053
Cdd:COG5271 415 EEEEEADEdasagETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDASDDGDEE 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4054 EM---------SDDVGIDDEIQPDIQENNSQPPPENEDhLDLPEDlKLDEKEGDVSKDSDLEDMDMEAADENKEEADAEK 4124
Cdd:COG5271 495 EAeedaeaeadSDELTAEETSADDGADTDAAADPEDSD-EDALED-ETEGEENAPGSDQDADETDEPEATAEEDEPDEAE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4125 DEPMQDfedplEENNTLDEDIQQDDFSDLAEDDEKMNEDGfEENVQENEESTEDGVKSDEELEQGEVPEDQAIDNhpkmD 4204
Cdd:COG5271 573 AETEDA-----TENADADETEESADESEEAEASEDEAAEE-EEADDDEADADADGAADEEETEEEAAEDEAAEPE----T 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4205 AKSTFASAEADEENTDKGIVGENEELGEEDGAAESgvrGNGTADGEFSSAEQVQKGEDTSTPKEAMSEADRQyqslGDHL 4284
Cdd:COG5271 643 DASEAADEDADAETEAEASADESEEEAEDESETSS---EDAEEDADAAAAEASDDEEETEEADEDAETASEE----ADAE 715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4285 REWQQANRIHEWEDLTESQSQAFD-DSEFMHVKEDEEEDLQALGNAEKDQIK----SIDRDESANQNPDSMNSTNIAEDE 4359
Cdd:COG5271 716 EADTEADGTAEEAEEAAEEAESADeEAASLPDEADAEEEAEEAEEAEEDDADgleeALEEEKADAEEAATDEEAEAAAEE 795
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4360 ADEVGDKQLQDGQDISDIKQTGEDTLPTEFGSINQSEKVFELSEDEDIEDELPDyNVKITNLPAAMPIDEARDLWNKHED 4439
Cdd:COG5271 796 KEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETADEALEDIEAGIAEDDEED-DDAAAAKDVDADLDLDADLAADEHE 874
|
....*...
gi 1685823625 4440 STKQLSIE 4447
Cdd:COG5271 875 AEEAQEAE 882
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
896-1032 |
2.48e-23 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 98.52 E-value: 2.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 896 PILIQGPTSSGKTSMIEYVAKKT-GHKFVRINNHEHTDLQEYIGTYVTDDNGSlSFREGVLVEALRNGYWIVLDELNLAP 974
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1685823625 975 TDVLEALNRLLDDNRELFIPETQVLVKPHPEFMLFATQNPPgvYAGRKHLSRAFRNRF 1032
Cdd:pfam07728 80 PDVLNSLLSLLDERRLLLPDGGELVKAAPDGFRLIATMNPL--DRGLNELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1712-1813 |
3.28e-20 |
|
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: 88.51 E-value: 3.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1712 DMIEIAaCNYHQVNEDWRLKIIKFMFRLQDNIEKDISFGSFGSPWEFNLRDTLRWLQLLNDA-----PKYTCVSPADYLE 1786
Cdd:pfam17867 1 DLEQIL-SHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLSSLlptllSPTVREEIFLEAV 79
|
90 100
....*....|....*....|....*..
gi 1685823625 1787 VMVLHRMRTVEDRVRTCELFKEVFDID 1813
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1188-1382 |
3.59e-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: 89.66 E-value: 3.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1188 PVLLVGDTGCGKTTVCQILAECLH-KELHIINAHQDTENGDIIGaQRPVRNRsavnyslhsqlcekfnvqesldsiddli 1266
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTRDTTEEDLFG-RRNIDPG---------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1267 ekfeklsssekndnlsnlierqiikyrsLFEWHDGALVTAMKQGDFFLLDEISLADDSVLERLNSVLELSRTLTLvehSN 1346
Cdd:pfam07728 52 ----------------------------GASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDERRLLLP---DG 100
|
170 180 190
....*....|....*....|....*....|....*.
gi 1685823625 1347 AAVSLTAKDGFAFFATMNPgGDYGKKELSPALRNRF 1382
Cdd:pfam07728 101 GELVKAAPDGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1561-1700 |
2.13e-17 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 81.57 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1561 PILLEGSPGVGKTSLITALARETGHQ-LVRINLSDQTDLMDLFGSDVPVEGGeggqFAWRDAPFLAAMRNGHWVLLDELN 1639
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRpVFYVQLTRDTTEEDLFGRRNIDPGG----ASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1685823625 1640 LASQSVLEGLNACLDHRnEAYIPELDKVFKAHP-NFRVFAAQNPQHQGGgrKGLPRSFINRF 1700
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPdGFRLIATMNPLDRGL--NELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1044-1138 |
1.27e-16 |
|
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: 78.50 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1044 ELETILHKRCKIAPSYAAKIVQVFRELSLRRQTTRIFEQKNS--FATLRDLFRWA---------FREAVGYQQLAENGYM 1112
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGSprEFNLRDLLRWCrrlssllptLLSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....*.
gi 1685823625 1113 LLAERARDQKDKLAVQEVIEKVMKVK 1138
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
154-269 |
2.08e-16 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 78.87 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 154 PILLAGPEGIGKKFLITQIAAKLGQQIIR-IHLSDSTDPKMLIGTYtSPKPGEFEWQPGVLTQAVITGKWILFTNIEHAP 232
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFyVQLTRDTTEEDLFGRR-NIDPGGASWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 1685823625 233 SEVLSVLLPLLEKRQLVIPSRGETIYAKG-SFQMFATS 269
Cdd:pfam07728 80 PDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIATM 117
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1560-1716 |
1.83e-14 |
|
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: 77.52 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1560 KPILLEGSPGVGKTSLITALARETGHQLVRINLSdqTDLM--DLFGSDVPVEggEGGQFAWRDAPFLAAMrnghwVLLDE 1637
Cdd:COG0714 32 GHLLLEGVPGVGKTTLAKALARALGLPFIRIQFT--PDLLpsDILGTYIYDQ--QTGEFEFRPGPLFANV-----LLADE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1638 LNLAS---QSVLegLNAcLDHRnEAYIPelDKVFKAHPNFRVFAAQNPQHQGGGRKgLPRSFINRFSV-VYVEALKEKDM 1713
Cdd:COG0714 103 INRAPpktQSAL--LEA-MEER-QVTIP--GGTYKLPEPFLVIATQNPIEQEGTYP-LPEAQLDRFLLkLYIGYPDAEEE 175
|
...
gi 1685823625 1714 IEI 1716
Cdd:COG0714 176 REI 178
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
883-1099 |
1.68e-13 |
|
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: 74.43 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 883 LLNIARACstRMfPILIQGPTSSGKTSMIEYVAKKTGHKFVRINNHEHTDLQEYIGTYVTD-DNGSLSFREGVLveaLRN 961
Cdd:COG0714 23 LVLIALLA--GG-HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDqQTGEFEFRPGPL---FAN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 962 gywIVL-DELNLAPTDV----LEALnrlldDNRELFIPETQVLVkPHPeFMLFATQNPPGvYAGRKHLSRAFRNRFL-EI 1035
Cdd:COG0714 97 ---VLLaDEINRAPPKTqsalLEAM-----EERQVTIPGGTYKL-PEP-FLVIATQNPIE-QEGTYPLPEAQLDRFLlKL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1685823625 1036 HFD--DiPENELEtILHKRCKIAPSYAAKIVQVFRELSLRRQTTRIFEQKNSFATLRDLFRwAFRE 1099
Cdd:COG0714 166 YIGypD-AEEERE-ILRRHTGRHLAEVEPVLSPEELLALQELVRQVHVSEAVLDYIVDLVR-ATRE 228
|
|
| Mpp10 |
pfam04006 |
Mpp10 protein; This family includes proteins related to Mpp10 (M phase phosphoprotein 10). The ... |
3983-4209 |
5.73e-13 |
|
Mpp10 protein; This family includes proteins related to Mpp10 (M phase phosphoprotein 10). The U3 small nucleolar ribonucleoprotein (snoRNP) is required for three cleavage events that generate the mature 18S rRNA from the pre-rRNA. In Saccharomyces cerevisiae, depletion of Mpp10, a U3 snoRNP-specific protein, halts 18S rRNA production and impairs cleavage at the three U3 snoRNP-dependent sites.
Pssm-ID: 461128 [Multi-domain] Cd Length: 506 Bit Score: 75.00 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3983 DLDEE--------VND-IPEDLSNSLNEKLWDEpnEEDLLETEQKSNEQSAANNESDLVSKEDDNKALEDKDRQEKEDEE 4053
Cdd:pfam04006 47 GFDEEqiwqqlelQNEpVLDQLLKKIGSLLKDE--KELRLLLDSEQDDEEDEDEEEDEEDEEDEEEDEDEEEEEEEEEED 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4054 EMSDDVGIDDEIQPDIQENNSQPPPENEDH-----------LDLPED--LKLDEKEGDVSK-DSDLEDMDMEAADENKEE 4119
Cdd:pfam04006 125 DEDEDSDDEGLEEEDVKELEQKTKKDAKKGrksvvddkffkLDEMEKflEDEEKKEERKDKgKEDEDDIDYFEDDDSEDD 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4120 ADAEKDEPM-QDFEDPLEEnntLDEDIQQDDFSDLAEDDEKMNEDGFEENVQENEESTEDGVKSDEELEQGEVPEDQAID 4198
Cdd:pfam04006 205 EDDGARNLKyEDFFDPPEE---EDEKETKKKKDKKKEEDEKDDEEEEDEEDDAMEEEKEDEFAEDEDEEEDDDEDSDDEE 281
|
250
....*....|.
gi 1685823625 4199 NHPKMDAKSTF 4209
Cdd:pfam04006 282 EEASPEELSSF 292
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
3984-4195 |
9.75e-12 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 72.13 E-value: 9.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3984 LDEEVNDIPEDLSNSLNEKLwdEPN-EEDLLETEQKSNEQSAANNESDLVSKEDDNKALEDKDRQEKEDEEEMSDDvGID 4062
Cdd:PTZ00341 924 INKELKNQNENVPEHLKEHA--EANiEEDAEENVEEDAEENVEENVEENVEENVEENVEENVEENVEENVEENVEE-NVE 1000
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4063 DEIQPDIQENNSQPPPENEDHLDLP--EDLKLDEKEGDVSKDSDLEDMDMEAADENKEEADAEKDEP-MQDFEDPLEENn 4139
Cdd:PTZ00341 1001 ENIEENVEENVEENIEENVEEYDEEnvEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEEnVEEIEENIEEN- 1079
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1685823625 4140 tLDEDIQQDdfsdlAEDDEKMNEDGFEENVQEN-EESTEDGVKSDEELEQGEVPEDQ 4195
Cdd:PTZ00341 1080 -IEENVEEN-----VEENVEEIEENVEENVEENaEENAEENAEENAEEYDDENPEEH 1130
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
294-405 |
7.47e-11 |
|
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: 61.93 E-value: 7.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 294 VEVVSTLYPVLSIICPTLYSVYKDIFDLFSQRSFLATSKIYRRLCLRDFYKFIKRVAFLYHKFmipsdhvvISQELQDAV 373
Cdd:pfam17867 3 EQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLSSLLPTL--------LSPTVREEI 74
|
90 100 110
....*....|....*....|....*....|..
gi 1685823625 374 FKEAIDMFGAFIPSRDGFDLVVRNVAIELNIP 405
Cdd:pfam17867 75 FLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2012-2098 |
1.60e-09 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 58.84 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 2012 GRFEWFDGYLLKAVEEGHWFVLDNANLCSPAVLDRLNSLLEHKgVLIVNEKTTEDGHPKtikphPNFRLFLTVNPVYG-- 2089
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDER-RLLLPDGGELVKAAP-----DGFRLIATMNPLDRgl 124
|
90
....*....|
gi 1685823625 2090 -ELSRAMRNR 2098
Cdd:pfam07728 125 nELSPALRSR 134
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
625-711 |
7.38e-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: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 625 FSFVEGALVKAVRSGHWVLLDEINLASLETLEPIGQLLSsyESGILLSERGDITPITPHkNFRLFGCMNPsTDVGKRELE 704
Cdd:pfam07728 53 ASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLD--ERRLLLPDGGELVKAAPD-GFRLIATMNP-LDRGLNELS 128
|
....*..
gi 1685823625 705 PSFRSRF 711
Cdd:pfam07728 129 PALRSRF 135
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1546-1702 |
1.76e-08 |
|
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: 56.39 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1546 LMNASKVLRALQVLKPILLEGSPGVGKTSLITALARETGHQLVRINlsdQTDLMDLFGSDvpVEGGEGGQFAWRDAPFLA 1625
Cdd:cd00009 6 AIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFL---YLNASDLLEGL--VVAELFGHFLVRLLFELA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1685823625 1626 AMRNGHWVLLDELNLASQSVLEGLNACLDHRNEAYIPeldkvfkaHPNFRVFAAQNPQHQGGGRKGLPRSFINRFSV 1702
Cdd:cd00009 81 EKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRID--------RENVRVIGATNRPLLGDLDRALYDRLDIRIVI 149
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4032-4326 |
7.52e-08 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 59.24 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4032 VSKEDDNKAledKDRQEKEDEEEMSDDVGidDEIQPDIQENNSQPPPENEDHLDlpedlklDEKEGDVSKDSDLEDMDME 4111
Cdd:TIGR00927 630 LSKGDVAEA---EHTGERTGEEGERPTEA--EGENGEESGGEAEQEGETETKGE-------NESEGEIPAERKGEQEGEG 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4112 AADENKEEADAEKDEPMQDFEDPLEENNTLDEDIQQddfsdlAEDDEKMNEDGFEENVQENEESTEDGVKSDEELEQGEV 4191
Cdd:TIGR00927 698 EIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIE------TGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETE 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4192 PEDQAIDNHPKMDAKSTfASAEADEENTDKGIVGENEELGEEDGAAESGVRGNGTADGEFSSAEQVQKGEDTSTPKEAMS 4271
Cdd:TIGR00927 772 AEGKEDEDEGEIQAGED-GEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEK 850
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1685823625 4272 EADRQYQSLGDHLREWQqanrihEWEDLTESQSQAFDDSEfmhvkEDEEEDLQAL 4326
Cdd:TIGR00927 851 GVDGGGGSDGGDSEEEE------EEEEEEEEEEEEEEEEE-----EEEEENEEPL 894
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
3615-4143 |
2.30e-07 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 57.49 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3615 KNVYSEVGVNGSPLESFNNSS-FNEVSSLGYDHDFENRAQAVSMLcqiyAIVIQKHSSISptaSFQSIGHELSRF----- 3688
Cdd:PTZ00341 631 KKMYNKFGYDGIKGVNFIHPSiFYLLASLEKFADFTGSPQIVTLL----KFFFEKKLSMN---DLDNKSEHLLKFmeqyq 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3689 -------ADLLSNKLFPSsiplyasadkVSSIRDQQKGINDLIEYCRKKRTELP---ELSYCFKHlVSLQSLKSISRTQV 3758
Cdd:PTZ00341 704 kereahiSENLINILQPC----------IAGDRKWDVPIIDKIEELKGSPFDIAiidSIGWIFKH-VAKSHLKKPKKAAK 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3759 DL-----TNDEFL-----NLMNFVLNLFDSLlSSIETATKNMRTfkelaeTSSFIEMSSCFSKVLrafNLKFQSMKlsSL 3828
Cdd:PTZ00341 773 KLeqrskANKEELanennKLMNILKEYFGNN-EQINSITYNFEN------INLNEDNENGSKKIL---DLNHKDQK--EI 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3829 KEKLRSSSVDKMSCQLLMLFLPVCEQFINLaESVLDYFINVHNSNLDSLSKISTLFFMVANNGFCSPDlpQEGKSNSGEL 3908
Cdd:PTZ00341 841 FEEIISYIVDISLSDIENTAKNAAEQILSD-EGLDEKKLKKRAESLKKLANAIEKYAGGGKKDKKAKK--KDAKDLSGNI 917
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3909 ESGTGLgsgvgaedITNTL-NEDDDLEELANEEDTAN-QSDLDESEARELESDMNGVTKDSVvsenensdseeeNQDLDE 3986
Cdd:PTZ00341 918 AHEINL--------INKELkNQNENVPEHLKEHAEANiEEDAEENVEEDAEENVEENVEENV------------EENVEE 977
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3987 EVND-IPEDLSNSLNEKLwDEPNEEDLLETEQKSNEQSAANN--ESDLVSKEDDNKALEDKDRQEKEDEEEMSDDvGIDD 4063
Cdd:PTZ00341 978 NVEEnVEENVEENVEENV-EENVEENIEENVEENVEENIEENveEYDEENVEEVEENVEEYDEENVEEIEENAEE-NVEE 1055
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4064 EIQPDIQENNSQPPPENEDHLD--LPEDLKLDEKEGDVSKDSDLEDMDMEAADENKEEaDAEKDEPMQDFEDPLEENNTL 4141
Cdd:PTZ00341 1056 NIEENIEEYDEENVEEIEENIEenIEENVEENVEENVEEIEENVEENVEENAEENAEE-NAEENAEEYDDENPEEHNEEY 1134
|
..
