|
Name |
Accession |
Description |
Interval |
E-value |
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
392-587 |
3.99e-40 |
|
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.
Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 144.41 E-value: 3.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 392 ALAGATGSGKSQLFNSLAGVAISETGVRRPTTAAPIACSWSDGaatlidrlgipgrlrrrpmhspdneaqLRGLVLVDLP 471
Cdd:cd11383 1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQAYVWQTG---------------------------GDGLVLLDLP 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 472 DHDSAAVQHR---EQVDRILRLVDAVIWVVDPEKYADAMLHERYLRPMAGHAEVMFIVLNQVDrlpgdaadqvlddlrrl 548
Cdd:cd11383 54 GVGERGRRDReyeELYRRLLPEADLVLWLLDADDRALAADHDFYLLPLAGHDAPLLFVLNQVD----------------- 116
|
170 180 190
....*....|....*....|....*....|....*....
gi 2756311615 549 ldedgialgehgepgaTVLALSALTGEGVGELREVLGQF 587
Cdd:cd11383 117 ----------------PVLAVSARTGWGLDELAEALITA 139
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
369-584 |
4.44e-30 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 121.41 E-value: 4.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 369 AEAGRVLDEAAARRKLSGRHTVVALAGATGSGKSQLFNSLAGVAISETGVRRPTTAAPIACSWSdgaatlidrlgipgrl 448
Cdd:COG3596 20 QVLRELLAEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRLE---------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 449 rrrpmhspdnEAQLRGLVLVDLPDHDSAAVQHRE--QVDRILRLVDAVIWVVDPEKYADAMLHERYLRPMAGHA-EVMFI 525
Cdd:COG3596 84 ----------SDGLPGLVLLDTPGLGEVNERDREyrELRELLPEADLILWVVKADDRALATDEEFLQALRAQYPdPPVLV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2756311615 526 VLNQVDRL-PGDAADQVLD--------DLRRLLDEDGIALGEHGEPGATVLALSALTGEGVGELREVL 584
Cdd:COG3596 154 VLTQVDRLePEREWDPPYNwpsppkeqNIRRALEAIAEQLGVPIDRVIPVSAAEDRTGYGLEELVDAL 221
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
45-250 |
2.05e-08 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 57.99 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 45 RAGGLAHARLSLAKEGPGDDGSGPGGRHEGRDDAREDANGGEYEGGGGGREGDGTGVLHARVPDETAEGGPDPGRARPAR 124
Cdd:PRK12678 59 RGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAAR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 125 VRD-------------EDHDSRAATGPRERPARLRGENAARAQGQGTESEHSRDADRGRGRGRGTERDHGRDTDRDRERE 191
Cdd:PRK12678 139 RGAarkageggeqpatEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREER 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2756311615 192 SDGHAEAVEGGDRHAVQDRDCHAVHDRDRGGAQDRDRHGEAGGNGDR--DRSARGRGAEQG 250
Cdd:PRK12678 219 GRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRfrDRDRRGRRGGDG 279
|
|
| Dynamin_N |
pfam00350 |
Dynamin family; |
391-530 |
2.31e-08 |
|
Dynamin family;
Pssm-ID: 459775 [Multi-domain] Cd Length: 168 Bit Score: 54.16 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 391 VALAGATGSGKSQLFNSLAGVAISETGVRrPTTAAPIA---------------CSWSDGAATLID----RLGIPGRLRRR 451
Cdd:pfam00350 1 IAVVGDQSSGKSSVLNALLGRDILPRGPG-PTTRRPTVlrlgespgasegavkVEYKDGEKKFEDfselREEIEKETEKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 452 P--------------MHSPDNEaqlrGLVLVDLPDHDSAAVQHREQVDRILRLVDAVIWVVD---PEKYADAMLHERYLR 514
Cdd:pfam00350 80 AgtgkgissepivleILSPLVP----GLTLVDTPGLDSVAVGDQELTKEYIKPADIILAVTPanvDLSTSEALFLAREVD 155
|
170
....*....|....*.
