|
Name |
Accession |
Description |
Interval |
E-value |
| FxSxx_TPR |
NF040586 |
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
329-1007 |
3.75e-96 |
|
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.
Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 327.65 E-value: 3.75e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 329 RKNSRFVGREEEISKI-EGLIMQKDSPGRIAICGLGGVGKTQIALELAYRMRNrDHECsVLWISCTSYESVEQAYMSIAL 407
Cdd:NF040586 3 PRNPNFTGREELLERLrDQLRSGGAAVVPQALHGLGGVGKTQLALEYAHRFRA-DYDL-VWWIPADQPELVRASLAELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 408 KLGITDPkPVEVKQQVK-VY--LSQGST-ARWLLVFDNADDMEMwkTADFLPESERGHILFTTRTRQVAVRLASSHVImi 483
Cdd:NF040586 81 RLGLPLG-PDDVDEAARaVLdaLRRGEPyRRWLLVFDNADDPED--LRDLLPTGGPGHVLITSRNRAWSEVAAATLEV-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 484 sEP-DAETAVEILRRSLitGDLLNDREA-AIAllKELACLPLAIAQAAAYINENDIRLSAYTTLLHESEPDVIellsedf 561
Cdd:NF040586 156 -DVfSREESVALLRRRV--PGLTSEEDAdRLA--EALGDLPLALEQAAAWLAETGMPVDEYLRLLDEQATAAL------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 562 GDEGRYKDIQNPVATTWWISFQQIQQLNPTAIDYLLFMACINHRHIPQSLL------------PQTTSSKKRTDAIGLLK 629
Cdd:NF040586 224 LLELKPPGYPTSVAATWRLSLDRLRERSPAAARLLELCAFFGPEPIPLDLLrssdemarlllpYDLRLRELLLDGILLSR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 630 AFSFVNEEG------KACSLNIHRLVHLATRNWMRKNQLfsQQILKTADR-LSEAFPNNYHTNRELW---REYLPHVLSL 699
Cdd:NF040586 304 ALRELGRYAlarvdsGRRTLQVHRLVQAVLRDRLSEEER--ARARHEVHRiLAAAAPGDEPDDPRNWpryAELWPHLEPS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 700 TEEAEFQKEEEKYV-DMIDkigdCLRSDGRSKEAEYQFLQVLKIRKQVLGPEHPKTLtsmgdMVSTYL-----SQGRLTE 773
Cdd:NF040586 382 GALESDDPEVRRLLlDQVR----YLYLRGDYESARDLAERALERWRERLGPDDRQTL-----RLRFHLanalrSLGRYEE 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 774 AEKLAVEVLSI--RERVLGSEHPDTLGSMSGLAATYLNQGRWKDAEKLQEQVMEICKQVLGLEDPRTLTSIVNLASSYQL 851
Cdd:NF040586 453 ARELDEDTLERqrRVLGLGEDHPHTLMTAGGLGADLRALGRFREALELDEETLERHRRVFGEDHPRTLRAANNLAVSLRL 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 852 QGRWKEAEVLNLQVVERRKQALGPEHPETLNSMSHLATTYLCQRRWKEAEELNVEVTRIQKQVL-GPEHPDTLFSMGNLA 930
Cdd:NF040586 533 LGDYREALELDREVLRRRRRVLGPDHPRTLLSANNLARDLRELGRYAEALDLLEEALERYREVLgGPDHPDTLRAAKSLA 612
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1833963602 931 sICW-KQGRWKEAEVLEMQVMERRKQVLGPEHPDTLFSMANLAFYWKSQGKTQAASALLKQCLALQMKVLGPDHPDTL 1007
Cdd:NF040586 613 -VALrRAGRLEEALELAEDTYERYRRRFGPDHPDTLAAALSLANDLRALGDADEARELAREVLDRYRRVLGEDHPFTL 689
|
|
| RNase_H_Dikarya_like |
cd13934 |
Fungal (dikarya) Ribonuclease H, uncharacterized; This family contains dikarya RNase H, many ... |
1117-1274 |
4.10e-70 |
|
Fungal (dikarya) Ribonuclease H, uncharacterized; This family contains dikarya RNase H, many of which are uncharacterized. Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. It is widely present in various organisms, including bacteria, archaea and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site residues and have the same catalytic mechanism and functions in cells. RNase H is involved in DNA replication, repair and transcription. An important RNase H function is to remove Okazaki fragments during DNA replication.
Pssm-ID: 260014 [Multi-domain] Cd Length: 153 Bit Score: 231.32 E-value: 4.10e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1117 LIYTDGACLGNGEANPRAGCGVVFREERSGrvgHFAFPLELQGPTghprPQTSNRAELRAVIAALQFRFWA----GEGWT 1192
Cdd:cd13934 1 LVYIDGACRNNGRPDARAGYGVYFGPDSSY---NVSGRLEDTGGH----PQTSQRAELRAAIAALRFRSWIidpdGEGLK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1193 KVVIATDSEYVVEGATSWSKGWIRNGWRTSTGRPVKNKDLWKCLLGWCEDAAttRAKTKLEFWRIPREWNAEADGWAKLA 1272
Cdd:cd13934 74 TVVIATDSEYVVKGATEWIPKWKRNGWRTSKGKPVKNRDLFELLLDEIEDLE--EGGVEVQFWHVPRELNKEADRLAKAA 151
|
..
gi 1833963602 1273 AD 1274
Cdd:cd13934 152 AE 153
|
|
| RNase_H |
pfam00075 |
RNase H; RNase H digests the RNA strand of an RNA/DNA hybrid. Important enzyme in retroviral ... |
1113-1241 |
6.39e-31 |
|
RNase H; RNase H digests the RNA strand of an RNA/DNA hybrid. Important enzyme in retroviral replication cycle, and often found as a domain associated with reverse transcriptases. Structure is a mixed alpha+beta fold with three a/b/a layers.
Pssm-ID: 395028 [Multi-domain] Cd Length: 141 Bit Score: 119.02 E-value: 6.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1113 PNEMLIYTDGACLGNGeanPRAGCGVVF---REERSGRVghfafplelqgptghPRPQTSNRAELRAVIAALQfrfwAGE 1189
Cdd:pfam00075 1 PKAVTVYTDGSCLGNP---GPGGAGAVLyrgHENISAPL---------------PGRTTNNRAELQAVIEALK----ALK 58
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1833963602 1190 GWTKVVIATDSEYVVEGATSWSKGWIRNGWR-TSTGRPVKNKDLWKCLLGWCE 1241
Cdd:pfam00075 59 SPSKVNIYTDSQYVIGGITQWVHGWKKNGWPtTSEGKPVKNKDLWQLLKALCK 111
|
|
| RnhA |
COG0328 |
Ribonuclease HI [Replication, recombination and repair]; |
1114-1273 |
1.07e-30 |
|
Ribonuclease HI [Replication, recombination and repair];
Pssm-ID: 440097 [Multi-domain] Cd Length: 136 Bit Score: 118.02 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1114 NEMLIYTDGACLGNgeanP-RAGCGVVFRE-----ERSGRVGHfafplelqgptghprpQTSNRAELRAVIAALQfrfWA 1187
Cdd:COG0328 1 KMIEIYTDGACRGN----PgPGGWGAVIRYggeekELSGGLGD----------------TTNNRAELTALIAALE---AL 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1188 GE-GWTKVVIATDSEYVVEGATSWSKGWIRNGWrtstgRPVKNKDLWKCLlgwceDAATTRAKTKLEfWrIPRE----WN 1262
Cdd:COG0328 58 KElGPCEVEIYTDSQYVVNQITGWIHGWKKNGW-----KPVKNPDLWQRL-----DELLARHKVTFE-W-VKGHaghpGN 125
|
170
....*....|.
gi 1833963602 1263 AEADGWAKLAA 1273
Cdd:COG0328 126 ERADALANKAL 136
|
|
| rnhA |
PRK00203 |
ribonuclease H; Reviewed |
1118-1275 |
1.56e-26 |
|
ribonuclease H; Reviewed
Pssm-ID: 178927 [Multi-domain] Cd Length: 150 Bit Score: 106.45 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1118 IYTDGACLGNgeanP-RAGCGVVFR---EERsgrvghfafplELQGptGHPrPQTSNRAELRAVIAALQfrfwAGEGWTK 1193
Cdd:PRK00203 6 IYTDGACLGN----PgPGGWGAILRykgHEK-----------ELSG--GEA-LTTNNRMELMAAIEALE----ALKEPCE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1194 VVIATDSEYVVEGATSWSKGWIRNGWRTSTGRPVKNKDLWKCLlgwceDAATTRAKTKlefWRipreW---------NAE 1264
Cdd:PRK00203 64 VTLYTDSQYVRQGITEWIHGWKKNGWKTADKKPVKNVDLWQRL-----DAALKRHQIK---WH----WvkghaghpeNER 131
|
170
....*....|.
gi 1833963602 1265 ADGWAKLAADK 1275
Cdd:PRK00203 132 CDELARAGAEE 142
|
|
| MTAN |
cd09008 |
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ... |
16-285 |
2.83e-22 |
|
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both bacterial and plant 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidases (MTANs): bacterial MTANs show comparable efficiency in hydrolyzing MTA and SAH, while plant enzymes are highly specific for MTA and are unable to metabolize SAH or show significantly reduced activity towards SAH. MTAN is involved in methionine and S-adenosyl-methionine recycling, polyamine biosynthesis, and bacterial quorum sensing. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.