gi 1685823625 4142 DE 4143
Cdd:PTZ00341 1135 DE 1136
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
153-269 |
4.83e-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: 54.79 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 153 RPILLAGPEGIGKKFLITQIAAKLGQQIIRIHLSDSTDPKMLIGTY-TSPKPGEFEWQPGVLTQAVitgkwILFTNIEHA 231
Cdd:COG0714 32 GHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYiYDQQTGEFEFRPGPLFANV-----LLADEINRA 106
|
90 100 110
....*....|....*....|....*....|....*...
gi 1685823625 232 PSEVLSVLLPLLEKRQLVIPsrGETIYAKGSFQMFATS 269
Cdd:COG0714 107 PPKTQSALLEAMEERQVTIP--GGTYKLPEPFLVIATQ 142
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
896-1038 |
6.46e-07 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 55.12 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 896 PILIQGPTSSGKTSMIEYVAKKTGHKFVRINnhehTDLQEYIGTYVTDDNGSlsFREGVLVEALRNGYWIVLDELNLAPT 975
Cdd:PHA02244 121 PVFLKGGAGSGKNHIAEQIAEALDLDFYFMN----AIMDEFELKGFIDANGK--FHETPFYEAFKKGGLFFIDEIDASIP 194
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1685823625 976 DVLEALNRLLDDNRELFIPETqvlVKPHPEFMLFATQNPPG-----VYAGRKHLSRAFRNRFLEIHFD 1038
Cdd:PHA02244 195 EALIIINSAIANKFFDFADER---VTAHEDFRVISAGNTLGkgadhIYVARNKIDGATLDRFAPIEFD 259
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
1560-1595 |
1.13e-06 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 54.93 E-value: 1.13e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1685823625 1560 KPILLEGSPGVGKTSLITALARETGHQLVRINLSDQ 1595
Cdd:PRK04195 40 KALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQ 75
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
4506-4658 |
4.06e-06 |
|
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: 50.15 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4506 VMISIDDSKSMSESGSTvLALETLALVTKALSLLEVG-QIAVMKFGEQPELLHPFDKQFSSE---SGVQMFSHFTFEQSN 4581
Cdd:smart00327 2 VVFLLDGSGSMGGNRFE-LAKEFVLKLVEQLDIGPDGdRVGLVTFSDDARVLFPLNDSRSKDallEALASLSYKLGGGTN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1685823625 4582 TNvLALADAsmkcFNYANTASHhRSNSDIRQLEIIISDGICEDHDS-IRKLLRRAQEEKVMIVFV-ILDNVNTQKKSSI 4658
Cdd:smart00327 81 LG-AALQYA----LENLFSKSA-GSRRGAPKVVILITDGESNDGPKdLLKAAKELKRSGVKVFVVgVGNDVDEEELKKL 153
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
886-1035 |
1.44e-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: 48.30 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 886 IARACSTRMFPILIQGPTSSGKTSMIEYVAK---KTGHKFVRINNHEhtdlqEYIGTYVTDDNGSLSFREGVLVEALRNG 962
Cdd:cd00009 11 REALELPPPKNLLLYGPPGTGKTTLARAIANelfRPGAPFLYLNASD-----LLEGLVVAELFGHFLVRLLFELAEKAKP 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1685823625 963 YWIVLDELNLAPTDVLEALNRLLDDNRELFIPETQVLVkphpefmLFATQNPPGVyagrkHLSRAFRNRFLEI 1035
Cdd:cd00009 86 GVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRENVRV-------IGATNRPLLG-----DLDRALYDRLDIR 146
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1166-1411 |
2.36e-05 |
|
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: 49.78 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1166 VVWTRPMIRLfCLVwrCLLAKEPVLLVGDTGCGKTTVCQILAECLHKELHIINAHQDTENGDIIGAQRPVRNRSAvnysl 1245
Cdd:COG0714 14 YVGQEELIEL-VLI--ALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQQTGE----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1246 hsqlcekfnvqesldsiddliekfeklsssekndnlsnlierqiikyrslFEWHDGALVTAmkqgdFFLLDEISLADDSV 1325
Cdd:COG0714 86 --------------------------------------------------FEFRPGPLFAN-----VLLADEINRAPPKT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1326 ----LErlnsVLElSRTLTLvehsnAAVSLTAKDGFAFFATMNPGGDYGKKELSPALRNRFT-EIWVP-PmvDTEDILKI 1399
Cdd:COG0714 111 qsalLE----AME-ERQVTI-----PGGTYKLPEPFLVIATQNPIEQEGTYPLPEAQLDRFLlKLYIGyP--DAEEEREI 178
|
250
....*....|..
gi 1685823625 1400 VEGKLHNNKIEL 1411
Cdd:COG0714 179 LRRHTGRHLAEV 190
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1560-1689 |
8.47e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.83 E-value: 8.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1560 KPILLEGSPGVGKTSLITALARE---TGHQLVRINLSD----QTDLMDLFGSDVPVEGGEGGQFAwRDAPFLAAMRNGHW 1632
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDileeVLDQLLLIIVGGKKASGSGELRL-RLALALARKLKPDV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1685823625 1633 VLLDELNLASQSVLEGLnacldhRNEAYIPELDKVFKAHPNFRVFAAQNPQHQGGGR 1689
Cdd:smart00382 82 LILDEITSLLDAEQEAL------LLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPA 132
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
896-1032 |
2.40e-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: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 896 PILIQGPTSSGKTSMIEYVAK---KTGHKFVRIN--NHEHTDLQEYIGTYVTDDNGSLSFREGV-----LVEALRNGyWI 965
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARelgPPGGGVIYIDgeDILEEVLDQLLLIIVGGKKASGSGELRLrlalaLARKLKPD-VL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1685823625 966 VLDELNLAPTDVLEALNRLLDDNRELFIpetqvLVKPHPEFMLFATQNPPGVyaGRKHLSRAFRNRF 1032
Cdd:smart00382 83 ILDEITSLLDAEQEALLLLLEELRLLLL-----LKSEKNLTVILTTNDEKDL--GPALLRRRFDRRI 142
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1381-1641 |
5.01e-04 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 46.30 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1381 RFTEIWVPPMVDTEDILKIVEGKLHNNKIELARPLVEYAKWHANEYLYTDVISIRDVLSAVEFINACEILDLNLVLFNAV 1460
Cdd:COG1401 45 RLAERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1461 SMVFIDALGSFTTFSLSNNLASLHAERQRCFAKLNELAGSNIMASKSADISIKFSDSSFFIGDFGIPLGDsvESDSTYSL 1540
Cdd:COG1401 125 RSDALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLES--EDDYLKDL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1541 HTDTTLMNASKVLRALQVLKPILLEGSPGVGKTSLITALARETG------HQLV--RINLSDQTDLMDLfgsdVPVEGGe 1612
Cdd:COG1401 203 LREKFEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGgedngrIEFVqfHPSWSYEDFLLGY----RPSLDE- 277
|
250 260 270
....*....|....*....|....*....|....*.
gi 1685823625 1613 gGQFAWRDAPFL----AAMRNG---HWVLLDELNLA 1641
Cdd:COG1401 278 -GKYEPTPGIFLrfclKAEKNPdkpYVLIIDEINRA 312
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1178-1238 |
8.68e-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: 42.90 E-value: 8.68e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1685823625 1178 LVWRCLLAKEPVLLVGDTGCGKTTVCQILAECLHK---ELHIINAHQDTENGDIIGAQRPVRNR 1238
Cdd:cd00009 11 REALELPPPKNLLLYGPPGTGKTTLARAIANELFRpgaPFLYLNASDLLEGLVVAELFGHFLVR 74
|
|
| |
|
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 ... |
4444-4717 |
9.23e-140 |
|
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: 437.55 E-value: 9.23e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4444 LSIELCEQLRLILEPTLATKMQGDFRTGKRLNMKRIIPYIASQFKKDKIWMRRVKPSKRTYQVMISIDDSKSMSESGSTV 4523
Cdd:cd01460 1 LSSELCEQLRLILEPTLATKLKGDYRTGKRLNMKKIIPYIASQFRKDKIWLRRTKPAKRDYQILIAIDDSKSMSENNSKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4524 LALETLALVTKALSLLEVGQIAVMKFGEQPELLHPFDKQFSSESGVQMFSHFTFEQSNTNVLALADASMKCFNYANTASH 4603
Cdd:cd01460 81 LALESLCLVSKALTLLEVGQLGVCSFGEDVQILHPFDEQFSSQSGPRILNQFTFQQDKTDIANLLKFTAQIFEDARTQSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4604 HRSnsdIRQLEIIISDGICEDHDSIRKL-LRRAQEEKVMIVFVILDNVNtqKKSSILDIKKVYYDTKEDGtmdlKIQPYI 4682
Cdd:cd01460 161 SGS---LWQLLLIISDGRGEFSEGAQKVrLREAREQNVFVVFIIIDNPD--NKQSILDIKVVSFKNDKSG----VITPYL 231
|
250 260 270
....*....|....*....|....*....|....*
gi 1685823625 4683 DEFAFDYYLVVRNIEELPQLLSSALRQWFQQMSNT 4717
Cdd:cd01460 232 DEFPFPYYVIVRDLNQLPSVLSDALRQWFELVNSS 266
|
|
| AAA_lid_5 |
pfam17865 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
725-819 |
2.23e-30 |
|
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: 117.68 E-value: 2.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 725 DLLSIIQKYIGSLCIgNEHVIREVAELYQVAKSLSLdGSLVDGAGQRPHYTVRTLSRTLSYVTEIAPIYGLRRSLYEGFC 804
Cdd:pfam17865 1 DLELLVKAYLKGVSS-DDDLVRDIVKFYLEAKKLAE-KSLVDGAGQRPHYSLRTLCRALSYARAIAPRYGLRRALYEGFC 78
|
90
....*....|....*
gi 1685823625 805 MSFLTLLDHTSESLL 819
Cdd:pfam17865 79 MSFLTQLDAESRKIV 93
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
3899-4447 |
3.96e-27 |
|
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: 122.43 E-value: 3.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3899 QEGKSNSGELESGTGLGSGVGAEDITNTLNEDDDLEElANEEDTANQSDLDESEARELESDMNGVTKDSvvsenensDSE 3978
Cdd:COG5271 344 EDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGAD-TDAAADEADAAADDSADDEEASADGGTSPTS--------DTD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3979 EENQDLDE-----EVNDIPEDLSNSLNEKLWDEPNEEDLLETEQKSNEQSAANNESDLVSKEDDNKALEDKDRQEKEDEE 4053
Cdd:COG5271 415 EEEEEADEdasagETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDASDDGDEE 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4054 EM---------SDDVGIDDEIQPDIQENNSQPPPENEDhLDLPEDlKLDEKEGDVSKDSDLEDMDMEAADENKEEADAEK 4124
Cdd:COG5271 495 EAeedaeaeadSDELTAEETSADDGADTDAAADPEDSD-EDALED-ETEGEENAPGSDQDADETDEPEATAEEDEPDEAE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4125 DEPMQDfedplEENNTLDEDIQQDDFSDLAEDDEKMNEDGfEENVQENEESTEDGVKSDEELEQGEVPEDQAIDNhpkmD 4204
Cdd:COG5271 573 AETEDA-----TENADADETEESADESEEAEASEDEAAEE-EEADDDEADADADGAADEEETEEEAAEDEAAEPE----T 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4205 AKSTFASAEADEENTDKGIVGENEELGEEDGAAESgvrGNGTADGEFSSAEQVQKGEDTSTPKEAMSEADRQyqslGDHL 4284
Cdd:COG5271 643 DASEAADEDADAETEAEASADESEEEAEDESETSS---EDAEEDADAAAAEASDDEEETEEADEDAETASEE----ADAE 715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4285 REWQQANRIHEWEDLTESQSQAFD-DSEFMHVKEDEEEDLQALGNAEKDQIK----SIDRDESANQNPDSMNSTNIAEDE 4359
Cdd:COG5271 716 EADTEADGTAEEAEEAAEEAESADeEAASLPDEADAEEEAEEAEEAEEDDADgleeALEEEKADAEEAATDEEAEAAAEE 795
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4360 ADEVGDKQLQDGQDISDIKQTGEDTLPTEFGSINQSEKVFELSEDEDIEDELPDyNVKITNLPAAMPIDEARDLWNKHED 4439
Cdd:COG5271 796 KEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETADEALEDIEAGIAEDDEED-DDAAAAKDVDADLDLDADLAADEHE 874
|
....*...