gi 2756311615 515 PmagHAEVMFIVLNQV 530
Cdd:pfam00350 156 P---NGKRTIGVLTKA 168
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
127-309 |
1.64e-07 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 55.30 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 127 DEDHDSRAATGPRERPARLRGENAARAQGQGTESEHSRDADRGRGRGRGTERDHGRDTDRDRERESDGHAEAVEGGDRHA 206
Cdd:NF033609 733 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 207 VQDRDCHAVHDRDRGGAQDRDRHGEAGGNGDRDRSARGRGAEQGVSVPRPHPHPARS----PKPRPAPETTSPRTSTATG 282
Cdd:NF033609 813 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNnnvvPPNSPKNGTNASNKNEAKD 892
|
170 180
....*....|....*....|....*..
gi 2756311615 283 AATPTPTSATDGEAGASQeTWddGLIA 309
Cdd:NF033609 893 SKEPLPDTGSEDEANTSL-IW--GLLA 916
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
249-784 |
8.33e-07 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 52.95 E-value: 8.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 249 QGVSVPRPHPHPARspKPRPAPETTSPRTSTATGAATPTPTSATDGEAGASQETWDDGLIARRVTGSASAERSSSGEQPH 328
Cdd:COG3321 843 AGVPVDWSALYPGR--GRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALA 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 329 RVPGSQVPVPLAYDGPLRSRLNALRELVGLSRTRLDSHTLAEAGRVLDEAAARRKLSGRHTVVALAGATGSGKSQLFNSL 408
Cdd:COG3321 921 LAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAA 1000
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 409 AGVAISETGVRRPTTAAPIAcswsdgAATLIDRLGIPGRLRRRPMHSPDNEAQLRGLVLVDLPDHDSAAVQHREQVDRIL 488
Cdd:COG3321 1001 ALALLAAAALLLAAAAAAAA------LLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAAL 1074
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 489 RLVDAVIWVVDPEKYADAMLHERYLRPMAGHAEVmfiVLNQVDRLPGDAADQVLDDLRRLLDEDGIALGEHGEPGATVLA 568
Cdd:COG3321 1075 AELALAAAALALAAALAAAALALALAALAAALLL---LALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALA 1151
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 569 LSALTGEGVGELREVLGQFVAERGAAARRVAADLDAAAAGLRPVYATGRRAGLTEEAREEFAARLADAVGATAAGEAAER 648
Cdd:COG3321 1152 LAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAA 1231
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 649 AWLRNANRACGTPWLRLWRWYQGRGEATTGRHAVRGQADEEATARQRVEQAVRTVADRASAGLPAPWAQAVREAAVRGSQ 728
Cdd:COG3321 1232 ALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAA 1311
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2756311615 729 GLSEALDALSARAGLPPGRPPRPGWWPVAVLVQAAMTLLQIVGGGWLAGQIAGLMA 784
Cdd:COG3321 1312 AAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAA 1367
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
391-584 |
1.74e-05 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 47.35 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 391 VALAGATGSGKSQLFNSLAG--VAI-SetgvRRP-TTAAPIacswsdgaatlidrLGIpgrlrrrpMHspDNEAQLrglV 466
Cdd:PRK00089 8 VAIVGRPNVGKSTLLNALVGqkISIvS----PKPqTTRHRI--------------RGI--------VT--EDDAQI---I 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 467 LVDLPD-HDSAAVQHR---EQVDRILRLVDAVIWVVDPEKYADAmlHERY-LRPMAGHAEVMFIVLNQVDRL-PGDAADQ 540
Cdd:PRK00089 57 FVDTPGiHKPKRALNRamnKAAWSSLKDVDLVLFVVDADEKIGP--GDEFiLEKLKKVKTPVILVLNKIDLVkDKEELLP 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2756311615 541 VLDDLRRLLDEDGIalgehgepgatvLALSALTGEGVGELREVL 584
Cdd:PRK00089 135 LLEELSELMDFAEI------------VPISALKGDNVDELLDVI 166
|
|
| SF-CC1 |
TIGR01622 |
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ... |
177-268 |
4.00e-04 |
|
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.
Pssm-ID: 273721 [Multi-domain] Cd Length: 494 Bit Score: 43.75 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 177 ERDHGRDTDRDRERESDGhaeaveggDRHAVQDRDchavHDRDRGGAQDRDRHGEaggnGDRDRSARGRGAEQGvsvPRP 256
Cdd:TIGR01622 8 ERLRDSSSAGDRDRRRDK--------GRERSRDRS----RDRERSRSRRRDRHRD----RDYYRGRERRSRSRR---PNR 68
|
90
....*....|..
gi 2756311615 257 HPHPARSPKPRP 268
Cdd:TIGR01622 69 RYRPREKRRRRG 80
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
392-587 |
3.99e-40 |
|
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.
Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 144.41 E-value: 3.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 392 ALAGATGSGKSQLFNSLAGVAISETGVRRPTTAAPIACSWSDGaatlidrlgipgrlrrrpmhspdneaqLRGLVLVDLP 471
Cdd:cd11383 1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQAYVWQTG---------------------------GDGLVLLDLP 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 472 DHDSAAVQHR---EQVDRILRLVDAVIWVVDPEKYADAMLHERYLRPMAGHAEVMFIVLNQVDrlpgdaadqvlddlrrl 548
Cdd:cd11383 54 GVGERGRRDReyeELYRRLLPEADLVLWLLDADDRALAADHDFYLLPLAGHDAPLLFVLNQVD----------------- 116
|
170 180 190
....*....|....*....|....*....|....*....
gi 2756311615 549 ldedgialgehgepgaTVLALSALTGEGVGELREVLGQF 587
Cdd:cd11383 117 ----------------PVLAVSARTGWGLDELAEALITA 139
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
369-584 |
4.44e-30 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 121.41 E-value: 4.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 369 AEAGRVLDEAAARRKLSGRHTVVALAGATGSGKSQLFNSLAGVAISETGVRRPTTAAPIACSWSdgaatlidrlgipgrl 448
Cdd:COG3596 20 QVLRELLAEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRLE---------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 449 rrrpmhspdnEAQLRGLVLVDLPDHDSAAVQHRE--QVDRILRLVDAVIWVVDPEKYADAMLHERYLRPMAGHA-EVMFI 525
Cdd:COG3596 84 ----------SDGLPGLVLLDTPGLGEVNERDREyrELRELLPEADLILWVVKADDRALATDEEFLQALRAQYPdPPVLV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2756311615 526 VLNQVDRL-PGDAADQVLD--------DLRRLLDEDGIALGEHGEPGATVLALSALTGEGVGELREVL 584
Cdd:COG3596 154 VLTQVDRLePEREWDPPYNwpsppkeqNIRRALEAIAEQLGVPIDRVIPVSAAEDRTGYGLEELVDAL 221
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
392-582 |
7.15e-22 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 93.29 E-value: 7.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 392 ALAGATGSGKSQLFNSLAGVAISETGVRRPTTAAPIACSWSdgaatlidrlgipgrlrrrpmhspdNEAQLRGLVLVDLP 471
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKE-------------------------LDKGKVKLVLVDTP 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 472 DHDSAAVQHREQ-VDRILRLVDAVIWVVDPEKYA-DAMLHERYLRPMAGHAEVMFIVLNQVDRLPGDAADQVLDDLRRLL 549
Cdd:cd00882 56 GLDEFGGLGREElARLLLRGADLILLVVDSTDREsEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAK 135
|
170 180 190
....*....|....*....|....*....|...
gi 2756311615 550 dedgialgehgEPGATVLALSALTGEGVGELRE 582
Cdd:cd00882 136 -----------ILGVPVFEVSAKTGEGVDELFE 157
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
392-582 |
1.74e-14 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 71.89 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 392 ALAGATGSGKSQLFNSLAGVAISETGVRRPTTAAPIacswsdgaatlidrlgipgrlrRRPMHSPDneaqLRGLVLVDLP 471
Cdd:cd00880 1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPV----------------------RKEWELLP----LGPVVLIDTP 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 472 DHDSAAVQHREQVDRILRL---VDAVIWVVD-----PEKYADAMLHERYLRPmaghaevMFIVLNQVDRLPGDAADQVLD 543
Cdd:cd00880 55 GLDEEGGLGRERVEEARQVadrADLVLLVVDsdltpVEEEAKLGLLRERGKP-------VLLVLNKIDLVPESEEEELLR 127
|
170 180 190
....*....|....*....|....*....|....*....