Pssm-ID: 350159 Cd Length: 222 Bit Score: 96.80 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 16 ICALPLETAAAKVMLDEVHASlsqpKTDHNVYTLGNVGGHNVVVACLpiGVyGTVSASTVVSHMVSTYpNIQFGLMVGIG 95
Cdd:cd09008 4 IGAMEEEIAPLLELLENVEEE----TIAGRTFYEGTLGGKEVVLVQS--GI-GKVNAAIATQLLIDRF-KPDAIINTGVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 96 GGVpskSADIRLGDVVVSKptatsgGVIQYDYGKTLRGGhfqrtgslnkPPPILLKGVAQLESDhmtgKNLVSRIigdal 175
Cdd:cd09008 76 GGL---DPDLKIGDVVIAT------KVVYHDVDATAFGY----------EGGQPPGMPAYFPAD----PELLELA----- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 176 qkeeirrkfsrpecdwlfqptydhegkeancsacdqEQLVDRPPRTtaepyIHYGLIASGDQVIKDAGTRDFIARKEDIL 255
Cdd:cd09008 128 ------------------------------------KKAAKELGPK-----VHTGLIASGDQFVASSEKKEELRENFPAL 166
|
250 260 270
....*....|....*....|....*....|....*
gi 1833963602 256 CFEMEAAGL-----MDELPSLVIRGICDYCDSHKN 285
Cdd:cd09008 167 AVEMEGAAIaqvcyLNGVPFLVIRSISDLADGEAD 201
|
|
| MtnN |
COG0775 |
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ... |
12-290 |
2.14e-21 |
|
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase MtnN and futalosine hydrolase MqnB [Nucleotide transport and metabolism, Coenzyme transport and metabolism]; Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase MtnN and futalosine hydrolase MqnB is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440538 Cd Length: 231 Bit Score: 94.59 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 12 TVAWICALPLETAAakvmldeVHASLSQPKTDH---NVYTLGNVGGHNVVVAClpIGVyGTVSASTVVSHMVSTYpNIQF 88
Cdd:COG0775 2 TIGIIGAMEEEVAA-------LLEALEDKKEVQiagFTFYLGTLGGKEVVLVN--SGI-GKVNAATATTLLIARF-RPDA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 89 GLMVGIGGGVpskSADIRLGDVVVSKptatsgGVIQYDYGKTLRGGHFqrtGSLNKPPPILlkgvaqlESDhmtgKNLVS 168
Cdd:COG0775 71 VINTGVAGGL---DPDLKIGDVVLAT------EVVQHDVDVTAFGYPR---GQVPGMPALF-------EAD----PALLE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 169 RIIgDALQKEEIRrkfsrpecdwlfqptydhegkeancsacdqeqlvdrpprttaepyIHYGLIASGDQVIKDAGTRDFI 248
Cdd:COG0775 128 AAK-EAAKESGLK---------------------------------------------VVTGTIATGDRFVWSAEEKRRL 161
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1833963602 249 ARK-EDILCFEMEAAGL-----MDELPSLVIRGICDYCDSHKNKQWQE 290
Cdd:COG0775 162 RERfPGALAVDMEGAAIaqvcyRFGVPFLVIRAISDLAGEKAPNDFDE 209
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
720-995 |
6.69e-19 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 88.25 E-value: 6.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 720 GDCLRSDGRSKEAEYQFLQVLKIRkqvlgPEHPKTLTSMGDMvstYLSQGRLTEAEKlavevlsIRERVLgSEHPDTLGS 799
Cdd:COG2956 15 GLNYLLNGQPDKAIDLLEEALELD-----PETVEAHLALGNL---YRRRGEYDRAIR-------IHQKLL-ERDPDRAEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 800 MSGLAATYLNQGRWKDAEKLQEQVMEickqvlglEDPRTLTSIVNLASSYQLQGRWKEA-EVLnlqvveRRKQALGPEHP 878
Cdd:COG2956 79 LLELAQDYLKAGLLDRAEELLEKLLE--------LDPDDAEALRLLAEIYEQEGDWEKAiEVL------ERLLKLGPENA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 879 ETLNsmsHLATTYLCQRRWKEAEELnvevtriQKQVLG--PEHPDTLFSMGNLASicwKQGRWKEA-EVLEmQVMERrkq 955
Cdd:COG2956 145 HAYC---ELAELYLEQGDYDEAIEA-------LEKALKldPDCARALLLLAELYL---EQGDYEEAiAALE-RALEQ--- 207
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1833963602 956 vlgpeHPDTLFSMANLAFYWKSQGKTQAASALLKQCLALQ 995
Cdd:COG2956 208 -----DPDYLPALPRLAELYEKLGDPEEALELLRKALELD 242
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
754-829 |
1.21e-14 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 70.11 E-value: 1.21e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1833963602 754 TLTSMGDMVSTYLSQGRLTEAEKLAVEVLSIRERVLGSEHPDTLGSMSGLAATYLNQGRWKDAEKLQEQVMEICKQ 829
Cdd:pfam13424 2 VATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
|
|
| FxSxx_TPR |
NF040586 |
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
723-840 |
3.22e-10 |
|
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.
Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 64.55 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 723 LRSDGRSKEAEYQFLQVLKIRKQVLGPEHPKTLTSMGDMVSTYLSQGRLTEAEKLAV----EVLSIRERVLGSEHPDTLG 798
Cdd:NF040586 699 LRALGDPEEARELAEAALEGLRERLGPDHPYTLAAAVNLANDLAALGDLDAALGEEAlerlRRLLGEDLRAGPDHPDTLA 778
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1833963602 799 SMSGLAATYLNQGRWKDAEKLQEQVMEICKQVLGLEDPRTLT 840
Cdd:NF040586 779 CAANLALDLRATGRTEEAEELRADTLARLRRVLGPDHPDTVA 820
|
|
| TIGR02928 |
TIGR02928 |
orc1/cdc6 family replication initiation protein; Members of this protein family are found ... |
333-416 |
1.56e-06 |
|
orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 274354 [Multi-domain] Cd Length: 365 Bit Score: 51.86 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 333 RFVGREEEISKIEGL---IMQKDSPGRIAICGLGGVGKTQIAL----ELAYRMRNRDHECSVLWISCTSYESVEQAYMSI 405
Cdd:TIGR02928 16 RIVHRDEQIEELAKAlrpILRGSRPSNVFIYGKTGTGKTAVTKyvmkELEEAAEDRDVRVVTVYVNCQILDTLYQVLVEL 95
|
90
....*....|.
gi 1833963602 406 ALKLGITDPKP 416
Cdd:TIGR02928 96 ANQLRGSGEEV 106
|
|
| FxSxx_TPR |
NF040586 |
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
721-802 |
3.44e-05 |
|
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.
Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 48.38 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 721 DCLRSDGRSKEAEYQFLQVLKIRKQVLGPEHPKTLTSMGDMVSTYLSQGRLTEAEKLAVEVLSIRERVLGSEHPDTLGSM 800
Cdd:NF040586 743 ALGDLDAALGEEALERLRRLLGEDLRAGPDHPDTLACAANLALDLRATGRTEEAEELRADTLARLRRVLGPDHPDTVAAR 822
|
..
gi 1833963602 801 SG 802
Cdd:NF040586 823 EG 824
|
|
| PNP_UDP_1 |
pfam01048 |
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ... |
12-288 |
7.38e-05 |
|
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase (PNP) Uridine phosphorylase (UdRPase) 5'-methylthioadenosine phosphorylase (MTA phosphorylase)
Pssm-ID: 426013 Cd Length: 233 Bit Score: 45.80 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 12 TVAWICALPLETAA-AKVMLDEVHaslSQPKTDHNVYTLGNVGGHNVVVACLPIgvyGTVSASTVVSHMVstypNIQFG- 89
Cdd:pfam01048 1 KIAIIGGSPEELALlAELLDDETP---VGPPSRGGKFYTGTLGGVPVVLVRHGI---GPPNAAILAAIRL----LKEFGv 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 90 ---LMVGIGGGVpskSADIRLGDVVVSKptatsgGVIQYDYGKTLRG-GHFQRTGSLNKPPPIllkgvaqlesdhmtgKN 165
Cdd:pfam01048 71 daiIRTGTAGGL---NPDLKVGDVVIPT------DAINHDGRSPLFGpEGGPYFPDMAPAPAD---------------PE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 166 LVSRIIgDALQKEEIRrkfsrpecdwlfqptydhegkeancsacdqeqlvdrpprttaepyIHYGLIASGDQVIKDAGTR 245
Cdd:pfam01048 127 LRALAK-EAAERLGIP---------------------------------------------VHRGVYATGDGFYFETPAE 160
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1833963602 246 DFIARKEDILCFEMEAAGL-----MDELPSLVIRGICDYCDSHKNKQW 288
Cdd:pfam01048 161 IRLLRRLGADAVEMETAAEaqvarEAGIPFAAIRVVSDLAAGGADGEL 208
|
|
| PRK05584 |
PRK05584 |
5'-methylthioadenosine/adenosylhomocysteine nucleosidase; |
45-278 |
1.29e-04 |
|
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
Pssm-ID: 180148 Cd Length: 230 Bit Score: 44.73 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 45 NVYTLGNVGGHNVVVACLPIG-VYGTVSASTVVSHmvstypniqFG----LMVGIGGGVpskSADIRLGDVVVskptATS 119
Cdd:PRK05584 31 REFYTGTLHGHEVVLVLSGIGkVAAALTATILIEH---------FKvdavINTGVAGGL---APGLKVGDVVV----ADE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 120 ggVIQYD---------YGKTLRGGHFqrtgslnkpppillkgvaqLESDhmtgKNLVsriigDALQKeeirrkfsrpecd 190
Cdd:PRK05584 95 --LVQHDvdvtafgypYGQVPGLPAA-------------------FKAD----EKLV-----ALAEK------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 191 wlfqptydhegkeancsACDQeqlvdrpprttAEPYIHYGLIASGDQVIKDAGTRDFIaRKE--DILCFEMEAAGLM--- 265
Cdd:PRK05584 132 -----------------AAKE-----------LNLNVHRGLIASGDQFIAGAEKVAAI-RAEfpDALAVEMEGAAIAqvc 182
|
250
....*....|....*
gi 1833963602 266 DEL--PSLVIRGICD 278
Cdd:PRK05584 183 HEFgvPFVVVRAISD 197
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
353-505 |
1.43e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.43 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 353 SPGRIAICGLGGVGKTQIALELAYRMRNRDHecSVLWISCTSYEsvEQAYMSIALKLGITDPKPVEVKQQVKVYLSQGST 432
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG--GVIYIDGEDIL--EEVLDQLLLIIVGGKKASGSGELRLRLALALARK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1833963602 433 ARW-LLVFDNADDMEMWKTADFLPESERGHILFTTRTRQVAVRLASSHVIMISEPDAetAVEILRRSLITGDLL 505
Cdd:smart00382 77 LKPdVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPAL--LRRRFDRRIVLLLIL 148
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
335-484 |
2.15e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 40.21 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 335 VGREEEISKIEGLImQKDSPGRIAICGLGGVGKTQIALELAYRMRNRDHecSVLWISCTSYesVEQAYMSIALKLGITDp 414
Cdd:cd00009 1 VGQEEAIEALREAL-ELPPPKNLLLYGPPGTGKTTLARAIANELFRPGA--PFLYLNASDL--LEGLVVAELFGHFLVR- 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 415 kpvevKQQVKVYLSQGSTarwlLVFDNADDMEMWKTADFLPESergHILFTTRTRQVAVRlasshVIMIS 484
Cdd:cd00009 75 -----LLFELAEKAKPGV----LFIDEIDSLSRGAQNALLRVL---ETLNDLRIDRENVR-----VIGAT 127
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FxSxx_TPR |
NF040586 |
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
329-1007 |
3.75e-96 |
|
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.
Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 327.65 E-value: 3.75e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 329 RKNSRFVGREEEISKI-EGLIMQKDSPGRIAICGLGGVGKTQIALELAYRMRNrDHECsVLWISCTSYESVEQAYMSIAL 407
Cdd:NF040586 3 PRNPNFTGREELLERLrDQLRSGGAAVVPQALHGLGGVGKTQLALEYAHRFRA-DYDL-VWWIPADQPELVRASLAELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 408 KLGITDPkPVEVKQQVK-VY--LSQGST-ARWLLVFDNADDMEMwkTADFLPESERGHILFTTRTRQVAVRLASSHVImi 483
Cdd:NF040586 81 RLGLPLG-PDDVDEAARaVLdaLRRGEPyRRWLLVFDNADDPED--LRDLLPTGGPGHVLITSRNRAWSEVAAATLEV-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 484 sEP-DAETAVEILRRSLitGDLLNDREA-AIAllKELACLPLAIAQAAAYINENDIRLSAYTTLLHESEPDVIellsedf 561
Cdd:NF040586 156 -DVfSREESVALLRRRV--PGLTSEEDAdRLA--EALGDLPLALEQAAAWLAETGMPVDEYLRLLDEQATAAL------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 562 GDEGRYKDIQNPVATTWWISFQQIQQLNPTAIDYLLFMACINHRHIPQSLL------------PQTTSSKKRTDAIGLLK 629
Cdd:NF040586 224 LLELKPPGYPTSVAATWRLSLDRLRERSPAAARLLELCAFFGPEPIPLDLLrssdemarlllpYDLRLRELLLDGILLSR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 630 AFSFVNEEG------KACSLNIHRLVHLATRNWMRKNQLfsQQILKTADR-LSEAFPNNYHTNRELW---REYLPHVLSL 699
Cdd:NF040586 304 ALRELGRYAlarvdsGRRTLQVHRLVQAVLRDRLSEEER--ARARHEVHRiLAAAAPGDEPDDPRNWpryAELWPHLEPS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 700 TEEAEFQKEEEKYV-DMIDkigdCLRSDGRSKEAEYQFLQVLKIRKQVLGPEHPKTLtsmgdMVSTYL-----SQGRLTE 773
Cdd:NF040586 382 GALESDDPEVRRLLlDQVR----YLYLRGDYESARDLAERALERWRERLGPDDRQTL-----RLRFHLanalrSLGRYEE 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 774 AEKLAVEVLSI--RERVLGSEHPDTLGSMSGLAATYLNQGRWKDAEKLQEQVMEICKQVLGLEDPRTLTSIVNLASSYQL 851
Cdd:NF040586 453 ARELDEDTLERqrRVLGLGEDHPHTLMTAGGLGADLRALGRFREALELDEETLERHRRVFGEDHPRTLRAANNLAVSLRL 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 852 QGRWKEAEVLNLQVVERRKQALGPEHPETLNSMSHLATTYLCQRRWKEAEELNVEVTRIQKQVL-GPEHPDTLFSMGNLA 930
Cdd:NF040586 533 LGDYREALELDREVLRRRRRVLGPDHPRTLLSANNLARDLRELGRYAEALDLLEEALERYREVLgGPDHPDTLRAAKSLA 612
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1833963602 931 sICW-KQGRWKEAEVLEMQVMERRKQVLGPEHPDTLFSMANLAFYWKSQGKTQAASALLKQCLALQMKVLGPDHPDTL 1007
Cdd:NF040586 613 -VALrRAGRLEEALELAEDTYERYRRRFGPDHPDTLAAALSLANDLRALGDADEARELAREVLDRYRRVLGEDHPFTL 689
|
|
| RNase_H_Dikarya_like |
cd13934 |
Fungal (dikarya) Ribonuclease H, uncharacterized; This family contains dikarya RNase H, many ... |
1117-1274 |
4.10e-70 |
|
Fungal (dikarya) Ribonuclease H, uncharacterized; This family contains dikarya RNase H, many of which are uncharacterized. Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. It is widely present in various organisms, including bacteria, archaea and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site residues and have the same catalytic mechanism and functions in cells. RNase H is involved in DNA replication, repair and transcription. An important RNase H function is to remove Okazaki fragments during DNA replication.
Pssm-ID: 260014 [Multi-domain] Cd Length: 153 Bit Score: 231.32 E-value: 4.10e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1117 LIYTDGACLGNGEANPRAGCGVVFREERSGrvgHFAFPLELQGPTghprPQTSNRAELRAVIAALQFRFWA----GEGWT 1192
Cdd:cd13934 1 LVYIDGACRNNGRPDARAGYGVYFGPDSSY---NVSGRLEDTGGH----PQTSQRAELRAAIAALRFRSWIidpdGEGLK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1193 KVVIATDSEYVVEGATSWSKGWIRNGWRTSTGRPVKNKDLWKCLLGWCEDAAttRAKTKLEFWRIPREWNAEADGWAKLA 1272
Cdd:cd13934 74 TVVIATDSEYVVKGATEWIPKWKRNGWRTSKGKPVKNRDLFELLLDEIEDLE--EGGVEVQFWHVPRELNKEADRLAKAA 151
|
..
gi 1833963602 1273 AD 1274
Cdd:cd13934 152 AE 153
|
|
| RNase_HI_eukaryote_like |
cd09280 |
Eukaryotic RNase H is essential and is longer and more complex than their prokaryotic ... |
1118-1274 |
1.76e-37 |
|
Eukaryotic RNase H is essential and is longer and more complex than their prokaryotic counterparts; Ribonuclease H (RNase H) is classified into two families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is involved in DNA replication, repair and transcription. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. RNase H is widely present in various organisms, including bacteria, archaea and eukaryote and most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site (DEDD) residues and have the same catalytic mechanism and functions in cells. Eukaryotic RNase H is longer and more complex than in prokaryotes. Almost all eukaryotic RNase HI have highly conserved regions at their N-termini called hybrid binding domain (HBD). It is speculated that the HBD contributes to binding the RNA/DNA hybrid. Prokaryotes and some single-cell eukaryotes do not require RNase H for viability, but RNase H is essential in higher eukaryotes. RNase H knockout mice lack mitochondrial DNA replication and die as embryos.
Pssm-ID: 260012 [Multi-domain] Cd Length: 145 Bit Score: 137.70 E-value: 1.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1118 IYTDGACLGNGEANPRAGCGVVFREERSGRVGHfafPLelqgptgHPRPQTSNRAELRAVIAALQfRFWAGEGwTKVVIA 1197
Cdd:cd09280 2 VYTDGSCLNNGKPGARAGIGVYFGPGDPRNVSE---PL-------PGRKQTNNRAELLAVIHALE-QAPEEGI-RKLEIR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1198 TDSEYVVEGATSWSKGWIRNGWRTSTGRPVKNKDLWKCLlgwceDAATTRAKTKLEFWRIP----REWNAEADGWAKLAA 1273
Cdd:cd09280 70 TDSKYAINCITKWIPKWKKNGWKTSKGKPVKNQDLIKEL-----DKLLRKRGIKVKFEHVKghsgDPGNEEADRLAREGA 144
|
.
gi 1833963602 1274 D 1274
Cdd:cd09280 145 D 145
|
|
| RNase_HI_prokaryote_like |
cd09278 |
RNase HI family found mainly in prokaryotes; Ribonuclease H (RNase H) is classified into two ... |
1118-1274 |
1.27e-32 |
|
RNase HI family found mainly in prokaryotes; Ribonuclease H (RNase H) is classified into two evolutionarily unrelated families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is involved in DNA replication, repair and transcription. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes and most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site (DEDD), residues and have the same catalytic mechanism and functions in cells. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. Prokaryotic RNase H varies greatly in domain structures and substrate specificities. Prokaryotes and some single-cell eukaryotes do not require RNase H for viability.
Pssm-ID: 260010 [Multi-domain] Cd Length: 139 Bit Score: 123.75 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1118 IYTDGACLGNgeanP-RAGCGVVFREERSGRVGhfafplelqgpTGHPRPQTSNRAELRAVIAALQfrfWAGEGWtKVVI 1196
Cdd:cd09278 4 IYTDGACLGN----PgPGGWAAVIRYGDHEKEL-----------SGGEPGTTNNRMELTAAIEALE---ALKEPC-PVTI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1197 ATDSEYVVEGATSWSKGWIRNGWRTSTGRPVKNKDLWKCLLGWCedaattrAKTKLEFwriprEW---------NAEADG 1267
Cdd:cd09278 65 YTDSQYVINGITKWIKGWKKNGWKTADGKPVKNRDLWQELDALL-------AGHKVTW-----EWvkghaghpgNERADR 132
|
....*..
gi 1833963602 1268 WAKLAAD 1274
Cdd:cd09278 133 LANKAAD 139
|
|
| RNase_H |
pfam00075 |
RNase H; RNase H digests the RNA strand of an RNA/DNA hybrid. Important enzyme in retroviral ... |
1113-1241 |
6.39e-31 |
|
RNase H; RNase H digests the RNA strand of an RNA/DNA hybrid. Important enzyme in retroviral replication cycle, and often found as a domain associated with reverse transcriptases. Structure is a mixed alpha+beta fold with three a/b/a layers.
Pssm-ID: 395028 [Multi-domain] Cd Length: 141 Bit Score: 119.02 E-value: 6.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1113 PNEMLIYTDGACLGNGeanPRAGCGVVF---REERSGRVghfafplelqgptghPRPQTSNRAELRAVIAALQfrfwAGE 1189
Cdd:pfam00075 1 PKAVTVYTDGSCLGNP---GPGGAGAVLyrgHENISAPL---------------PGRTTNNRAELQAVIEALK----ALK 58
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1833963602 1190 GWTKVVIATDSEYVVEGATSWSKGWIRNGWR-TSTGRPVKNKDLWKCLLGWCE 1241
Cdd:pfam00075 59 SPSKVNIYTDSQYVIGGITQWVHGWKKNGWPtTSEGKPVKNKDLWQLLKALCK 111
|
|
| RnhA |
COG0328 |
Ribonuclease HI [Replication, recombination and repair]; |
1114-1273 |
1.07e-30 |
|
Ribonuclease HI [Replication, recombination and repair];
Pssm-ID: 440097 [Multi-domain] Cd Length: 136 Bit Score: 118.02 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1114 NEMLIYTDGACLGNgeanP-RAGCGVVFRE-----ERSGRVGHfafplelqgptghprpQTSNRAELRAVIAALQfrfWA 1187
Cdd:COG0328 1 KMIEIYTDGACRGN----PgPGGWGAVIRYggeekELSGGLGD----------------TTNNRAELTALIAALE---AL 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1188 GE-GWTKVVIATDSEYVVEGATSWSKGWIRNGWrtstgRPVKNKDLWKCLlgwceDAATTRAKTKLEfWrIPRE----WN 1262
Cdd:COG0328 58 KElGPCEVEIYTDSQYVVNQITGWIHGWKKNGW-----KPVKNPDLWQRL-----DELLARHKVTFE-W-VKGHaghpGN 125
|
170
....*....|.
gi 1833963602 1263 AEADGWAKLAA 1273
Cdd:COG0328 126 ERADALANKAL 136
|
|
| rnhA |
PRK00203 |
ribonuclease H; Reviewed |
1118-1275 |
1.56e-26 |
|
ribonuclease H; Reviewed
Pssm-ID: 178927 [Multi-domain] Cd Length: 150 Bit Score: 106.45 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1118 IYTDGACLGNgeanP-RAGCGVVFR---EERsgrvghfafplELQGptGHPrPQTSNRAELRAVIAALQfrfwAGEGWTK 1193
Cdd:PRK00203 6 IYTDGACLGN----PgPGGWGAILRykgHEK-----------ELSG--GEA-LTTNNRMELMAAIEALE----ALKEPCE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1194 VVIATDSEYVVEGATSWSKGWIRNGWRTSTGRPVKNKDLWKCLlgwceDAATTRAKTKlefWRipreW---------NAE 1264
Cdd:PRK00203 64 VTLYTDSQYVRQGITEWIHGWKKNGWKTADKKPVKNVDLWQRL-----DAALKRHQIK---WH----WvkghaghpeNER 131
|
170
....*....|.
gi 1833963602 1265 ADGWAKLAADK 1275
Cdd:PRK00203 132 CDELARAGAEE 142
|
|
| MTAN |
cd09008 |
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ... |
16-285 |
2.83e-22 |
|
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both bacterial and plant 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidases (MTANs): bacterial MTANs show comparable efficiency in hydrolyzing MTA and SAH, while plant enzymes are highly specific for MTA and are unable to metabolize SAH or show significantly reduced activity towards SAH. MTAN is involved in methionine and S-adenosyl-methionine recycling, polyamine biosynthesis, and bacterial quorum sensing. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.