gi 1685823625 4440 STKQLSIE 4447
Cdd:COG5271 875 AEEAQEAE 882
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
3873-4406 |
1.98e-23 |
|
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: 110.10 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3873 NLDSLSKISTLFFMVANNGFCSPDLPQEGKSNSGELESGTGLGSGVGAEDITNtlNEDDDLEELANEEDTANQSDLDESE 3952
Cdd:COG5271 220 DLAAEEGASAVVEEEDASEDAVAAADETLLADDDDTESAGATAEVGGTPDTDD--EATDDADGLEAAEDDALDAELTAAQ 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3953 ARELESDMNGVTKDSVVSENENSDSEEENQDLDEEVNDIPEDLSNSLNEKLwDEPNEEDLLETEQKSNEQSAANNESDLV 4032
Cdd:COG5271 298 AADPESDDDADDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAEDAAE-EAATAEDSAAEDTQDAEDEAAGEAADES 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4033 SKEDDNKALEDkdrqekEDEEEMSDDVGIDDEIQPDIQENNSQPPPENEdhldlpedlkLDEKEGDVSKDSDLEDMdmeA 4112
Cdd:COG5271 377 EGADTDAAADE------ADAAADDSADDEEASADGGTSPTSDTDEEEEE----------ADEDASAGETEDESTDV---T 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4113 ADENKEEADAEKDEPMQDFEDPLEENNTLDEDiqQDDFSDLAEDDEKMNEDGFEENVQENEESTEDGVKSDEELEQGEVP 4192
Cdd:COG5271 438 SAEDDIATDEEADSLADEEEEAEAELDTEEDT--ESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETS 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4193 EDQAIDNHPKMDAKSTFASAEADE--------------ENTDKGIVGENEELGEEDGAAESGVRGNGTADGEFSSAEQVQ 4258
Cdd:COG5271 516 ADDGADTDAAADPEDSDEDALEDEtegeenapgsdqdaDETDEPEATAEEDEPDEAEAETEDATENADADETEESADESE 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4259 KGEDTS-TPKEAMSEADRQYQSLGDHLREwQQANRIHEWEDLTESQSQAFDDsefmhvKEDEEEDLQALGNAEKDQIksi 4337
Cdd:COG5271 596 EAEASEdEAAEEEEADDDEADADADGAAD-EEETEEEAAEDEAAEPETDASE------AADEDADAETEAEASADES--- 665
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1685823625 4338 drDESANQNPDSmnSTNIAEDEADEVGDKQLQDGQDIS----DIKQTGEDTLPTEF-----GSINQSEKVFELSEDED 4406
Cdd:COG5271 666 --EEEAEDESET--SSEDAEEDADAAAAEASDDEEETEeadeDAETASEEADAEEAdteadGTAEEAEEAAEEAESAD 739
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
896-1032 |
2.48e-23 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 98.52 E-value: 2.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 896 PILIQGPTSSGKTSMIEYVAKKT-GHKFVRINNHEHTDLQEYIGTYVTDDNGSlSFREGVLVEALRNGYWIVLDELNLAP 974
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGGA-SWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1685823625 975 TDVLEALNRLLDDNRELFIPETQVLVKPHPEFMLFATQNPPgvYAGRKHLSRAFRNRF 1032
Cdd:pfam07728 80 PDVLNSLLSLLDERRLLLPDGGELVKAAPDGFRLIATMNPL--DRGLNELSPALRSRF 135
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
3919-4424 |
1.56e-21 |
|
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: 103.94 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3919 GAEDITNTLNEDDDLEELA---NEEDTANQSDLDESEARELESDMNGVTKDSVvsENENSDSEEENQ-DLDEEVNDIPED 3994
Cdd:COG5271 519 GADTDAAADPEDSDEDALEdetEGEENAPGSDQDADETDEPEATAEEDEPDEA--EAETEDATENADaDETEESADESEE 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3995 lsnslNEKLWDEPNEEDLLETEQKSNEQSAANNESDLVSKEDDNkALEDKDRQEKEDEEEMSDDVGID----DEIQPDIQ 4070
Cdd:COG5271 597 -----AEASEDEAAEEEEADDDEADADADGAADEEETEEEAAED-EAAEPETDASEAADEDADAETEAeasaDESEEEAE 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4071 EN---NSQPPPENEDhlDLPEDLKLDEKEGDVSkDSDLEDMDmEAADEnkEEADAEKDEPMQDFEDPLEENNTLDEDI-- 4145
Cdd:COG5271 671 DEsetSSEDAEEDAD--AAAAEASDDEEETEEA-DEDAETAS-EEADA--EEADTEADGTAEEAEEAAEEAESADEEAas 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4146 ---QQDDFSDLAEDDEKMNEDG-FEENVQENEESTEDGVKSDEELEQGEVPEDQAIDNHPKMDAKSTFASAEADEENTDK 4221
Cdd:COG5271 745 lpdEADAEEEAEEAEEAEEDDAdGLEEALEEEKADAEEAATDEEAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLD 824
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4222 givGENEELGEEDGAAESGVRGNGTADGEFSSAEQVQKGEDTSTPKEAMSEADRQYQSLGDHLREWQQANRIHEWEDLTE 4301
Cdd:COG5271 825 ---GEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAETDADADADAGEADSSGESS 901
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4302 SQSQAFDDSEfmhvKEDEEEDLQALGNAEKDQIKSIDRDESANQNPDSMNSTNIAEDEADEVGDKQLQDGQDISDIKQTG 4381
Cdd:COG5271 902 AAAEDDDAAE----DADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALALDEAGDEESDDAAADDAGDDSLADDD 977
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1685823625 4382 EDTLPTEFGSINQSEKVFELSEDEDIEDELPDYNVKITNLPAA 4424
Cdd:COG5271 978 EALADAADDAEADDSELDASESTGEAEGDEDDDELEDGEAAAG 1020
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1712-1813 |
3.28e-20 |
|
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: 88.51 E-value: 3.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1712 DMIEIAaCNYHQVNEDWRLKIIKFMFRLQDNIEKDISFGSFGSPWEFNLRDTLRWLQLLNDA-----PKYTCVSPADYLE 1786
Cdd:pfam17867 1 DLEQIL-SHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLSSLlptllSPTVREEIFLEAV 79
|
90 100
....*....|....*....|....*..
gi 1685823625 1787 VMVLHRMRTVEDRVRTCELFKEVFDID 1813
Cdd:pfam17867 80 DVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1188-1382 |
3.59e-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: 89.66 E-value: 3.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1188 PVLLVGDTGCGKTTVCQILAECLH-KELHIINAHQDTENGDIIGaQRPVRNRsavnyslhsqlcekfnvqesldsiddli 1266
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTRDTTEEDLFG-RRNIDPG---------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1267 ekfeklsssekndnlsnlierqiikyrsLFEWHDGALVTAMKQGDFFLLDEISLADDSVLERLNSVLELSRTLTLvehSN 1346
Cdd:pfam07728 52 ----------------------------GASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDERRLLLP---DG 100
|
170 180 190
....*....|....*....|....*....|....*.
gi 1685823625 1347 AAVSLTAKDGFAFFATMNPgGDYGKKELSPALRNRF 1382
Cdd:pfam07728 101 GELVKAAPDGFRLIATMNP-LDRGLNELSPALRSRF 135
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
3907-4413 |
3.30e-19 |
|
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: 96.62 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3907 ELESGTGLGSGVGAEDITNTLNEDDDLEELANE---EDTANQSDLDESEARELESDMNGVTKDSVVSENENSDSEEENQD 3983
Cdd:COG5271 210 DPGDSVAADDDLAAEEGASAVVEEEDASEDAVAaadETLLADDDDTESAGATAEVGGTPDTDDEATDDADGLEAAEDDAL 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3984 LDEEVNDIPEDLSNSLNEklwDEPNEEDLLETEQKSNEQSAANNESDLVSKEDDNKALEDKDRQEkEDEEEMSDDVGIDD 4063
Cdd:COG5271 290 DAELTAAQAADPESDDDA---DDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAEDAAEEAA-TAEDSAAEDTQDAE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4064 EIQPDIQENNSQPPPENEDHLDLPEDLKLDEKEGDVSKDSDL-EDMDMEAADENKEEADAEKDEPmQDFEDPLEENNTLD 4142
Cdd:COG5271 366 DEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTsPTSDTDEEEEEADEDASAGETE-DESTDVTSAEDDIA 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4143 EDIQQDDFSDLAEDDEkMNEDGFEENVQENEESTEDGVKSDEELEQGEVPEDQAIDN--HPKMDAKSTFASAEADEENTD 4220
Cdd:COG5271 445 TDEEADSLADEEEEAE-AELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEEDAeaEADSDELTAEETSADDGADTD 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4221 -KGIVGENEELGEEDGAAESGVRGNGTADGEFSSAEQVQKGEDTSTPKEAMSEADRQYQSLGDHLREWQQANRIHEWEDL 4299
Cdd:COG5271 524 aAADPEDSDEDALEDETEGEENAPGSDQDADETDEPEATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDE 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4300 TESQSQAFDDSEFMHVKEDEEEDLQAlGNAEKDQIKSIDRDESANQNPDSmNSTNIAEDEADEVGDKQLQDGQDISDIKQ 4379
Cdd:COG5271 604 AAEEEEADDDEADADADGAADEEETE-EEAAEDEAAEPETDASEAADEDA-DAETEAEASADESEEEAEDESETSSEDAE 681
|
490 500 510
....*....|....*....|....*....|....
gi 1685823625 4380 TGEDTLPTEfgSINQSEKVFELSEDEDIEDELPD 4413
Cdd:COG5271 682 EDADAAAAE--ASDDEEETEEADEDAETASEEAD 713
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
3894-4365 |
1.29e-18 |
|
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: 94.70 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3894 SPDLPQEGkSNSGELESGTGLGSGVGAEDITNTLNEDDDLEELANEEDTANQSDLD------ESEARELESDMNGVTKDS 3967
Cdd:COG5271 548 GSDQDADE-TDEPEATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDeaaeeeEADDDEADADADGAADEE 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3968 vvsenenSDSEEENQDLDEEVNDIPEDLSNSLNEKLWDEPNEEDLL------ETEQKSNEQSAANNESDLVSKEDDNKAL 4041
Cdd:COG5271 627 -------ETEEEAAEDEAAEPETDASEAADEDADAETEAEASADESeeeaedESETSSEDAEEDADAAAAEASDDEEETE 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4042 E-DKDRQEKEDEEEMSDDVGIDDEIQPDIQENNSQPPPENEDHLDLPE--DLKLDEKEGDVSKDSDLEDMDMEAADENKE 4118
Cdd:COG5271 700 EaDEDAETASEEADAEEADTEADGTAEEAEEAAEEAESADEEAASLPDeaDAEEEAEEAEEAEEDDADGLEEALEEEKAD 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4119 EADAEKDEPMQDFEDPLEENNtlDEDIQQDDFSDLAEDDEKMNEDGFEENVQENEESTEDgvKSDEELEQGEVPEDQAID 4198
Cdd:COG5271 780 AEEAATDEEAEAAAEEKEKVA--DEDQDTDEDALLDEAEADEEEDLDGEDEETADEALED--IEAGIAEDDEEDDDAAAA 855
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4199 NHPKMDAKSTFASAEADEENTDKGIVGENEELGEEDGAAESGVRGNGTADGEFSSAEQVQKGEDTSTPK-EAMSEADRQY 4277
Cdd:COG5271 856 KDVDADLDLDADLAADEHEAEEAQEAETDADADADAGEADSSGESSAAAEDDDAAEDADSDDGANDEDDdDDAEEERKDA 935
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4278 QSLGDHLREwqQANRIHEWEDLTESQS------QAFDDSEFMHVKEDEEEDLQALGNAEKDQIKSIDRDESANQNPDSMN 4351
Cdd:COG5271 936 EEDELGAAE--DDLDALALDEAGDEESddaaadDAGDDSLADDDEALADAADDAEADDSELDASESTGEAEGDEDDDELE 1013
|
490
....*....|....
gi 1685823625 4352 STNIAEDEADEVGD 4365
Cdd:COG5271 1014 DGEAAAGEATADLA 1027
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
3912-4411 |
5.42e-18 |
|
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: 92.39 E-value: 5.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3912 TGLGSGVGAEDITNTLNEDDDLEELANEEDTANQSDLDESEARELES---DMNGVTKDSVVSENENSDSEEENQDLDEEV 3988
Cdd:COG5271 94 LEEGDIAGNAADDSADEESDANAKEDATDDADSSGDAQGDPLATDTLgggDLDLATKDGDELLPSLADNDEAAADEGDEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3989 NDIPEDLSNSLNEKLwdEPNEEDLLETEQKSNEQSAANNESDLVSKEDDNKALEDKDRQEKEDEEEMSDDVGIDDEIQPD 4068
Cdd:COG5271 174 AADGDDTLAVADAIE--ATPGGTDAVELTATLGATVTTDPGDSVAADDDLAAEEGASAVVEEEDASEDAVAAADETLLAD 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4069 IQENNSQPPPENEDHLDLPEDLKLDEK---------EGDVSKDSDLEDMDMEAADENKEEADAEKDEPMQDFEDPLEENN 4139
Cdd:COG5271 252 DDDTESAGATAEVGGTPDTDDEATDDAdgleaaeddALDAELTAAQAADPESDDDADDSTLAALEGAAEDTEIATADELA 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4140 TLDEDIQQDDFSDLAEDDEKMNEDGFEENVQENEESTEDGVKSDEELEQGEVPEDQAIDNHPKMDAKSTFASA------- 4212
Cdd:COG5271 332 AADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADggtspts 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4213 -------EADEENTDKGIVGENEELGEEDGAAESGVRGNGTADGEFSSAEQVQKGEDTSTPKEAmSEADRQYQS---LGD 4282
Cdd:COG5271 412 dtdeeeeEADEDASAGETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEED-ADGDEATDEddaSDD 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4283 HL-REWQQANRIHEWEDLTESQSQAFD-----DSEfmhvKEDEEEDLQALGNAEKDQIKSIDRDESANQNPD-------- 4348
Cdd:COG5271 491 GDeEEAEEDAEAEADSDELTAEETSADdgadtDAA----ADPEDSDEDALEDETEGEENAPGSDQDADETDEpeataeed 566
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1685823625 4349 ------SMNSTNIAEDEADEVGDKQLQDG--QDISDIKQTGEDTLPTEFGSINQSEKVFELSEDEDIEDEL 4411
Cdd:COG5271 567 epdeaeAETEDATENADADETEESADESEeaEASEDEAAEEEEADDDEADADADGAADEEETEEEAAEDEA 637
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1561-1700 |
2.13e-17 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 81.57 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1561 PILLEGSPGVGKTSLITALARETGHQ-LVRINLSDQTDLMDLFGSDVPVEGGeggqFAWRDAPFLAAMRNGHWVLLDELN 1639
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRpVFYVQLTRDTTEEDLFGRRNIDPGG----ASWVDGPLVRAAREGEIAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1685823625 1640 LASQSVLEGLNACLDHRnEAYIPELDKVFKAHP-NFRVFAAQNPQHQGGgrKGLPRSFINRF 1700
Cdd:pfam07728 77 RANPDVLNSLLSLLDER-RLLLPDGGELVKAAPdGFRLIATMNPLDRGL--NELSPALRSRF 135
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
1044-1138 |
1.27e-16 |
|
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: 78.50 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1044 ELETILHKRCKIAPSYAAKIVQVFRELSLRRQTTRIFEQKNS--FATLRDLFRWA---------FREAVGYQQLAENGYM 1112
Cdd:pfam17867 1 DLEQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGSprEFNLRDLLRWCrrlssllptLLSPTVREEIFLEAVD 80
|
90 100
....*....|....*....|....*.
gi 1685823625 1113 LLAERARDQKDKLAVQEVIEKVMKVK 1138
Cdd:pfam17867 81 VFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
154-269 |
2.08e-16 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 78.87 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 154 PILLAGPEGIGKKFLITQIAAKLGQQIIR-IHLSDSTDPKMLIGTYtSPKPGEFEWQPGVLTQAVITGKWILFTNIEHAP 232
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFyVQLTRDTTEEDLFGRR-NIDPGGASWVDGPLVRAAREGEIAVLDEINRAN 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 1685823625 233 SEVLSVLLPLLEKRQLVIPSRGETIYAKG-SFQMFATS 269
Cdd:pfam07728 80 PDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIATM 117
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1560-1716 |
1.83e-14 |
|
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: 77.52 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1560 KPILLEGSPGVGKTSLITALARETGHQLVRINLSdqTDLM--DLFGSDVPVEggEGGQFAWRDAPFLAAMrnghwVLLDE 1637
Cdd:COG0714 32 GHLLLEGVPGVGKTTLAKALARALGLPFIRIQFT--PDLLpsDILGTYIYDQ--QTGEFEFRPGPLFANV-----LLADE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1638 LNLAS---QSVLegLNAcLDHRnEAYIPelDKVFKAHPNFRVFAAQNPQHQGGGRKgLPRSFINRFSV-VYVEALKEKDM 1713
Cdd:COG0714 103 INRAPpktQSAL--LEA-MEER-QVTIP--GGTYKLPEPFLVIATQNPIEQEGTYP-LPEAQLDRFLLkLYIGYPDAEEE 175
|
...
gi 1685823625 1714 IEI 1716
Cdd:COG0714 176 REI 178
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
883-1099 |
1.68e-13 |
|
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: 74.43 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 883 LLNIARACstRMfPILIQGPTSSGKTSMIEYVAKKTGHKFVRINNHEHTDLQEYIGTYVTD-DNGSLSFREGVLveaLRN 961
Cdd:COG0714 23 LVLIALLA--GG-HLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDqQTGEFEFRPGPL---FAN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 962 gywIVL-DELNLAPTDV----LEALnrlldDNRELFIPETQVLVkPHPeFMLFATQNPPGvYAGRKHLSRAFRNRFL-EI 1035
Cdd:COG0714 97 ---VLLaDEINRAPPKTqsalLEAM-----EERQVTIPGGTYKL-PEP-FLVIATQNPIE-QEGTYPLPEAQLDRFLlKL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1685823625 1036 HFD--DiPENELEtILHKRCKIAPSYAAKIVQVFRELSLRRQTTRIFEQKNSFATLRDLFRwAFRE 1099
Cdd:COG0714 166 YIGypD-AEEERE-ILRRHTGRHLAEVEPVLSPEELLALQELVRQVHVSEAVLDYIVDLVR-ATRE 228
|
|
| Mpp10 |
pfam04006 |
Mpp10 protein; This family includes proteins related to Mpp10 (M phase phosphoprotein 10). The ... |
3983-4209 |
5.73e-13 |
|
Mpp10 protein; This family includes proteins related to Mpp10 (M phase phosphoprotein 10). The U3 small nucleolar ribonucleoprotein (snoRNP) is required for three cleavage events that generate the mature 18S rRNA from the pre-rRNA. In Saccharomyces cerevisiae, depletion of Mpp10, a U3 snoRNP-specific protein, halts 18S rRNA production and impairs cleavage at the three U3 snoRNP-dependent sites.
