|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
373-686 |
0e+00 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 531.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 373 KLAEKPKKEGFFSRLKKGLLKTRVNIGSGFASIFSGKKIDDDLFEDLETQLLTADLGVDTTMKLIDSLTDAANRKQLKDG 452
Cdd:PRK10416 6 KKKKKEKKEGWFERLKKGLSKTRENFGEGINGLFAKKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKNLKDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 453 DALYDLMKQEMAAMLKTAEQPLEIrADKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVW 532
Cdd:PRK10416 86 EELKELLKEELAEILEPVEKPLNI-EEKKPFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAGDTFRAAAIEQLQVW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 533 GERNSIPVIAQHTGADSASVVFDAFQAAKARNVDVLIADTAGRLQNKDNLMQELEKIARVMKKIDPDAPHEVMLTIDAGT 612
Cdd:PRK10416 165 GERVGVPVIAQKEGADPASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVIKKADPDAPHEVLLVLDATT 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184249154 613 GQNAISQVNLFNQCVGLTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGIDDLRAFKSDDFIDALFSQDE 686
Cdd:PRK10416 245 GQNALSQAKAFHEAVGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFVDALLGGED 318
|
|
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
383-685 |
0e+00 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 530.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 383 FFSRLKKGLLKTRVNIGSGFASIFSG-KKIDDDLFEDLETQLLTADLGVDTTMKLIDSLTDAANRKQLKDGDALYDLMKQ 461
Cdd:COG0552 1 FFERLKEGLSKTRSGLGEKLKSLFSGkKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKDPEELKEALKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 462 EMAAMLKTAEQPLEIrADKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVI 541
Cdd:COG0552 81 ELLEILDPVDKPLAI-EEKKPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGERVGVPVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 542 AQHTGADSASVVFDAFQAAKARNVDVLIADTAGRLQNKDNLMQELEKIARVMKKIDPDAPHEVMLTIDAGTGQNAISQVN 621
Cdd:COG0552 160 AQKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKKLDPDAPHEVLLVLDATTGQNALSQAK 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184249154 622 LFNQCVGLTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGIDDLRAFKSDDFIDALFSQD 685
Cdd:COG0552 240 VFNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDALFGEE 303
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
410-682 |
6.12e-129 |
|
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and SRP54; both are GTPases. In E.coli, ftsY is an essential gene located in an operon with cell division genes ftsE and ftsX, but its apparent function is as the signal recognition particle docking protein. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 272883 [Multi-domain] Cd Length: 277 Bit Score: 382.37 E-value: 6.12e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 410 KIDDDLFEDLETQLLTADLGVDTTMKLIDSLTDAANRKQLKDGDALYDLMKQEMAAMLKTAE----QPLEIRADKKPFVI 485
Cdd:TIGR00064 1 KDDEDFFEELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEDLlkntDLELIVEENKPNVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 486 LMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKARNV 565
Cdd:TIGR00064 81 LFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGADPAAVAFDAIQKAKARNI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 566 DVLIADTAGRLQNKDNLMQELEKIARVMKKIDPDAPHEVMLTIDAGTGQNAISQVNLFNQCVGLTGITLSKLDGTAKGGV 645
Cdd:TIGR00064 161 DVVLIDTAGRLQNKVNLMDELKKIKRVIKKVDKDAPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGGI 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1184249154 646 IFAVADKFNIPIRYIGVGEGIDDLRAFKSDDFIDALF 682
Cdd:TIGR00064 241 ILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEALF 277
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
483-681 |
8.61e-110 |
|
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle (SRP) receptor (SR), is homologous to the SRP receptor alpha-subunit (SRalpha) of the eukaryotic SR. It interacts with the signal-recognition particle (SRP) and is required for the co-translational membrane targeting of proteins.
Pssm-ID: 349783 Cd Length: 199 Bit Score: 329.92 E-value: 8.61e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 483 FVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKA 562
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGADPAAVAFDAIQAAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 563 RNVDVLIADTAGRLQNKDNLMQELEKIARVMKKIDPDAPHEVMLTIDAGTGQNAISQVNLFNQCVGLTGITLSKLDGTAK 642
Cdd:cd17874 81 RGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKKKDPEAPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTAK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1184249154 643 GGVIFAVADKFNIPIRYIGVGEGIDDLRAFKSDDFIDAL 681
Cdd:cd17874 161 GGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
482-682 |
2.01e-96 |
|
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species. The GTPase domain is evolutionary related to P-loop NTPase domains found in a variety of other proteins.
Pssm-ID: 214940 Cd Length: 197 Bit Score: 295.47 E-value: 2.01e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 482 PFVILMVGVNGVGKTTTIGKLAKQFQ-NEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAA 560
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKlKGGKKVLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGADPVAVAKDAVELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 561 KARNVDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVNLFNQCVGLTGITLSKLDGT 640
Cdd:smart00962 81 KARGYDVVLIDTAGRLHNDENLMEELKKIKRVIK------PDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1184249154 641 AKGGVIFAVADKFNIPIRYIGVGEGIDDLRAFKSDDFIDALF 682
Cdd:smart00962 155 AKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLL 196
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
483-681 |
2.37e-91 |
|
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.
Pssm-ID: 459814 [Multi-domain] Cd Length: 193 Bit Score: 282.12 E-value: 2.37e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 483 FVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKA 562
Cdd:pfam00448 1 NVILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGADPAAVAFDAVEKAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 563 RNVDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVNLFNQCVGLTGITLSKLDGTAK 642
Cdd:pfam00448 81 ENYDVVLVDTAGRLQNDKNLMDELKKIKRVVA------PDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1184249154 643 GGVIFAVADKFNIPIRYIGVGEGIDDLRAFKSDDFIDAL 681
Cdd:pfam00448 155 GGAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
483-681 |
1.11e-81 |
|
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognate receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349769 [Multi-domain] Cd Length: 193 Bit Score: 256.92 E-value: 1.11e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 483 FVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKA 562
Cdd:cd03115 1 NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGTDPASIAQEAVEKAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 563 RNVDVLIADTAGRLQNKDNLMQELEKIARVmkkidpDAPHEVMLTIDAGTGQNAISQVNLFNQCVGLTGITLSKLDGTAK 642
Cdd:cd03115 81 EGYDVLLVDTAGRLQKDEPLMEELKKVKEV------ESPDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTKLDGTAK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1184249154 643 GGVIFAVADKFNIPIRYIGVGEGIDDLRAFKSDDFIDAL 681
Cdd:cd03115 155 GGAALSIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
350-683 |
2.07e-77 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 251.05 E-value: 2.07e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 350 AAEAEADRLEQERITAELAKEEAKLAEKPKKEGFFSRLKkgllktrvnigsgfASIFSGKKIDDDLfEDLETQLLTADLG 429
Cdd:PRK14974 16 VEEKIEEEEEEEAPEAEEEEEEEDEEEKKEKPGFFDKAK--------------ITEIKEKDIEDLL-EELELELLESDVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 430 VDTTMKLIDSL--------------TDAANRKQLKDgdALYDLMKQEmaamlKTAEQPLEIRADKKPFVILMVGVNGVGK 495
Cdd:PRK14974 81 LEVAEEILESLkeklvgkkvkrgedVEEIVKNALKE--ALLEVLSVG-----DLFDLIEEIKSKGKPVVIVFVGVNGTGK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 496 TTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKARNVDVLIADTAGR 575
Cdd:PRK14974 154 TTTIAKLAYYLKKNGFSVVIAAGDTFRAGAIEQLEEHAERLGVKVIKHKYGADPAAVAYDAIEHAKARGIDVVLIDTAGR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 576 LQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVNLFNQCVGLTGITLSKLDGTAKGGVIFAVADKFNI 655
Cdd:PRK14974 234 MHTDANLMDELKKIVRVTK------PDLVIFVGDALAGNDAVEQAREFNEAVGIDGVILTKVDADAKGGAALSIAYVIGK 307
|
330 340
....*....|....*....|....*...
gi 1184249154 656 PIRYIGVGEGIDDLRAFKSDDFIDALFS 683
Cdd:PRK14974 308 PILFLGVGQGYDDLIPFDPDWFVDKLLG 335
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
423-672 |
8.59e-63 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 214.88 E-value: 8.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 423 LLTADLGVDTTMKLIDSLTDAAN----RKQLKDGDALYDLMKQEMAAMLKTAEQPLEIrADKKPFVILMVGVNGVGKTTT 498
Cdd:COG0541 38 LLEADVNLKVVKDFIERVKERALgeevLKSLTPGQQVIKIVHDELVELLGGENEELNL-AKKPPTVIMMVGLQGSGKTTT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 499 IGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKARNVDVLIADTAGRLQN 578
Cdd:COG0541 117 AAKLAKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPVFPEEDGKDPVDIAKRALEYAKKNGYDVVIVDTAGRLHI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 579 KDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVNLFNQCVGLTGITLSKLDGTAKGGVIFAVADKFNIPIR 658
Cdd:COG0541 197 DEELMDELKAIKAAVN------PDETLLVVDAMTGQDAVNVAKAFNEALGLTGVILTKLDGDARGGAALSIRAVTGKPIK 270
|
250
....*....|....
gi 1184249154 659 YIGVGEGIDDLRAF 672
Cdd:COG0541 271 FIGTGEKLDDLEPF 284
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
484-675 |
3.79e-59 |
|
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349786 Cd Length: 193 Bit Score: 197.44 E-value: 3.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 484 VILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKAR 563
Cdd:cd18539 2 VILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQSPVDIAKRALEKAKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 564 NVDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVNLFNQCVGLTGITLSKLDGTAKG 643
Cdd:cd18539 82 GFDVVIVDTAGRLHIDEELMDELKEIKEVLN------PDEVLLVVDAMTGQDAVNVAKAFNERLGLTGVVLTKLDGDARG 155
|
170 180 190
....*....|....*....|....*....|..
gi 1184249154 644 GVIFAVADKFNIPIRYIGVGEGIDDLRAFKSD 675
Cdd:cd18539 156 GAALSIRHVTGKPIKFIGVGEKIEDLEPFHPD 187
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
409-678 |
2.51e-53 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 189.65 E-value: 2.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 409 KKIDDDLFEDLETQLLTADLGVDTTMKLIDSLTDAANRKQLKDG----DALYDLMKQEMAAMLKTAEQPLEIraDKKPFV 484
Cdd:PRK00771 20 EKTVKEVVKDIQRALLQADVNVKLVKELSKSIKERALEEEPPKGltprEHVIKIVYEELVKLLGEETEPLVL--PLKPQT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 485 ILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKarN 564
Cdd:PRK00771 98 IMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPFYGDPDNKDAVEIAKEGLEKFK--K 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 565 VDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVNLFNQCVGLTGITLSKLDGTAKGG 644
Cdd:PRK00771 176 ADVIIVDTAGRHALEEDLIEEMKEIKEAVK------PDEVLLVIDATIGQQAKNQAKAFHEAVGIGGIIITKLDGTAKGG 249
|
250 260 270
....*....|....*....|....*....|....
gi 1184249154 645 VIFAVADKFNIPIRYIGVGEGIDDLRAFKSDDFI 678
Cdd:PRK00771 250 GALSAVAETGAPIKFIGTGEKIDDLERFDPDRFI 283
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
483-681 |
6.48e-46 |
|
C-terminal domain of signal recognition particle receptor alpha subunit; The signal-recognition particle (SRP) receptor (SR) alpha-subunit (SRalpha) of the eukaryotic SR interacts with the signal-recognition particle (SRP) and is essential for the co-translational membrane targeting of proteins.
Pssm-ID: 349785 Cd Length: 204 Bit Score: 162.01 E-value: 6.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 483 FVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKA 562
Cdd:cd17876 1 YVIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRLGVELYEKGYGKDPAAVAKEAIKYARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 563 RNVDVLIADTAGRLQNKDNLMQELEKIARVMKkidPDApheVMLTIDAGTGQNAISQVNLFNQCV----------GLTGI 632
Cdd:cd17876 81 QGFDVVLIDTAGRMQNNEPLMRALAKLIKENN---PDL---VLFVGEALVGNDAVDQLKKFNQALadyspsdnprLIDGI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1184249154 633 TLSKLDgTA--KGGVIFAVADKFNIPIRYIGVGEGIDDLRAFKSDDFIDAL 681
Cdd:cd17876 155 VLTKFD-TIddKVGAALSMVYATGQPIVFVGTGQTYTDLKKLNVKAVVNSL 204
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
483-678 |
1.55e-45 |
|
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349784 Cd Length: 193 Bit Score: 160.44 E-value: 1.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 483 FVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKA 562
Cdd:cd17875 1 NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYGSYTEKDPVKIAKEGVEKFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 563 RNVDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVNLFNQCVGLTGITLSKLDGTAK 642
Cdd:cd17875 81 EKFDIIIVDTSGRHKQEEELFEEMKQISDAVK------PDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITKLDGHAK 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1184249154 643 -GGVIFAVAdKFNIPIRYIGVGEGIDDLRAFKSDDFI 678
Cdd:cd17875 155 gGGALSAVA-ATGAPIIFIGTGEHIDDLEPFDPKRFV 190
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
398-681 |
5.26e-36 |
|
signal recognition particle protein SRP54; This model represents examples from the eukaryotic cytosol of the signal recognition particle protein component, SRP54. This GTP-binding protein is a component of the eukaryotic signal recognition particle, along with several other protein subunits and a 7S RNA. Some species, including Arabidopsis, have several closely related forms. The extreme C-terminal region is glycine-rich and lower in complexity, poorly conserved between species, and excluded from this model.