gi 2756311615 544 DLRRLLdedgialgehgEPGATVLALSALTGEGVGELRE 582
Cdd:cd00880 128 ERKLEL-----------LPDLPVIAVSALPGEGIDELRK 155
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
45-250 |
2.05e-08 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 57.99 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 45 RAGGLAHARLSLAKEGPGDDGSGPGGRHEGRDDAREDANGGEYEGGGGGREGDGTGVLHARVPDETAEGGPDPGRARPAR 124
Cdd:PRK12678 59 RGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAAR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 125 VRD-------------EDHDSRAATGPRERPARLRGENAARAQGQGTESEHSRDADRGRGRGRGTERDHGRDTDRDRERE 191
Cdd:PRK12678 139 RGAarkageggeqpatEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREER 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2756311615 192 SDGHAEAVEGGDRHAVQDRDCHAVHDRDRGGAQDRDRHGEAGGNGDR--DRSARGRGAEQG 250
Cdd:PRK12678 219 GRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRfrDRDRRGRRGGDG 279
|
|
| Dynamin_N |
pfam00350 |
Dynamin family; |
391-530 |
2.31e-08 |
|
Dynamin family;
Pssm-ID: 459775 [Multi-domain] Cd Length: 168 Bit Score: 54.16 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 391 VALAGATGSGKSQLFNSLAGVAISETGVRrPTTAAPIA---------------CSWSDGAATLID----RLGIPGRLRRR 451
Cdd:pfam00350 1 IAVVGDQSSGKSSVLNALLGRDILPRGPG-PTTRRPTVlrlgespgasegavkVEYKDGEKKFEDfselREEIEKETEKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 452 P--------------MHSPDNEaqlrGLVLVDLPDHDSAAVQHREQVDRILRLVDAVIWVVD---PEKYADAMLHERYLR 514
Cdd:pfam00350 80 AgtgkgissepivleILSPLVP----GLTLVDTPGLDSVAVGDQELTKEYIKPADIILAVTPanvDLSTSEALFLAREVD 155
|
170
....*....|....*.
gi 2756311615 515 PmagHAEVMFIVLNQV 530
Cdd:pfam00350 156 P---NGKRTIGVLTKA 168
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
391-584 |
6.07e-08 |
|
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.
Pssm-ID: 206726 [Multi-domain] Cd Length: 168 Bit Score: 53.23 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 391 VALAGATGSGKSQLFNSLAG--VAI-SetgvRRP-TTAAPIACSWSDGAATLI--DrlgIPGrlrrrpMHSPDNeaqLRG 464
Cdd:cd04163 6 VAIIGRPNVGKSTLLNALVGqkISIvS----PKPqTTRNRIRGIYTDDDAQIIfvD---TPG------IHKPKK---KLG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 465 LVLVdlpdhdsaavqhrEQVDRILRLVDAVIWVVDPEKYADAmlHERYLRPMAGHAEV-MFIVLNQVDRLPgdaADQVLD 543
Cdd:cd04163 70 ERMV-------------KAAWSALKDVDLVLFVVDASEWIGE--GDEFILELLKKSKTpVILVLNKIDLVK---DKEDLL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2756311615 544 DLRRLLDEDGialgehgePGATVLALSALTGEGVGELREVL 584
Cdd:cd04163 132 PLLEKLKELH--------PFAEIFPISALKGENVDELLEYI 164
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
127-309 |
1.64e-07 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 55.30 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 127 DEDHDSRAATGPRERPARLRGENAARAQGQGTESEHSRDADRGRGRGRGTERDHGRDTDRDRERESDGHAEAVEGGDRHA 206
Cdd:NF033609 733 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 207 VQDRDCHAVHDRDRGGAQDRDRHGEAGGNGDRDRSARGRGAEQGVSVPRPHPHPARS----PKPRPAPETTSPRTSTATG 282
Cdd:NF033609 813 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNnnvvPPNSPKNGTNASNKNEAKD 892
|
170 180
....*....|....*....|....*..