Pssm-ID: 461128 [Multi-domain] Cd Length: 506 Bit Score: 75.00 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3983 DLDEE--------VND-IPEDLSNSLNEKLWDEpnEEDLLETEQKSNEQSAANNESDLVSKEDDNKALEDKDRQEKEDEE 4053
Cdd:pfam04006 47 GFDEEqiwqqlelQNEpVLDQLLKKIGSLLKDE--KELRLLLDSEQDDEEDEDEEEDEEDEEDEEEDEDEEEEEEEEEED 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4054 EMSDDVGIDDEIQPDIQENNSQPPPENEDH-----------LDLPED--LKLDEKEGDVSK-DSDLEDMDMEAADENKEE 4119
Cdd:pfam04006 125 DEDEDSDDEGLEEEDVKELEQKTKKDAKKGrksvvddkffkLDEMEKflEDEEKKEERKDKgKEDEDDIDYFEDDDSEDD 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4120 ADAEKDEPM-QDFEDPLEEnntLDEDIQQDDFSDLAEDDEKMNEDGFEENVQENEESTEDGVKSDEELEQGEVPEDQAID 4198
Cdd:pfam04006 205 EDDGARNLKyEDFFDPPEE---EDEKETKKKKDKKKEEDEKDDEEEEDEEDDAMEEEKEDEFAEDEDEEEDDDEDSDDEE 281
|
250
....*....|.
gi 1685823625 4199 NHPKMDAKSTF 4209
Cdd:pfam04006 282 EEASPEELSSF 292
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
3984-4195 |
9.75e-12 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 72.13 E-value: 9.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3984 LDEEVNDIPEDLSNSLNEKLwdEPN-EEDLLETEQKSNEQSAANNESDLVSKEDDNKALEDKDRQEKEDEEEMSDDvGID 4062
Cdd:PTZ00341 924 INKELKNQNENVPEHLKEHA--EANiEEDAEENVEEDAEENVEENVEENVEENVEENVEENVEENVEENVEENVEE-NVE 1000
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4063 DEIQPDIQENNSQPPPENEDHLDLP--EDLKLDEKEGDVSKDSDLEDMDMEAADENKEEADAEKDEP-MQDFEDPLEENn 4139
Cdd:PTZ00341 1001 ENIEENVEENVEENIEENVEEYDEEnvEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEEnVEEIEENIEEN- 1079
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1685823625 4140 tLDEDIQQDdfsdlAEDDEKMNEDGFEENVQEN-EESTEDGVKSDEELEQGEVPEDQ 4195
Cdd:PTZ00341 1080 -IEENVEEN-----VEENVEEIEENVEENVEENaEENAEENAEENAEEYDDENPEEH 1130
|
|
| AAA_lid_7 |
pfam17867 |
Midasin AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found ... |
294-405 |
7.47e-11 |
|
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: 61.93 E-value: 7.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 294 VEVVSTLYPVLSIICPTLYSVYKDIFDLFSQRSFLATSKIYRRLCLRDFYKFIKRVAFLYHKFmipsdhvvISQELQDAV 373
Cdd:pfam17867 3 EQILSHRFPLLASLAEKLIEVYSRLQELVSSSRSFGSSGSPREFNLRDLLRWCRRLSSLLPTL--------LSPTVREEI 74
|
90 100 110
....*....|....*....|....*....|..
gi 1685823625 374 FKEAIDMFGAFIPSRDGFDLVVRNVAIELNIP 405
Cdd:pfam17867 75 FLEAVDVFAGRFRTPEDREAVAELIAEVLGIS 106
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2012-2098 |
1.60e-09 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 58.84 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 2012 GRFEWFDGYLLKAVEEGHWFVLDNANLCSPAVLDRLNSLLEHKgVLIVNEKTTEDGHPKtikphPNFRLFLTVNPVYG-- 2089
Cdd:pfam07728 51 GGASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLDER-RLLLPDGGELVKAAP-----DGFRLIATMNPLDRgl 124
|
90
....*....|
gi 1685823625 2090 -ELSRAMRNR 2098
Cdd:pfam07728 125 nELSPALRSR 134
|
|
| AAA_3 |
pfam07726 |
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ... |
1562-1700 |
1.99e-09 |
|
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: 58.72 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1562 ILLEGSPGVGKTSLITALARETGHQLVRINLSdqTDLM--DLFGSDVPVEggEGGQFAWRDAPFLAAMrnghwVLLDELN 1639
Cdd:pfam07726 2 VLLEGVPGLAKTLLVRTLARSLGLDFRRIQFT--PDLLpsDITGTEVFDQ--KTREFEFRPGPVFANV-----LLADEIN 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1685823625 1640 LAS---QSVLeglnacLDHRNEAYIPELDKVFKAHPNFRVFAAQNPQHQGGGRKgLPRSFINRF 1700
Cdd:pfam07726 73 RAPpktQSAL------LEAMQERQVTIDGETHPLPEPFFVLATQNPIEQEGTYP-LPEAQLDRF 129
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
625-711 |
7.38e-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: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 625 FSFVEGALVKAVRSGHWVLLDEINLASLETLEPIGQLLSsyESGILLSERGDITPITPHkNFRLFGCMNPsTDVGKRELE 704
Cdd:pfam07728 53 ASWVDGPLVRAAREGEIAVLDEINRANPDVLNSLLSLLD--ERRLLLPDGGELVKAAPD-GFRLIATMNP-LDRGLNELS 128
|
....*..
gi 1685823625 705 PSFRSRF 711
Cdd:pfam07728 129 PALRSRF 135
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
4029-4242 |
1.60e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 60.37 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4029 SDLVSKEDDNKALEDKDRQEKEDEEEMSDDVGIDDEiqpdiQENNSQPPPENEDHLDLPE-DLKLDEKEGDvskdsdlED 4107
Cdd:PHA03169 50 APTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKE-----ERGQGGPSGSGSESVGSPTpSPSGSAEELA-------SG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4108 MDMEAADENKEEADAEKDEPMQDFEDPLEENNTLDEDIQQDDFSDLAEDDEKMNEDGFEENVQENEESTEDGVKSDEELE 4187
Cdd:PHA03169 118 LSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSET 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1685823625 4188 QGEVPEDQAIDNHPKMDAKSTfaSAEADEENTDKGIVGENEELG-EEDGAAESGVR 4242
Cdd:PHA03169 198 PTSSPPPQSPPDEPGEPQSPT--PQQAPSPNTQQAVEHEDEPTEpEREGPPFPGHR 251
|
|
| Granin |
pfam01271 |
Granin (chromogranin or secretogranin); |
3928-4361 |
1.75e-08 |
|
Granin (chromogranin or secretogranin);
Pssm-ID: 279595 [Multi-domain] Cd Length: 584 Bit Score: 60.82 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3928 NEDDDLEELANEEDTANQSDLDESE-ARELESDMNGVTKDSVVSENENSDSEEENQDLDEEVN-DIPEDLSNSLNEKLW- 4004
Cdd:pfam01271 53 NPYFEVRLLRDLADQSEASHLSSRSrDGLSDEDMQIITEALRQAENEPGGHSRENQPYALQVEkEFKTDHSDDYETQQWe 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4005 -------------DEPNEEDLLE-TEQKSNEQSAANNESDLVSKEDDNKALE--DKDRQEKEDEEEMSddvGIDDEIQPD 4068
Cdd:pfam01271 133 eeklkhmrfplryEENSEEKHSErEGELSEVFENPRSQATLKKVFEEVSRLDtpSKQKREKSDEREKS---SQESGEDTY 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4069 IQENNSQP---PPENEDhldlPEDLKLDEKEGDVSKDSDledmdmEAADENKEEADAEKDEPMQDFED-PLEENNTLDED 4144
Cdd:pfam01271 210 RQENIPQEdqvGPEDQE----PSEEGEEDATQEEVKRSR------PRTHHGRSLPDESSRGGQLGLEEeASEEEEEYGEE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4145 IqqDDFSDLAEDDEKMNE---DGFEENVQENEEStedgvksdEELEqgEVPEDQaidNHPKMDAKSTfASAEADEENTDK 4221
Cdd:pfam01271 280 S--RGLSAVQTYLLRLVNargRGRSEKRAERERS--------EESE--EEELKR---ASPYEELEIT-ANLQIPPSEEER 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4222 GIVGENEE---LGEEDGAAESGVRGN--GTADGEFSSAEQVQKGEDTSTPKEAMSEADRQYQSLGDHLRE--WQQanrih 4294
Cdd:pfam01271 344 MLKKAGRSprgRVDEAGALEALEALEekRKLDLDHSRVFESSEDGAPRAPQGAWVEALRNYLSYGEEGMEgkWNQ----- 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1685823625 4295 ewedltesQSQAFDDSEfmhvkEDEEE---DLQALGNAEKDQIKS---IDRDESANQNPDSMNSTNIAEDEAD 4361
Cdd:pfam01271 419 --------QGPYFPNEE-----NREEArfrLPQYLGELSNPWEDPkqwKPSDFERKELTADKFLEGEEENEYT 478
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1546-1702 |
1.76e-08 |
|
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: 56.39 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1546 LMNASKVLRALQVLKPILLEGSPGVGKTSLITALARETGHQLVRINlsdQTDLMDLFGSDvpVEGGEGGQFAWRDAPFLA 1625
Cdd:cd00009 6 AIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFL---YLNASDLLEGL--VVAELFGHFLVRLLFELA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1685823625 1626 AMRNGHWVLLDELNLASQSVLEGLNACLDHRNEAYIPeldkvfkaHPNFRVFAAQNPQHQGGGRKGLPRSFINRFSV 1702
Cdd:cd00009 81 EKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRID--------RENVRVIGATNRPLLGDLDRALYDRLDIRIVI 149
|
|
| TFIIF_alpha |
pfam05793 |
Transcription initiation factor IIF, alpha subunit (TFIIF-alpha); Transcription initiation ... |
3985-4263 |
2.93e-08 |
|
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: 59.96 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3985 DEEVNDIPEDLSNSLNEKlwDEPNEEDLLETEQKSNEQSAANNESDLVSKE----DDNKAleDKDRQEKEDEEEMSDDVg 4060
Cdd:pfam05793 211 DLKIKDLEGDDEDDGDES--DKGGEDGDEEKKKKKKKKLAKNKKKLDDDKKkkrgGDDDA--FEYDSDDGDDEGREEDY- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4061 IDDEiqpdiqENNSQPPPENEDHLDLPEDLKLDEKEGDVSKDSDLEDMDmEAADENKEEADAEKdepmqdfedPLEENNT 4140
Cdd:pfam05793 286 ISDS------SASGNDPEEREDKLSPEEPAKGEIEQSDDSEESEEEKNE-EEGKLSKKGKKAKK---------LKGKKNG 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4141 LDEDIQQDDFSDLAEDDEKMNEDGFEENVQENEESTEDGVKSDEELEQGEVPEdqaidnHPKMDAKSTFASAEADEENTD 4220
Cdd:pfam05793 350 KDKSESSDGDDSDDSDIDDEDSVPLFTAKKKKEPKKEEPVDSGPSSPGNSGPA------RPSPESGSTSSKRKAAAEVSK 423
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1685823625 4221 KGIVGENEELG-EEDGAAESGVRGNGTADGEFSS--AEQVQKGEDT 4263
Cdd:pfam05793 424 SPASVPAKKLKtENGPKSSSGKSTPQTFSGSKSSsnAADGGVTEEA 469
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
3769-4234 |
3.02e-08 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 60.57 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3769 MNFVLNLFDSLLSSIETatknmrtFKELAETSSFIE-MSSCFSKVLRAFNLKFQSMKLSSLKEKLRSSSVDKMSCQLLML 3847
Cdd:PTZ00341 645 VNFIHPSIFYLLASLEK-------FADFTGSPQIVTlLKFFFEKKLSMNDLDNKSEHLLKFMEQYQKEREAHISENLINI 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3848 FLPVCEQFINLAESVLDYFINVHNSNLDS--LSKISTLFFMVANNGFCSPD-----LPQEGKSNSGELESGTG------- 3913
Cdd:PTZ00341 718 LQPCIAGDRKWDVPIIDKIEELKGSPFDIaiIDSIGWIFKHVAKSHLKKPKkaakkLEQRSKANKEELANENNklmnilk 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3914 --LGSGVGAEDIT-----NTLNEDddleelaNEEDTANQSDLDESEARELESDMNGVTkdsvvsenensdseeenqdLDE 3986
Cdd:PTZ00341 798 eyFGNNEQINSITynfenINLNED-------NENGSKKILDLNHKDQKEIFEEIISYI-------------------VDI 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3987 EVNDIPEDLSNSLNEKLWDEPNEEDLLETEQKS----------------NEQSAAN-----------NESDLVSKEDDNK 4039
Cdd:PTZ00341 852 SLSDIENTAKNAAEQILSDEGLDEKKLKKRAESlkklanaiekyagggkKDKKAKKkdakdlsgniaHEINLINKELKNQ 931
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4040 ALEDKDRQEKEDEEEMSDDvgIDDEIQPDIQENNSQPPPEN-EDHLDLPEDLKLDEK-EGDVSK--DSDLEDMDMEAADE 4115
Cdd:PTZ00341 932 NENVPEHLKEHAEANIEED--AEENVEEDAEENVEENVEENvEENVEENVEENVEENvEENVEEnvEENVEENIEENVEE 1009
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4116 NKEEADAEKDEPMQdfEDPLEENNTLDEDIQQDDFSDLAEDDEKMNEDGFEENVQENEESTEDGVKSDEELEQGEVPEDQ 4195
Cdd:PTZ00341 1010 NVEENIEENVEEYD--EENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEIEENIEENIEENVEEN 1087
|
490 500 510
....*....|....*....|....*....|....*....