Pssm-ID: 273615 [Multi-domain] Cd Length: 428 Bit Score: 140.74 E-value: 5.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 398 IGSGFASIFSGKKIDDD----LFEDLETQLLTADLGVDTTMKLIDSLTDAANRKQLKDGDALYDLMKQ----EMAAMLKT 469
Cdd:TIGR01425 9 LVTALRSMSSATVIDEEvintMLKEICTALLESDVNPKLVRQMRNNIKKKINLEDIASGINKRKLIQDavfeELCNLVDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 470 AEQPLEIRADKkPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADS 549
Cdd:TIGR01425 89 GVEAFTPKKGK-TCVIMFVGLQGAGKTTTCTKLAYYYKRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYGSYEESDP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 550 ASVVFDAFQAAKARNVDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVNLFNQCVGL 629
Cdd:TIGR01425 168 VKIASEGVEKFRKEKFDIIIVDTSGRHKQEKELFEEMQQVREAIK------PDSIIFVMDGSIGQAAFGQAKAFKDSVEV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1184249154 630 TGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGIDDLRAFKSDDFIDAL 681
Cdd:TIGR01425 242 GSVIITKLDGHAKGGGALSAVAATKSPIIFIGTGEHVDEFEIFDAEPFVSKL 293
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
413-682 |
6.87e-32 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 127.29 E-value: 6.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 413 DDLFEDLETQLLTADLGVDTTMKLIDSLtdaanrKQLKDGDALYDLMKQEMAAMLKTAEQPLEiradKKPFVILMVGVNG 492
Cdd:COG1419 105 PPELAELLERLLEAGVSPELARELLEKL------PEDLSAEEAWRALLEALARRLPVAEDPLL----DEGGVIALVGPTG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 493 VGKTTTIGKLAKQF-QNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVfdafqaAKARNVDVLIAD 571
Cdd:COG1419 175 VGKTTTIAKLAARFvLRGKKKVALITTDTYRIGAVEQLKTYARILGVPVEVAYDPEELKEAL------ERLRDKDLVLID 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 572 TAGRLQNKDNLMQELEKIARVMKKIdpdaphEVMLTIDAGT-GQNAISQVNLFNQcVGLTGITLSKLDGTAKGGVIFAVA 650
Cdd:COG1419 249 TAGRSPRDPELIEELKALLDAGPPI------EVYLVLSATTkYEDLKEIVEAFSS-LGLDGLILTKLDETASLGSILNLL 321
|
250 260 270
....*....|....*....|....*....|...
gi 1184249154 651 DKFNIPIRYIGVGEGI-DDLRAFKSDDFIDALF 682
Cdd:COG1419 322 IRTGLPLSYITNGQRVpEDIEVADPERLARLLL 354
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
484-669 |
4.63e-28 |
|
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP)-type GTPase that is essential for the placement and assembly of polar flagella. It is similar to the 54 kd subunit (SRP54) of the signal recognition particle (SRP) that mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR).
Pssm-ID: 349782 [Multi-domain] Cd Length: 189 Bit Score: 111.49 E-value: 4.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 484 VILMVGVNGVGKTTTIGKLAKQFQ-NEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAqhtgADSAsvvfDAFQAAKA 562
Cdd:cd17873 2 VIALVGPTGVGKTTTLAKLAARYVlKKGKKVALITTDTYRIGAVEQLKTYAEIMGIPVEV----AEDP----EDLADALE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 563 R--NVDVLIADTAGRLQNKDNLMQELEKIARVMKKIdpdaphEVMLTIDAGT-GQNAISQVNLFnQCVGLTGITLSKLDG 639
Cdd:cd17873 74 RlsDRDLILIDTAGRSPRDKEQLEELKELLGAGEDI------EVHLVLSATTkAKDLKEIIERF-SPLGYRGLILTKLDE 146
|
170 180 190
....*....|....*....|....*....|.
gi 1184249154 640 TAKGGVIFAVADKFNIPIRYIGVGEGI-DDL 669
Cdd:cd17873 147 TTSLGSVLSVLAESQLPVSYVTTGQRVpEDI 177
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
305-683 |
1.07e-21 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 98.43 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 305 IVA---EAEAERLEQQRIAAEQAEAERLE--QERIAQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKPK 379
Cdd:PRK05703 47 VTAavdEDETPKKNPVLREEKRKPAKSILslQALLEKRPSRTNSQDALLQAENALPEWKKELEKPSEPKEEEPKAAAESK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 380 -KEGFFSRLK------KGLLKTRVnigsgfASIFSGKKIDDdLFEDLETQLLTADLGVDTTMKLIDSLTDAANRKQLKDG 452
Cdd:PRK05703 127 vVQKELDELRdelkelKNLLEDQL------SGLRQVERIPP-EFAELYKRLKRSGLSPEIAEKLLKLLLEHMPPRERTAW 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 453 DALYDLMKQemaaMLKTAEQPLEIRadKKpfVILMVGVNGVGKTTTIGKLAKQF--QNEGKSVMLAAGDTFRAAAVEQLQ 530
Cdd:PRK05703 200 RYLLELLAN----MIPVRVEDILKQ--GG--VVALVGPTGVGKTTTLAKLAARYalLYGKKKVALITLDTYRIGAVEQLK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 531 VWGERNSIPVIaqhtgadsasVVFDAFQAAKA----RNVDVLIADTAGRLQNKDNLMQELEKIARvmkkiDPDAPHEVML 606
Cdd:PRK05703 272 TYAKIMGIPVE----------VVYDPKELAKAleqlRDCDVILIDTAGRSQRDKRLIEELKALIE-----FSGEPIDVYL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 607 TIDAgTGQN----AIsqVNLFNQCvGLTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGI-DDLRAFKSDDFIDAL 681
Cdd:PRK05703 337 VLSA-TTKYedlkDI--YKHFSRL-PLDGLIFTKLDETSSLGSILSLLIESGLPISYLTNGQRVpDDIKVANPEELVRLL 412
|
..
gi 1184249154 682 FS 683
Cdd:PRK05703 413 LG 414
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
57-372 |
7.66e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.70 E-value: 7.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 57 KAQAERLAIEKANAELLAKEQAEAQAQQQAQAARLAEQEAQMRLEQERMAAQRAEQQRLDTEREQAEQDEKLAIEkanae 136
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE----- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 137 llakeqaeaqvqqqaqaarlaeqeaqmRLEQERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIA 216
Cdd:COG1196 310 ---------------------------RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 217 AEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGE 296
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184249154 297 AERAEQERIVAEAEAERLEQQRIAAEQAEAERLEQERIAQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEA 372
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
15-429 |
2.16e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.54 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 15 KSDKKQAEADKQQALAQQQEAERLAAEKAEAEREEQARIAAEKAQAERLAIEKANAELLAKEQAEAQAQQQAQAARLAEQ 94
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 95 EAQMRLEQERMAAQRAEQQRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEK 174
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 175 AEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAER 254
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 255 AEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAERLEQERI 334
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 335 AQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKPKKEGFFSRLKKGLLKTRVNIGSGFASIFSGKKIDDD 414
Cdd:COG1196 539 ALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL 618
|
410
....*....|....*
gi 1184249154 415 LFEDLETQLLTADLG 429
Cdd:COG1196 619 GDTLLGRTLVAARLE 633
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
15-381 |
2.77e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 96.36 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 15 KSDKKQAEADKQQALAQQQEAERLAAEKAEAEREEQARIAAEKAQAERL---AIEKANAELLAKEQAEAQAQQQAQAARL 91
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAkkkAEEAKKAEEAKKKAEEAKKADEAKKKAE 1480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 92 AEQEAQMRLEQERMAAQRAEQQRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVA 171
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKA 1560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 172 AE--KAEAERLEQERIAQEQAEAERAEQ-ERIAAEKAEADRLEQERIAAEQAEAErvEQERIAAEQAEAERVEQERIAQ- 247
Cdd:PTZ00121 1561 EEkkKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKA--EEAKIKAEELKKAEEEKKKVEQl 1638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 248 ---EQAEAERAEQQRIAAEQAEAERLEQQRIAAEQA----EAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIA 320
Cdd:PTZ00121 1639 kkkEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKkkaeEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA 1718
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184249154 321 AEQAEAErlEQERIAQEQAEAERAEQERIAAEAEADRLEQERItAELAKEEAKLAEKPKKE 381
Cdd:PTZ00121 1719 EELKKAE--EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI-AHLKKEEEKKAEEIRKE 1776
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
18-381 |
2.12e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 93.67 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 18 KKQAEADKQQALAQQQEAERLAAEKAEAEREEQARIAAEKAQAERLAIEKANAELLAKEQAEAQAQQQAQAARLAEQEAQ 97
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 98 MRLEQERMAAQRAEQ-QRLDTEREQAEQDEKLAIEKANAELL---AKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAE 173
Cdd:PTZ00121 1408 DELKKAAAAKKKADEaKKKAEEKKKADEAKKKAEEAKKADEAkkkAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE 1487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 174 ---KAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQA 250
Cdd:PTZ00121 1488 akkKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE 1567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 251 EAERAEQQRIAAEQ--AEAERLEQQRIaaeqAEAERLEQERIAQEQGEAERAEQERIVAEaEAERLEQQRIAAEQAEAER 328
Cdd:PTZ00121 1568 EAKKAEEDKNMALRkaEEAKKAEEARI----EEVMKLYEEEKKMKAEEAKKAEEAKIKAE-ELKKAEEEKKKVEQLKKKE 1642
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1184249154 329 LEQERIAQEQAEAEraEQERIAAEAEADRLEQERITAELAK----EEAKLAEKPKKE 381
Cdd:PTZ00121 1643 AEEKKKAEELKKAE--EENKIKAAEEAKKAEEDKKKAEEAKkaeeDEKKAAEALKKE 1697
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
15-381 |
4.11e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.51 E-value: 4.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 15 KSDKKQAEADKQQALAQQQEAERLAAEKAEAEREEQARIAAE--KAQAERL---AIEKANAELLAKEQAEAQAQQQAQAA 89
Cdd:PTZ00121 1360 EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEedKKKADELkkaAAAKKKADEAKKKAEEKKKADEAKKK 1439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 90 RLAEQEAQMRLEQERMAAQRAEQQRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLaeqEAQMRLEQER 169
Cdd:PTZ00121 1440 AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA---EAKKKADEAK 1516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 170 VAAEKAEAERLEQERIAQEQAEAERAEQERIAAE--KAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIaq 247
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADElkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI-- 1594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 248 EQAEAERAEQQRIAAEQAEAErlEQQRIAAEQAEAErlEQERIAQEQGEAERAEQERIVAEAEAERlEQQRIAAEQAEAE 327
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKA--EEAKIKAEELKKA--EEEKKKVEQLKKKEAEEKKKAEELKKAE-EENKIKAAEEAKK 1669
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1184249154 328 RLEQERIAQEQAEAEraEQERIAAEAEADRLEQERITAELAK---EEAKLAEKPKKE 381
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAE--EDEKKAAEALKKEAEEAKKAEELKKkeaEEKKKAEELKKA 1724
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-381 |
5.79e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.13 E-value: 5.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 2 AKKSKFMSWLGFGKSDKKQAEADKQQALAQQQEAERLAAEKAEAEREEQARIAAEKAQAERLaieKANAELLAKEQAEAQ 81
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA---KKKAEEKKKADEAKK 1438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 82 AQQQAQAARLAEQEAQMRLEQERMAAQRAEQQRLDTEREQAEQDEKLAIEKANAELLAKeqaeaqvqqqAQAARLAEQEA 161
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKK----------KADEAKKAAEA 1508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 162 QMRLEQERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAE--KAEADRLEQERIAAEQAEAERVEQERIAAEQAEAER 239
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADElkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK 1588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 240 VEQERIAQEQA-----------EAERAEQQRIAAEQAEAErlEQQRIAAEQAEAERLEQERIAQEQGEAEraEQERIVAE 308
Cdd:PTZ00121 1589 AEEARIEEVMKlyeeekkmkaeEAKKAEEAKIKAEELKKA--EEEKKKVEQLKKKEAEEKKKAEELKKAE--EENKIKAA 1664
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184249154 309 AEAERLEQQRIAAEQA----EAERLEQERIAQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKPKKE 381
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEEAkkaeEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
319-574 |
4.13e-18 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 85.08 E-value: 4.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 319 IAAEQAEAERLEQERIAQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKPKKEGFFSRLKKgLLKTRVNI 398
Cdd:TIGR03499 48 AAIDEEEAAAASAEEEASKALEQADPKPLSATAEPLELPAPQEEPAAPAAQAAEPLLPEEELRKELEALRE-LLERLLAG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 399 GSgfasifsgKKIDDDLFEDLETQLLTADLGVDTTMKLIDSLtdaanrKQLKDGDALYDLMKQEMAAMLKTAeqPLEIRA 478
Cdd:TIGR03499 127 LA--------WLQRPPERAKLYERLLEAGVSEELARELLEKL------PEDADAEDAWRWLREALEGMLPVK--PEEDPI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 479 DKKPFVILMVGVNGVGKTTTIGKLAKQF--QNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADsasvvfda 556
Cdd:TIGR03499 191 LEQGGVIALVGPTGVGKTTTLAKLAARFalEHGKKKVALITTDTYRIGAVEQLKTYAEILGIPVKVARDPKE-------- 262
|
250 260
....*....|....*....|
gi 1184249154 557 FQAAKA--RNVDVLIADTAG 574
Cdd:TIGR03499 263 LREALDrlRDKDLILIDTAG 282
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
18-395 |
5.07e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.04 E-value: 5.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 18 KKQAEADKQQALAQQQEAERLAAEKAEAEREEQARIAAEKAQAERlaiEKANAELLAKEQAEAQAQQQAQAARLAEQEAQ 97
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA---EAAADEAEAAEEKAEAAEKKKEEAKKKADAAK 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 98 MRLEQERMAAQraEQQRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQmrlEQERVAAEKAEA 177
Cdd:PTZ00121 1385 KKAEEKKKADE--AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD---EAKKKAEEAKKA 1459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 178 ERLEQEriAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEqaEAERVEQERIAQEQAEAERAEQ 257
Cdd:PTZ00121 1460 EEAKKK--AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD--EAKKAEEAKKADEAKKAEEAKK 1535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 258 QRiaaeqaEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRiAAEQAEAERLEQERIAQE 337
Cdd:PTZ00121 1536 AD------EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMK 1608