Pssm-ID: 350159 Cd Length: 222 Bit Score: 96.80 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 16 ICALPLETAAAKVMLDEVHASlsqpKTDHNVYTLGNVGGHNVVVACLpiGVyGTVSASTVVSHMVSTYpNIQFGLMVGIG 95
Cdd:cd09008 4 IGAMEEEIAPLLELLENVEEE----TIAGRTFYEGTLGGKEVVLVQS--GI-GKVNAAIATQLLIDRF-KPDAIINTGVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 96 GGVpskSADIRLGDVVVSKptatsgGVIQYDYGKTLRGGhfqrtgslnkPPPILLKGVAQLESDhmtgKNLVSRIigdal 175
Cdd:cd09008 76 GGL---DPDLKIGDVVIAT------KVVYHDVDATAFGY----------EGGQPPGMPAYFPAD----PELLELA----- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 176 qkeeirrkfsrpecdwlfqptydhegkeancsacdqEQLVDRPPRTtaepyIHYGLIASGDQVIKDAGTRDFIARKEDIL 255
Cdd:cd09008 128 ------------------------------------KKAAKELGPK-----VHTGLIASGDQFVASSEKKEELRENFPAL 166
|
250 260 270
....*....|....*....|....*....|....*
gi 1833963602 256 CFEMEAAGL-----MDELPSLVIRGICDYCDSHKN 285
Cdd:cd09008 167 AVEMEGAAIaqvcyLNGVPFLVIRSISDLADGEAD 201
|
|
| MtnN |
COG0775 |
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ... |
12-290 |
2.14e-21 |
|
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase MtnN and futalosine hydrolase MqnB [Nucleotide transport and metabolism, Coenzyme transport and metabolism]; Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase MtnN and futalosine hydrolase MqnB is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440538 Cd Length: 231 Bit Score: 94.59 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 12 TVAWICALPLETAAakvmldeVHASLSQPKTDH---NVYTLGNVGGHNVVVAClpIGVyGTVSASTVVSHMVSTYpNIQF 88
Cdd:COG0775 2 TIGIIGAMEEEVAA-------LLEALEDKKEVQiagFTFYLGTLGGKEVVLVN--SGI-GKVNAATATTLLIARF-RPDA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 89 GLMVGIGGGVpskSADIRLGDVVVSKptatsgGVIQYDYGKTLRGGHFqrtGSLNKPPPILlkgvaqlESDhmtgKNLVS 168
Cdd:COG0775 71 VINTGVAGGL---DPDLKIGDVVLAT------EVVQHDVDVTAFGYPR---GQVPGMPALF-------EAD----PALLE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 169 RIIgDALQKEEIRrkfsrpecdwlfqptydhegkeancsacdqeqlvdrpprttaepyIHYGLIASGDQVIKDAGTRDFI 248
Cdd:COG0775 128 AAK-EAAKESGLK---------------------------------------------VVTGTIATGDRFVWSAEEKRRL 161
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1833963602 249 ARK-EDILCFEMEAAGL-----MDELPSLVIRGICDYCDSHKNKQWQE 290
Cdd:COG0775 162 RERfPGALAVDMEGAAIaqvcyRFGVPFLVIRAISDLAGEKAPNDFDE 209
|
|
| RNase_H_like |
cd06222 |
Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of ... |
1118-1270 |
3.58e-19 |
|
Ribonuclease H-like superfamily, including RNase H, HI, HII, HIII, and RNase-like domain IV of spliceosomal protein Prp8; Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. It is widely present in various organisms, including bacteria, archaea, and eukaryotes. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site residues and have the same catalytic mechanism and functions in cells. RNase H is involved in DNA replication, repair and transcription. An important RNase H function is to remove Okazaki fragments during DNA replication. RNase H inhibitors have been explored as anti-HIV drug targets since RNase H inactivation inhibits reverse transcription. This model also includes the Prp8 domain IV, which adopts the RNase fold but shows low sequence homology; domain IV is implicated in key spliceosomal interactions.
Pssm-ID: 259998 [Multi-domain] Cd Length: 121 Bit Score: 84.67 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1118 IYTDGACLGNGeanPRAGCGVVFREeRSGRVgHFAFplelqgpTGHPRPQTSNRAELRAVIAALQFrfWAGEGWTKVVIA 1197
Cdd:cd06222 1 INVDGSCRGNP---GPAGIGGVLRD-HEGGW-LGGF-------ALKIGAPTALEAELLALLLALEL--ALDLGYLKVIIE 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1833963602 1198 TDSEYVVEGATSWSKGWIRNGwrtstgrpVKNKDLWKCLLGwcedaattraKTKLEFWRIPREWNAEADGWAK 1270
Cdd:cd06222 67 SDSKYVVDLINSGSFKWSPNI--------LLIEDILLLLSR----------FWSVKISHVPREGNQVADALAK 121
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
720-995 |
6.69e-19 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 88.25 E-value: 6.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 720 GDCLRSDGRSKEAEYQFLQVLKIRkqvlgPEHPKTLTSMGDMvstYLSQGRLTEAEKlavevlsIRERVLgSEHPDTLGS 799
Cdd:COG2956 15 GLNYLLNGQPDKAIDLLEEALELD-----PETVEAHLALGNL---YRRRGEYDRAIR-------IHQKLL-ERDPDRAEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 800 MSGLAATYLNQGRWKDAEKLQEQVMEickqvlglEDPRTLTSIVNLASSYQLQGRWKEA-EVLnlqvveRRKQALGPEHP 878
Cdd:COG2956 79 LLELAQDYLKAGLLDRAEELLEKLLE--------LDPDDAEALRLLAEIYEQEGDWEKAiEVL------ERLLKLGPENA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 879 ETLNsmsHLATTYLCQRRWKEAEELnvevtriQKQVLG--PEHPDTLFSMGNLASicwKQGRWKEA-EVLEmQVMERrkq 955
Cdd:COG2956 145 HAYC---ELAELYLEQGDYDEAIEA-------LEKALKldPDCARALLLLAELYL---EQGDYEEAiAALE-RALEQ--- 207
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1833963602 956 vlgpeHPDTLFSMANLAFYWKSQGKTQAASALLKQCLALQ 995
Cdd:COG2956 208 -----DPDYLPALPRLAELYEKLGDPEEALELLRKALELD 242
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
747-943 |
2.50e-18 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 85.83 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 747 LGPEHPKTLTSMGDmvsTYLSQGRLTEAEKLAVEVLSIrervlgseHPDTLGSMSGLAATYLNQGRWKDAEKLQEQVMEI 826
Cdd:COG0457 3 LDPDDAEAYNNLGL---AYRRLGRYEEAIEDYEKALEL--------DPDDAEALYNLGLAYLRLGRYEEALADYEQALEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 827 ckqvlgleDPRTLTSIVNLASSYQLQGRWKEAEVLNLQVVErrkqaLGPEHPETLNsmsHLATTYLCQRRWKEAEELNVE 906
Cdd:COG0457 72 --------DPDDAEALNNLGLALQALGRYEEALEDYDKALE-----LDPDDAEALY---NLGLALLELGRYDEAIEAYER 135
|
170 180 190
....*....|....*....|....*....|....*..
gi 1833963602 907 VTRIQkqvlgPEHPDTLFsmgNLASICWKQGRWKEAE 943
Cdd:COG0457 136 ALELD-----PDDADALY---NLGIALEKLGRYEEAL 164
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
794-995 |
7.06e-17 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 81.59 E-value: 7.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 794 PDTLGSMSGLAATYLNQGRWKDAEKLQEQVMEIckqvlgleDPRTLTSIVNLASSYQLQGRWKEAEVLNLQVVErrkqaL 873
Cdd:COG0457 5 PDDAEAYNNLGLAYRRLGRYEEAIEDYEKALEL--------DPDDAEALYNLGLAYLRLGRYEEALADYEQALE-----L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 874 GPEHPETLNsmsHLATTYLCQRRWKEAEELNVEVTRIQkqvlgPEHPDTLFsmgNLASICWKQGRWKEA-----EVLEMQ 948
Cdd:COG0457 72 DPDDAEALN---NLGLALQALGRYEEALEDYDKALELD-----PDDAEALY---NLGLALLELGRYDEAieayeRALELD 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1833963602 949 vmerrkqvlgpehPDTLFSMANLAFYWKSQGKTQAASALLKQCLALQ 995
Cdd:COG0457 141 -------------PDDADALYNLGIALEKLGRYEEALELLEKLEAAA 174
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
719-903 |
3.11e-16 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 79.67 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 719 IGDCLRSDGRSKEAEYQFLQVLKIRkqvlgPEHPKTLTSMGDmvsTYLSQGRLTEAEKLAVEVLSIrervlgseHPDTLG 798
Cdd:COG0457 14 LGLAYRRLGRYEEAIEDYEKALELD-----PDDAEALYNLGL---AYLRLGRYEEALADYEQALEL--------DPDDAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 799 SMSGLAATYLNQGRWKDAEKLQEQVMEIckqvlgleDPRTLTSIVNLASSYQLQGRWKEAEVLNLQVVErrkqaLGPEHP 878
Cdd:COG0457 78 ALNNLGLALQALGRYEEALEDYDKALEL--------DPDDAEALYNLGLALLELGRYDEAIEAYERALE-----LDPDDA 144
|
170 180
....*....|....*....|....*
gi 1833963602 879 ETLNsmsHLATTYLCQRRWKEAEEL 903
Cdd:COG0457 145 DALY---NLGIALEKLGRYEEALEL 166
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
835-1011 |
1.17e-14 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 75.04 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 835 DPRTLTSIVNLASSYQLQGRWKEAEVLNLQVVErrkqaLGPEHPETLNsmsHLATTYLCQRRWKEAEELNVEVTRIQkqv 914
Cdd:COG0457 4 DPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALE-----LDPDDAEALY---NLGLAYLRLGRYEEALADYEQALELD--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 915 lgPEHPDTLFsmgNLASICWKQGRWKEAEVLEMQVMErrkqvLGPEHPDTLFsmaNLAFYWKSQGKTQAASALLKQCLAL 994
Cdd:COG0457 73 --PDDAEALN---NLGLALQALGRYEEALEDYDKALE-----LDPDDAEALY---NLGLALLELGRYDEAIEAYERALEL 139
|
170
....*....|....*..
gi 1833963602 995 QmkvlgPDHPDTLDHDG 1011
Cdd:COG0457 140 D-----PDDADALYNLG 151
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
754-829 |
1.21e-14 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 70.11 E-value: 1.21e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1833963602 754 TLTSMGDMVSTYLSQGRLTEAEKLAVEVLSIRERVLGSEHPDTLGSMSGLAATYLNQGRWKDAEKLQEQVMEICKQ 829
Cdd:pfam13424 2 VATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
879-955 |
6.44e-14 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 68.18 E-value: 6.44e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1833963602 879 ETLNSMSHLATTYLCQRRWKEAEELNVEVTRIQKQVLGPEHPDTLFSMGNLASICWKQGRWKEAEVLEMQVMERRKQ 955
Cdd:pfam13424 1 DVATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
|
|
| PRK08719 |
PRK08719 |
ribonuclease H; Reviewed |
1118-1234 |
6.44e-14 |
|
ribonuclease H; Reviewed
Pssm-ID: 236334 [Multi-domain] Cd Length: 147 Bit Score: 70.27 E-value: 6.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1118 IYTDGACLGNGEANPRAGCGVVFREERSGRVGHFAFPLElqgptghpRPQTSNRAELRAVIAALQFrfwAGEGwtkVVIA 1197
Cdd:PRK08719 7 IYIDGAAPNNQHGCVRGGIGLVVYDEAGEIVDEQSITVN--------RYTDNAELELLALIEALEY---ARDG---DVIY 72
|
90 100 110
....*....|....*....|....*....|....*..
gi 1833963602 1198 TDSEYVVEGATSWSKGWIRNGWRTSTGRPVKNKDLWK 1234
Cdd:PRK08719 73 SDSDYCVRGFNEWLDTWKQKGWRKSDKKPVANRDLWQ 109
|
|
| RNase_HI_like |
cd09279 |
RNAse HI family that includes archaeal, some bacterial as well as plant RNase HI; Ribonuclease ... |
1118-1274 |
7.58e-14 |
|
RNAse HI family that includes archaeal, some bacterial as well as plant RNase HI; Ribonuclease H (RNase H) is classified into two evolutionarily unrelated families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is involved in DNA replication, repair and transcription. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes and most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site (DEDD) residues and have the same catalytic mechanism and functions in cells. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. Most archaeal genomes contain only type 2 RNase H (RNase HII); however, a few contain RNase HI as well. Although archaeal RNase HI sequences conserve the DEDD active-site motif, they lack other common features important for catalytic function, such as the basic protrusion region. Archaeal RNase HI homologs are more closely related to retroviral RNase HI than bacterial and eukaryotic type I RNase H in enzymatic properties.