gi 1685823625 4196 AIDNHPKMDAKSTFASAEADEENTDKGIVGENEELGEED 4234
Cdd:PTZ00341 1088 VEENVEEIEENVEENVEENAEENAEENAEENAEEYDDEN 1126
|
|
| Mpp10 |
COG5384 |
U3 small nucleolar ribonucleoprotein component [Translation, ribosomal structure and ... |
3930-4160 |
3.88e-08 |
|
U3 small nucleolar ribonucleoprotein component [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227674 [Multi-domain] Cd Length: 569 Bit Score: 59.70 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3930 DDDL----EELANEED---TANQSDLDESEARELESDMNGVTKDSVVSENENSDSEEENQDLDEE-VNDIPEDLSNSLNE 4001
Cdd:COG5384 67 DGDLiqgiQELKDPSLdgsTLNSSSGEESELEEAESVFKEKQMLSADVSEIEEQSNDSLSENDEEpSMDDEKTSAEAARE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4002 KLWDEPNEEDLLETE------QKSNEQSAA---NNESDLVSKEDDNKALEDKDRQEKEDEEEMSDDVgiddeiqpdIQEN 4072
Cdd:COG5384 147 EFAEEKRIPDPYGINdkffdlEKFNRDTLAaedSNEASEGSEDEDIDYFQDMPSDDEEEEAIYYEDF---------FDKP 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4073 NSQPPPENEDHLDLPEDLKLDEKEGDVSKDSDLEDMDMEAADE-NKEEADAEKDEPMQDFEdplEENNTLDEDIQQDDFS 4151
Cdd:COG5384 218 TKEPVKKHSDVKDPKEDEELDEEEHDSAMDKVKLDLFADEEDEpNAEGVGEASDKNLSSFE---KQQIEMDEQIEELEKE 294
|
....*....
gi 1685823625 4152 DLAEDDEKM 4160
Cdd:COG5384 295 LVAPKEWKY 303
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4014-4419 |
7.04e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 7.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4014 ETEQKSNEQSAANN--ESDLVSK-EDDNKALEDKDRQEKEDEEEMSDDVGIDDEIQPDIQENNSQPPPE--NEDHLDLPE 4088
Cdd:PTZ00121 1531 EEAKKADEAKKAEEkkKADELKKaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKlyEEEKKMKAE 1610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4089 DLKLDEKEG----DVSKDSD----LEDMDMEAADENKEEADAEKDEPMQDFEDPlEENNTLDEDIQQDDFSDLAEDDEKM 4160
Cdd:PTZ00121 1611 EAKKAEEAKikaeELKKAEEekkkVEQLKKKEAEEKKKAEELKKAEEENKIKAA-EEAKKAEEDKKKAEEAKKAEEDEKK 1689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4161 NEDGFEENVQENEESTEdgVKSDEELEQGEVPEDQAIDNHPKMDAKSTFASAEADEENTDKGIVGEneelGEEDGAAESG 4240
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEE--LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE----EEKKKIAHLK 1763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4241 VRGNGTADGEFSSAEQVQKGEDTSTPKEAMSEADRQYQSLGDHLREWQQANR-----IHEWEDLTESQSQAFDDSEFMHV 4315
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKegnlvINDSKEMEDSAIKEVADSKNMQL 1843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4316 KE-DEEEDLQALGNAEKDqiksidrdESANQNPDSMNSTNIAEDEADEVgdkqlqdgQDISDIKQTGEDTLPTEFGSINQ 4394
Cdd:PTZ00121 1844 EEaDAFEKHKFNKNNENG--------EDGNKEADFNKEKDLKEDDEEEI--------EEADEIEKIDKDDIEREIPNNNM 1907
|
410 420
....*....|....*....|....*
gi 1685823625 4395 SEKVFELSEDEDIEDELPDYNVKIT 4419
Cdd:PTZ00121 1908 AGKNNDIIDDKLDKDEYIKRDAEET 1932
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4032-4326 |
7.52e-08 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 59.24 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4032 VSKEDDNKAledKDRQEKEDEEEMSDDVGidDEIQPDIQENNSQPPPENEDHLDlpedlklDEKEGDVSKDSDLEDMDME 4111
Cdd:TIGR00927 630 LSKGDVAEA---EHTGERTGEEGERPTEA--EGENGEESGGEAEQEGETETKGE-------NESEGEIPAERKGEQEGEG 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4112 AADENKEEADAEKDEPMQDFEDPLEENNTLDEDIQQddfsdlAEDDEKMNEDGFEENVQENEESTEDGVKSDEELEQGEV 4191
Cdd:TIGR00927 698 EIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIE------TGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETE 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4192 PEDQAIDNHPKMDAKSTfASAEADEENTDKGIVGENEELGEEDGAAESGVRGNGTADGEFSSAEQVQKGEDTSTPKEAMS 4271
Cdd:TIGR00927 772 AEGKEDEDEGEIQAGED-GEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEK 850
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1685823625 4272 EADRQYQSLGDHLREWQqanrihEWEDLTESQSQAFDDSEfmhvkEDEEEDLQAL 4326
Cdd:TIGR00927 851 GVDGGGGSDGGDSEEEE------EEEEEEEEEEEEEEEEE-----EEEEENEEPL 894
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
3615-4143 |
2.30e-07 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 57.49 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3615 KNVYSEVGVNGSPLESFNNSS-FNEVSSLGYDHDFENRAQAVSMLcqiyAIVIQKHSSISptaSFQSIGHELSRF----- 3688
Cdd:PTZ00341 631 KKMYNKFGYDGIKGVNFIHPSiFYLLASLEKFADFTGSPQIVTLL----KFFFEKKLSMN---DLDNKSEHLLKFmeqyq 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3689 -------ADLLSNKLFPSsiplyasadkVSSIRDQQKGINDLIEYCRKKRTELP---ELSYCFKHlVSLQSLKSISRTQV 3758
Cdd:PTZ00341 704 kereahiSENLINILQPC----------IAGDRKWDVPIIDKIEELKGSPFDIAiidSIGWIFKH-VAKSHLKKPKKAAK 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3759 DL-----TNDEFL-----NLMNFVLNLFDSLlSSIETATKNMRTfkelaeTSSFIEMSSCFSKVLrafNLKFQSMKlsSL 3828
Cdd:PTZ00341 773 KLeqrskANKEELanennKLMNILKEYFGNN-EQINSITYNFEN------INLNEDNENGSKKIL---DLNHKDQK--EI 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3829 KEKLRSSSVDKMSCQLLMLFLPVCEQFINLaESVLDYFINVHNSNLDSLSKISTLFFMVANNGFCSPDlpQEGKSNSGEL 3908
Cdd:PTZ00341 841 FEEIISYIVDISLSDIENTAKNAAEQILSD-EGLDEKKLKKRAESLKKLANAIEKYAGGGKKDKKAKK--KDAKDLSGNI 917
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3909 ESGTGLgsgvgaedITNTL-NEDDDLEELANEEDTAN-QSDLDESEARELESDMNGVTKDSVvsenensdseeeNQDLDE 3986
Cdd:PTZ00341 918 AHEINL--------INKELkNQNENVPEHLKEHAEANiEEDAEENVEEDAEENVEENVEENV------------EENVEE 977
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3987 EVND-IPEDLSNSLNEKLwDEPNEEDLLETEQKSNEQSAANN--ESDLVSKEDDNKALEDKDRQEKEDEEEMSDDvGIDD 4063
Cdd:PTZ00341 978 NVEEnVEENVEENVEENV-EENVEENIEENVEENVEENIEENveEYDEENVEEVEENVEEYDEENVEEIEENAEE-NVEE 1055
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4064 EIQPDIQENNSQPPPENEDHLD--LPEDLKLDEKEGDVSKDSDLEDMDMEAADENKEEaDAEKDEPMQDFEDPLEENNTL 4141
Cdd:PTZ00341 1056 NIEENIEEYDEENVEEIEENIEenIEENVEENVEENVEEIEENVEENVEENAEENAEE-NAEENAEEYDDENPEEHNEEY 1134
|
..
gi 1685823625 4142 DE 4143
Cdd:PTZ00341 1135 DE 1136
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
3982-4177 |
3.50e-07 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 57.10 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3982 QDLDEEVND-IPEDLSNSLNEKLwDEPNEEDLLETEQKSNEQSAANNESDLVSKEDDNKALEDKDRQEKEDEEEMSDDVG 4060
Cdd:PTZ00341 957 EDAEENVEEnVEENVEENVEENV-EENVEENVEENVEENVEENVEENIEENVEENVEENIEENVEEYDEENVEEVEENVE 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4061 -IDDEIQPDIQENNSQPPPEN-EDHLDLPEDLKLDEKEGDVskDSDLEDMDMEAADENKEEadaekdepmqdfedpLEEN 4138
Cdd:PTZ00341 1036 eYDEENVEEIEENAEENVEENiEENIEEYDEENVEEIEENI--EENIEENVEENVEENVEE---------------IEEN 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1685823625 4139 ntLDEDIQQDDFSDLAEDDEKMNEDGFEENVQE-NEESTE 4177
Cdd:PTZ00341 1099 --VEENVEENAEENAEENAEENAEEYDDENPEEhNEEYDE 1136
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
153-269 |
4.83e-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: 54.79 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 153 RPILLAGPEGIGKKFLITQIAAKLGQQIIRIHLSDSTDPKMLIGTY-TSPKPGEFEWQPGVLTQAVitgkwILFTNIEHA 231
Cdd:COG0714 32 GHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYiYDQQTGEFEFRPGPLFANV-----LLADEINRA 106
|
90 100 110
....*....|....*....|....*....|....*...
gi 1685823625 232 PSEVLSVLLPLLEKRQLVIPsrGETIYAKGSFQMFATS 269
Cdd:COG0714 107 PPKTQSALLEAMEERQVTIP--GGTYKLPEPFLVIATQ 142
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
896-1038 |
6.46e-07 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 55.12 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 896 PILIQGPTSSGKTSMIEYVAKKTGHKFVRINnhehTDLQEYIGTYVTDDNGSlsFREGVLVEALRNGYWIVLDELNLAPT 975
Cdd:PHA02244 121 PVFLKGGAGSGKNHIAEQIAEALDLDFYFMN----AIMDEFELKGFIDANGK--FHETPFYEAFKKGGLFFIDEIDASIP 194
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1685823625 976 DVLEALNRLLDDNRELFIPETqvlVKPHPEFMLFATQNPPG-----VYAGRKHLSRAFRNRFLEIHFD 1038
Cdd:PHA02244 195 EALIIINSAIANKFFDFADER---VTAHEDFRVISAGNTLGkgadhIYVARNKIDGATLDRFAPIEFD 259
|
|
| COG5137 |
COG5137 |
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics] ... |
4038-4196 |
7.85e-07 |
|
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics];
Pssm-ID: 227466 [Multi-domain] Cd Length: 279 Bit Score: 54.23 E-value: 7.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4038 NKALEDKDRQEKEDEEEMSDDVGIDD-----------EIQPDIQENNsqpPPENEDHLDLPEDLKLDEKEGDVSKDSDLE 4106
Cdd:COG5137 114 NNEYPGITKLEKSDVEEPSEKVDEEDvereilaekprVTRFNIVWDN---DEDNDEAPPAQPDVDNEEEERLEESDGREE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4107 DMDMEAADENKEEADAEKDEPMQDFEDPLEENNTlDEDIQQDDFSDLAEDDEKMNED-GFEENVQENEESTEDGVKSDEE 4185
Cdd:COG5137 191 EEDEEVGSDSYGEGNRELNEEEEEEAEGSDDGED-VVDYEGERIDKKQGEEEEMEEEvINLFEIEWEEESPSEEVPRNNE 269
|
170
....*....|.
gi 1685823625 4186 leqgEVPEDQA 4196
Cdd:COG5137 270 ----ESPAKKQ 276
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1562-1704 |
8.95e-07 |
|
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: 51.05 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1562 ILLEGSPGVGKTSLITALARETGHQLVRINLSDQTDLMdlfgsdvpveGGEGGQFAwRDAPFLAAMRNGHWVLLDELNLA 1641
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKY----------VGESEKRL-RELFEAAKKLAPCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1685823625 1642 SQSVLEGLNACLDHRNEAYIPELDKVFKAHPNFRVFAAQN-PQHqgggrkgLPRSFINRFSVVY 1704
Cdd:pfam00004 70 AGSRGSGGDSESRRVVNQLLTELDGFTSSNSKVIVIAATNrPDK-------LDPALLGRFDRII 126
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
1560-1595 |
1.13e-06 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 54.93 E-value: 1.13e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1685823625 1560 KPILLEGSPGVGKTSLITALARETGHQLVRINLSDQ 1595
Cdd:PRK04195 40 KALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQ 75
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3983-4448 |
1.53e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3983 DLDEEVNDI----PEDLSNSLNEKLwDEPNEEdlLETEQKSNEQSAAnnesdlvSKEDDNKALEDKdRQEKEDEEEMSDD 4058
Cdd:PRK02224 191 QLKAQIEEKeekdLHERLNGLESEL-AELDEE--IERYEEQREQARE-------TRDEADEVLEEH-EERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4059 VgidDEIQPDIQENNSqpppENEDHLDLPEDLK-----LDEKEGDVSKDSDLEDMDMEAADENKEEADAEKDEPMQDFE- 4132
Cdd:PRK02224 260 I---EDLRETIAETER----EREELAEEVRDLRerleeLEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEe 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4133 -------------------DPLEENN--------TLDEDIqQDDFSDLAEDDEKMNEdgFEENVQENEESTEDgvkSDEE 4185
Cdd:PRK02224 333 crvaaqahneeaeslredaDDLEERAeelreeaaELESEL-EEAREAVEDRREEIEE--LEEEIEELRERFGD---APVD 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4186 LEQGEVPEDQAIDNHPkmDAKSTFASAEADEENTDKGIvGENEELGEEDGAAESG--VRGNGTADGEFSSAEQVQKGEdt 4263
Cdd:PRK02224 407 LGNAEDFLEELREERD--ELREREAELEATLRTARERV-EEAEALLEAGKCPECGqpVEGSPHVETIEEDRERVEELE-- 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4264 stpkEAMSEADRQYQSLgdhlrewqqANRIHEWEDLTESQSQAfddsefmhvkEDEEEDLQALGNAEKDQIKSIDRD--- 4340
Cdd:PRK02224 482 ----AELEDLEEEVEEV---------EERLERAEDLVEAEDRI----------ERLEERREDLEELIAERRETIEEKrer 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4341 -ESANQNPDSMNStniAEDEADEVGDKQLQDGQDISDIKQTGEDTLPTEFGSINQSEKVFE-LSEDEDIEDELPDYNVKI 4418
Cdd:PRK02224 539 aEELRERAAELEA---EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTlLAAIADAEDEIERLREKR 615
|
490 500 510
....*....|....*....|....*....|
gi 1685823625 4419 TNLpAAMPiDEARDLWNKHEDSTKQLSIEL 4448
Cdd:PRK02224 616 EAL-AELN-DERRERLAEKRERKRELEAEF 643
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
1546-1594 |
1.92e-06 |
|
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: 50.74 E-value: 1.92e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1546 LMNASKVLRALQVL-KPILLEGSPGVGKTSLITALARETGHQLVRINLSD 1594
Cdd:cd19481 12 PRRGSRLRRYGLGLpKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSS 61
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4005-4417 |
2.64e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4005 DEPNEEDLLETEQKSNEQSAANNESDLVSKEDDNKALEDKDRQEKEDEEEMSDDVGIDDEIQPDIQE-NNSQPPPENEDH 4083
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEkKKADEAKKKAEE 1442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4084 LDLPEDLKLDEKEGDVSKDSDLEDMDMEAADENKEEADAEK--DEPMQDFEDP---LEENNTLDEDIQQDDFSDLAEDDE 4158
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkaDEAKKKAEEAkkkADEAKKAAEAKKKADEAKKAEEAK 1522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4159 KMNEDGFEENVQENEESTE-------DGVKSDEELEQGEvpEDQAIDNHPKMDAKSTFASAEADE-ENTDKGIVGENEEL 4230
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKaeekkkaDELKKAEELKKAE--EKKKAEEAKKAEEDKNMALRKAEEaKKAEEARIEEVMKL 1600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4231 GEEDGA--AESGVRgngtADGEFSSAEQVQKGEDTSTPKEAMSEADRQYQSLGDHLREWQQANRIHEWEDLTESQSQAFD 4308
Cdd:PTZ00121 1601 YEEEKKmkAEEAKK----AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK 1676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4309 DSEFMHVKEDEEEDLQALGNAEKDQIKSIDRDESANQNPDSMNSTNIAEDE----ADEVGDKQLQDGQDISDIKQTGEDT 4384
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
410 420 430
....*....|....*....|....*....|....*
gi 1685823625 4385 LPTEFGSINQSEKVFELSEDED--IEDELPDYNVK 4417
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRKEKEavIEEELDEEDEK 1791
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
4506-4658 |
4.06e-06 |
|
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: 50.15 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4506 VMISIDDSKSMSESGSTvLALETLALVTKALSLLEVG-QIAVMKFGEQPELLHPFDKQFSSE---SGVQMFSHFTFEQSN 4581
Cdd:smart00327 2 VVFLLDGSGSMGGNRFE-LAKEFVLKLVEQLDIGPDGdRVGLVTFSDDARVLFPLNDSRSKDallEALASLSYKLGGGTN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1685823625 4582 TNvLALADAsmkcFNYANTASHhRSNSDIRQLEIIISDGICEDHDS-IRKLLRRAQEEKVMIVFV-ILDNVNTQKKSSI 4658
Cdd:smart00327 81 LG-AALQYA----LENLFSKSA-GSRRGAPKVVILITDGESNDGPKdLLKAAKELKRSGVKVFVVgVGNDVDEEELKKL 153
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4000-4195 |
6.01e-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: 53.08 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4000 NEKLWDEPNE-----EDLLETEQKSNEQSAANNESDLVSK--------EDDNKALEDKDRQEKEDEEEMSDDVGIDDEIQ 4066
Cdd:TIGR00927 679 NESEGEIPAErkgeqEGEGEIEAKEADHKGETEAEEVEHEgeteaegtEDEGEIETGEEGEEVEDEGEGEAEGKHEVETE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4067 PDIQENNSQPPPENEdhldlpedLKLDEKEGDVSKDSDLE----DMDMEAADENKEEADAEKDEPMQDFEDPLEENNTLD 4142
Cdd:TIGR00927 759 GDRKETEHEGETEAE--------GKEDEDEGEIQAGEDGEmkgdEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKD 830
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1685823625 4143 EDIQQD---DFSDLAEDDEKMNEDGFE------ENVQENEESTEDGVKSDEELEQGEVPEDQ 4195
Cdd:TIGR00927 831 ETGEQElnaENQGEAKQDEKGVDGGGGsdggdsEEEEEEEEEEEEEEEEEEEEEEEEEENEE 892
|
|
| vWFA |
cd00198 |
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
4504-4649 |
6.80e-06 |
|
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.