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184249154 338 QAEAERAEQERIAAEaEADRLEQERITAELAK----EEAKLAEKPKKEGFFSRLKKGLLKTR 395
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAE-ELKKAEEEKKKVEQLKkkeaEEKKKAEELKKAEEENKIKAAEEAKK 1669
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
55-381 |
4.81e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.41 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 55 AEKAQAERLAIEKANAELLAKEQAEAQAQQQAQAARLAEQEAQMRLEQERmaaqRAEQQRLDTEREQAEQDEKLAIEKAN 134
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAK----KAEAVKKAEEAKKDAEEAKKAEEERN 1250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 135 AELLAKEQAEAQVQQQAQAARLAEQEAQmRLEQERVAAEKAEAERLeqeRIAQEQAEAERAEQEriAAEKAEADRLEQEr 214
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFARRQAAIKAEEAR-KADELKKAEEKKKADEA---KKAEEKKKADEAKKK--AEEAKKADEAKKK- 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 215 iaAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQ 294
Cdd:PTZ00121 1324 --AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 295 GEAERAEQERIVAEAEAERLEQQRIAAEQAEAERLEQERIAQEQA-EAERAEQERIAAEAEADRLEQERITAELAK--EE 371
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAdEAKKKAEEAKKAEEAKKKAEEAKKADEAKKkaEE 1481
|
330
....*....|
gi 1184249154 372 AKLAEKPKKE 381
Cdd:PTZ00121 1482 AKKADEAKKK 1491
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
164-370 |
6.70e-15 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 78.63 E-value: 6.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 164 RLEQERVAAEKAEAER-LEQERIAQEQAEAERAEQERIAAEKAEADRL------EQERIAAEQA--EAERVEQERIAAE- 233
Cdd:pfam17380 295 KMEQERLRQEKEEKAReVERRRKLEEAEKARQAEMDRQAAIYAEQERMamererELERIRQEERkrELERIRQEEIAMEi 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 234 -------------QAEAERVEQE-RIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERiaqeQGEAER 299
Cdd:pfam17380 375 srmrelerlqmerQQKNERVRQElEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER----AREMER 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184249154 300 AEQERIVAEAEAERLEQQRiaaEQAEAERLEQERIAQEQAEAERAEQERIAAEAEADR---LEQERITAELAKE 370
Cdd:pfam17380 451 VRLEEQERQQQVERLRQQE---EERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKqamIEEERKRKLLEKE 521
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
56-381 |
8.60e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.64 E-value: 8.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 56 EKAQAERLAIEKANAELLAKEQAEAQAQQQAQAARLAEQEAQMRLEQERMA--AQRAEQQRLDTEREQAEQDEKLAIEKa 133
Cdd:PTZ00121 1080 DFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAeeARKAEDARKAEEARKAEDAKRVEIAR- 1158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 134 naellaKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEKAEAE---RLEQERIAQEQ---AEAERAEQERIAAEKAEA 207
Cdd:PTZ00121 1159 ------KAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEdarKAEAARKAEEErkaEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 208 DRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQ 287
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAE 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 288 ERIAQEQGEaERAEQERIVAEAEAERLEQQRIAAEQAEAErleqeriaqEQAEAERAEQERIAAEAEADRLEQERITAEL 367
Cdd:PTZ00121 1313 EAKKADEAK-KKAEEAKKKADAAKKKAEEAKKAAEAAKAE---------AEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
330
....*....|....*..
gi 1184249154 368 AK---EEAKLAEKPKKE 381
Cdd:PTZ00121 1383 AKkkaEEKKKADEAKKK 1399
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
15-381 |
2.18e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.90 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 15 KSDKKQAEADKQQALAQQQEAErlaaEKAEAEREEQARIAAEKAQAERLAIEKANAELLAKEQAEAQAQQQAQAARLAEQ 94
Cdd:COG1196 403 EELEEAEEALLERLERLEEELE----ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 95 EAQMRLEQERMAAQRAEQQRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAqmRLEQERVAAEK 174
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA--AALQNIVVEDD 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 175 AEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAER 254
Cdd:COG1196 557 EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 255 AEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAERLEQERI 334
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1184249154 335 AQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKPKKE 381
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
17-381 |
3.07e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.72 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 17 DKKQAEADKQQALAQQQEAERLAAEKAEAEREEQARIAAEKAQAERLAIEKANAELLAKEQAEAQAQQQAQAARLAEQEA 96
Cdd:PTZ00121 1198 DARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA 1277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 97 QMRLEQERMAAQR-AEQQRLDTEREQAEQDEKLAIEKANAELLAKEQAEA---------QVQQQAQAARLAEQEAQMRLE 166
Cdd:PTZ00121 1278 RKADELKKAEEKKkADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkkadaakkKAEEAKKAAEAAKAEAEAAAD 1357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 167 QERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAE----KAEADRLEQERIAAEQAEAERVEQERIAAEQAE-----A 237
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADeakkKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKkadeaK 1437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 238 ERVEQERIAQE----QAEAERAEQQRIAAEQA-EAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEaEAE 312
Cdd:PTZ00121 1438 KKAEEAKKADEakkkAEEAKKAEEAKKKAEEAkKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD-EAK 1516
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184249154 313 RLEQQRIAAEQAEAE---RLEQERIAQEQAEAE---RAEQERIAAEA----EADRLEQERITAELAKEEAKLAEKPKKE 381
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEeakKADEAKKAEEKKKADelkKAEELKKAEEKkkaeEAKKAEEDKNMALRKAEEAKKAEEARIE 1595
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
55-381 |
3.55e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.72 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 55 AEKAQAERLAIEKANAELLAKEQAEAQAQQQAQAARLAEQEAQMRLEQERMA--AQRAEQQRLDTEREQAEqDEKLAIEK 132
Cdd:PTZ00121 1103 AKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVeiARKAEDARKAEEARKAE-DAKKAEAA 1181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 133 ANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEKAEAERLEQ-ERIAQEQAEAERAEQERIAAEKAEADRLE 211
Cdd:PTZ00121 1182 RKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKaEEAKKDAEEAKKAEEERNNEEIRKFEEAR 1261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 212 QERIAAEQAeAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEqaEAERLEQQRIAAEQAEAERLEQERIA 291
Cdd:PTZ00121 1262 MAHFARRQA-AIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAE--EAKKADEAKKKAEEAKKKADAAKKKA 1338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 292 QEQGEAERAEQERivAEAEAERLEQQRIAAEQAEAERLEQERIAQEQAEaeRAEQERIAAEAEADRLEQERITAELAK-- 369
Cdd:PTZ00121 1339 EEAKKAAEAAKAE--AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK--KAEEKKKADEAKKKAEEDKKKADELKKaa 1414
|
330
....*....|..
gi 1184249154 370 EEAKLAEKPKKE 381
Cdd:PTZ00121 1415 AAKKKADEAKKK 1426
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
99-381 |
4.93e-14 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 75.55 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 99 RLEQERMAAQRAEQQRLDTEREQAEQDEKlaiekanaellAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEKAEAE 178
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVERRRKLEEAEK-----------ARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 179 RLEQERIAQE--------------QAEAERAEQERIAAEKAEADRLEQERIAAEQ-AEAERVEQERIAAEQAEAERVEQE 243
Cdd:pfam17380 364 RIRQEEIAMEisrmrelerlqmerQQKNERVRQELEAARKVKILEEERQRKIQQQkVEMEQIRAEQEEARQREVRRLEEE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 244 RIAQ----EQAEAERAEQQRIAAEQAEAER---LEQQRIAAEQAEAERLEQERIAQEQGEAERA--EQERIVAEAEAERL 314
Cdd:pfam17380 444 RAREmervRLEEQERQQQVERLRQQEEERKrkkLELEKEKRDRKRAEEQRRKILEKELEERKQAmiEEERKRKLLEKEME 523
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184249154 315 EQQRIAAEQAEAERLEQERIAQEQAEAERAEQERI-AAEAEADRLEQERITAELAKeEAKLAEKPKKE 381
Cdd:pfam17380 524 ERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMrKATEERSRLEAMEREREMMR-QIVESEKARAE 590
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
9-381 |
2.42e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.02 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 9 SWLGFGKSDKKQAEADKQQALAQQQEAERLAAEKAEAEREEQARIAAEKAQAERLAIEKANAELLAKEQAEAQAQQQAQA 88
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRV 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 89 ARLAEQEAQMRLEQERMA--AQRAEQQRLDTEREQAEQDEKlAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLE 166
Cdd:PTZ00121 1155 EIARKAEDARKAEEARKAedAKKAEAARKAEEVRKAEELRK-AEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 167 QERVAAE---KAEAERLEQE--------------RIAQEQAEAER-AEQERIAAEKAEADRLEQERIAAEQAEAERVEQE 228
Cdd:PTZ00121 1234 EAKKDAEeakKAEEERNNEEirkfeearmahfarRQAAIKAEEARkADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 229 RIAAEQAEAERVEQERIAQE-QAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVA 307
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAaKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA 1393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 308 EAEAERLEQQRIAAEQ---AEAERLEQERIAQEQAEAERAEQERIAAEA-----EADRLEQERITAELAK---EEAKLAE 376
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADElkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEakkadEAKKKAEEAKKAEEAKkkaEEAKKAD 1473
|
....*
gi 1184249154 377 KPKKE 381
Cdd:PTZ00121 1474 EAKKK 1478
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
172-395 |
5.00e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.87 E-value: 5.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 172 AEKAEAERLEQERIAQEQAEaeRAEQERIAAEkaeADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEqae 251
Cdd:PTZ00121 1103 AKKTETGKAEEARKAEEAKK--KAEDARKAEE---ARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAED--- 1174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 252 AERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAE---RAEQERIVAEA-----EAERLEQQRIAAEQ 323
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEdakKAEAVKKAEEAkkdaeEAKKAEEERNNEEI 1254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 324 AEAERLEQERIAQEQA-----EAERAEQERIAAEA----EADRLEQERITAELAK--EEAKLAEKPKKEGFFSRLKKGLL 392
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAaikaeEARKADELKKAEEKkkadEAKKAEEKKKADEAKKkaEEAKKADEAKKKAEEAKKKADAA 1334
|
...
gi 1184249154 393 KTR 395
Cdd:PTZ00121 1335 KKK 1337
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
188-373 |
8.87e-13 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 71.14 E-value: 8.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 188 EQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIaaEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEA 267
Cdd:pfam15709 326 EKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQL--ERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 268 ERLEQQRIAAEQAEAER-----------LEQERIAQEQGEAERAEQERIVAEAEAERL-EQQRIAAEQAEAERLEQERIA 335
Cdd:pfam15709 404 EEEERKQRLQLQAAQERarqqqeefrrkLQELQRKKQQEEAERAEAEKQRQKELEMQLaEEQKRLMEMAEEERLEYQRQK 483
|
170 180 190
....*....|....*....|....*....|....*....
gi 1184249154 336 QEQAEAERAE-QERIAAEAEADRLEQERITaELAKEEAK 373
Cdd:pfam15709 484 QEAEEKARLEaEERRQKEEEAARLALEEAM-KQAQEQAR 521
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
481-607 |
2.14e-12 |
|
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: 65.09 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 481 KPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVwgernsIPVIAQHTGADSASVVFDAFQAA 560
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLL------IIVGGKKASGSGELRLRLALALA 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1184249154 561 KARNVDVLIADTAGRLQNKDNLMQELEKI-ARVMKKIDPDAPHEVMLT 607
Cdd:smart00382 75 RKLKPDVLILDEITSLLDAEQEALLLLLEeLRLLLLLKSEKNLTVILT 122
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
160-377 |
2.23e-12 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 70.36 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 160 EAQMRLE--QERVAAEKAE-AERLEQ--ERIAQEQAEAERAEQERIAAEKAEADRL----------EQERIAAEQAEAER 224
Cdd:PRK05035 450 EAKARFEarQARLEREKAArEARHKKaaEARAAKDKDAVAAALARVKAKKAAATQPivikagarpdNSAVIAAREARKAQ 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 225 VEQERIAAEQAEAERVEQERIAQ--EQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAE--RLEQERIAQEQGEAERA 300
Cdd:PRK05035 530 ARARQAEKQAAAAADPKKAAVAAaiARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKakKAAQQAASAEPEEQVAE 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 301 EQERIVAEAEAERLEQQRIAAEQAEAERLEQE--RIAQEQAEAERAEQERIAAEAEADRLEQE------RITAELAKEEA 372
Cdd:PRK05035 610 VDPKKAAVAAAIARAKAKKAEQQANAEPEEPVdpRKAAVAAAIARAKARKAAQQQANAEPEEAedpkkaAVAAAIARAKA 689
|
....*
gi 1184249154 373 KLAEK 377
Cdd:PRK05035 690 KKAAQ 694
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
17-361 |
2.73e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 17 DKKQAEADKQQALAQQQEAERLAAEKAEAEREEQARIAAEKAQAERLAIEKANAELLAKEQAEAQAQQQAQAARLAEQEA 96
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 97 QMRL------------EQERMAAQRAEQQRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMR 164
Cdd:COG1196 518 GLRGlagavavligveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAI 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 165 LEQERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQER 244
Cdd:COG1196 598 GAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 245 IAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQA 324
Cdd:COG1196 678 EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP 757
|
330 340 350
....*....|....*....|....*....|....*....