Pssm-ID: 260011 [Multi-domain] Cd Length: 128 Bit Score: 69.42 E-value: 7.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1118 IYTDGACLGNGEanpRAGCGVVFREErSGRVGHFAFPLelqgptghPRPQTSNRAELRAVIAALQfrfWAGE-GWTKVVI 1196
Cdd:cd09279 3 LYFDGASRGNPG---PAGAGVVIYSP-GGEVLELSERL--------GFPATNNEAEYEALIAGLE---LALElGAEKLEI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1197 ATDSEYVVEGatswskgwIRNGWRtstgrpVKNKDLwKCLLgwceDAATTRAKtKLEFWR---IPREWNAEADGWAKLAA 1273
Cdd:cd09279 68 YGDSQLVVNQ--------LNGEYK------VKNERL-KPLL----EKVLELLA-KFELVElkwIPREQNKEADALANQAL 127
|
.
gi 1833963602 1274 D 1274
Cdd:cd09279 128 D 128
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
795-871 |
1.26e-13 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 67.03 E-value: 1.26e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1833963602 795 DTLGSMSGLAATYLNQGRWKDAEKLQEQVMEICKQVLGLEDPRTLTSIVNLASSYQLQGRWKEAEVLNLQVVERRKQ 871
Cdd:pfam13424 1 DVATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
838-913 |
2.12e-13 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 66.64 E-value: 2.12e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1833963602 838 TLTSIVNLASSYQLQGRWKEAEVLNLQVVERRKQALGPEHPETLNSMSHLATTYLCQRRWKEAEELNVEVTRIQKQ 913
Cdd:pfam13424 2 VATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
921-994 |
3.45e-12 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 63.18 E-value: 3.45e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1833963602 921 DTLFSMGNLASICWKQGRWKEAEVLEMQVMERRKQVLGPEHPDTLFSMANLAFYWKSQGKTQAASALLKQCLAL 994
Cdd:pfam13424 1 DVATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALAL 74
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
719-904 |
2.37e-11 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 65.41 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 719 IGDCLRSDGRSKEAEYQFLQVLKIRkqvlgPEHPKTLTSMGDmvsTYLSQGRLTEAEKLAVEVLSIRervlgsehPDTLG 798
Cdd:COG0457 48 LGLAYLRLGRYEEALADYEQALELD-----PDDAEALNNLGL---ALQALGRYEEALEDYDKALELD--------PDDAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 799 SMSGLAATYLNQGRWKDAEKLQEQVMEIckqvlgleDPRTLTSIVNLASSYQLQGRWKEAevlnLQVVERRKQALGPEHP 878
Cdd:COG0457 112 ALYNLGLALLELGRYDEAIEAYERALEL--------DPDDADALYNLGIALEKLGRYEEA----LELLEKLEAAALAALL 179
|
170 180
....*....|....*....|....*.
gi 1833963602 879 ETLNSMSHLATTYLCQRRWKEAEELN 904
Cdd:COG0457 180 AAALGEAALALAAAEVLLALLLALEQ 205
|
|
| TPR_10 |
pfam13374 |
Tetratricopeptide repeat; |
922-963 |
6.47e-11 |
|
Tetratricopeptide repeat;
Pssm-ID: 463861 [Multi-domain] Cd Length: 42 Bit Score: 58.28 E-value: 6.47e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1833963602 922 TLFSMGNLASICWKQGRWKEAEVLEMQVMERRKQVLGPEHPD 963
Cdd:pfam13374 1 TASSLNNLANALRAQGRYDEAEELLEEALAIRERVLGPDHPD 42
|
|
| TPR_10 |
pfam13374 |
Tetratricopeptide repeat; |
754-795 |
6.59e-11 |
|
Tetratricopeptide repeat;
Pssm-ID: 463861 [Multi-domain] Cd Length: 42 Bit Score: 58.28 E-value: 6.59e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1833963602 754 TLTSMGDMVSTYLSQGRLTEAEKLAVEVLSIRERVLGSEHPD 795
Cdd:pfam13374 1 TASSLNNLANALRAQGRYDEAEELLEEALAIRERVLGPDHPD 42
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
803-943 |
6.64e-11 |
|
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 61.36 E-value: 6.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 803 LAATYLNQGRWKDAEKLQEQVMEickqvlglEDPRTLTSIVNLASSYQLQGRWKEAEVLNLQVVErrkqaLGPEHPETLN 882
Cdd:COG4783 10 LAQALLLAGDYDEAEALLEKALE--------LDPDNPEAFALLGEILLQLGDLDEAIVLLHEALE-----LDPDEPEARL 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1833963602 883 SmshLATTYLCQRRWKEAEELnvevtrIQKQV-LGPEHPDTLFsmgNLASICWKQGRWKEAE 943
Cdd:COG4783 77 N---LGLALLKAGDYDEALAL------LEKALkLDPEHPEAYL---RLARAYRALGRPDEAI 126
|
|
| TPR_10 |
pfam13374 |
Tetratricopeptide repeat; |
838-879 |
1.44e-10 |
|
Tetratricopeptide repeat;
Pssm-ID: 463861 [Multi-domain] Cd Length: 42 Bit Score: 57.51 E-value: 1.44e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1833963602 838 TLTSIVNLASSYQLQGRWKEAEVLNLQVVERRKQALGPEHPE 879
Cdd:pfam13374 1 TASSLNNLANALRAQGRYDEAEELLEEALAIRERVLGPDHPD 42
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
719-787 |
1.55e-10 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 58.55 E-value: 1.55e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1833963602 719 IGDCLRSDGRSKEAEYQFLQVLKIRKQVLGPEHPKTLTSMGDMVSTYLSQGRLTEAEKLAVEVLSIRER 787
Cdd:pfam13424 9 LAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
|
|
| TPR_10 |
pfam13374 |
Tetratricopeptide repeat; |
880-921 |
3.21e-10 |
|
Tetratricopeptide repeat;
Pssm-ID: 463861 [Multi-domain] Cd Length: 42 Bit Score: 56.36 E-value: 3.21e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1833963602 880 TLNSMSHLATTYLCQRRWKEAEELNVEVTRIQKQVLGPEHPD 921
Cdd:pfam13374 1 TASSLNNLANALRAQGRYDEAEELLEEALAIRERVLGPDHPD 42
|
|
| FxSxx_TPR |
NF040586 |
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
723-840 |
3.22e-10 |
|
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.
Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 64.55 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 723 LRSDGRSKEAEYQFLQVLKIRKQVLGPEHPKTLTSMGDMVSTYLSQGRLTEAEKLAV----EVLSIRERVLGSEHPDTLG 798
Cdd:NF040586 699 LRALGDPEEARELAEAALEGLRERLGPDHPYTLAAAVNLANDLAALGDLDAALGEEAlerlRRLLGEDLRAGPDHPDTLA 778
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1833963602 799 SMSGLAATYLNQGRWKDAEKLQEQVMEICKQVLGLEDPRTLT 840
Cdd:NF040586 779 CAANLALDLRATGRTEEAEELRADTLARLRRVLGPDHPDTVA 820
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
845-1009 |
3.45e-10 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 64.24 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 845 LASSYQLQGRWKEAEVLnlqvvERRKQALGPEHPETLNsmsHLATTYLCQRRWKEAEELNVEVTRIQkqvlgPEHPDTLF 924
Cdd:COG3914 84 AALLLQALGRYEEALAL-----YRRALALNPDNAEALF---NLGNLLLALGRLEEALAALRRALALN-----PDFAEAYL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 925 smgNLASICWKQGRWKEAEVLEMQVMERRkqvlgPEHPDTLFsmaNLAFYWKSQGKTQAASALLKQCLALQmkvlgPDHP 1004
Cdd:COG3914 151 ---NLGEALRRLGRLEEAIAALRRALELD-----PDNAEALN---NLGNALQDLGRLEEAIAAYRRALELD-----PDNA 214
|
....*
gi 1833963602 1005 DTLDH 1009
Cdd:COG3914 215 DAHSN 219
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
845-995 |
4.53e-10 |
|
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 59.05 E-value: 4.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 845 LASSYQLQGRWKEAEVLNLQVVERRkqalgPEHPETLNsmsHLATTYLCQRRWKEAEELnvevtrIQKQV-LGPEHPDTL 923
Cdd:COG4783 10 LAQALLLAGDYDEAEALLEKALELD-----PDNPEAFA---LLGEILLQLGDLDEAIVL------LHEALeLDPDEPEAR 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1833963602 924 FsmgNLASICWKQGRWKEAEVLEMQVMErrkqvLGPEHPDTLFSMANLafYWKsQGKTQAASALLKQCLALQ 995
Cdd:COG4783 76 L---NLGLALLKAGDYDEALALLEKALK-----LDPEHPEAYLRLARA--YRA-LGRPDEAIAALEKALELD 136
|
|
| TPR_10 |
pfam13374 |
Tetratricopeptide repeat; |
796-836 |
1.10e-09 |
|
Tetratricopeptide repeat;
Pssm-ID: 463861 [Multi-domain] Cd Length: 42 Bit Score: 54.82 E-value: 1.10e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1833963602 796 TLGSMSGLAATYLNQGRWKDAEKLQEQVMEICKQVLGLEDP 836
Cdd:pfam13374 1 TASSLNNLANALRAQGRYDEAEELLEEALAIRERVLGPDHP 41
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
765-972 |
2.15e-09 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 61.93 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 765 YLSQGRLTEAEKLAVEVLSIrervlgseHPDTLGSMSGLAATYLNQGRWKDAEKLQEQVMEIckqvlgleDPRTLTSIVN 844
Cdd:COG3914 88 LQALGRYEEALALYRRALAL--------NPDNAEALFNLGNLLLALGRLEEALAALRRALAL--------NPDFAEAYLN 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 845 LASSYQLQGRWKEAEVLNLQVVERRkqalgPEHPETLNsmsHLATTYLCQRRWKEAEELNVEVTRIQkqvlgpehPDTLF 924
Cdd:COG3914 152 LGEALRRLGRLEEAIAALRRALELD-----PDNAEALN---NLGNALQDLGRLEEAIAAYRRALELD--------PDNAD 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1833963602 925 SMGNLASICWKQGRWKEAEVLEmqvmERRKQVLGPEHPDTLFSMANLA 972
Cdd:COG3914 216 AHSNLLFALRQACDWEVYDRFE----ELLAALARGPSELSPFALLYLP 259
|
|
| NB-ARC |
pfam00931 |
NB-ARC domain; |
337-526 |
2.54e-09 |
|
NB-ARC domain;
Pssm-ID: 395745 [Multi-domain] Cd Length: 245 Bit Score: 59.32 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 337 REEEISKIEGLIMQKDSPGRIAICGLGGVGKTQIALELayrmrNRDHEC------SVLWISCTSYESVEQAYMSIALKLG 410
Cdd:pfam00931 1 REDMVEKVIGKLSEKDEPGIVGIHGMGGVGKTTLAAQI-----FNDFDEveghfdSVAWVVVSKTFTISTLQQTILQNLG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 411 ITD-----PKPVEVKQQVKVYLSQGstaRWLLVFDNADDMEMW-KTADFLPESERG-HILFTTRTRQVAVRLASSHVIM- 482
Cdd:pfam00931 76 LSEddwdnKEEGELARKIRRALLTK---RFLLVLDDVWDEEDWdKIGIPLPDRENGcRVLLTTRSEEVAGRVGGPSDPHe 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1833963602 483 --ISEPDaeTAVEIL-----RRSLITGDLLNDreaaiaLLKELA--C--LPLAIA 526
Cdd:pfam00931 153 veLLEPD--EAWELFenkvfPKTLGECELLED------VAKEIVekCrgLPLALK 199
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
357-530 |
5.13e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 60.80 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 357 IAICGLGGVGKTQIALELAYRMRNRDHEcSVLWISCTSYESVEQAYMSIALKLGITDPKPVEVKQQVKVYLSQGstaRWL 436
Cdd:COG3903 179 VTLTGPGGVGKTRLALEVAHRLADRFPD-GVWFVDLAGVTDPALVLAAVARALGVRDAPGRDPAARLRAALADR---RLL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 437 LVFDNADDMeMWKTADF----LPESERGHILFTTRtrqVAVRLASSHVIMIS-----EPDAETA--------VEILRRSL 499
Cdd:COG3903 255 LVLDNCEHV-VDAAAALvrplLPAAPGLRVLATSR---EPLGLPGERVLPLPplavpPPGAEALaseavalfVERAGAAR 330
|
170 180 190
....*....|....*....|....*....|..