gi 2756311615 283 AATPTPTSATDGEAGASQeTWddGLIA 309
Cdd:NF033609 893 SKEPLPDTGSEDEANTSL-IW--GLLA 916
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
391-584 |
2.48e-07 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 53.07 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 391 VALAGATGSGKSQLFNSLAG--VAI-SetgvRRP-TTAAPIacswsdgaatlidrLGIpgrlrrrpMHSPDneAQlrgLV 466
Cdd:COG1159 6 VAIVGRPNVGKSTLLNALVGqkVSIvS----PKPqTTRHRI--------------RGI--------VTRED--AQ---IV 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 467 LVDLPD-HDSaavQHR------EQVDRILRLVDAVIWVVDPEKYA---DAMLHERyLRPMAGHAevmFIVLNQVDRLPGD 536
Cdd:COG1159 55 FVDTPGiHKP---KRKlgrrmnKAAWSALEDVDVILFVVDATEKIgegDEFILEL-LKKLKTPV---ILVINKIDLVKKE 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2756311615 537 AADQVLDDLRRLLDEDGIalgehgepgatvLALSALTGEGVGELREVL 584
Cdd:COG1159 128 ELLPLLAEYSELLDFAEI------------VPISALKGDNVDELLDEI 163
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
249-784 |
8.33e-07 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 52.95 E-value: 8.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 249 QGVSVPRPHPHPARspKPRPAPETTSPRTSTATGAATPTPTSATDGEAGASQETWDDGLIARRVTGSASAERSSSGEQPH 328
Cdd:COG3321 843 AGVPVDWSALYPGR--GRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALA 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 329 RVPGSQVPVPLAYDGPLRSRLNALRELVGLSRTRLDSHTLAEAGRVLDEAAARRKLSGRHTVVALAGATGSGKSQLFNSL 408
Cdd:COG3321 921 LAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAA 1000
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 409 AGVAISETGVRRPTTAAPIAcswsdgAATLIDRLGIPGRLRRRPMHSPDNEAQLRGLVLVDLPDHDSAAVQHREQVDRIL 488
Cdd:COG3321 1001 ALALLAAAALLLAAAAAAAA------LLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAAL 1074
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 489 RLVDAVIWVVDPEKYADAMLHERYLRPMAGHAEVmfiVLNQVDRLPGDAADQVLDDLRRLLDEDGIALGEHGEPGATVLA 568
Cdd:COG3321 1075 AELALAAAALALAAALAAAALALALAALAAALLL---LALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALA 1151
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 569 LSALTGEGVGELREVLGQFVAERGAAARRVAADLDAAAAGLRPVYATGRRAGLTEEAREEFAARLADAVGATAAGEAAER 648
Cdd:COG3321 1152 LAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAA 1231
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 649 AWLRNANRACGTPWLRLWRWYQGRGEATTGRHAVRGQADEEATARQRVEQAVRTVADRASAGLPAPWAQAVREAAVRGSQ 728
Cdd:COG3321 1232 ALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAA 1311
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2756311615 729 GLSEALDALSARAGLPPGRPPRPGWWPVAVLVQAAMTLLQIVGGGWLAGQIAGLMA 784
Cdd:COG3321 1312 AAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAA 1367
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
391-587 |
2.37e-06 |
|
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 48.70 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 391 VALAGATGSGKSQLFNSLAGVAISETGVRrPTTAAPiacswsdgaaTLIdRLGIpgrlrrrpmhspdneaqLRGLVLVDL 470
Cdd:cd09912 3 LAVVGEFSAGKSTLLNALLGEEVLPTGVT-PTTAVI----------TVL-RYGL-----------------LKGVVLVDT 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 471 PDHDSAAVQHREQVDRILRLVDAVIWVVDpekyAD--AMLHER-----YLRPMAGHaevMFIVLNQVDRLpgdAADQVLD 543
Cdd:cd09912 54 PGLNSTIEHHTEITESFLPRADAVIFVLS----ADqpLTESEReflkeILKWSGKK---IFFVLNKIDLL---SEEELEE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2756311615 544 DLRRLLDEDGIAlgEHGEPGATVLALSA--------------LTGEGVGELREVLGQF 587
Cdd:cd09912 124 VLEYSREELGVL--ELGGGEPRIFPVSAkealearlqgdeelLEQSGFEELEEHLEEF 179
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
391-584 |
1.74e-05 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 47.35 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 391 VALAGATGSGKSQLFNSLAG--VAI-SetgvRRP-TTAAPIacswsdgaatlidrLGIpgrlrrrpMHspDNEAQLrglV 466
Cdd:PRK00089 8 VAIVGRPNVGKSTLLNALVGqkISIvS----PKPqTTRHRI--------------RGI--------VT--EDDAQI---I 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 467 LVDLPD-HDSAAVQHR---EQVDRILRLVDAVIWVVDPEKYADAmlHERY-LRPMAGHAEVMFIVLNQVDRL-PGDAADQ 540
Cdd:PRK00089 57 FVDTPGiHKPKRALNRamnKAAWSSLKDVDLVLFVVDADEKIGP--GDEFiLEKLKKVKTPVILVLNKIDLVkDKEELLP 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2756311615 541 VLDDLRRLLDEDGIalgehgepgatvLALSALTGEGVGELREVL 584
Cdd:PRK00089 135 LLEELSELMDFAEI------------VPISALKGDNVDELLDVI 166
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
73-250 |
4.42e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 47.21 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 73 EGRDDAREDANGGEYEGGGGGREGDGTGVLHARVPDETAEGGPDPGRARPARVRDEDHDSRAATGPRERPARLRGENAAR 152
Cdd:PRK12678 57 EARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 153 AQ---------GQGTESEHSRDADRGRGRGRGTERDHGRDTDRDRERESDGHAEAVEGGDRHAVQDRDchAVHDRDRGGA 223
Cdd:PRK12678 137 ARrgaarkageGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRD--RRDRREQGDR 214
|
170 180
....*....|....*....|....*..