gi 1184249154 325 EAERLEQERIAQEQAEAERAEQERI--AAEAEADRLEQE 361
Cdd:COG1196 758 EPPDLEELERELERLEREIEALGPVnlLAIEEYEELEER 796
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
54-376 |
4.19e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 54 AAEKAQAERLAIEKANAELLAKEQAEAQAQQQAQAARLAEQEAQMRLEQERMAAQRAEQqrlDTEREQAEQDEKLAIEKA 133
Cdd:TIGR02168 664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE---ELSRQISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 134 NAELLAKEQAEAQVQQQAQAARLAEQEAqmRLEQERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQE 213
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEE--RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 214 riAAEQAEAERVEQERIAAEQAEAERVEQeRIAQEQAEAERAE------QQRIAAEQAEAERLEQQRIAAEQAEAERLEQ 287
Cdd:TIGR02168 819 --AANLRERLESLERRIAATERRLEDLEE-QIEELSEDIESLAaeieelEELIEELESELEALLNERASLEEALALLRSE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 288 ERIAQEqgEAERAEQERIVAEAEAERLeQQRIAAEQAEAERLEQER--IAQEQAEAERAEQERIAAEAEADRLEQERITA 365
Cdd:TIGR02168 896 LEELSE--ELRELESKRSELRRELEEL-REKLAQLELRLEGLEVRIdnLQERLSEEYSLTLEEAEALENKIEDDEEEARR 972
|
330
....*....|.
gi 1184249154 366 ELAKEEAKLAE 376
Cdd:TIGR02168 973 RLKRLENKIKE 983
|
|
| SRP54_N |
smart00963 |
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle ... |
397-467 |
4.69e-12 |
|
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species.
Pssm-ID: 214941 [Multi-domain] Cd Length: 77 Bit Score: 61.80 E-value: 4.69e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184249154 397 NIGSGFASIFSGKKIDDDLFEDLETQLLTADLGVDTTMKLIDSLTDAANR---KQLKDGDALYDLMKQEMAAML 467
Cdd:smart00963 4 ALGKLLGELFLTEKDDEELLEELEEALLEADVGVEVVKEIIERVKEKAKGevlKGLTPKQEVKKILKEELVKIL 77
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
17-381 |
6.30e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.40 E-value: 6.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 17 DKKQAEADKQQALAQQQEAERLAAEKAEAEREEQARIAAEKAQ-AERLAIEKANAELLAKEQAEAQAQQQAQAARLAEQ- 94
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHfARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEk 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 95 ----EAQMRLEQERMAAQ---RAEQ--QRLDTEREQAEQDEKLA------IEKANAELLAKEQAEAQVQQQAQAARLAEQ 159
Cdd:PTZ00121 1302 kkadEAKKKAEEAKKADEakkKAEEakKKADAAKKKAEEAKKAAeaakaeAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 160 EAQMRLEQERVAAE---KAEAERLEQERIAQEQAEAERAEQ-ERIAAEKAEADRLEQERIAAEQA-EAERVEQERIAAEQ 234
Cdd:PTZ00121 1382 AAKKKAEEKKKADEakkKAEEDKKKADELKKAAAAKKKADEaKKKAEEKKKADEAKKKAEEAKKAdEAKKKAEEAKKAEE 1461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 235 AEaERVEQERIAQE----QAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERivAEAE 310
Cdd:PTZ00121 1462 AK-KKAEEAKKADEakkkAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK--KADE 1538
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184249154 311 AERLEQQRIAAEQAEAERLEQERIAQEQAEAERAEQERIAAEAEADRLEQ------ERITAELAKEEAKLAEKPKKE 381
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeeariEEVMKLYEEEKKMKAEEAKKA 1615
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
97-381 |
1.05e-11 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 66.87 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 97 QMRLEQERMAAQRAEQQRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLE-QERVAAEKA 175
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEiVERIQEEDQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 176 EAERLEQERIAQEQAEAERAEQERIA--AEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIA----QEQ 249
Cdd:pfam13868 116 AEAEEKLEKQRQLREEIDEFNEEQAEwkELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARlraqQEK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 250 AEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEqgeaERAEQERIVAEAEAERLEQQRIAAEQAEAERL 329
Cdd:pfam13868 196 AQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQ----AREEQIELKERRLAEEAEREEEEFERMLRKQA 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1184249154 330 EQERIAQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKPKKE 381
Cdd:pfam13868 272 EDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREE 323
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
484-668 |
1.13e-10 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 63.99 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 484 VILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAqhtgADSASVVFDAFQAAKAR 563
Cdd:PRK12726 208 IISLIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTDTFRSGAVEQFQGYADKLDVELIV----ATSPAELEEAVQYMTYV 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 564 N-VDVLIADTAGRlqnkdNLMQElEKIARVMKKIDPDAPHEVMLTIDAGTGQNAISQVNLFNQCVGLTGITLSKLDGTAK 642
Cdd:PRK12726 284 NcVDHILIDTVGR-----NYLAE-ESVSEISAYTDVVHPDLTCFTFSSGMKSADVMTILPKLAEIPIDGFIITKMDETTR 357
|
170 180
....*....|....*....|....*.
gi 1184249154 643 GGVIFAVADKFNIPIRYIGVGEGIDD 668
Cdd:PRK12726 358 IGDLYTVMQETNLPVLYMTDGQNITE 383
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-377 |
1.71e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 174 KAEAERLEQERIAQEQAEAErAEQERIAAEKaEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAE 253
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAE-LEKALAELRK-ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 254 RAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAqEQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAERLEQER 333
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI-EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1184249154 334 IAQEQAEAERAEQ--ERIAAEAEADRLEQERITAELAKEEAKLAEK 377
Cdd:TIGR02168 833 IAATERRLEDLEEqiEELSEDIESLAAEIEELEELIEELESELEAL 878
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
56-354 |
1.81e-10 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 63.01 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 56 EKAQAERLAIEKANAELLAKEQAEAQAQQQAQAARLAEQEAQMRLEQERMAAQRAEQQRLDTEREQAEQDEKLAI-EKAN 134
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIvERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 135 AELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEKAEAERLE--QERIAQEQAEAERAEQERIAAEKAEADRL-- 210
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILeyLKEKAEREEEREAEREEIEEEKEREIARLra 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 211 EQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERI 290
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQA 271
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184249154 291 AQEQGEAERAEQERIVAEAEAERLEQQRIAAEQA-EAERLEQERIAQEQAEAERAEQERIAAEAE 354
Cdd:pfam13868 272 EDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQrAAEREEELEEGERLREEEAERRERIEEERQ 336
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
202-361 |
2.22e-10 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 63.35 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 202 AEKAEADRLEQERIAAEQAEaervEQERIAAEQAEAErVEQERIAQEQAEAERAEqqriAAEQAEAERleqQRIAAEQA- 280
Cdd:COG2268 201 ARIAEAEAERETEIAIAQAN----REAEEAELEQERE-IETARIAEAEAELAKKK----AEERREAET---ARAEAEAAy 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 281 EAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAERLEQERIAQEQAEAErAEQERIAAEAEADRLEQ 360
Cdd:COG2268 269 EIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAE-AIRAKGLAEAEGKRALA 347
|
.
gi 1184249154 361 E 361
Cdd:COG2268 348 E 348
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
168-370 |
2.90e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 168 ERVAAEKAEAERLEQE-RIAQEQAEA---ERAEQERIAAEKAEADRLEQERIAAEQAEAERveqeRIAAEQAEAERVEQE 243
Cdd:COG4913 228 DALVEHFDDLERAHEAlEDAREQIELlepIRELAERYAAARERLAELEYLRAALRLWFAQR----RLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 244 riaQEQAEAERAE-QQRIAAEQAEAERLEQQRIAAEQAEAERLEQErIAQEQGEAERAEQERIVAEAEAERLEQQRIAAE 322
Cdd:COG4913 304 ---LARLEAELERlEARLDALREELDELEAQIRGNGGDRLEQLERE-IERLERELEERERRRARLEALLAALGLPLPASA 379
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1184249154 323 QAEAERLEQERIAQEQAEAERAEQERIAAEAEADRLEQERITAELAKE 370
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
184-289 |
3.15e-10 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 63.60 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 184 RIAQEQAEAERAEQERIAAEKAEADRLEQERIA-AEQAEAERVEQERIaaEQAEAERVEQERIAQEQAEAERAEQQRIaa 262
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIErLEREERERLERERM--ERIERERLERERLERERLERDRLERDRL-- 504
|
90 100
....*....|....*....|....*..
gi 1184249154 263 eqaeaERLEQQRIaaEQAEAERLEQER 289
Cdd:PTZ00266 505 -----DRLERERV--DRLERDRLEKAR 524
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
326-668 |
3.45e-10 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 62.43 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 326 AERLEQERIAQEQAeAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKPKKEGFfsrlkKGLLktrvnigsgfasi 405
Cdd:PRK14722 5 ARRLPADEPAAAKP-ALRLPEDTAAAVADAVKARIERIVNDTVMQELGSLRELMEEQF-----AGLM------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 406 FSGKKIDDDLFEDLETQLLTADLGVDTTMKLIDSLTDAANRKQLkdgDALYDLMKQEMAAMLKT--AEQPLEIRADkkpf 483
Cdd:PRK14722 66 WNERQRRNPVHGALTKYLFAAGFSAQLVRMIVDNLPEGEGYDTL---DAAADWAQSVLAANLPVldSEDALMERGG---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 484 VILMVGVNGVGKTTTIGKLAKQ--FQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVfdafqaAK 561
Cdd:PRK14722 139 VFALMGPTGVGKTTTTAKLAARcvMRFGASKVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDGGDLQLAL------AE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 562 ARNVDVLIADTAGRLQNKDNLMQELEKIArvmkkiDPDAPHEVMLTIDAGTGQNAISQV-NLFNQCVG--------LTGI 632
Cdd:PRK14722 213 LRNKHMVLIDTIGMSQRDRTVSDQIAMLH------GADTPVQRLLLLNATSHGDTLNEVvQAYRSAAGqpkaalpdLAGC 286
|
330 340 350
....*....|....*....|....*....|....*.
gi 1184249154 633 TLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGIDD 668
Cdd:PRK14722 287 ILTKLDEASNLGGVLDTVIRYKLPVHYVSTGQKVPE 322
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
160-381 |
5.21e-10 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 63.09 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 160 EAQMRLEQERVAAEKAEAErLEQERIAQEQAEAERAEQEriAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAER 239
Cdd:TIGR00927 666 EAEQEGETETKGENESEGE-IPAERKGEQEGEGEIEAKE--ADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVE 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 240 VEQERIAQ----EQAEAERAEQQRIAAEQAEAERLEQQriaAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLE 315
Cdd:TIGR00927 743 DEGEGEAEgkheVETEGDRKETEHEGETEAEGKEDEDE---GEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQS 819
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184249154 316 QQRIAAEQAEAERLEQERIAQEQAEAERAEqERIAAEAEADRLEQERITAELAKEEAKLAEKPKKE 381
Cdd:TIGR00927 820 ETQADDTEVKDETGEQELNAENQGEAKQDE-KGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEE 884
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
175-452 |
7.36e-10 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 62.54 E-value: 7.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 175 AEAERLEQERIAQEQAEAERAEQERIA-AEKAEAD--RLEQER------IAAEQAEAERVEQERIA--------AEQAEA 237
Cdd:NF012221 1536 ATSESSQQADAVSKHAKQDDAAQNALAdKERAEADrqRLEQEKqqqlaaISGSQSQLESTDQNALEtngqaqrdAILEES 1615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 238 ERVEQERI----------AQEQAEAERAEQQR----------IAAEQAEAERLEQQRIA-AEQAEAERLEQERIAQEQGE 296
Cdd:NF012221 1616 RAVTKELTtlaqgldaldSQATYAGESGDQWRnpfagglldrVQEQLDDAKKISGKQLAdAKQRHVDNQQKVKDAVAKSE 1695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 297 AERAEQERIVAEAEaerleqQRIAAEQAEAERLEQERIAQEQaEAERAEQERIAAEAEAD-RLEQERITAEL----AKEE 371
Cdd:NF012221 1696 AGVAQGEQNQANAE------QDIDDAKADAEKRKDDALAKQN-EAQQAESDANAAANDAQsRGEQDASAAENkanqAQAD 1768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 372 AKLA-----EKPKKEGFFSRLKKGLLKTRVNIG--SGFASIFSGKKIDDDLFEDLETQLLTAdlgvdttmklIDSLTDAA 444
Cdd:NF012221 1769 AKGAkqdesDKPNRQGAAGSGLSGKAYSVEGVAepGSHINPDSPAAADGRFSEGLTEQEQEA----------LEGATNAV 1838
|
....*...