gi 1833963602 500 ITGDLL-NDREAAIALLKELACLPLAIAQAAA 530
Cdd:COG3903 331 PGFALDaAEAAAVAEICRRLDGLPLAIELAAA 362
|
|
| TPR_10 |
pfam13374 |
Tetratricopeptide repeat; |
964-1005 |
6.42e-09 |
|
Tetratricopeptide repeat;
Pssm-ID: 463861 [Multi-domain] Cd Length: 42 Bit Score: 52.50 E-value: 6.42e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1833963602 964 TLFSMANLAFYWKSQGKTQAASALLKQCLALQMKVLGPDHPD 1005
Cdd:pfam13374 1 TASSLNNLANALRAQGRYDEAEELLEEALAIRERVLGPDHPD 42
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
718-859 |
1.81e-08 |
|
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 54.43 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 718 KIGDCLRSDGRSKEAEYQFLQVLKIRkqvlgPEHPKTLTSMGDMvstYLSQGRLTEAEKLAVEVLSIrervlgseHPDTL 797
Cdd:COG4783 9 ALAQALLLAGDYDEAEALLEKALELD-----PDNPEAFALLGEI---LLQLGDLDEAIVLLHEALEL--------DPDEP 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1833963602 798 GSMSGLAATYLNQGRWKDAEKLQEQVMEIckqvlgleDPRTLTSIVNLASSYQLQGRWKEAE 859
Cdd:COG4783 73 EARLNLGLALLKAGDYDEALALLEKALKL--------DPEHPEAYLRLARAYRALGRPDEAI 126
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
649-869 |
6.89e-08 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 55.51 E-value: 6.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 649 VHLATRNWmrknqlfsQQILKTADRLSEAFPNNYHTNRELWREYLphvlslteeaefqkeeekyvdmidkigdclrSDGR 728
Cdd:COG2956 119 IYEQEGDW--------EKAIEVLERLLKLGPENAHAYCELAELYL-------------------------------EQGD 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 729 SKEAEYQFLQVLKIRkqvlgPEHPKTLTSMGDMvstYLSQGRLTEAEKLAVEVLSIrervlgseHPDTLGSMSGLAATYL 808
Cdd:COG2956 160 YDEAIEALEKALKLD-----PDCARALLLLAEL---YLEQGDYEEAIAALERALEQ--------DPDYLPALPRLAELYE 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1833963602 809 NQGRWKDAEKLQEQVMEICKQvlgledprtLTSIVNLASSYQLQGRWKEAEVLNLQVVERR 869
Cdd:COG2956 224 KLGDPEEALELLRKALELDPS---------DDLLLALADLLERKEGLEAALALLERQLRRH 275
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
671-826 |
7.24e-08 |
|
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 53.43 E-value: 7.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 671 ADRLSEAFPNNYHTNRELWREYLPHVLSLTEEAEFQKEEEKYVDMIDKIGDCLRSDGRSKEAEYQFLQVLKirkqvLGPE 750
Cdd:COG5010 12 LYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQ-----LDPN 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1833963602 751 HPKTLTSMGDMvstYLSQGRLTEAEKLAVEVLSIrervlgseHPDTLGSMSGLAATYLNQGRWKDAEKLQEQVMEI 826
Cdd:COG5010 87 NPELYYNLALL---YSRSGDKDEAKEYYEKALAL--------SPDNPNAYSNLAALLLSLGQDDEAKAALQRALGT 151
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
765-873 |
9.78e-08 |
|
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 50.94 E-value: 9.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 765 YLSQGRLTEAEKLAVEVLSIrervlgseHPDTLGSMSGLAATYLNQGRWKDAEKLqEQVMEIckqvlgleDPRTLTSIVN 844
Cdd:COG3063 2 YLKLGDLEEAEEYYEKALEL--------DPDNADALNNLGLLLLEQGRYDEAIAL-EKALKL--------DPNNAEALLN 64
|
90 100
....*....|....*....|....*....
gi 1833963602 845 LASSYQLQGRWKEAEVLNLQVVERRKQAL 873
Cdd:COG3063 65 LAELLLELGDYDEALAYLERALELDPSAL 93
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
849-957 |
1.67e-07 |
|
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 50.55 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 849 YQLQGRWKEAEVLNLQVVErrkqaLGPEHPETLNSmshLATTYLCQRRWKEAEELNvevtRIQKqvLGPEHPDTLFsmgN 928
Cdd:COG3063 2 YLKLGDLEEAEEYYEKALE-----LDPDNADALNN---LGLLLLEQGRYDEAIALE----KALK--LDPNNAEALL---N 64
|
90 100
....*....|....*....|....*....
gi 1833963602 929 LASICWKQGRWKEAEVLEMQVMERRKQVL 957
Cdd:COG3063 65 LAELLLELGDYDEALAYLERALELDPSAL 93
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
722-826 |
1.67e-07 |
|
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 50.55 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 722 CLRSDGRSKEAEYQFLQVLKIRkqvlgPEHPKTLTSMGDMvstYLSQGRLTEAEKLavevlsirERVLgSEHPDTLGSMS 801
Cdd:COG3063 1 LYLKLGDLEEAEEYYEKALELD-----PDNADALNNLGLL---LLEQGRYDEAIAL--------EKAL-KLDPNNAEALL 63
|
90 100
....*....|....*....|....*
gi 1833963602 802 GLAATYLNQGRWKDAEKLQEQVMEI 826
Cdd:COG3063 64 NLAELLLELGDYDEALAYLERALEL 88
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
781-903 |
3.13e-07 |
|
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 50.77 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 781 VLSIRERVlgSEHPDTLGSMSGLAATYLNQGRWKDAEKLQEQVMEIckqvlgleDPRTLTSIVNLASSYQLQGRWKEAEV 860
Cdd:COG4235 3 IARLRQAL--AANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRL--------DPDNADALLDLAEALLAAGDTEEAEE 72
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1833963602 861 LNLQVVerrkqALGPEHPETLnsmSHLATTYLCQRRWKEAEEL 903
Cdd:COG4235 73 LLERAL-----ALDPDNPEAL---YLLGLAAFQQGDYAEAIAA 107
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
891-995 |
5.29e-07 |
|
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 49.01 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 891 YLCQRRWKEAEELNVEVTRIQkqvlgPEHPDTLFsmgNLASICWKQGRWKEAEVLEmQVMErrkqvLGPEHPDTLFSMAN 970
Cdd:COG3063 2 YLKLGDLEEAEEYYEKALELD-----PDNADALN---NLGLLLLEQGRYDEAIALE-KALK-----LDPNNAEALLNLAE 67
|
90 100
....*....|....*....|....*
gi 1833963602 971 LAFywkSQGKTQAASALLKQCLALQ 995
Cdd:COG3063 68 LLL---ELGDYDEALAYLERALELD 89
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
719-897 |
7.18e-07 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 53.84 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 719 IGDCLRSDGRSKEAEYQFLQVLKirkqvLGPEHPKTLTSMGdmvSTYLSQGRLTEAEKLAVEVLSIRervlgsehPDTLG 798
Cdd:COG3914 118 LGNLLLALGRLEEALAALRRALA-----LNPDFAEAYLNLG---EALRRLGRLEEAIAALRRALELD--------PDNAE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 799 SMSGLAATYLNQGRWKDAEKLQEQVMEIckqvlgleDPRTLTSIVNLASSYQLQGRWKEAEVLN--LQVVERRKQALGPE 876
Cdd:COG3914 182 ALNNLGNALQDLGRLEEAIAAYRRALEL--------DPDNADAHSNLLFALRQACDWEVYDRFEelLAALARGPSELSPF 253
|
170 180
....*....|....*....|.
gi 1833963602 877 HPETLNSMShLATTYLCQRRW 897
Cdd:COG3914 254 ALLYLPDDD-PAELLALARAW 273
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
764-859 |
7.98e-07 |
|
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 50.34 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 764 TYLSQGRLTEAEKLAVEVLSIrervlgseHPDTLGSMSGLAATYLNQGRWKDAEKLQEQVMEIckqvlgleDPRTLTSIV 843
Cdd:COG5010 63 LYNKLGDFEESLALLEQALQL--------DPNNPELYYNLALLYSRSGDKDEAKEYYEKALAL--------SPDNPNAYS 126
|
90
....*....|....*.