gi 2756311615 224 QDRDRHGEAGGNGDRDRSARGRGAEQG 250
Cdd:PRK12678 215 REERGRRDGGDRRGRRRRRDRRDARGD 241
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
463-584 |
1.17e-04 |
|
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.
Pssm-ID: 425418 [Multi-domain] Cd Length: 187 Bit Score: 43.67 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 463 RGLVLVDLPDHdsaaVQHREQVDRILRLVDAVIWVVDpekyADA---------MLHERYLR-PMaghaevmFIVLNQVDR 532
Cdd:pfam00009 69 YLINLIDTPGH----VDFVKEVIRGLAQADGAILVVD----AVEgvmpqtrehLRLARQLGvPI-------IVFINKMDR 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2756311615 533 LPGDAADQVLDDLRRLLDEDgiaLGEHGEpGATVLALSALTGEGVGELREVL 584
Cdd:pfam00009 134 VDGAELEEVVEEVSRELLEK---YGEDGE-FVPVVPGSALKGEGVQTLLDAL 181
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
391-587 |
2.12e-04 |
|
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.
Pssm-ID: 206665 [Multi-domain] Cd Length: 170 Bit Score: 42.88 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 391 VALAGATGSGKSQLFNSLA---GVA-ISETgvrrpttaapiacswsdgaatlidrlgiPGRlRRRPmhspdNEAQL-RGL 465
Cdd:cd01876 2 VAFAGRSNVGKSSLINALTnrkKLArTSKT----------------------------PGR-TQLI-----NFFNVgDKF 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 466 VLVDLPDHDSAAVQHREQvDRILRLVD----------AVIWVVD----PEKYADAMLHerylrpMAGHAEV-MFIVLNQV 530
Cdd:cd01876 48 RLVDLPGYGYAKVSKEVR-EKWGKLIEeylenrenlkGVVLLIDarhgPTPIDLEMLE------FLEELGIpFLIVLTKA 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2756311615 531 DRLPGDAADQVLDDLRRLLDEDGIALgehgepgaTVLALSALTGEGVGELREVLGQF 587
Cdd:cd01876 121 DKLKKSELAKVLKKIKEELNLFNILP--------PVILFSSKKGTGIDELRALIAEW 169
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
391-587 |
3.47e-04 |
|
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.
Pssm-ID: 206727 [Multi-domain] Cd Length: 159 Bit Score: 42.10 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 391 VALAGATGSGKSQLFNSLAG--VAIsetgVrrpttaapiacswSDgaatlidrlgIPGRLR---RRPMHspdneaqLRG- 464
Cdd:cd04164 6 VVIAGKPNVGKSSLLNALAGrdRAI----V-------------SD----------IAGTTRdviEEEID-------LGGi 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 465 -LVLVD---LPDHDSAaVQhREQVDRILRLV---DAVIWVVDPEKYADAMLHERYLRPMAGHaevMFIVLNQVDRLPGDA 537
Cdd:cd04164 52 pVRLIDtagLRETEDE-IE-KIGIERAREAIeeaDLVLLVVDASEGLDEEDLEILELPAKKP---VIVVLNKSDLLSDAE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2756311615 538 adqvlddlrrlldedgialGEHGEPGATVLALSALTGEGVGELREVLGQF 587
Cdd:cd04164 127 -------------------GISELNGKPIIAISAKTGEGIDELKEALLEL 157
|
|
| SF-CC1 |
TIGR01622 |
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ... |
177-268 |
4.00e-04 |
|
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.