gi 1184249154 445 NRKQLKDG 452
Cdd:NF012221 1839 NRLQINAG 1846
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
95-391 |
9.22e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 9.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 95 EAQMRLEQERMAAQRAEQQRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEK 174
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 175 AEAERLEQERiaqEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQeriAQEQAEAER 254
Cdd:TIGR02168 316 RQLEELEAQL---EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ---LETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 255 AEQQRIAAEQAEAERLEQQrIAAEQAEAERLEQERIAQEQG--EAERAEQERIVAE--AEAERLEQQRIAAEQAEAERLE 330
Cdd:TIGR02168 390 QLELQIASLNNEIERLEAR-LERLEDRRERLQQEIEELLKKleEAELKELQAELEEleEELEELQEELERLEEALEELRE 468
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184249154 331 QERIAQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKPKKEGFFSRLKKGL 391
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELI 529
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
484-669 |
1.07e-09 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 61.54 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 484 VILMVGVNGVGKTTTIGKLAKQF--QNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPViaqHTgADSASVVFDAFQaaK 561
Cdd:PRK12727 352 VIALVGPTGAGKTTTIAKLAQRFaaQHAPRDVALVTTDTQRVGGREQLHSYGRQLGIAV---HE-ADSAESLLDLLE--R 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 562 ARNVDVLIADTAGRLQNKDNLMQELE--KIARVMKKidpdaphevMLTIDAGTGQNAISQVNLFNQCVGLTGITLSKLDG 639
Cdd:PRK12727 426 LRDYKLVLIDTAGMGQRDRALAAQLNwlRAARQVTS---------LLVLPANAHFSDLDEVVRRFAHAKPQGVVLTKLDE 496
|
170 180 190
....*....|....*....|....*....|.
gi 1184249154 640 TAKGGVIFAVADKFNIPIRYIGVGEGI-DDL 669
Cdd:PRK12727 497 TGRFGSALSVVVDHQMPITWVTDGQRVpDDL 527
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
168-599 |
1.10e-09 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 61.21 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 168 ERVAAEKAEAERLEQERiAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQ 247
Cdd:COG3064 6 EEKAAEAAAQERLEQAE-AEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 248 EQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAE 327
Cdd:COG3064 85 AAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 328 RLEQERIAQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKPKKEGFFSRLKKGLLKTRVNIGSGFASIFS 407
Cdd:COG3064 165 AAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 408 GKKIDDDLFEDLETQLLTADLGVDTTMKLIDSLTDAANRKQLKDGDALYDLMKQEMAAMLKTAEQPLEIRADKKPFVILM 487
Cdd:COG3064 245 LGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 488 VGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKARNVDV 567
Cdd:COG3064 325 GALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLR 404
|
410 420 430
....*....|....*....|....*....|..
gi 1184249154 568 LIADTAGRLQNKDNLMQELEKIARVMKKIDPD 599
Cdd:COG3064 405 LDLGAALLEAASAVELRVLLALAGAAGAVVAL 436
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
101-345 |
1.17e-09 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 61.94 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 101 EQERMAAQRAEQ-QRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEKAEAER 179
Cdd:TIGR00927 648 EGERPTEAEGENgEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTE 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 180 LEQERIAQEQAEAERAEQERIA----AEKAEADRLEQERIAAEQAEAERVEQEriaaEQAEAERVEQERIAQEQAEAERA 255
Cdd:TIGR00927 728 DEGEIETGEEGEEVEDEGEGEAegkhEVETEGDRKETEHEGETEAEGKEDEDE----GEIQAGEDGEMKGDEGAEGKVEH 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 256 EQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEqERIVAEAEAERLEQQRIAAEQAEAERLEQERIA 335
Cdd:TIGR00927 804 EGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDE-KGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEE 882
|
250
....*....|
gi 1184249154 336 QEQAEAERAE 345
Cdd:TIGR00927 883 EEEEEEENEE 892
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
169-381 |
2.08e-09 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 61.16 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 169 RVAAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEaervEQERIAAEQAEAErVEQERIAQE 248
Cdd:TIGR00927 619 RPVAKVMALGDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEG----ETETKGENESEGE-IPAERKGEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 249 QAEAERAEQQriAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQE-----RIVAEAEAERLEQQRIAAEQ 323
Cdd:TIGR00927 694 EGEGEIEAKE--ADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEgeaegKHEVETEGDRKETEHEGETE 771
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 324 AEAERLEQER--IAQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKPKKE 381
Cdd:TIGR00927 772 AEGKEDEDEGeiQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDE 831
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
249-362 |
2.54e-09 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 60.52 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 249 QAEAERAEQQRIAAEQAEAERLEQQRIaaEQAEAERLEQERIaqeqgeaERAEQERIvaeaeaERLEQQRIAAEQAEAER 328
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKIL--EKKRIERLEREER-------ERLERERM------ERIERERLERERLERER 493
|
90 100 110
....*....|....*....|....*....|....
gi 1184249154 329 LEQERIAQEQaeAERAEQERIaAEAEADRLEQER 362
Cdd:PTZ00266 494 LERDRLERDR--LDRLERERV-DRLERDRLEKAR 524
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
214-318 |
2.84e-09 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 60.52 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 214 RIAAEQAEAERVEQERIAAEQAEAERVEQERIAQ-EQAEAERAEQQRIaaEQAEAERLEQQRIAAEQAEAERLEQERIaq 292
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIERlEREERERLERERM--ERIERERLERERLERERLERDRLERDRL-- 504
|
90 100
....*....|....*....|....*.
gi 1184249154 293 eqgeaERAEQERiVAEAEAERLEQQR 318
Cdd:PTZ00266 505 -----DRLERER-VDRLERDRLEKAR 524
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
259-384 |
3.45e-09 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 60.14 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 259 RIAAEQAEAERLEQQRIAAEQAEAERLEQERIaqeqgeaERAEQERIvaeaeaERLEQQRIaaEQAEAERLEQERIAQEQ 338
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRI-------ERLEREER------ERLERERM--ERIERERLERERLERER 493
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1184249154 339 AEAERAEQERIaaeaeaDRLEQERITaelaKEEAKLAEKPKKEGFF 384
Cdd:PTZ00266 494 LERDRLERDRL------DRLERERVD----RLERDRLEKARRNSYF 529
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
398-463 |
4.35e-09 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 53.24 E-value: 4.35e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184249154 398 IGSGFASIFSGKKIDDDLFED----LETQLLTADLGVDTTMKLIDSLTDAA-NRKQLKDGDALYDLMKQEM 463
Cdd:pfam02881 5 LSSLFKGLRGKGKIDEEDLEEalkeLEEALLEADVGVEVVKKIIERLREKAvGEKKLKPPQEVKKILKEEL 75
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
54-342 |
4.97e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 59.75 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 54 AAEKAQAERLAIEKaNAELlakeqaeaqaqqqaqaarlaeqeAQMRLEQERMAAQRAEQQRLDTEREQAEQDEKLAIEKA 133
Cdd:pfam17380 333 AAIYAEQERMAMER-EREL-----------------------ERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 134 NAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEKAEAERLEQERIAQEQA-EAERAEQERIA-AEKAEADRLE 211
Cdd:pfam17380 389 QKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERArEMERVRLEEQErQQQVERLRQQ 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 212 QERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEaerlEQQRIAAEQAEAERLEQERIA 291
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEME----ERQKAIYEEERRREAEEERRK 544
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1184249154 292 QEQGEAERAEQERIVAEAEaerlEQQRIAAEQAEAERLEQeRIAQEQAEAE 342
Cdd:pfam17380 545 QQEMEERRRIQEQMRKATE----ERSRLEAMEREREMMRQ-IVESEKARAE 590
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
187-377 |
5.06e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 59.58 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 187 QEQAEAERAEQERIAAEKAeadrleQERIAAEQAEAERVEQERIA-AEQAEAERVEQERIAQEQAEAERAEQQRIAAEQA 265
Cdd:PRK05035 433 QAKAEIRAIEQEKKKAEEA------KARFEARQARLEREKAAREArHKKAAEARAAKDKDAVAAALARVKAKKAAATQPI 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 266 EAERLEQQRIAAEQAEAE-RLEQERIAQEQGEAERAEQER------IVAEAEAERLEQQRIAAEQAEAERLEQERIAQEQ 338
Cdd:PRK05035 507 VIKAGARPDNSAVIAAREaRKAQARARQAEKQAAAAADPKkaavaaAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAI 586
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1184249154 339 AEAERAEQERIAAEAEAD------RLEQERITAELAKEEAKLAEK 377
Cdd:PRK05035 587 ARAKAKKAAQQAASAEPEeqvaevDPKKAAVAAAIARAKAKKAEQ 631
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
479-666 |
8.52e-09 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 57.06 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 479 DKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHtgaDSASVVFDAFQ 558
Cdd:PRK06731 72 EKEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVR---DEAAMTRALTY 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 559 AAKARNVDVLIADTAGRLQNKDnlmQELEKIARVMKKIDPDApheVMLTIDAGTGQNAISQVNLFNQCVGLTGITLSKLD 638
Cdd:PRK06731 149 FKEEARVDYILIDTAGKNYRAS---ETVEEMIETMGQVEPDY---ICLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFD 222
|
170 180
....*....|....*....|....*...
gi 1184249154 639 GTAKGGVIFAVADKFNIPIRYIGVGEGI 666
Cdd:PRK06731 223 ETASSGELLKIPAVSSAPIVLMTDGQDV 250
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
184-374 |
8.70e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.89 E-value: 8.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 184 RIAQEQAEAERAEQERIAAEKAEADRLEQErIAAEQAEAERVEQERIAAEQAEAERVEQERIA---QEQAEAERAEQQRI 260
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQK-QAAEQERLKQLEKERLAAQEQKKQAEEAAKQAalkQKQAEEAAAKAAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 261 AAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAE-QAEAERLEQERIAQEQA 339
Cdd:PRK09510 145 AKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEaKKKAAAEAKKKAAAEAK 224
|
170 180 190
....*....|....*....|....*....|....*
gi 1184249154 340 EAERAEQERIAAEAEADRLEQERITAELAKEEAKL 374
Cdd:PRK09510 225 AAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
186-377 |
9.57e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 9.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 186 AQEQAEAERAEQERIAAEKAEAdrleQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQA 265
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEA----EERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 266 --EAERLEQQrIAAEQAEAERLEQERIAQeQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAERLEQERIAQEQAEAER 343
Cdd:COG4913 684 sdDLAALEEQ-LEELEAELEELEEELDEL-KGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD 761
|
170 180 190
....*....|....*....|....*....|....
gi 1184249154 344 AEQERIAAEAEAdrlEQERITAELAKEEAKLAEK 377
Cdd:COG4913 762 AVERELRENLEE---RIDALRARLNRAEEELERA 792
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
64-362 |
1.04e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 64 AIEKANAELLAKEQAEAQAQQQAQAARLAEQEAQMRLEQ-----ERMAAQRAE-QQRLDTEREQAEQ--DEKLAIEKANA 135
Cdd:PRK04863 349 KIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAaeeevDELKSQLADyQQALDVQQTRAIQyqQAVQALERAKQ 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 136 ELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQ--ERVAAEKAEAERLEQ--ERIAQEQAEAERAEQERIAAEKAEadRLE 211
Cdd:PRK04863 429 LCGLPDLTADNAEDWLEEFQAKEQEATEELLSleQKLSVAQAAHSQFEQayQLVRKIAGEVSRSEAWDVARELLR--RLR 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 212 QERIAAEQAEAERV---EQERIAAEQAEAERVEQE---RIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERL 285
Cdd:PRK04863 507 EQRHLAEQLQQLRMrlsELEQRLRQQQRAERLLAEfckRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQ 586
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184249154 286 EQERIAQEQGEAERAEQERIVAEAEAERLEQQrIAAEQAEAERLEQERiaQEQAEAER-AEQERIAAEAEADRLEQER 362
Cdd:PRK04863 587 QLEQLQARIQRLAARAPAWLAAQDALARLREQ-SGEEFEDSQDVTEYM--QQLLEREReLTVERDELAARKQALDEEI 661
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
164-332 |
1.06e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 57.96 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 164 RLEQERVAAEKAEAERLEQERIAQEQAEAERAEQEriaaekAEADR-LEQERIAAEQAEAERVEQEriaaEQAEAERVEQ 242
Cdd:COG2268 193 KIAEIIRDARIAEAEAERETEIAIAQANREAEEAE------LEQEReIETARIAEAEAELAKKKAE----ERREAETARA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 243 ERIAQEQAEAERAEQQrIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQErIVAEAEAERLEQQRIAae 322
Cdd:COG2268 263 EAEAAYEIAEANAERE-VQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAE-AEAEAEAEAIRAKGLA-- 338
|
170
....*....|
gi 1184249154 323 QAEAERLEQE 332
Cdd:COG2268 339 EAEGKRALAE 348
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
106-381 |
1.06e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 57.62 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 106 AAQRAEQQRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRlEQERVAAEKAEAERLEQERI 185
Cdd:pfam13868 25 DAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIE-EREQKRQEEYEEKLQEREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 186 AQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERiaaeqaEAERVEQERIAQEQAEAERAEQQRiAAEQA 265
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEK------EEEREEDERILEYLKEKAEREEER-EAERE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 266 EAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERleqqriaaEQAEAERLEQERIAQEQAEAERAE 345
Cdd:pfam13868 177 EIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKER--------EEAEKKARQRQELQQAREEQIELK 248
|
250 260 270
....*....|....*....|....*....|....*.