gi 1833963602 844 NLASSYQLQGRWKEAE 859
Cdd:COG5010 127 NLAALLLSLGQDDEAK 142
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
803-954 |
9.75e-07 |
|
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 49.96 E-value: 9.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 803 LAATYLNQGRWKDAEKLQEQVMEICKQVLGLEDPRTLTSIVNLAssYQLQGRWKEAEVLNLQVVErrkqaLGPEHPETLN 882
Cdd:COG5010 20 LRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNL--YNKLGDFEESLALLEQALQ-----LDPNNPELYY 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1833963602 883 SmshLATTYLCQRRWKEAEELNVEVTRIQkqvlgPEHPDTLFsmgNLASICWKQGRWKEAEVLEMQVMERRK 954
Cdd:COG5010 93 N---LALLYSRSGDKDEAKEYYEKALALS-----PDNPNAYS---NLAALLLSLGQDDEAKAALQRALGTSP 153
|
|
| TIGR02928 |
TIGR02928 |
orc1/cdc6 family replication initiation protein; Members of this protein family are found ... |
333-416 |
1.56e-06 |
|
orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 274354 [Multi-domain] Cd Length: 365 Bit Score: 51.86 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 333 RFVGREEEISKIEGL---IMQKDSPGRIAICGLGGVGKTQIAL----ELAYRMRNRDHECSVLWISCTSYESVEQAYMSI 405
Cdd:TIGR02928 16 RIVHRDEQIEELAKAlrpILRGSRPSNVFIYGKTGTGKTAVTKyvmkELEEAAEDRDVRVVTVYVNCQILDTLYQVLVEL 95
|
90
....*....|.
gi 1833963602 406 ALKLGITDPKP 416
Cdd:TIGR02928 96 ANQLRGSGEEV 106
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
845-1007 |
2.31e-06 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 51.92 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 845 LASSYQLQGRWKEAEVLNLQVVERRKQALGPEHPETLNSMSHLATTYLCQRRWKEAEELNVEVTRIQKQV-LGPEHPDTL 923
Cdd:COG3914 36 ALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALaLNPDNAEAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 924 FsmgNLASICWKQGRWKEAEVLEMQVMErrkqvLGPEHPDTLFSMANLAFywkSQGKTQAASALLKQCLALQmkvlgPDH 1003
Cdd:COG3914 116 F---NLGNLLLALGRLEEALAALRRALA-----LNPDFAEAYLNLGEALR---RLGRLEEAIAALRRALELD-----PDN 179
|
....
gi 1833963602 1004 PDTL 1007
Cdd:COG3914 180 AEAL 183
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
727-990 |
8.63e-06 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 50.47 E-value: 8.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 727 GRSKEAEYQFLQVLKIRkqvlgPEHPKTLTSMGDMvstYLSQGRLTEAEKLAVEVLSIrervlgseHPDTLGSMSGLAAT 806
Cdd:TIGR02917 479 GDLAKAREAFEKALSIE-----PDFFPAAANLARI---DIQEGNPDDAIQRFEKVLTI--------DPKNLRAILALAGL 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 807 YLNQGRWKDAEKLQEQVMEickqvlglEDPRTLTSIVNLASSYQLQGRWKEAEvlnlqVVERRKQALGPEHPETLnsmSH 886
Cdd:TIGR02917 543 YLRTGNEEEAVAWLEKAAE--------LNPQEIEPALALAQYYLGKGQLKKAL-----AILNEAADAAPDSPEAW---LM 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 887 LATTYLCQRRWKEAeelnveVTRIQKQV-LGPEHPDTLFSmgnLASICWKQGRWKEAEVLEMQVMERRkqvlgPEHPDTL 965
Cdd:TIGR02917 607 LGRAQLAAGDLNKA------VSSFKKLLaLQPDSALALLL---LADAYAVMKNYAKAITSLKRALELK-----PDNTEAQ 672
|
250 260
....*....|....*....|....*
gi 1833963602 966 FSMANLAFywkSQGKTQAASALLKQ 990
Cdd:TIGR02917 673 IGLAQLLL---AAKRTESAKKIAKS 694
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
887-1009 |
9.30e-06 |
|
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 46.72 E-value: 9.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 887 LATTYLCQRRWKEAEELNVEVTRIQkqvlgPEHPDTLFsmgNLASICWKQGRWKEAEV-LEmQVMErrkqvLGPEHPDTL 965
Cdd:COG4783 10 LAQALLLAGDYDEAEALLEKALELD-----PDNPEAFA---LLGEILLQLGDLDEAIVlLH-EALE-----LDPDEPEAR 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1833963602 966 FsmaNLAFYWKSQGKTQAASALLKQCLALQmkvlgPDHPDTLDH 1009
Cdd:COG4783 76 L---NLGLALLKAGDYDEALALLEKALKLD-----PEHPEAYLR 111
|
|
| RVT_3 |
pfam13456 |
Reverse transcriptase-like; This domain is found in plants and appears to be part of a ... |
1120-1272 |
1.15e-05 |
|
Reverse transcriptase-like; This domain is found in plants and appears to be part of a retrotransposon.
Pssm-ID: 433223 [Multi-domain] Cd Length: 123 Bit Score: 46.10 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1120 TDGACLGNgeaNPRAGCGVVFREERSGRVGHFAFPLelqgptgHPRpQTSNRAELRAVIAALQFRfWAGeGWTKVVIATD 1199
Cdd:pfam13456 2 FDGAFKCD---SGLAGAGVVIRDPNGNVLLAGQKKL-------GPG-ASVLEAEAQALIIGLQLA-WKL-GIRHLIVEGD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1200 SEYVVEgatswskgWIRNGWRTStgRPVKN---------KDLWKCLLGWcedaattraktklefwrIPREWNAEADGWAK 1270
Cdd:pfam13456 69 SATVVQ--------LINGRSPKQ--SKLANlldeirkllKRFESVSFEH-----------------IPREQNRVADTLAK 121
|
..
gi 1833963602 1271 LA 1272
Cdd:pfam13456 122 MA 123
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
876-994 |
1.47e-05 |
|
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 45.77 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 876 EHPETLNSMSHLATTYLCQRRWKEAEELNVEVTRIQkqvlgPEHPDTLFsmgNLASICWKQGRWKEAEVLEMQVMErrkq 955
Cdd:COG4235 12 ANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLD-----PDNADALL---DLAEALLAAGDTEEAEELLERALA---- 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 1833963602 956 vLGPEHPDTLFSMANLAFywkSQGKTQAASALLKQCLAL 994
Cdd:COG4235 80 -LDPDNPEALYLLGLAAF---QQGDYAEAIAAWQKLLAL 114
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
849-995 |
1.70e-05 |
|
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 46.49 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 849 YQLQGRWKEAEVLNLQVVERRKQALGPEHPETLNSMSHLATTYLCQRRWKEAEELNVEVTRiqkqvLGPEHPDTLFsmgN 928
Cdd:COG5010 22 TLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQ-----LDPNNPELYY---N 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1833963602 929 LASICWKQGRWKEAEVLEMQVMErrkqvLGPEHPDTLfsmANLAFYWKSQGKTQAASALLKQCLALQ 995
Cdd:COG5010 94 LALLYSRSGDKDEAKEYYEKALA-----LSPDNPNAY---SNLAALLLSLGQDDEAKAALQRALGTS 152
|
|
| FxSxx_TPR |
NF040586 |
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
721-802 |
3.44e-05 |
|
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.
Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 48.38 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 721 DCLRSDGRSKEAEYQFLQVLKIRKQVLGPEHPKTLTSMGDMVSTYLSQGRLTEAEKLAVEVLSIRERVLGSEHPDTLGSM 800
Cdd:NF040586 743 ALGDLDAALGEEALERLRRLLGEDLRAGPDHPDTLACAANLALDLRATGRTEEAEELRADTLARLRRVLGPDHPDTVAAR 822
|
..
gi 1833963602 801 SG 802
Cdd:NF040586 823 EG 824
|
|
| PNP_UDP_1 |
pfam01048 |
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ... |
12-288 |
7.38e-05 |
|
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase (PNP) Uridine phosphorylase (UdRPase) 5'-methylthioadenosine phosphorylase (MTA phosphorylase)
Pssm-ID: 426013 Cd Length: 233 Bit Score: 45.80 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 12 TVAWICALPLETAA-AKVMLDEVHaslSQPKTDHNVYTLGNVGGHNVVVACLPIgvyGTVSASTVVSHMVstypNIQFG- 89
Cdd:pfam01048 1 KIAIIGGSPEELALlAELLDDETP---VGPPSRGGKFYTGTLGGVPVVLVRHGI---GPPNAAILAAIRL----LKEFGv 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 90 ---LMVGIGGGVpskSADIRLGDVVVSKptatsgGVIQYDYGKTLRG-GHFQRTGSLNKPPPIllkgvaqlesdhmtgKN 165
Cdd:pfam01048 71 daiIRTGTAGGL---NPDLKVGDVVIPT------DAINHDGRSPLFGpEGGPYFPDMAPAPAD---------------PE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 166 LVSRIIgDALQKEEIRrkfsrpecdwlfqptydhegkeancsacdqeqlvdrpprttaepyIHYGLIASGDQVIKDAGTR 245
Cdd:pfam01048 127 LRALAK-EAAERLGIP---------------------------------------------VHRGVYATGDGFYFETPAE 160
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1833963602 246 DFIARKEDILCFEMEAAGL-----MDELPSLVIRGICDYCDSHKNKQW 288
Cdd:pfam01048 161 IRLLRRLGADAVEMETAAEaqvarEAGIPFAAIRVVSDLAAGGADGEL 208
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
720-826 |
1.03e-04 |
|
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 43.64 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 720 GDCLRSDGRSKEAEYQFLQVLKIRkqvlgPEHPKTLTSMGDmvsTYLSQGRLTEAEKLAVEVLSirervLGSEHPDTLgs 799
Cdd:COG4783 45 GEILLQLGDLDEAIVLLHEALELD-----PDEPEARLNLGL---ALLKAGDYDEALALLEKALK-----LDPEHPEAY-- 109
|
90 100
....*....|....*....|....*..
gi 1833963602 800 mSGLAATYLNQGRWKDAEKLQEQVMEI 826
Cdd:COG4783 110 -LRLARAYRALGRPDEAIAALEKALEL 135
|
|
| CDC6 |
COG1474 |
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair]; |
332-416 |
1.12e-04 |
|
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
Pssm-ID: 441083 [Multi-domain] Cd Length: 389 Bit Score: 45.99 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 332 SRFVGREEEISKIEGLI---MQKDSPGRIAICGLGGVGKTQIAL----ELAYRMRNRDHECSVLWISCTSYESVEQAYMS 404
Cdd:COG1474 26 DRLPHREEEIEELASALrpaLRGERPSNVLIYGPTGTGKTAVAKyvleELEEEAEERGVDVRVVYVNCRQASTRYRVLSR 105
|
90
....*....|..