Pssm-ID: 273721 [Multi-domain] Cd Length: 494 Bit Score: 43.75 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 177 ERDHGRDTDRDRERESDGhaeaveggDRHAVQDRDchavHDRDRGGAQDRDRHGEaggnGDRDRSARGRGAEQGvsvPRP 256
Cdd:TIGR01622 8 ERLRDSSSAGDRDRRRDK--------GRERSRDRS----RDRERSRSRRRDRHRD----RDYYRGRERRSRSRR---PNR 68
|
90
....*....|..
gi 2756311615 257 HPHPARSPKPRP 268
Cdd:TIGR01622 69 RYRPREKRRRRG 80
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
345-586 |
8.84e-04 |
|
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.
Pssm-ID: 206666 [Multi-domain] Cd Length: 204 Bit Score: 41.29 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 345 LRSRLNALR-ELVGLSRTRldshtlaEAGRvldeaaARRKLSGrHTVVALAGATGSGKSQLFNSLAGvaiSETGVR---- 419
Cdd:cd01878 11 IRERIAKLRkELEKVKKQR-------ELQR------ARRKRSG-VPTVALVGYTNAGKSTLFNALTG---ADVLAEdqlf 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 420 ---RPTTaapiacswsdgaatlidrlgipgrlRRrpMHSPDNeaqlRGLVLVD-------LPDHDSAA----VQHREQVD 485
Cdd:cd01878 74 atlDPTT-------------------------RR--IKLPGG----REVLLTDtvgfirdLPHQLVEAfrstLEEVAEAD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 486 RILRLVDAviwvVDPEkyADAMLH--ERYLRPMAGHAEVMFIVLNQVDRLPGDAADQVLddlrrlldedgialgEHGEPG 563
Cdd:cd01878 123 LLLHVVDA----SDPD--REEQIEtvEEVLKELGADDIPIILVLNKIDLLDDEELEERL---------------RAGRPD 181
|
250 260
....*....|....*....|...
gi 2756311615 564 AtvLALSALTGEGVGELREVLGQ 586
Cdd:cd01878 182 A--VFISAKTGEGLDLLKEAIEE 202
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
466-867 |
9.37e-04 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 42.92 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 466 VLVDLPDHDSAAVQHREQVDRILRLVDAViwVVDPEKYADAMLHERYLRPMAGHAEVMFIVLnqVDRLPGDAADQVLDDL 545
Cdd:COG1020 891 ALLQHPGVREAVVVAREDAPGDKRLVAYV--VPEAGAAAAAALLRLALALLLPPYMVPAAVV--LLLPLPLTGNGKLDRL 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 546 RRLLDEDGIALGEHGEPGATVLALSALTGEGVGELREVLGQF-------------VAERGAAARRVAADLDAAAAGLRPV 612
Cdd:COG1020 967 ALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFfffggglglllllALARAARLLLLLLLLLLLFLAAAAA 1046
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 613 YATGRRAGLTEEAREEFAARLADAVGATAAGEAAERAWLRNANRACGTPWLRLWRWYQGRGEATTGRHAVRGQADEEATA 692
Cdd:COG1020 1047 AAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALR 1126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 693 RQRVEQAVRTVADRASAGLPAPWAQAVREAAVRGSQGLSEALDALSARAGLPPGRPPRPGWWPVAVLVQAAMTLLQIVGG 772
Cdd:COG1020 1127 ARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLL 1206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 773 GWLAGQIAGLMAPNLGVPVLLMVCGIVGGPLVEWGCRMAARGPARRYGQEAERRLREAAAGCGRARVLDPVAAELLRYRE 852
Cdd:COG1020 1207 LLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARA 1286
|
410
....*....|....*
gi 2756311615 853 VREQYGRVARSRTGV 867
Cdd:COG1020 1287 RAARTARALALLLLL 1301
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
391-528 |
1.33e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 39.14 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 391 VALAGATGSGKSQLFNSLAGvAISETGvRRP-TTaapiacswsdgaatlIDRlgIPGRLRRRPMHspdneaqlrgLVLVD 469
Cdd:pfam01926 2 VALVGRPNVGKSTLINALTG-AKAIVS-DYPgTT---------------RDP--NEGRLELKGKQ----------IILVD 52