gi 1184249154 346 QERIAAEAEADRLEQERITAELAKEEAKLAEKPKKE 381
Cdd:pfam13868 249 ERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKR 284
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
196-386 |
1.21e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 196 EQERIAAEKAEADRLEQERIAAEQaEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRI 275
Cdd:PTZ00121 1078 DFDFDAKEDNRADEATEEAFGKAE-EAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEI 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 276 AAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEqaEAERLEQERIAQEQAEAE---RAEQERIAAE 352
Cdd:PTZ00121 1157 ARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAE--AARKAEEERKAEEARKAEdakKAEAVKKAEE 1234
|
170 180 190
....*....|....*....|....*....|....
gi 1184249154 353 AEADRLEQERITAELAKEEAKLAEKPKKEGFFSR 386
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARR 1268
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
484-666 |
1.28e-08 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 57.67 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 484 VILMVGVNGVGKTTTIGKLA-KQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTgadsasvvFDAFQAAKA 562
Cdd:PRK12724 225 VVFFVGPTGSGKTTSIAKLAaKYFLHMGKSVSLYTTDNYRIAAIEQLKRYADTMGMPFYPVKD--------IKKFKETLA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 563 RNVDVLI-ADTAGRLQNKdnlMQELEKIARVMKKIDPDAPHEVMLTIDAGTGQNAISQVNLFNQCVGLTGITLSKLDGTA 641
Cdd:PRK12724 297 RDGSELIlIDTAGYSHRN---LEQLERMQSFYSCFGEKDSVENLLVLSSTSSYHHTLTVLKAYESLNYRRILLTKLDEAD 373
|
170 180
....*....|....*....|....*
gi 1184249154 642 KGGVIFAVADKFNIPIRYIGVGEGI 666
Cdd:PRK12724 374 FLGSFLELADTYSKSFTYLSVGQEV 398
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
479-666 |
1.34e-08 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 57.77 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 479 DKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHtgaDSASVVFDAFQ 558
Cdd:PRK11889 238 EKEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVR---DEAAMTRALTY 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 559 AAKARNVDVLIADTAGRlqnKDNLMQELEKIARVMKKIDPDApheVMLTIDAGTGQNAISQVNLFNQCVGLTGITLSKLD 638
Cdd:PRK11889 315 FKEEARVDYILIDTAGK---NYRASETVEEMIETMGQVEPDY---ICLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFD 388
|
170 180
....*....|....*....|....*...
gi 1184249154 639 GTAKGGVIFAVADKFNIPIRYIGVGEGI 666
Cdd:PRK11889 389 ETASSGELLKIPAVSSAPIVLMTDGQDV 416
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
212-435 |
1.95e-08 |
|
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.
Pssm-ID: 411439 [Multi-domain] Cd Length: 1306 Bit Score: 57.80 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 212 QERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAER-AEQQRIAAEQAEAERLEQ-QRIAAEQAEAERLEQER 289
Cdd:NF033875 80 QKDTTSQPTKVEEVASEKNGAEQSSATPNDTTNAQQPTVGAEKsAQEQPVVSPETTNEPLGQpTEVAPAENEANKSTSIP 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 290 IAQEQGEAERAEQER------IVAEAEAERL---EQQRIAAEQAEAERLEQE---RIAQEQAEAeRAEQERIAAE----A 353
Cdd:NF033875 160 KEFETPDVDKAVDEAkkdpniTVVEKPAEDLgnvSSKDLAAKEKEVDQLQKEqakKIAQQAAEL-KAKNEKIAKEnaeiA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 354 EADRLEQERITAELAK------EEAKLAEKPKKEGFFSRlkkgllkTRVNIGSGFASIFSGKKIDDDLFEDL---ETQLL 424
Cdd:NF033875 239 AKNKAEKERYEKEVAEynkhknENGYVNEAISKNLVFDQ-------SVVTKDTKISSIKGGKFIKATDFNKVnagDSKDI 311
|
250
....*....|.
gi 1184249154 425 TADLGVDTTMK 435
Cdd:NF033875 312 FTKLSKDMGGK 322
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
112-318 |
2.27e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 112 QQRLDTEREQAEQDEKlaIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEKAEAERLEQERiaqEQAE 191
Cdd:COG4913 241 HEALEDAREQIELLEP--IRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEL---ERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 192 AERAEQEriaaekAEADRLEQERIAAEQAEAERVEQERiaaEQAEAERVEQERIAQEQAEAerAEQQRIAAEQAEAERLE 271
Cdd:COG4913 316 ARLDALR------EELDELEAQIRGNGGDRLEQLEREI---ERLERELEERERRRARLEAL--LAALGLPLPASAEEFAA 384
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1184249154 272 QQRIAAEQAEAERLEQERIAQEQGEAERAEQErivAEAEAERLEQQR 318
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRD---LRRELRELEAEI 428
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
164-259 |
3.53e-08 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 57.05 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 164 RLEQERVAAEKAEAERLEQERIAQ-EQAEAERAEQERIaaEKAEADRLEQERIAAEQAEAERVEQERIaaeqaeaERVEQ 242
Cdd:PTZ00266 439 RIEKENAHRKALEMKILEKKRIERlEREERERLERERM--ERIERERLERERLERERLERDRLERDRL-------DRLER 509
|
90
....*....|....*..
gi 1184249154 243 ERIaqEQAEAERAEQQR 259
Cdd:PTZ00266 510 ERV--DRLERDRLEKAR 524
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
95-379 |
3.58e-08 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 56.95 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 95 EAQMRLEQermAAQRAEQQRLDTEREQAEQDEK-LAIEKANAELLAKEQAEAQVQQQAQAARLaeqEAQMRLEQERVAAE 173
Cdd:NF033838 143 EATKKVEE---AEKKAKDQKEEDRRNYPTNTYKtLELEIAESDVEVKKAELELVKEEAKEPRD---EEKIKQAKAKVESK 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 174 KAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEqeriAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAE 253
Cdd:NF033838 217 KAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVA----TSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSSVGE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 254 R---AEQQRIAAEQAEAER--LEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAER 328
Cdd:NF033838 293 EtlpSPSLKPEKKVAEAEKkvEEAKKKAKDQKEEDRRNYPTNTYKTLELEIAESDVKVKEAELELVKEEAKEPRNEEKIK 372
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1184249154 329 LEQERIAQEQAEAERAEQ---ERIAAEAEAdrleqERITAELAKEEAKLAEKPK 379
Cdd:NF033838 373 QAKAKVESKKAEATRLEKiktDRKKAEEEA-----KRKAAEEDKVKEKPAEQPQ 421
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
104-377 |
4.14e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.88 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 104 RMAAQRAE--QQRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRL------EQERVAAEKA 175
Cdd:COG3096 275 RHANERRElsERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLvqtalrQQEKIERYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 176 EAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAER---VEQER-IAAEQA-----EAERVEQ---- 242
Cdd:COG3096 355 DLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQaldVQQTRaIQYQQAvqaleKARALCGlpdl 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 243 ------ERIAQEQAEAERAEQQRIAAEQ------AEAERLEQ-----QRIAAE--------------------QAEAERL 285
Cdd:COG3096 435 tpenaeDYLAAFRAKEQQATEEVLELEQklsvadAARRQFEKayelvCKIAGEversqawqtarellrryrsqQALAQRL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 286 EQerIAQEQGEAERAEQERIVAEAEAERLeQQRIAAEQAEAERLEQEriaQEQAEAERAEQERIAAEAEADRLEQERITA 365
Cdd:COG3096 515 QQ--LRAQLAELEQRLRQQQNAERLLEEF-CQRIGQQLDAAEELEEL---LAELEAQLEELEEQAAEAVEQRSELRQQLE 588
|
330
....*....|..
gi 1184249154 366 ELAKEEAKLAEK 377
Cdd:COG3096 589 QLRARIKELAAR 600
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
227-382 |
7.14e-08 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 56.16 E-value: 7.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 227 QERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEaerlEQQRIAAEQAEAErLEQERIAQEQGEAErAEQERIV 306
Cdd:TIGR00927 632 KGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEG----ETETKGENESEGE-IPAERKGEQEGEGE-IEAKEAD 705
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184249154 307 AEAEAERLEQQRIAAEQAEAERLEQERIAQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKPKKEG 382
Cdd:TIGR00927 706 HKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEG 781
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
201-377 |
7.34e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 54.85 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 201 AAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQA 280
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 281 EAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAERLEQERIAQEQAEAERAEQERIAAEAEADRLEQ 360
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKA 205
|
170
....*....|....*..
gi 1184249154 361 ERITAELAKEEAKLAEK 377
Cdd:TIGR02794 206 AAEAAAKAEAEAAAAAA 222
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
214-380 |
1.03e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.81 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 214 RIAAEQAEAERVEQER------IAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQ 287
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRkkkeqqQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 288 ERIAQEqgEAERAEQERIVAEAEAERLEQQRIAAEQAEAERLEQERIAQEQAEAERAEQERIAAEAEADRLEQERITAEL 367
Cdd:PRK09510 146 KAKAEA--EAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEA 223
|
170
....*....|...
gi 1184249154 368 AKEEAKLAEKPKK 380
Cdd:PRK09510 224 KAAAAKAAAEAKA 236
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
171-365 |
1.24e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 54.08 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 171 AAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQE-- 248
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEak 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 249 -QAEAERAEQQRIAAEQAEAERLEQQRiaaeQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAE 327
Cdd:TIGR02794 126 aKQAAEAKAKAEAEAERKAKEEAAKQA----EEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAA 201
|
170 180 190
....*....|....*....|....*....|....*...
gi 1184249154 328 RLEQERIAQEQAEAERAEQERIAAEAEADRLEQERITA 365
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFG 239
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
456-666 |
1.25e-07 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 54.52 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 456 YDLMKQEMAA-MLKTAEQPLEIRADKKPFVILMVGVNGVGKTTTIGKLAKQF----QNEGKSVMLAAGDTFRAAAVEQLQ 530
Cdd:PRK12723 147 YDKVRDSVIIyIAKTIKCSGSIIDNLKKRVFILVGPTGVGKTTTIAKLAAIYginsDDKSLNIKIITIDNYRIGAKKQIQ 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 531 VWGERNSIPVIAQHTGADSASVVFDafqaakARNVDVLIADTAGRlQNKDNLmqELEKIARVMKKIDPDAphEVMLTIDA 610
Cdd:PRK12723 227 TYGDIMGIPVKAIESFKDLKEEITQ------SKDFDLVLVDTIGK-SPKDFM--KLAEMKELLNACGRDA--EFHLAVSS 295
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1184249154 611 GTGQNAISQVNLFNQCVGLTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGI 666
Cdd:PRK12723 296 TTKTSDVKEIFHQFSPFSYKTVIFTKLDETTCVGNLISLIYEMRKEVSYVTDGQIV 351
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
244-381 |
1.73e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.04 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 244 RIAQEQAEAERAEQQRIAAEQAEAERLeQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQ 323
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEEL-QQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAA 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1184249154 324 AEAERLEQERIAQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKPKKE 381
Cdd:PRK09510 145 AKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK 202
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
54-317 |
2.29e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 54.18 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 54 AAEKAQA------ERLAIEKAnaellakeqaeaqaqqqaqaarlaeqeaqmrlEQERMAAQRAEQQRLDTEREQAEQDEK 127
Cdd:PRK05035 447 KAEEAKArfearqARLEREKA--------------------------------AREARHKKAAEARAAKDKDAVAAALAR 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 128 LAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEA 207
Cdd:PRK05035 495 VKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEE 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 208 DRLEQERIAAEQAEAE--RVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQA-EAERLEQQRIAAEQAEAER 284
Cdd:PRK05035 575 VDPKKAAVAAAIARAKakKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANaEPEEPVDPRKAAVAAAIAR 654
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1184249154 285 LEQERIAQEQGEAERAEQERI--------VAEAEAERLEQQ 317
Cdd:PRK05035 655 AKARKAAQQQANAEPEEAEDPkkaavaaaIARAKAKKAAQQ 695
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
97-328 |
2.63e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 53.80 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 97 QMRLEQERMAAQRAEQQRLDTEREQAEQDEKLAIEKANAEllakeqaeaqvqqqaqaaRLAEQEAQMRLEQERVAAE-KA 175
Cdd:pfam15709 330 QEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLE------------------RAEKMREELELEQQRRFEEiRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 176 EAERLEQERIAQEQAEAERAEQERIAAEKAeadRLEQERIAAEQAEAERVEQeriaaeQAEAERVEQERIAQEQAEAERA 255
Cdd:pfam15709 392 RKQRLEEERQRQEEEERKQRLQLQAAQERA---RQQQEEFRRKLQELQRKKQ------QEEAERAEAEKQRQKELEMQLA 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184249154 256 EQQRIAAEQAEAERLeqqriaaeqaeaERLEQERIAQEQGEAEraEQERIVAEAEAERLEQQRIAAEQAEAER 328
Cdd:pfam15709 463 EEQKRLMEMAEEERL------------EYQRQKQEAEEKARLE--AEERRQKEEEAARLALEEAMKQAQEQAR 521
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
246-381 |
2.83e-07 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 53.87 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 246 AQEQAeaerAEQQRIAAEQAEAERLEQQRIAaEQAEAErleQERIAQEQGEAERAEQE---RIVAEAEAErleqqriaae 322
Cdd:PTZ00491 663 SQEAA----ARHQAELLEQEARGRLERQKMH-DKAKAE---EQRTKLLELQAESAAVEssgQSRAEALAE---------- 724
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 323 qAEAERLEQERiAQEQAEAeRAEQERIAAEAEADRLEQER-ITAELAKEEAKLAEKPKKE 381
Cdd:PTZ00491 725 -AEARLIEAEA-EVEQAEL-RAKALRIEAEAELEKLRKRQeLELEYEQAQNELEIAKAKE 781
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
192-376 |
2.90e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 52.93 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 192 AERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLE 271