Pssm-ID: 238119 [Multi-domain] Cd Length: 161 Bit Score: 49.49 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4504 YQVMISIDDSKSMSESGSTVLALETLALVTKALSLLEVGQIAVMKFGEQPELLHPFDKQFSSESGVQMFSHFTFEQS-NT 4582
Cdd:cd00198 1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGgGT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1685823625 4583 NVLALADASMKCFNYANTASHHRSNsdirqleIIISDGICEDH-DSIRKLLRRAQEEKVMIVFVILDN 4649
Cdd:cd00198 81 NIGAALRLALELLKSAKRPNARRVI-------ILLTDGEPNDGpELLAEAARELRKLGITVYTIGIGD 141
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
4060-4454 |
8.54e-06 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 52.44 E-value: 8.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4060 GIDDEIQPDIQENNSQPPPENEDHLdlpEDLKLDEKE----------GDVSKDSDLEDMDMEAADENKEEADAEKDEpmq 4129
Cdd:COG5192 289 GVGDFRMADVEVLIDPCPPPDADHG---RRRRLSLKSkliyspmsdiGGILKDKDRVYIEVPTSNFSKDENSEAGEG--- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4130 dfedplEENNTLDEDIQQDDFSDLAEDDEKMNEDGFEENVQENEESTEDGVKSDEELEQGEVPEDQA-IDNHPKMDAKST 4208
Cdd:COG5192 363 ------EKMKMQLQEIEQDPGVDGVGLQLFSNSDAIDTVDRESSEIDNVGRKTRRQPTGKAIAEETSrEDELSFDDSDVS 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4209 FASAEADEENTDKGIVGENE-ELGEEDGAAESgvrgngtaDGEFSSAEQVQKGEDTSTPKEAMSEADRQYQSLGDHLREw 4287
Cdd:COG5192 437 TSDENEDVDFTGKKGAINNEdESDNEEVAFDS--------DSQFDESEGNLRWKEGLASKLAYSQSGKRGRNIQKIFYD- 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4288 qqaNRIHEWEDLTESQSQAFDDSEFMHVKEDEEEDL---------QALGNAEKDQIKSIDRDESANQNPDSMNS------ 4352
Cdd:COG5192 508 ---ESLSPEECIEEYKGESAKSSESDLVVQDEPEDFfdvskvaneSISSNHEKLMESEFEELKKKWSSLAQLKSrfqkda 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4353 -TNIAEDEADEVGDKQLQDGQDISDIKQTGEDTLPTEFGSINQSEKVfELSEDEDIEDELPDYNVKITNLPAAMPIDEAR 4431
Cdd:COG5192 585 tLDSIEGEEELIQDDEKGNFEDLEDEENSSDNEMEESRGSSVTAENE-ESADEVDYETEREENARKKEELRGNFELEERG 663
|
410 420
....*....|....*....|...
gi 1685823625 4432 DLWNKHEDSTKQLSIELCEQLRL 4454
Cdd:COG5192 664 DPEKKDVDWYTEEKRKIEEQLKI 686
|
|
| PRK05901 |
PRK05901 |
RNA polymerase sigma factor; Provisional |
4014-4213 |
9.63e-06 |
|
RNA polymerase sigma factor; Provisional
Pssm-ID: 235640 [Multi-domain] Cd Length: 509 Bit Score: 51.92 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4014 ETEQKSNEQSAANNESDLVSKEDDNKALEDKD---RQEKEDEEEMSDDVGIDDEIQPDIQENNSQPPPENEDHLDLPEDL 4090
Cdd:PRK05901 15 EAKKKLKKLAAKSKSKGFITKEEIKEALESKKktpEQIDQVLIFLSGMVKDTDDATESDIPKKKTKTAAKAAAAKAPAKK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4091 KLDEKEGDVSKDSDLEDMDMEAADENKEEADAEKDEPMQDFEDPLEENNtlDEDIQQDDfsDLAEDDEKMNEDGFEENVQ 4170
Cdd:PRK05901 95 KLKDELDSSKKAEKKNALDKDDDLNYVKDIDVLNQADDDDDDDDDDDLD--DDDIDDDD--DDEDDDEDDDDDDVDDEDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1685823625 4171 ENEESTEDGVKSDEELEQGEVPEDQAiDNHPKMDAKSTfASAE 4213
Cdd:PRK05901 171 EKKEAKELEKLSDDDDFVWDEDDSEA-LRQARKDAKLT-ATAD 211
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
886-1035 |
1.44e-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: 48.30 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 886 IARACSTRMFPILIQGPTSSGKTSMIEYVAK---KTGHKFVRINNHEhtdlqEYIGTYVTDDNGSLSFREGVLVEALRNG 962
Cdd:cd00009 11 REALELPPPKNLLLYGPPGTGKTTLARAIANelfRPGAPFLYLNASD-----LLEGLVVAELFGHFLVRLLFELAEKAKP 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1685823625 963 YWIVLDELNLAPTDVLEALNRLLDDNRELFIPETQVLVkphpefmLFATQNPPGVyagrkHLSRAFRNRFLEI 1035
Cdd:cd00009 86 GVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRENVRV-------IGATNRPLLG-----DLDRALYDRLDIR 146
|
|
| PHA02244 |
PHA02244 |
ATPase-like protein |
1525-1703 |
1.95e-05 |
|
ATPase-like protein
Pssm-ID: 107157 [Multi-domain] Cd Length: 383 Bit Score: 50.50 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1525 GIPLGDSVESDSTYSLHTDTTLMNASKVLRALQVLKPILLEGSPGVGKTSLITALAretghQLVRINLSDQTDLMDLFgs 1604
Cdd:PHA02244 85 GKPAGDISGIDTTKIASNPTFHYETADIAKIVNANIPVFLKGGAGSGKNHIAEQIA-----EALDLDFYFMNAIMDEF-- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1605 dvPVEGGEGGQFAWRDAPFLAAMRNGHWVLLDELNLASQSVLEGLNACLDHRneaYIPELDKVFKAHPNFRVFAAQNPQH 1684
Cdd:PHA02244 158 --ELKGFIDANGKFHETPFYEAFKKGGLFFIDEIDASIPEALIIINSAIANK---FFDFADERVTAHEDFRVISAGNTLG 232
|
170 180
....*....|....*....|....
gi 1685823625 1685 QGG-----GRKGLPRSFINRFSVV 1703
Cdd:PHA02244 233 KGAdhiyvARNKIDGATLDRFAPI 256
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
4099-4350 |
1.99e-05 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 51.15 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4099 VSKDSDLEDMDMEAADENK-------------EEADAEKDEPMQDFEDPLEENNTLDEDIQQDDF-SDLAEDDEKMNE-- 4162
Cdd:TIGR00927 621 VAKVMALGDLSKGDVAEAEhtgertgeegerpTEAEGENGEESGGEAEQEGETETKGENESEGEIpAERKGEQEGEGEie 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4163 --------DGFEENVQENEESTEDGVKSDEELEQGEVPEDQAIDNHPKMDAKSTFAS-AEADEENTDKGIVGENEElGEE 4233
Cdd:TIGR00927 701 akeadhkgETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETeGDRKETEHEGETEAEGKE-DED 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4234 DGAAESGvrGNGTADGEFSSAEQVQKGEDTSTPKEAMSEADRQYQSLGDHLR-EWQQANRIHEWEDLTESQSQAFD---- 4308
Cdd:TIGR00927 780 EGEIQAG--EDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKdETGEQELNAENQGEAKQDEKGVDgggg 857
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1685823625 4309 ----DSEFMHVKEDEEEDlqalgnaEKDQIKSIDRDESANQNPDSM 4350
Cdd:TIGR00927 858 sdggDSEEEEEEEEEEEE-------EEEEEEEEEEEEEENEEPLSL 896
|
|
| COG5644 |
COG5644 |
U3 small nucleolar RNA-associated protein 14 [Function unknown]; |
3913-4404 |
2.18e-05 |
|
U3 small nucleolar RNA-associated protein 14 [Function unknown];
Pssm-ID: 227931 [Multi-domain] Cd Length: 869 Bit Score: 50.86 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3913 GLGSGVGAEDI----TNTLNEDDDLEELANEEDTANQSDLDESEARELESDMNGVTKDSvvsenensdseeenqdlDEEV 3988
Cdd:COG5644 43 GYSFGVNSEDDeeidSDEAFDEEDEKRFADWSFNASKSGKSNKDHKNLNNTKEISLNDS-----------------DDSV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3989 NDIPEDlsnslNEKLWDEPNEEDLLETEQ-----KSNEQSAANNESDLVSK---EDDNKALEDKDRQEKEDEEEM-SDDV 4059
Cdd:COG5644 106 NSDKLE-----NEGSVSSIDENELVDLDTlldndQPEKNESGNNDHATDKEnllESDASSSNDSESEESDSESEIeSSDS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4060 GIDDEIQPD-------------IQENNSQPPPENEDHlDLPEDLKLD----EKEGDVSKDSDLEDM----DMEAADENKE 4118
Cdd:COG5644 181 DHDDENSDSkldnlrnyivslkKDEADAESVLSSDDN-DSIEEIKYDphetNKESGSSETIDITDLldsiPMEQLKVSLK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4119 EADAEK---DEPM-QDFEDPLEENNTLDEDIQQ-DDFSDLAEDDEK-------MNEDGfEENVQENEESTEDGVKSDEEL 4186
Cdd:COG5644 260 PLVSESsklDAPLaKSIQDRLERQAAYEQTKNDlEKWKPIVADNRKsdqlifpMNETA-RPVPSNNGLASSFEPRTESER 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4187 EQGEVPEDQAIDNHPKMDAKSTFASAEADEENTDKGI------------------------------VGENEELGEEDGA 4236
Cdd:COG5644 339 KMHQALLDAGLENESALKKQEELALNKLSVEEVAERTrqlrfmrelmfreerkakrvakiksktyrkIRKNRKEKEMALI 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4237 AESGVRGNGTADGEFSSAEQVQKGEDTST--------------PKEAMSEADRQyqslGDHLREwqqanRIHEWEDLTES 4302
Cdd:COG5644 419 PKSEDLENEKSEEARALERMTQRHKNTSSwtrkmlerashgegTREAVNEQIRK----GDELMQ-----RIHGKEIMDGE 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4303 QSQAFDDSEFmHVKEDEEEDLQALGNAEkdqiksidrDESANQNPDSMNSTNIAEDEADEVGDKQLQDGQDISDIKQTGE 4382
Cdd:COG5644 490 DVSEFSDSDY-DTNEQVSTAFEKIRNEE---------ELKGVLGMKFMRDASNRQMAASKISVADLVKVENGDDIDVGEL 559
|
570 580
....*....|....*....|...
gi 1685823625 4383 DTLPTEFGSINQS-EKVFELSED 4404
Cdd:COG5644 560 DEVGGDAIYANAGrREVFPVVEQ 582
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
1166-1411 |
2.36e-05 |
|
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: 49.78 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1166 VVWTRPMIRLfCLVwrCLLAKEPVLLVGDTGCGKTTVCQILAECLHKELHIINAHQDTENGDIIGAQRPVRNRSAvnysl 1245
Cdd:COG0714 14 YVGQEELIEL-VLI--ALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPDLLPSDILGTYIYDQQTGE----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1246 hsqlcekfnvqesldsiddliekfeklsssekndnlsnlierqiikyrslFEWHDGALVTAmkqgdFFLLDEISLADDSV 1325
Cdd:COG0714 86 --------------------------------------------------FEFRPGPLFAN-----VLLADEINRAPPKT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1326 ----LErlnsVLElSRTLTLvehsnAAVSLTAKDGFAFFATMNPGGDYGKKELSPALRNRFT-EIWVP-PmvDTEDILKI 1399
Cdd:COG0714 111 qsalLE----AME-ERQVTI-----PGGTYKLPEPFLVIATQNPIEQEGTYPLPEAQLDRFLlKLYIGyP--DAEEEREI 178
|
250
....*....|..