gi 1833963602 405 IALKLGITDPKP 416
Cdd:COG1474 106 ILEELGSGEDIP 117
|
|
| PRK05584 |
PRK05584 |
5'-methylthioadenosine/adenosylhomocysteine nucleosidase; |
45-278 |
1.29e-04 |
|
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
Pssm-ID: 180148 Cd Length: 230 Bit Score: 44.73 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 45 NVYTLGNVGGHNVVVACLPIG-VYGTVSASTVVSHmvstypniqFG----LMVGIGGGVpskSADIRLGDVVVskptATS 119
Cdd:PRK05584 31 REFYTGTLHGHEVVLVLSGIGkVAAALTATILIEH---------FKvdavINTGVAGGL---APGLKVGDVVV----ADE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 120 ggVIQYD---------YGKTLRGGHFqrtgslnkpppillkgvaqLESDhmtgKNLVsriigDALQKeeirrkfsrpecd 190
Cdd:PRK05584 95 --LVQHDvdvtafgypYGQVPGLPAA-------------------FKAD----EKLV-----ALAEK------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 191 wlfqptydhegkeancsACDQeqlvdrpprttAEPYIHYGLIASGDQVIKDAGTRDFIaRKE--DILCFEMEAAGLM--- 265
Cdd:PRK05584 132 -----------------AAKE-----------LNLNVHRGLIASGDQFIAGAEKVAAI-RAEfpDALAVEMEGAAIAqvc 182
|
250
....*....|....*
gi 1833963602 266 DEL--PSLVIRGICD 278
Cdd:PRK05584 183 HEFgvPFVVVRAISD 197
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
719-826 |
1.76e-04 |
|
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 42.69 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 719 IGDCLRSDGRSKEAEYQFLQVLKIRkqvlgPEHPKTLTSMGDMvstYLSQGRLTEAEKLAVEVLSIrervlgseHPDTLG 798
Cdd:COG4235 23 LGRAYLRLGRYDEALAAYEKALRLD-----PDNADALLDLAEA---LLAAGDTEEAEELLERALAL--------DPDNPE 86
|
90 100
....*....|....*....|....*...
gi 1833963602 799 SMSGLAATYLNQGRWKDAEKLQEQVMEI 826
Cdd:COG4235 87 ALYLLGLAAFQQGDYAEAIAAWQKLLAL 114
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
915-1007 |
2.26e-04 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 44.23 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 915 LGPEHPDTLFsmgNLASICWKQGRWKEAEVLEMQVMErrkqvLGPEHPDTLFsmaNLAFYWKSQGKTQAASALLKQCLAL 994
Cdd:COG0457 3 LDPDDAEAYN---NLGLAYRRLGRYEEAIEDYEKALE-----LDPDDAEALY---NLGLAYLRLGRYEEALADYEQALEL 71
|
90
....*....|...
gi 1833963602 995 QmkvlgPDHPDTL 1007
Cdd:COG0457 72 D-----PDDAEAL 79
|
|
| PRK06548 |
PRK06548 |
ribonuclease H; Provisional |
1114-1232 |
3.76e-04 |
|
ribonuclease H; Provisional
Pssm-ID: 75628 [Multi-domain] Cd Length: 161 Bit Score: 42.49 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1114 NEMLIYTDGACLgngeANPRAGCGVVFREERSGRVGHFAFplelqgptghprpQTSNRAELRAVIAALqfrFWAGEGWTK 1193
Cdd:PRK06548 4 NEIIAATDGSSL----ANPGPSGWAWYVDENTWDSGGWDI-------------ATNNIAELTAVRELL---IATRHTDRP 63
|
90 100 110
....*....|....*....|....*....|....*....
gi 1833963602 1194 VVIATDSEYVVEGATSWSKGWIRNGWRTSTGRPVKNKDL 1232
Cdd:PRK06548 64 ILILSDSKYVINSLTKWVYSWKMRKWRKADGKPVLNQEI 102
|
|
| TPR_10 |
pfam13374 |
Tetratricopeptide repeat; |
723-752 |
4.48e-04 |
|
Tetratricopeptide repeat;
Pssm-ID: 463861 [Multi-domain] Cd Length: 42 Bit Score: 39.02 E-value: 4.48e-04
10 20 30
....*....|....*....|....*....|
gi 1833963602 723 LRSDGRSKEAEYQFLQVLKIRKQVLGPEHP 752
Cdd:pfam13374 12 LRAQGRYDEAEELLEEALAIRERVLGPDHP 41
|
|
| TPR_MalT |
pfam17874 |
MalT-like TPR region; This entry contains a series of TPR repeats. |
764-997 |
8.56e-04 |
|
MalT-like TPR region; This entry contains a series of TPR repeats.
Pssm-ID: 436107 [Multi-domain] Cd Length: 336 Bit Score: 43.07 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 764 TYLSQGRLTEAEKLAVEVLSIrERVLGSEHpDTLGSMSGLAATYLNQGRWKDAEKLQEQVMEICKQVLGLEDPRTLTSIV 843
Cdd:pfam17874 49 AYLCLGDLDAALQAMREAEAL-ARRADSPH-VTLWALLQQGEILRAQGRLHQALETYQQALQLARDHGLQHLPLHGFLLV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 844 NLASSYQLQGRWKEAE---VLNLQVVERrkqaLGPEHpeTLNSMSHLATTYLCQRRWKEAEELNVEVTRIQKQvlGPEHP 920
Cdd:pfam17874 127 GLADLLYEWNDLEEAEqhaQQGIQLGRQ----WEPDA--AVDAYVLLARIALAQGELEEALTLLRRAELLARQ--SFFHV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 921 DTL-----------FSMGNLASIcwkqGRWKEAEVLemqvmerrkqvlgPEHPDTLFS---MANLAFYWKSQGKTQAASA 986
Cdd:pfam17874 199 DWLanaervrvrlwLARGDLRAA----VRWLRAAEP-------------PSDADNHFLereLRNLARVLLALGRFDDALS 261
|
250
....*....|.
gi 1833963602 987 LLKQCLALQMK 997
Cdd:pfam17874 262 LLERLQNLAEQ 272
|
|
| Rnase_HI_RT_non_LTR |
cd09276 |
non-LTR RNase HI domain of reverse transcriptases; Ribonuclease H (RNase H) is classified into ... |
1118-1273 |
1.12e-03 |
|
non-LTR RNase HI domain of reverse transcriptases; Ribonuclease H (RNase H) is classified into two families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). Ribonuclease HI (RNase HI) is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as an adjunct domain to the reverse transcriptase gene in retroviruses, long-term repeat (LTR)-bearing retrotransposons and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamic acid residue (DEDD), are unvaried across all RNase H domains. The position of the RNase domain of non-LTR and LTR transposons is at the carboxyl terminal of the reverse transcriptase (RT) domain and their RNase domains group together, indicating a common evolutionary origin. Many non-LTR transposons have lost the RNase domain because their activity is at the nucleus and cellular RNase may suffice; however LTR retrotransposons always encode their own RNase domain because it requires RNase activity in RNA-protein particles in the cytoplasm. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription.
Pssm-ID: 260008 [Multi-domain] Cd Length: 131 Bit Score: 40.28 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1118 IYTDGAclgngEANPRAGCGVVFReeRSGRVGHFAFPLelqgptghPRPQTSNRAELRAVIAALQFRFWAGEGWTKVVIA 1197
Cdd:cd09276 2 IYTDGS-----KLEGSVGAGFVIY--RGGEVISRSYRL--------GTHASVFDAELEAILEALELALATARRARKVTIF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 1198 TDSEYVVEGatswskgwIRNGWRTSTGRPVKNKDLWKCLLgwcedaatTRAKTKLEFWRIPR----EWNAEADGWAKLAA 1273
Cdd:cd09276 67 TDSQSALQA--------LRNPRRSSGQVILIRILRLLRLL--------KAKGVKVRLRWVPGhvgiEGNEAADRLAKEAA 130
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
353-505 |
1.43e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.43 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 353 SPGRIAICGLGGVGKTQIALELAYRMRNRDHecSVLWISCTSYEsvEQAYMSIALKLGITDPKPVEVKQQVKVYLSQGST 432
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG--GVIYIDGEDIL--EEVLDQLLLIIVGGKKASGSGELRLRLALALARK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1833963602 433 ARW-LLVFDNADDMEMWKTADFLPESERGHILFTTRTRQVAVRLASSHVIMISEPDAetAVEILRRSLITGDLL 505
Cdd:smart00382 77 LKPdVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPAL--LRRRFDRRIVLLLIL 148
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
335-484 |
2.15e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 40.21 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 335 VGREEEISKIEGLImQKDSPGRIAICGLGGVGKTQIALELAYRMRNRDHecSVLWISCTSYesVEQAYMSIALKLGITDp 414
Cdd:cd00009 1 VGQEEAIEALREAL-ELPPPKNLLLYGPPGTGKTTLARAIANELFRPGA--PFLYLNASDL--LEGLVVAELFGHFLVR- 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 415 kpvevKQQVKVYLSQGSTarwlLVFDNADDMEMWKTADFLPESergHILFTTRTRQVAVRlasshVIMIS 484
Cdd:cd00009 75 -----LLFELAEKAKPGV----LFIDEIDSLSRGAQNALLRVL---ETLNDLRIDRENVR-----VIGAT 127
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
350-447 |
5.27e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.48 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 350 QKDSPGRIAICGLGGVGKTQIALElaYRMRNRDHECSVLWISCTSYESVEQAYMSIALKLGITDPKP---VEVKQQVKVY 426
Cdd:pfam13401 1 IRFGAGILVLTGESGTGKTTLLRR--LLEQLPEVRDSVVFVDLPSGTSPKDLLRALLRALGLPLSGRlskEELLAALQQL 78
|
90 100
....*....|....*....|.
gi 1833963602 427 LSQGSTARwLLVFDNADDMEM 447
Cdd:pfam13401 79 LLALAVAV-VLIIDEAQHLSL 98
|
|
| TPR_MalT |
pfam17874 |
MalT-like TPR region; This entry contains a series of TPR repeats. |
764-992 |
6.88e-03 |
|
MalT-like TPR region; This entry contains a series of TPR repeats.
Pssm-ID: 436107 [Multi-domain] Cd Length: 336 Bit Score: 40.37 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 764 TYLSQGRLTEAEKLAVEVLSIRErvlGSEHPDTLGSMSGLAATYLNQGRWKDAEKLQEQVMEICKQvlgLEDPR-TLTSI 842
Cdd:pfam17874 10 LAISKGDAERALELAEQALALLP---EDDLLARGLATFVLGEAYLCLGDLDAALQAMREAEALARR---ADSPHvTLWAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833963602 843 VNLASSYQLQGRWKEAEVLnlqvvERRKQALGPEHPETLNSMSHLATTYLCQ--RRW---KEAEElnvevtRIQK--QVL 915
Cdd:pfam17874 84 LQQGEILRAQGRLHQALET-----YQQALQLARDHGLQHLPLHGFLLVGLADllYEWndlEEAEQ------HAQQgiQLG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1833963602 916 GPEHPD-TLFSMGNLASICWKQGRWKEAEVLEMQVMERRKQvlGPEHPD-TLFSMANLAFYWKSQGKTQAASALLKQCL 992
Cdd:pfam17874 153 RQWEPDaAVDAYVLLARIALAQGELEEALTLLRRAELLARQ--SFFHVDwLANAERVRVRLWLARGDLRAAVRWLRAAE 229
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
333-395 |
9.05e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 38.64 E-value: 9.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1833963602 333 RFVGREEEISKIEGLI--MQKDSPGRIAICGLGGVGKTQIALELAYRMrnRDHECSVLWISCTSY 395
Cdd:pfam13191 1 RLVGREEELEQLLDALdrVRSGRPPSVLLTGEAGTGKTTLLRELLRAL--ERDGGYFLRGKCDEN 63
|
|
| |