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 272 QQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAERLEQERIAQEQAEAERAEQERIAA 351
Cdd:TIGR02794 127 KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAA 206
|
170 180
....*....|....*....|....*
gi 1184249154 352 EAEADRLEQERITAELAKEEAKLAE 376
Cdd:TIGR02794 207 AEAAAKAEAEAAAAAAAEAERKADE 231
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
216-362 |
3.43e-07 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 53.75 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 216 AAEQAEAERVEQERIAAEQAEAERVEQERiAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERiAQEQG 295
Cdd:PRK12678 66 AAATPAAPAAAARRAARAAAAARQAEQPA-AEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAAR-RGAAR 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184249154 296 EAERAEQERIVAEAEAERLEQQRIAAEQAEAERLEQERiAQEQAEAERAEQERIAAEAEADRLEQER 362
Cdd:PRK12678 144 KAGEGGEQPATEARADAAERTEEEERDERRRRGDREDR-QAEAERGERGRREERGRDGDDRDRRDRR 209
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
167-360 |
3.76e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.80 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 167 QERVAAEKAEAERLEQERIAQEQ----AEAERAEQER-------IAAEKAEADRLEQ-----ERIAAEQAEAERVEQ--- 227
Cdd:COG3096 440 EDYLAAFRAKEQQATEEVLELEQklsvADAARRQFEKayelvckIAGEVERSQAWQTarellRRYRSQQALAQRLQQlra 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 228 -----ERIAAEQAEAERVEQE---RIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAER 299
Cdd:COG3096 520 qlaelEQRLRQQQNAERLLEEfcqRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAA 599
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184249154 300 AEQERIVAEAEAERLEQQ-------RIAAEQAEAERLEQERiaQEQAEAERAEQERIAAEAEADRLEQ 360
Cdd:COG3096 600 RAPAWLAAQDALERLREQsgealadSQEVTAAMQQLLERER--EATVERDELAARKQALESQIERLSQ 665
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
237-373 |
4.19e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 52.95 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 237 AERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQR------IAAEQAEAERLEQEriAQEQGEAERAEQERIVAEAE 310
Cdd:COG2268 195 AEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEReietarIAEAEAELAKKKAE--ERREAETARAEAEAAYEIAE 272
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184249154 311 AERLEQQRIAAEQAEAERleqeRIAQEQAEAERAEQE-----RIAAEAEADRLEQE-RITAELAKEEAK 373
Cdd:COG2268 273 ANAEREVQRQLEIAERER----EIELQEKEAEREEAEleadvRKPAEAEKQAAEAEaEAEAEAIRAKGL 337
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
161-362 |
5.30e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 161 AQMRLEQERVAAEKAEAERL-EQERIAQEQAEAERAEQERIAAEKAEADRlEQERIAAEQAEAERVEQEriaAEQAEAER 239
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLvEAEDRIERLEERREDLEELIAERRETIEE-KRERAEELRERAAELEAE---AEEKREAA 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 240 VEQERIAQEQAEAERAEQQRIAAEQAEAERLEqqRIAAEQAEAERLEQERIAQEQGEAERAEQErivaEAEAERLEQQRI 319
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNSKLAELKERIESLE--RIRTLLAAIADAEDEIERLREKREALAELN----DERRERLAEKRE 634
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1184249154 320 AAEQAEAErLEQERIAQEQAEAERAEQERIAAEAEADRLEQER 362
Cdd:PRK02224 635 RKRELEAE-FDEARIEEAREDKERAEEYLEQVEEKLDELREER 676
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
236-359 |
5.58e-07 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 49.65 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 236 EAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLE 315
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1184249154 316 QQRIAAEQAEAERLEQERIAQEQAEAERAEQERIAAEAEADRLE 359
Cdd:pfam05672 91 REQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLE 134
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
101-382 |
7.21e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 7.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 101 EQERMAAQRAEQQRLDTEREQAeQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLeQERVAAEKAEAERL 180
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSL-QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL-KERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 181 EQERiaqeqaEAERAEQERIAAEKAEADR-LEQERIAAEQAEA----ERVEQERIAAEQAEAERVEQERIAQEQAEAERA 255
Cdd:TIGR02169 750 EQEI------ENVKSELKELEARIEELEEdLHKLEEALNDLEArlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 256 EQQRIAAEQAEAERLEQQRIAAEqaeaERLEQERIAQEQGEAERAEQERIVAEAEAERLEqqrIAAEQAEAERLEQERIA 335
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLK----EQIKSIEKEIENLNGKKEELEEELEELEAALRD---LESRLGDLKKERDELEA 896
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1184249154 336 QEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKPKKEG 382
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
484-682 |
7.77e-07 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 52.50 E-value: 7.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 484 VILMVGVNGVGKTTTIGKLAKQF-QNEGKS-VMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADsasvVFDAFQAAK 561
Cdd:PRK14723 187 VLALVGPTGVGKTTTTAKLAARCvAREGADqLALLTTDSFRIGALEQLRIYGRILGVPVHAVKDAAD----LRFALAALG 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 562 ARNVdVLIaDTAGRLQNKDNLMQELEKIARVmkkidpDAPHEVMLTIdagtgqNAISQVNLFNQCV---------GLTGI 632
Cdd:PRK14723 263 DKHL-VLI-DTVGMSQRDRNVSEQIAMLCGV------GRPVRRLLLL------NAASHGDTLNEVVhayrhgageDVDGC 328
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1184249154 633 TLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGI-DDLRAFKSDDFIDALF 682
Cdd:PRK14723 329 IITKLDEATHLGPALDTVIRHRLPVHYVSTGQKVpEHLELAQADELVDRAF 379
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
92-310 |
1.04e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.88 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 92 AEQEAQMRLEQERMaaQRAEQQRLDTEREQaeqdeklaiekanaellakeqaeaqvqqqaqaarlaeqeaqmrleQERVA 171
Cdd:pfam15709 355 REQEEQRRLQQEQL--ERAEKMREELELEQ---------------------------------------------QRRFE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 172 AEKAEAERLEQERIAQEQAEAERAEQERIAAEKAeadRLEQERIAAEQAEAERVEQeriaaeQAEAERVEQERIAQEQAE 251
Cdd:pfam15709 388 EIRLRKQRLEEERQRQEEEERKQRLQLQAAQERA---RQQQEEFRRKLQELQRKKQ------QEEAERAEAEKQRQKELE 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1184249154 252 AERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAE 310
Cdd:pfam15709 459 MQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
104-229 |
1.13e-06 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 52.05 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 104 RMAAQRAEQQRLDTEREQAEQDEKLAIEKANAELLAKeqaeaqvqqqaqaarlaeqEAQMRLEQERVaaEKAEAERLEQE 183
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIERLER-------------------EERERLERERM--ERIERERLERE 487
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1184249154 184 RIAQEQAEAERAEQERIaaekaeaDRLEQERIaaEQAEAERVEQER 229
Cdd:PTZ00266 488 RLERERLERDRLERDRL-------DRLERERV--DRLERDRLEKAR 524
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
58-376 |
1.37e-06 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 51.78 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 58 AQAERLAIEKANAELLAKEQAEAQAQQQAQAARLAEQEAQMRLEQERMAAQRAEQQRLDTEREQAEQDEKLAIEKANAEL 137
Cdd:COG3899 762 EEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILH 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 138 LAK--EQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERI 215
Cdd:COG3899 842 WLGplREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARL 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 216 AAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQG 295
Cdd:COG3899 922 AAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLAL 1001
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 296 EAERAEQERIVAEAEAERLEQQRIAAEQAEAERLEQERIAQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLA 375
Cdd:COG3899 1002 LAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAA 1081
|
.
gi 1184249154 376 E 376
Cdd:COG3899 1082 A 1082
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
15-379 |
1.61e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 15 KSDKKQAEADKQQALAQQQEAERLAAEKAEAEREEQARIAAEKAQAERlAIEKANAELLAKeqaeaqaqqqaqaarLAEQ 94
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK-KAEEARIEEVMK---------------LYEE 1603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 95 EAQMRLEQermaAQRAEQQRLDTEREQAEQDEKLAIEkanaellakeqaeaqvqqqaqaarlaeqEAQMRLEQERVAAEk 174
Cdd:PTZ00121 1604 EKKMKAEE----AKKAEEAKIKAEELKKAEEEKKKVE----------------------------QLKKKEAEEKKKAE- 1650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 175 aEAERLEQERIAQEQAEAERAEQERIAAEKAEADRlEQERIAAEQAEAErvEQERIAAEQAEAERVEQERIAQEQAEAEr 254
Cdd:PTZ00121 1651 -ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE-EDEKKAAEALKKE--AEEAKKAEELKKKEAEEKKKAEELKKAE- 1725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 255 aEQQRIAAEQAEAERLEQQRiAAEQAEAERLEQERIAQEQGEAE------RAEQERIVAEAEAERLEQQRIAAEQAEAER 328
Cdd:PTZ00121 1726 -EENKIKAEEAKKEAEEDKK-KAEEAKKDEEEKKKIAHLKKEEEkkaeeiRKEKEAVIEEELDEEDEKRRMEVDKKIKDI 1803
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1184249154 329 LEQERIAQEqAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKPK 379
Cdd:PTZ00121 1804 FDNFANIIE-GGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHK 1853
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
212-360 |
1.62e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 51.56 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 212 QEriAAEQAEAERVEQEriaaEQAEAER--------VEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEae 283
Cdd:PTZ00491 664 QE--AAARHQAELLEQE----ARGRLERqkmhdkakAEEQRTKLLELQAESAAVESSGQSRAEALAEAEARLIEAEAE-- 735
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184249154 284 rLEQERIaqeqgeaeRAEQERIVAEAEAERLEQQRiaaeqaeaerlEQErIAQEQAEAERA-EQERIAAEAEADRLEQ 360
Cdd:PTZ00491 736 -VEQAEL--------RAKALRIEAEAELEKLRKRQ-----------ELE-LEYEQAQNELEiAKAKELADIEATKFER 792
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
17-238 |
1.72e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 51.49 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 17 DKKQAEADKQQALAQQQEAERLAAEKAEAEREEQARIAAEKAQAERLAIEKANAELLAKEQAEAQAQQQAQAARLAEQEA 96
Cdd:PRK05035 464 REKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAA 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 97 QMRLEQ-----ERMAAQRAEQQRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQervA 171
Cdd:PRK05035 544 DPKKAAvaaaiARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAA---A 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184249154 172 AEKAEAERLEQERiAQEQAEAERAEQERIAAE--KAEADRLEQERIAAEQAEAERVEQERIAAEQAEAE 238
Cdd:PRK05035 621 IARAKAKKAEQQA-NAEPEEPVDPRKAAVAAAiaRAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAK 688
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
248-381 |
1.95e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.11 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 248 EQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERI--AQEQGEAERAEQERIVAEAE--AERLEQQRIAAEQ 323
Cdd:pfam15709 326 EKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLerAEKMREELELEQQRRFEEIRlrKQRLEEERQRQEE 405
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 324 AEAERLEQERIAQEQA------------EAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKPKKE 381
Cdd:pfam15709 406 EERKQRLQLQAAQERArqqqeefrrklqELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEE 475
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
171-423 |
1.97e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 171 AAEKAEAERLeQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAE-QAEAERVEQER----I 245
Cdd:TIGR02169 670 RSEPAELQRL-RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEeEKLKERLEELEedlsS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 246 AQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQG-----EAERAEQERIVAEAEAE--RLEQQR 318
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAelsklEEEVSRIEARLREIEQKlnRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 319 IAAEQAEAERLEQERIAQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKPKKEgffSRLKKGLLKTRVNI 398
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER---DELEAQLRELERKI 905
|
250 260
....*....|....*....|....*
gi 1184249154 399 GSGFASIFSGKKIDDDLFEDLETQL 423
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALE 930
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
109-374 |
2.13e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 109 RAEQQRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEKAEAERLEQER-IAQ 187
Cdd:TIGR02169 197 RQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQlLEE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 188 EQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERV-EQERIAAEQAEAE--------RVEQERIAQEQAEAERAEQQ 258
Cdd:TIGR02169 277 LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKErELEDAEERLAKLEaeidkllaEIEELEREIEEERKRRDKLT 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 259 RIAAEQAEAERLEQQRIAAEQAEAERLEQErIAQEQGEAERAEQERIVAEAEAERL--EQQRIAAEQAEAERlEQERIAQ 336
Cdd:TIGR02169 357 EEYAELKEELEDLRAELEEVDKEFAETRDE-LKDYREKLEKLKREINELKRELDRLqeELQRLSEELADLNA-AIAGIEA 434
|
250 260 270
....*....|....*....|....*....|....*...
gi 1184249154 337 EQAEAErAEQERIAAEAEADRLEQERITAELAKEEAKL 374
Cdd:TIGR02169 435 KINELE-EEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
172-355 |
2.51e-06 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 50.81 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 172 AEKAEAERLEQERIAQEQAEAERAEQERIAAEKAeadrleQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAE 251
Cdd:PRK10811 848 VRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEP------VVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIA 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 252 AERAEQQRIAAEQAEAERLEqqriAAEQAEAERLEQERIAQEQGEAERAEQEriVAEAEAERlEQQRIAAEQAEAERLEQ 331
Cdd:PRK10811 922 APVTEQPQVITESDVAVAQE----VAEHAEPVVEPQDETADIEEAAETAEVV--VAEPEVVA-QPAAPVVAEVAAEVETV 994
|
170 180
....*....|....*....|....