gi 1685823625 1400 VEGKLHNNKIEL 1411
Cdd:COG0714 179 LRRHTGRHLAEV 190
|
|
| COG5137 |
COG5137 |
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics] ... |
4004-4126 |
3.46e-05 |
|
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics];
Pssm-ID: 227466 [Multi-domain] Cd Length: 279 Bit Score: 49.22 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4004 WDEPNEEDLLETEQKSneqsaannesdlVSKEDDNKALEDKDRQEKEDEEEMSDDVGIDDEIQPDIQENNSQPPPENEDH 4083
Cdd:COG5137 158 WDNDEDNDEAPPAQPD------------VDNEEEERLEESDGREEEEDEEVGSDSYGEGNRELNEEEEEEAEGSDDGEDV 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1685823625 4084 LD----LPEDLKLDEKEGD-----VSKDSDLEDMDMEAADENKEEADAEKDE 4126
Cdd:COG5137 226 VDyegeRIDKKQGEEEEMEeevinLFEIEWEEESPSEEVPRNNEESPAKKQK 277
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
4015-4275 |
3.60e-05 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 50.56 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4015 TEQKSNEQSAANnesdlvSKEDDNKALEDKDRQEKEDEEEMSDDVGIDDEIQPDIQENNSQPPPENE--DHLDLPEDLKL 4092
Cdd:PTZ00341 309 NELKSLEHRAAK------AAEAEMKKRAEKPKKKKSKRRGWLCCGGGDIETVEPQQEEPVQDVGEHQinEYGDILPSLKA 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4093 DEKEG-----DVSKDSDLEDMDMEAADENKEEA--DAEKDEPMqDFEDPLEENNTldEDIQQDDFSDLAEDDEKMNEDGF 4165
Cdd:PTZ00341 383 SINNSainyyDAVKDGKYLDDDSSDALYTDEDLlfDLEKQKYM-DMLDGSEDESV--EDNEEEHSGDANEEELSVDEHVE 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4166 EENVQENEESTEDGvKSDEELEQGEVPEDQAIDNHPKMDAKSTFASAEADEENTDKGIVGENEELGEEDGAAESGVRGNG 4245
Cdd:PTZ00341 460 EHNADDSGEQQSDD-ESGEHQSVNEIVEEQSVNEHVEEPTVADIVEQETVDEHVEEPAVDENEEQQTADEHVEEPTIAEE 538
|
250 260 270
....*....|....*....|....*....|
gi 1685823625 4246 TADGEFSSAEqvQKGEDTSTPKEAMSEADR 4275
Cdd:PTZ00341 539 HVEEEISTAE--EHIEEPASDVQQDSEAAP 566
|
|
| COG5644 |
COG5644 |
U3 small nucleolar RNA-associated protein 14 [Function unknown]; |
3934-4410 |
5.04e-05 |
|
U3 small nucleolar RNA-associated protein 14 [Function unknown];
Pssm-ID: 227931 [Multi-domain] Cd Length: 869 Bit Score: 49.70 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3934 EELANEEDTANQSDLDESEARelesdmNGVT--KDSVVSENENSDSEEENQDLDEEVNDiPEDLSNSLNEKLWDEPNEED 4011
Cdd:COG5644 25 EEESAGFDSEELEDNDEQGYS------FGVNseDDEEIDSDEAFDEEDEKRFADWSFNA-SKSGKSNKDHKNLNNTKEIS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4012 LLETEQKSNEQSaannesdlvskeddnkaLEDKDRQEKEDEEEMSDDVGIDDEIQPDIQENNsqpppeNEDHldlpedlk 4091
Cdd:COG5644 98 LNDSDDSVNSDK-----------------LENEGSVSSIDENELVDLDTLLDNDQPEKNESG------NNDH-------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4092 ldekegDVSKDSDLEDMDMEAADENKEEADAEKDEPMQDfEDPLEENNTLDEDIQQDDFSDLAEDDEKM-------NEDG 4164
Cdd:COG5644 147 ------ATDKENLLESDASSSNDSESEESDSESEIESSD-SDHDDENSDSKLDNLRNYIVSLKKDEADAesvlssdDNDS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4165 FEENV----QENEESTEDG---------VKSDEELEQG-----------EVPEDQAIDNhpKMDAKSTFASAEADEENTd 4220
Cdd:COG5644 220 IEEIKydphETNKESGSSEtiditdlldSIPMEQLKVSlkplvsessklDAPLAKSIQD--RLERQAAYEQTKNDLEKW- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4221 KGIVGENEELGE----EDGAAESGVRGNGTA------------------DGEFSSAEQVQKGEDTSTPK---EAMSEADR 4275
Cdd:COG5644 297 KPIVADNRKSDQlifpMNETARPVPSNNGLAssfeprteserkmhqallDAGLENESALKKQEELALNKlsvEEVAERTR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4276 QYQSLGDHL-REWQQANRIHEWEDLTE---SQSQAFDDSEFMHVKEDEEedlqalgNAEKDQIKSIDRDESANQNPDSMN 4351
Cdd:COG5644 377 QLRFMRELMfREERKAKRVAKIKSKTYrkiRKNRKEKEMALIPKSEDLE-------NEKSEEARALERMTQRHKNTSSWT 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1685823625 4352 STNIA----EDEADEVGDKQLQDGQDISDiKQTGEDTLPTEFGSInQSEKVFELSEDEDIEDE 4410
Cdd:COG5644 450 RKMLErashGEGTREAVNEQIRKGDELMQ-RIHGKEIMDGEDVSE-FSDSDYDTNEQVSTAFE 510
|
|
| PRK08581 |
PRK08581 |
amidase domain-containing protein; |
3899-4182 |
6.10e-05 |
|
amidase domain-containing protein;
Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 49.40 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3899 QEGKSNSGElESGTGLGSGVGAEDITNTLNEDDDLEELANEEDTANQSD-LDESEARELESD--MNGVTKDSVVSENENS 3975
Cdd:PRK08581 42 DSKKSNDDE-TSKDTSSKDTDKADNNNTSNQDNNDKKFSTIDSSTSDSNnIIDFIYKNLPQTniNQLLTKNKYDDNYSLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3976 DSEEENQDLDEEVNDIPEDLSNSlneklWDEPNEEDLLETEQKSNeQSAANNESDLVSKEDDNKALEDKDRQ--EKEDEE 4053
Cdd:PRK08581 121 TLIQNLFNLNSDISDYEQPRNSE-----KSTNDSNKNSDSSIKND-TDTQSSKQDKADNQKAPSSNNTKPSTsnKQPNSP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4054 EMSDDVGIDDEIQPDIQENNSQPPPENEDHLDLPEDLKLDE---------------KEGDVSKDSDLEDMDMEAADENKE 4118
Cdd:PRK08581 195 KPTQPNQSNSQPASDDTANQKSSSKDNQSMSDSALDSILDQysedakktqkdyasqSKKDKTETSNTKNPQLPTQDELKH 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1685823625 4119 EADaekdePMQDFEDPLEENNTldediqqDDFSDLAEDDE-KMNEDGFEENVQENeESTEDGVKS 4182
Cdd:PRK08581 275 KSK-----PAQSFENDVNQSNT-------RSTSLFETGPSlSNNDDSGSFNVVDS-KDTRQFIKS 326
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3921-4411 |
8.43e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3921 EDITNTLNEDDDLEELAneedtanqSDLDEsEARELESDMNGVTKDSVVSENENSDSEEENQDLDEEVNDIPEDLSNS-- 3998
Cdd:PRK02224 265 ETIAETEREREELAEEV--------RDLRE-RLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECrv 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3999 ----LNEKLWDEPNEEDLLETEQKSNEQSAANNESDLvskEDDNKALEdkDRQEKEDEeemsddvgIDDEIQpDIQENNS 4074
Cdd:PRK02224 336 aaqaHNEEAESLREDADDLEERAEELREEAAELESEL---EEAREAVE--DRREEIEE--------LEEEIE-ELRERFG 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4075 QPPPENEDHLDLPEDLkLDEKEGDVSKDSDLEdMDMEAADENKEEADAEKDE---PM--QDFEDPlEENNTLDEDIQQdd 4149
Cdd:PRK02224 402 DAPVDLGNAEDFLEEL-REERDELREREAELE-ATLRTARERVEEAEALLEAgkcPEcgQPVEGS-PHVETIEEDRER-- 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4150 FSDLAEDDEKMNEDgfEENVQENEESTEDGVKSDEELEQgevPEDQAIDNHPKMDAKStfASAEADEENTdkgivgenEE 4229
Cdd:PRK02224 477 VEELEAELEDLEEE--VEEVEERLERAEDLVEAEDRIER---LEERREDLEELIAERR--ETIEEKRERA--------EE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4230 LGEEDGAAEsgvrgngtadgefssAEQVQKGEDTStpkEAMSEADRQYQSLGDHLREWQQ-ANRIHEWEDLTESQSQAFD 4308
Cdd:PRK02224 542 LRERAAELE---------------AEAEEKREAAA---EAEEEAEEAREEVAELNSKLAElKERIESLERIRTLLAAIAD 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4309 DSEFMHVKEDEEEDLQALGNAEKDQIKsiDRDESANQNPDSMNSTNIAEDEAD-EVGDKQLQDGQDISDIKQTGEDTLPT 4387
Cdd:PRK02224 604 AEDEIERLREKREALAELNDERRERLA--EKRERKRELEAEFDEARIEEAREDkERAEEYLEQVEEKLDELREERDDLQA 681
|
490 500
....*....|....*....|....
gi 1685823625 4388 EFGSINQsekvfELSEDEDIEDEL 4411
Cdd:PRK02224 682 EIGAVEN-----ELEELEELRERR 700
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1560-1689 |
8.47e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.83 E-value: 8.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1560 KPILLEGSPGVGKTSLITALARE---TGHQLVRINLSD----QTDLMDLFGSDVPVEGGEGGQFAwRDAPFLAAMRNGHW 1632
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDileeVLDQLLLIIVGGKKASGSGELRL-RLALALARKLKPDV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1685823625 1633 VLLDELNLASQSVLEGLnacldhRNEAYIPELDKVFKAHPNFRVFAAQNPQHQGGGR 1689
Cdd:smart00382 82 LILDEITSLLDAEQEAL------LLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPA 132
|
|
| PRK05901 |
PRK05901 |
RNA polymerase sigma factor; Provisional |
4001-4148 |
1.15e-04 |
|
RNA polymerase sigma factor; Provisional
Pssm-ID: 235640 [Multi-domain] Cd Length: 509 Bit Score: 48.45 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4001 EKLWDEPNEEDLLETEQKSNEQSAANNESdlvSKEDDNKALEDKDRQEKEDEEEMSDDVGIDdeiqPDIQENNSQPPPEN 4080
Cdd:PRK05901 63 VKDTDDATESDIPKKKTKTAAKAAAAKAP---AKKKLKDELDSSKKAEKKNALDKDDDLNYV----KDIDVLNQADDDDD 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1685823625 4081 EDHLDLPEDLKLDEKEGDVSKDSDLEDMDMEAADENKEEADAEKDEPMQDFEDPLEENNTLDEDIQQD 4148
Cdd:PRK05901 136 DDDDDDLDDDDIDDDDDDEDDDEDDDDDDVDDEDEEKKEAKELEKLSDDDDFVWDEDDSEALRQARKD 203
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
4006-4448 |
1.32e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.11 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4006 EPNEEDLLETEQKSNEQSAANNESDLVSKED-DNKALEDKDRQEKEDEEEMSDDVGIDDEIQPDIQENNSQPPPENEDHL 4084
Cdd:COG3064 22 EAEKRAAAEAEQKAKEEAEEERLAELEAKRQaEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4085 DLPEDLKLDEKEGDVSKDSDLEDMDMEAADENKEEADAEKDE-PMQDFEDPLEENNTLDEDIQQDDFSDLAEDDEKMNED 4163
Cdd:COG3064 102 KEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAaEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4164 GFEENVQENEESTEDGVKSDEELEQGEVPEDQAIDNHPKMDAKSTFASAEADEENTDKGIVGENEELGEEDGAAESGVRG 4243
Cdd:COG3064 182 LVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4244 NGTADGEFSSAEQVQKGEDTSTPKEAMSEADRQYQSLGDHLREWQQANRIHEWEDLTESQSQAFDDSEFMHVKEDEEEDL 4323
Cdd:COG3064 262 AALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAAL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4324 QALGNAEKDQIKSIDRDESANQNPDSMNSTNIAEDEADEVGDKQLQDGQDISDIKQTGEDTLPTEFGSINQSEkvfELSE 4403
Cdd:COG3064 342 SLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEA---ASAV 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1685823625 4404 DEDIEDELPDYNVKITNLPAAMPIDEARDLWNKHEDSTKQLSIEL 4448
Cdd:COG3064 419 ELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALL 463
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
1562-1638 |
1.45e-04 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 47.60 E-value: 1.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1685823625 1562 ILLEGSPGVGKTSLITALARETGHQLVRINLSdqtdlmDLFGSDVpvegGEGGQfAWRDApFLAAMRNGHWVLL-DEL 1638
Cdd:COG0464 194 LLLYGPPGTGKTLLARALAGELGLPLIEVDLS------DLVSKYV----GETEK-NLREV-FDKARGLAPCVLFiDEA 259
|
|
| COG5593 |
COG5593 |
Nucleic-acid-binding protein possibly involved in ribosomal biogenesis [Translation, ribosomal ... |
4089-4213 |
1.56e-04 |
|
Nucleic-acid-binding protein possibly involved in ribosomal biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227880 [Multi-domain] Cd Length: 821 Bit Score: 48.11 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4089 DLKLDEKEGDVskdsDLEDMDM-EAADENKEEADAEKDEPMQDFEDPLEEnntldediQQDDFSDLA--EDDEKMNEDGF 4165
Cdd:COG5593 700 DVEDDSDDSEL----DFAEDDFsDSTSDDEPKLDAIDDEDAKSEGSQESD--------QEEGLDEIFysFDGEQDNSDSF 767
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4166 EENVQENEESTEDgvksDEELEQGEVPEDQAIDNHPKMDAKS--TFASAE 4213
Cdd:COG5593 768 AESSEEDESSEEE----KEEEENKEVSAKRAKKKQRKNMLKSlpVFASAD 813
|
|
| Taf7 |
COG5414 |
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation ... |
4017-4189 |
1.62e-04 |
|
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation complex [Transcription];
Pssm-ID: 227701 Cd Length: 392 Bit Score: 47.39 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4017 QKSNEQSAANNESDLVSKEDDNkaLEDKDRQEKEDEEEMSDDVGIDDEIQPDIQENNSQPPPENEDHLDLPEDLKLDEKE 4096
Cdd:COG5414 190 ARRFRKKSSKIEIEEVEKKVDD--LLEKDMKAESVSVVLKDEKELARQERVSSWENFKEEPGEPLSRPALKKEKQGAEEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4097 GDVSKDSDleDMDMEAADENKEEADAEKDEPMQDFEDPLEENNTLDEDIQQDdfsdlaEDDEKMNEDgfEENvQENEEST 4176
Cdd:COG5414 268 GEEGMSEE--DLDVGAAEIENKEVSEGDKEQQQEEVENAEAHKEEVQSDRPD------EIGEEKEED--DEN-EENERHT 336
|
170
....*....|...
gi 1685823625 4177 EDGVKSDEELEQG 4189
Cdd:COG5414 337 ELLADELNELEKG 349
|
|
| CobT2 |
COG4547 |
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ... |
4105-4217 |
1.62e-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: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4105 LEDMDMEAADENKEEaDAEKDEPMQDFEDPLEENNTLDEDIQQDDFSDlAEDDEKMNEDGFEENVQENEESTEDGvKSDE 4184
Cdd:COG4547 202 LRDLDLAEELGEDED-EEDEDDEDDSGEQEEDEEDGEDEDEESDEGAE-AEDAEASGDDAEEGESEAAEAESDEM-AEEA 278
|
90 100 110
....*....|....*....|....*....|....*..