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2756311615 470 LPDHDSAAVQHREQVDRILRL--VDAVIWVVDPEKYADAMLHEryLRPMAGHAEV-MFIVLN 528
Cdd:pfam01926 53 TPGLIEGASEGEGLGRAFLAIieADLILFVVDSEEGITPLDEE--LLELLRENKKpIILVLN 112
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
510-584 |
1.38e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 40.84 E-value: 1.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2756311615 510 ERYLrPMAGHAEVMF-IVLNQVDRLPGDAADQVLDDLRRLldedgialgehgepGATVLALSALTGEGVGELREVL 584
Cdd:cd01854 23 DRYL-VAAEASGIEPvIVLNKADLVDDEELEELLEIYEKL--------------GYPVLAVSAKTGEGLDELRELL 83
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
107-306 |
2.29e-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: 41.90 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 107 PDETAEGGPDPGRARPARVRDEDHDSRAATGPRERPARLRGENAARAQGQGTESEHSRDADRGRGRGRGTERDHGRDTD- 185
Cdd:TIGR00927 651 RPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEg 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 186 --------RDRERESDGHAEAVEGGDRHAVQDRDCHAVHDRDRGGAQDRDRHGEAGGNGDR--DRSARGRGAEQGVSVPR 255
Cdd:TIGR00927 731 eietgeegEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMkgDEGAEGKVEHEGETEAG 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2756311615 256 PHPHPARSPKPRPAPETTSPRTSTATGAATpTPTSATDGEAGASQETWDDG 306
Cdd:TIGR00927 811 EKDEHEGQSETQADDTEVKDETGEQELNAE-NQGEAKQDEKGVDGGGGSDG 860
|
|
| PRK13863 |
PRK13863 |
T-DNA border endonuclease VirD2; |
109-329 |
2.68e-03 |
|
T-DNA border endonuclease VirD2;
Pssm-ID: 237533 [Multi-domain] Cd Length: 446 Bit Score: 41.09 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 109 ETAEGGPDPGRARPARVRDEDHDSRAATGPR--ERPARLRGENAARAQ------GQGTESEHSRDADRGRGRGRGTERDH 180
Cdd:PRK13863 215 DFEEFSPGEDHREPSQSFDTSPGEAPQGEPEsaERPEKLQNESEVRLQepagssIKADARIRVSLESERRAQPSASKIPV 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 181 GRDTDRDRERESDGHAEAVEG--GDRHAVQDRDCHAVHDRDRGGAQDRDRHGE-AGGNGDRDRSAR-GRGAEQGVSVPRP 256
Cdd:PRK13863 295 ADDFGIETSYVAEGDVRKLEGnsGTPRLATEVATHTTSERQQRRKRPRDDEGEpSGAKRTRLNGIAvGPEANAGEQDGRD 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2756311615 257 HPHPARSPKPRPAPETTSPRTSTATGAATPTPTSATDGEAGASQETWDDGLIARRvtGSASAERSSSGEQPHR 329
Cdd:PRK13863 375 DPITSPAQPPRSNPLADPVRASIATDSLPATADRQQQREPSSKRPRDDDGEPSIR--KRARDGRSQDGREGNR 445
|
|
| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
368-587 |
3.33e-03 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 40.86 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 368 LAEAGRVLDEAAARRKLsgRHTV-VALAGATGSGKSQLFNSLAG--VAIsetgVrrpttaapiacswSDGAATLIDRL-- 442
Cdd:PRK05291 196 IAELEALLASARQGEIL--REGLkVVIAGRPNVGKSSLLNALLGeeRAI----V-------------TDIAGTTRDVIee 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 443 -----GIPgrlrrrpmhspdneaqlrgLVLVD---LPDHDSA--------AVQHREQVDRILRLVDA-VIWVVDPEKYAD 505
Cdd:PRK05291 257 hinldGIP-------------------LRLIDtagIRETDDEvekigierSREAIEEADLVLLVLDAsEPLTEEDDEILE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756311615 506 AMLHERYLrpmaghaevmfIVLNQVDRLPGDAADQvlddlrrlldedgialgehgEPGATVLALSALTGEGVGELREVLG 585
Cdd:PRK05291 318 ELKDKPVI-----------VVLNKADLTGEIDLEE--------------------ENGKPVIRISAKTGEGIDELREAIK 366
|
..
gi 2756311615 586 QF 587
Cdd:PRK05291 367 EL 368
|
|
| |