gi 1685823625 4185 ELEQGEVPEDQAIDNHPKMDAKSTFA----SAEADEE 4217
Cdd:COG4547 279 EGEDSEEPGEPWRPNAPPPDDPADPDykvfTTAFDEV 315
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
896-1032 |
2.40e-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: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 896 PILIQGPTSSGKTSMIEYVAK---KTGHKFVRIN--NHEHTDLQEYIGTYVTDDNGSLSFREGV-----LVEALRNGyWI 965
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARelgPPGGGVIYIDgeDILEEVLDQLLLIIVGGKKASGSGELRLrlalaLARKLKPD-VL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1685823625 966 VLDELNLAPTDVLEALNRLLDDNRELFIpetqvLVKPHPEFMLFATQNPPGVyaGRKHLSRAFRNRF 1032
Cdd:smart00382 83 ILDEITSLLDAEQEALLLLLEELRLLLL-----LKSEKNLTVILTTNDEKDL--GPALLRRRFDRRI 142
|
|
| vWFA_subfamily_ECM |
cd01450 |
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
4510-4666 |
3.47e-04 |
|
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: 238727 [Multi-domain] Cd Length: 161 Bit Score: 44.20 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4510 IDDSKSMSESGSTvlalETLALVTKALSLLEVG----QIAVMKFGEQPELLHPFDKQFSSE---SGVQMFSHFTFEQSNT 4582
Cdd:cd01450 7 LDGSESVGPENFE----KVKDFIEKLVEKLDIGpdktRVGLVQYSDDVRVEFSLNDYKSKDdllKAVKNLKYLGGGGTNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4583 NvLALADAsmkcfnYANTASHHRSNSDIRQLEIIISDGICEDHDSIRKLLRRAQEEKVMIVFVILDNVNTQKKSSILDIK 4662
Cdd:cd01450 83 G-KALQYA------LEQLFSESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCP 155
|
....
gi 1685823625 4663 KVYY 4666
Cdd:cd01450 156 SERH 159
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
155-257 |
3.50e-04 |
|
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400187 [Multi-domain] Cd Length: 168 Bit Score: 44.49 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 155 ILLAGPEGIGKKFLITQIAAKLG---QQIIRIHLSDSTDPK---MLIGTytspKPG--EFEwQPGVLTQAVITGKW--IL 224
Cdd:pfam07724 6 FLFLGPTGVGKTELAKALAELLFgdeRALIRIDMSEYMEEHsvsRLIGA----PPGyvGYE-EGGQLTEAVRRKPYsiVL 80
|
90 100 110
....*....|....*....|....*....|...
gi 1685823625 225 FTNIEHAPSEVLSVLLPLLEKRQLvIPSRGETI 257
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTL-TDKQGRTV 112
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1381-1641 |
5.01e-04 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 46.30 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1381 RFTEIWVPPMVDTEDILKIVEGKLHNNKIELARPLVEYAKWHANEYLYTDVISIRDVLSAVEFINACEILDLNLVLFNAV 1460
Cdd:COG1401 45 RLAERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1461 SMVFIDALGSFTTFSLSNNLASLHAERQRCFAKLNELAGSNIMASKSADISIKFSDSSFFIGDFGIPLGDsvESDSTYSL 1540
Cdd:COG1401 125 RSDALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLES--EDDYLKDL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 1541 HTDTTLMNASKVLRALQVLKPILLEGSPGVGKTSLITALARETG------HQLV--RINLSDQTDLMDLfgsdVPVEGGe 1612
Cdd:COG1401 203 LREKFEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGgedngrIEFVqfHPSWSYEDFLLGY----RPSLDE- 277
|
250 260 270
....*....|....*....|....*....|....*.
gi 1685823625 1613 gGQFAWRDAPFL----AAMRNG---HWVLLDELNLA 1641
Cdd:COG1401 278 -GKYEPTPGIFLrfclKAEKNPdkpYVLIIDEINRA 312
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1178-1238 |
8.68e-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: 42.90 E-value: 8.68e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1685823625 1178 LVWRCLLAKEPVLLVGDTGCGKTTVCQILAECLHK---ELHIINAHQDTENGDIIGAQRPVRNR 1238
Cdd:cd00009 11 REALELPPPKNLLLYGPPGTGKTTLARAIANELFRpgaPFLYLNASDLLEGLVVAELFGHFLVR 74
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
2023-2083 |
9.33e-04 |
|
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of dynein heavy chain. The chain also contains ATPase activity and microtubule binding ability and acts as a motor for the movement of organelles and vesicles along microtubules. Dynein is also involved in cilia and flagella movement. The dynein subunit consists of at least two heavy chains and a number of intermediate and light chains. The 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This C-terminal domain carries the D6 region of the dynein motor where the P-loop has been lost in evolution but the general structure of a potential ATP binding site appears to be retained.
Pssm-ID: 460782 Cd Length: 115 Bit Score: 42.05 E-value: 9.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1685823625 2023 KAVEEGHWFVLDNANLcSPAVLDRLnsllehkgvlivnEKTTEDGHPKTikPHPNFRLFLT 2083
Cdd:pfam03028 52 EAAKEGGWVLLQNCHL-ALSWMPEL-------------EKILEELPEET--LHPDFRLWLT 96
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
3922-4196 |
1.31e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 45.12 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3922 DITNTlnEDDDLEELANEEDTanQSDLDESEARELESDMNGVTKDSVVSENENSDSEEENQDLDEE--VNDIPEDLSNSL 3999
Cdd:COG5192 452 AINNE--DESDNEEVAFDSDS--QFDESEGNLRWKEGLASKLAYSQSGKRGRNIQKIFYDESLSPEecIEEYKGESAKSS 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4000 NEKLWDEPNEEDLLETEQKSNEQSAANNESDLVSKEDDNKALEDKDRQEKED--EEEMSDDVGIDDEIQPDIQENNSQpp 4077
Cdd:COG5192 528 ESDLVVQDEPEDFFDVSKVANESISSNHEKLMESEFEELKKKWSSLAQLKSRfqKDATLDSIEGEEELIQDDEKGNFE-- 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4078 pENEDHLDLPEDlKLDEKEGDVSKDSDLEDMDMEAADENKEEADAEKDEPMQDFEdpLEENntldediqqddfsdlaEDD 4157
Cdd:COG5192 606 -DLEDEENSSDN-EMEESRGSSVTAENEESADEVDYETEREENARKKEELRGNFE--LEER----------------GDP 665
|
250 260 270
....*....|....*....|....*....|....*....
gi 1685823625 4158 EKMNEDGFEENVQENEESTEDGVKSDEELeqgeVPEDQA 4196
Cdd:COG5192 666 EKKDVDWYTEEKRKIEEQLKINRSEFETM----VPESRV 700
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
1562-1638 |
1.41e-03 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 44.23 E-value: 1.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1685823625 1562 ILLEGSPGVGKTSLITALARETGHQLVRINLSdqtDLMDLFgsdVpvegGEGGQfAWRDApFLAAMRNGHWVL-LDEL 1638
Cdd:COG1222 115 VLLYGPPGTGKTLLAKAVAGELGAPFIRVRGS---ELVSKY---I----GEGAR-NVREV-FELAREKAPSIIfIDEI 180
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
1551-1597 |
2.40e-03 |
|
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: 42.16 E-value: 2.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1685823625 1551 KVLRALQVLK-------PIL-LEGSPGVGKTSLITALARETGHQLVRINLSDQTD 1597
Cdd:cd19500 21 RILEYLAVRKlkgsmkgPILcLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRD 75
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
1552-1591 |
3.70e-03 |
|
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410911 [Multi-domain] Cd Length: 165 Bit Score: 41.51 E-value: 3.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1685823625 1552 VLRALQVLKP--ILLEGSPGVGKTSLITALARETGHQLVRIN 1591
Cdd:cd19503 25 LFRALGLKPPrgVLLHGPPGTGKTLLARAVANEAGANFLSIS 66
|
|
| DNA_pol_phi |
pfam04931 |
DNA polymerase phi; This family includes the fifth essential DNA polymerase in yeast EC:2.7.7. ... |
4011-4126 |
4.29e-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: 43.38 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4011 DLLETEQKSNEQSaannesDLVSKEDDNkalEDKDRQEKEDEEEMSDDVGIDDEiqpdiqENNSQpppENEDhldlpedl 4090
Cdd:pfam04931 621 DVLDARENPEGQQ------ELFEDEDED---EEDDDEEEDDDDEDDEDSEEDDD------EDDDD---EDEE-------- 674
|
90 100 110
....*....|....*....|....*....|....*.
gi 1685823625 4091 klDEKEGDVSKDSDLEDMDMEAADENKEEADAEKDE 4126
Cdd:pfam04931 675 --DDDDEDVDEIDELRAKLAEALGEHGDDADDDDSD 708
|
|
| RecA-like_BCS1 |
cd19510 |
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ... |
1563-1601 |
5.05e-03 |
|
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. 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: 410918 [Multi-domain] Cd Length: 153 Bit Score: 40.80 E-value: 5.05e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1685823625 1563 LLEGSPGVGKTSLITALARETGHQLVRINLSDQTDLMDL 1601
Cdd:cd19510 27 LLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVLTDDR 65
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
897-1035 |
5.12e-03 |
|
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400187 [Multi-domain] Cd Length: 168 Bit Score: 41.03 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 897 ILIQGPTSSGKTSMIEYVAK---KTGHKFVRINNHE----HTdLQEYIGT---YVTDDNGslsfreGVLVEALR-NGYWI 965
Cdd:pfam07724 6 FLFLGPTGVGKTELAKALAEllfGDERALIRIDMSEymeeHS-VSRLIGAppgYVGYEEG------GQLTEAVRrKPYSI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 966 VL-DELNLAPTDVLEALNRLLDDNR-------------ELFI---------PETQVLVKPHPEFMLFATQNPPGVyagRK 1022
Cdd:pfam07724 79 VLiDEIEKAHPGVQNDLLQILEGGTltdkqgrtvdfknTLFImtgnfgsekISDASRLGDSPDYELLKEEVMDLL---KK 155
|
170
....*....|...
gi 1685823625 1023 HLSRAFRNRFLEI 1035
Cdd:pfam07724 156 GFIPEFLGRLPII 168
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
3983-4206 |
6.15e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 43.19 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3983 DLDEEVNDIPEDLSNSLNEKLWDEPNEEDLLETEQKSNEQSAANNESDLVSKEDDNKALEDKDRQEKEDEEEMS----DD 4058
Cdd:COG5192 424 REDELSFDDSDVSTSDENEDVDFTGKKGAINNEDESDNEEVAFDSDSQFDESEGNLRWKEGLASKLAYSQSGKRgrniQK 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4059 VGIDDEIQPD--IQENNSQPPPENEDHL---DLPEDLKLDEKEGDVSKDSDLEDMDMEAADENKE--------------- 4118
Cdd:COG5192 504 IFYDESLSPEecIEEYKGESAKSSESDLvvqDEPEDFFDVSKVANESISSNHEKLMESEFEELKKkwsslaqlksrfqkd 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4119 ---EADAEKDEPMQDFED------PLEENNTLDEDIQQDDFSDLAEDDEKMNEDGFEENVQENEESTEDgVKSDEELEQG 4189
Cdd:COG5192 584 atlDSIEGEEELIQDDEKgnfedlEDEENSSDNEMEESRGSSVTAENEESADEVDYETEREENARKKEE-LRGNFELEER 662
|
250
....*....|....*..
gi 1685823625 4190 EVPEDQAIDNHPKMDAK 4206
Cdd:COG5192 663 GDPEKKDVDWYTEEKRK 679
|
|
| MCM2_N |
pfam12619 |
Mini-chromosome maintenance protein 2; This domain family is found in eukaryotes, and is ... |
4050-4163 |
6.92e-03 |
|
Mini-chromosome maintenance protein 2; This domain family is found in eukaryotes, and is typically between 138 and 153 amino acids in length. The family is found in association with pfam00493. Mini-chromosome maintenance (MCM) proteins are essential for DNA replication. These proteins use ATPase activity to perform this function.
Pssm-ID: 403724 Cd Length: 148 Bit Score: 40.09 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4050 EDEEEMSDDVGIDDEiqpdiqennsQPPPENEDHLDL-PEDLKLDEKE---------GDVSKDSDLEDMDME---AADE- 4115
Cdd:pfam12619 1 EDEEAEIDENDIDDL----------DPDEEEEDGEDLfGDNMEDDYRQnpeldrydlDDIDDEGDYEEMDAAerrRAEAq 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1685823625 4116 ----NKEEADAEKDEP---MQDFEDPLEENNTLDEDIQQ---------DDFSDLAEDDEKMNED 4163
Cdd:pfam12619 71 lnrrDRELGAARRRRPaafLQDDDDEDDLDGDYGLPIQRrrrrrhydeDQDEDMDEDIDPFEEE 134
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
3898-4197 |
6.92e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 42.68 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3898 PQEGKSNSGElESGTGLGSGVGAEDITNTLNEDDDLEELANEEDtanqsdlDESEARELESDMNGvtkDSVVSENENSDS 3977
Cdd:TIGR00927 652 PTEAEGENGE-ESGGEAEQEGETETKGENESEGEIPAERKGEQE-------GEGEIEAKEADHKG---ETEAEEVEHEGE 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 3978 EEENQDLDEEVNDIPEDlsnslneklWDEPNEEDLLETEQKSNEQSAANNESDLVSKEDDNKALEDKDRQEKEDEE--EM 4055
Cdd:TIGR00927 721 TEAEGTEDEGEIETGEE---------GEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEdgEM 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4056 SDDVGIDDEIQPDIQENNSQPPPENEDHLDLPEDLKLDEKEGdvSKDSDLEDMDMEAADEnkEEADAEKDEPMQDFEDPL 4135
Cdd:TIGR00927 792 KGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETG--EQELNAENQGEAKQDE--KGVDGGGGSDGGDSEEEE 867
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1685823625 4136 EEnntlDEDiqqddfsdlaEDDEKMNEDGFEENVQENEESTedgvksdeELEQGEVPEDQAI 4197
Cdd:TIGR00927 868 EE----EEE----------EEEEEEEEEEEEEEEEENEEPL--------SLEWPETRQKQAI 907
|
|
| CobT2 |
COG4547 |
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ... |
4021-4155 |
7.47e-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: 42.47 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1685823625 4021 EQSAANNESDLVSKEDDNKALEDKDRQ---------EKEDEEEMSDDVGIDDEIQPDIQENNSQPPPENEDHLDLPEDlk 4091
Cdd:COG4547 174 EEKAGADLDRLAELLDDQAAFARAVRDllrdldlaeELGEDEDEEDEDDEDDSGEQEEDEEDGEDEDEESDEGAEAED-- 251
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90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1685823625 4092 lDEKEGDVSKDSDLEDMDMEAADENKEEADAEKDEPMQDFEDPLEENNT------------LDEDIQQDDFSDLAE 4155
Cdd:COG4547 252 -AEASGDDAEEGESEAAEAESDEMAEEAEGEDSEEPGEPWRPNAPPPDDpadpdykvfttaFDEVVAAEDLCDPEE 326
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| RecA-like_ATAD1 |
cd19520 |
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ... |
1554-1597 |
8.51e-03 |
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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: 40.49 E-value: 8.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1685823625 1554 RALQVLKPILLEGSPGVGKTSLITALARETGHQLVRINLSDQTD 1597
Cdd:cd19520 30 RLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTD 73
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