gi 1184249154 332 ERIAQEQAEAERAEQERIAAEAEA 355
Cdd:PRK10811 995 TAVEPEVAPAQVPEATVEHNHATA 1018
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
167-364 |
2.73e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.11 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 167 QERVAAEKAEaERLEQERIAQEQAEaeraeqERIAAEKAEADRLEQERIAAEQ----AEAERVEQER-----------IA 231
Cdd:COG3096 417 QAVQALEKAR-ALCGLPDLTPENAE------DYLAAFRAKEQQATEEVLELEQklsvADAARRQFEKayelvckiageVE 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 232 AEQAEAERVEQERIAQEQ-AEAERAEQqrIAAEQAEAERLEQQriaaeQAEAERLEQERIAQEQGEAERAEQerivAEAE 310
Cdd:COG3096 490 RSQAWQTARELLRRYRSQqALAQRLQQ--LRAQLAELEQRLRQ-----QQNAERLLEEFCQRIGQQLDAAEE----LEEL 558
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1184249154 311 AERLEQQRIAAEQAEAERLEQERIAQEQAEAERAEQERIAAEAEADRLEQERIT 364
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALE 612
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
162-381 |
2.86e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 50.98 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 162 QMRLEQERVAAEK-AEAERLEQE---RIAQEQAEAERAEQERIAAEKAEADRLEQeriaAEQAEAERVEQERI------- 230
Cdd:NF041483 444 RLRGEAEQLRAEAvAEGERIRGEarrEAVQQIEEAARTAEELLTKAKADADELRS----TATAESERVRTEAIerattlr 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 231 --AAEQAEAERVEQERIAQEQAEaeRAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAE 308
Cdd:NF041483 520 rqAEETLERTRAEAERLRAEAEE--QAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALAD 597
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184249154 309 AEAERLEQQRIAAEQAEAERLE-QERIAQEQAEAErAEQERIAAEAEAD----RLEQERITAELAKEEAKLAEKPKKE 381
Cdd:NF041483 598 ARAEAERIRREAAEETERLRTEaAERIRTLQAQAE-QEAERLRTEAAADasaaRAEGENVAVRLRSEAAAEAERLKSE 674
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
54-377 |
3.27e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 54 AAEKAQAERLAIEKANAELLAK----EQAEAQAQQQAQAARLAEQEAQMRLEQERMAAQRAEQQrLDTEREQAEQDEKLA 129
Cdd:PRK02224 280 EVRDLRERLEELEEERDDLLAEagldDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEE-AESLREDADDLEERA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 130 IEKAN-AELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEKAEAERLEQ--ERIAQEQAEAERAEQERIAAEKAE 206
Cdd:PRK02224 359 EELREeAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDflEELREERDELREREAELEATLRTA 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 207 ADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQ------------AEAERLEQQR 274
Cdd:PRK02224 439 RERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEErleraedlveaeDRIERLEERR 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 275 IAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERlEQQRIAAEQAEAERLEQERIAQEQAE-AERAEQERIAAEA 353
Cdd:PRK02224 519 EDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKR-EAAAEAEEEAEEAREEVAELNSKLAElKERIESLERIRTL 597
|
330 340
....*....|....*....|....
gi 1184249154 354 EADRLEQERITAELAKEEAKLAEK 377
Cdd:PRK02224 598 LAAIADAEDEIERLREKREALAEL 621
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
83-527 |
3.42e-06 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 50.04 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 83 QQQAQAARLAEQEAQMRLEQERMAAQRAEQQRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQ 162
Cdd:COG3064 26 RAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 163 MRLEQERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQ 242
Cdd:COG3064 106 AAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 243 ERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAE 322
Cdd:COG3064 186 AAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 323 QAEAERLEQERIAQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKPKKEGFFSRLKKGLLKTRVNIGSGF 402
Cdd:COG3064 266 AAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 403 ASIFSGKKIDDDLFEDLETQLLTADLGVDTTMKLIDSLTDAANRKQLKDGDALYDLMKQEMAAMLKTAEQPLEIRADKKP 482
Cdd:COG3064 346 AGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLA 425
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1184249154 483 FVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVE 527
Cdd:COG3064 426 LAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVA 470
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
61-393 |
3.50e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 50.36 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 61 ERLAIEKANAELLAKEQAEAQAQQQAQAARLAEQEAQMRLEQERMAAQRAEQQRLDTEREQAEQDEKLAIEKANAELLAK 140
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 141 EQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQA 220
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 221 EAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERA 300
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 301 EQERIvaEAEAERLEQQRIAAEQAEAERLEQERIAQEQAEAERAEQERIAAEAEAD-RLEQERITAELAKEEAKLAEKPK 379
Cdd:pfam02463 929 ILLKY--EEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEfEEKEERYNKDELEKERLEEEKKK 1006
|
330
....*....|....
gi 1184249154 380 KEGFFSRLKKGLLK 393
Cdd:pfam02463 1007 LIRAIIEETCQRLK 1020
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
202-686 |
3.66e-06 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 50.04 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 202 AEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQqriaAEQAEAERLEQQRIAAEQAE 281
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEE----AREAKAEAEQRAAELAAEAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 282 AERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQAEA---ERLEQERIAQEQAEAERAEQERIAAEAEADRL 358
Cdd:COG3064 77 KKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKaeeAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 359 EQERITAELAKEEAKLAEKPKKEGFFSRLKKGLLKTRVNIGSGFASIFSGKKIDDDLFEDLETQLLTADLGVDTTMKLID 438
Cdd:COG3064 157 ARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 439 SLTDAANRKQLKDGDALYDLMKQEMAAMLKTAEQPLEIRADKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLA-A 517
Cdd:COG3064 237 VEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEeA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 518 GDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKARNVDVLIADTAGRLQNKDNLMQELEKIARVMKKID 597
Cdd:COG3064 317 VLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 598 PDAPHEVMLTIDAGTGQNAISQVNLFNQCVGLTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGIDDLRAFKSDDF 677
Cdd:COG3064 397 GGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAV 476
|
....*....
gi 1184249154 678 IDALFSQDE 686
Cdd:COG3064 477 LADLLLLGG 485
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
95-268 |
3.78e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.80 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 95 EAQMRLEQERMAAQRAEQQRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEk 174
Cdd:PRK09510 86 QQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAA- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 175 AEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAER 254
Cdd:PRK09510 165 AEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAA 244
|
170
....*....|....
gi 1184249154 255 AEQQRIAAEQAEAE 268
Cdd:PRK09510 245 KAAEKAAAAKAAAE 258
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
161-339 |
3.91e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 161 AQMRLEQERVAAEKAEAERLEQERIAQEQAEAERAE-QERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAER 239
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEElEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 240 VEQERIAQEQAEAERAE-QQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQgEAERAEQERIVAEAEAERLEQQR 318
Cdd:COG4717 151 LEERLEELRELEEELEElEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ-RLAELEEELEEAQEELEELEEEL 229
|
170 180
....*....|....*....|.
gi 1184249154 319 IAAEQAEAERLEQERIAQEQA 339
Cdd:COG4717 230 EQLENELEAAALEERLKEARL 250
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
160-574 |
4.39e-06 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 49.65 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 160 EAQMRLEQERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQA----EAERVEQERIAAEQA 235
Cdd:COG3064 38 EAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAkaakEAEAAAAAEKAAAAA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 236 EAERVEQERIAQEQAEAERAEQQRIAAEQAE--AERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAER 313
Cdd:COG3064 118 EKEKAEEAKRKAEEEAKRKAEEERKAAEAEAaaKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 314 LEQQRIAAEQAEAERLEQERIAQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKPKKEGFFSRLKKGLLK 393
Cdd:COG3064 198 AAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 394 TRVNIGSGFASIFSGKKIDDDLFEDLETQLLTADLGVDTTMKLIDSLTDAANRKQLKDGDALYDLMKQEMAAMLKTAEQP 473
Cdd:COG3064 278 LVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGA 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 474 LEIRADKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVV 553
Cdd:COG3064 358 LATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALL 437
|
410 420
....*....|....*....|.
gi 1184249154 554 FDAFQAAKARNVDVLIADTAG 574
Cdd:COG3064 438 VKLVADLAGGLVGIGKALTGD 458
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
172-373 |
5.89e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.48 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 172 AEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAE 251
Cdd:pfam02029 101 AERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVK 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 252 AERAEQQR------IAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAE-RLEQQRIAAEQA 324
Cdd:pfam02029 181 DEKIKKEKkvkyesKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEqKLEELRRRRQEK 260
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1184249154 325 EAERLEQERIAQEQAEAE------RAEQERIAAEAEADRLEQERITAELAKEEAK 373
Cdd:pfam02029 261 ESEEFEKLRQKQQEAELEleelkkKREERRKLLEEEEQRRKQEEAERKLREEEEK 315
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
160-317 |
6.38e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 6.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 160 EAQMRLEQERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAE-RVEQERIAAEQAEAE 238
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDlAALEEQLEELEAELE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 239 RVEQE------RIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERI-AQEQGEAERAEQERIVAEAEA 311
Cdd:COG4913 703 ELEEEldelkgEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGdAVERELRENLEERIDALRARL 782
|
....*.
gi 1184249154 312 ERLEQQ 317
Cdd:COG4913 783 NRAEEE 788
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
217-376 |
6.41e-06 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 49.65 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 217 AEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAErleqqrIAAEQAEAERLEQERIAQEQGE 296
Cdd:PRK10811 848 VRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPV------VVAEPQPEEVVVVETTHPEVIA 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 297 AERAEQERIVAEAEAERLEQqriAAEQAEAERLEQERIAQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAE 376
Cdd:PRK10811 922 APVTEQPQVITESDVAVAQE---VAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVE 998
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
214-359 |
6.51e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 48.89 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 214 RIAAEQAEAeRVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQrIAAEQAEAERLEQqriaaEQAEAERLEQERIAQE 293
Cdd:COG1566 75 RLDPTDLQA-ALAQAEAQLAAAEAQLARLEAELGAEAEIAAAEAQ-LAAAQAQLDLAQR-----ELERYQALYKKGAVSQ 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184249154 294 QgEAERAEQERIVAEAEAERLEQQRiaaEQAEAERLEQERIAQEQAEAERAEQERIAAEAEADRLE 359
Cdd:COG1566 148 Q-ELDEARAALDAAQAQLEAAQAQL---AQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
160-372 |
6.61e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.84 E-value: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 160 EAQMRLEQERVAAEKAEAE---RLEQERIAQEQAEAE---RAEQERIAAEKAEADRLEQERIAAEQAEAERV--EQERIA 231
Cdd:pfam12128 271 ETLIASRQEERQETSAELNqllRTLDDQWKEKRDELNgelSAADAAVAKDRSELEALEDQHGAFLDADIETAaaDQEQLP 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 232 AEQAEAERVEQERIAQE------QAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQE-- 303
Cdd:pfam12128 351 SWQSELENLEERLKALTgkhqdvTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLea 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184249154 304 -----RIVAEAEAERLEQQRIAAEQAEAERLEQERIAQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEA 372
Cdd:pfam12128 431 gklefNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQA 504
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
183-370 |
8.77e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 8.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 183 ERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAA 262
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 263 EQAEAERLEQQRIAAEQAEAERLEQ--ERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAERLE------QERI 334
Cdd:COG4717 129 PLYQELEALEAELAELPERLEELEErlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAeeleelQQRL 208
|
170 180 190
....*....|....*....|....*....|....*.
gi 1184249154 335 AQEQAEAERAEQERIAAEAEADRLEQERITAELAKE 370
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
160-383 |
1.23e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 160 EAQMRLEQERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAER 239
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 240 VEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRI 319
Cdd:COG4942 104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184249154 320 AAEQAEAERLEQER-IAQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKPKKEGF 383
Cdd:COG4942 184 EEERAALEALKAERqKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
53-319 |
2.11e-05 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 48.07 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 53 IAAEKAQAERLAiEKANAELLAKEQAEAQAQQQAQAARLAEQEAQMRLEQERMAAQRAEQQ-RLDTEREQAEQDEKLAIE 131
Cdd:TIGR00927 635 VAEAEHTGERTG-EEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEgEGEIEAKEADHKGETEAE 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 132 KANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEKAEAERLEQERIAQEQAEAERAEQE-RIAAEK------ 204
Cdd:TIGR00927 714 EVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEgEIQAGEdgemkg 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 205 ----AEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQqriaaEQA 280
Cdd:TIGR00927 794 degaEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEE-----EEE 868
|
250 260 270
....*....|....*....|....*....|....*....
gi 1184249154 281 EAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRI 319
Cdd:TIGR00927 869 EEEEEEEEEEEEEEEEEEEEENEEPLSLEWPETRQKQAI 907
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
100-377 |
2.16e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 100 LEQERMAAqRAEQQRLDTEREQAEQdeklaIEKANAELLAKEQAEAQVQQQAQaarlaeqEAQMRLEQERVAAEKAEAER 179
Cdd:PRK04863 326 LEQDYQAA-SDHLNLVQTALRQQEK-----IERYQADLEELEERLEEQNEVVE-------EADEQQEENEARAEAAEEEV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 180 LE--------QERIAQEQAEAERAEQERIAAEKAE----ADRLE----QERIAAEQAEAERVEQERIAAEQ----AEAER 239
Cdd:PRK04863 393 DElksqladyQQALDVQQTRAIQYQQAVQALERAKqlcgLPDLTadnaEDWLEEFQAKEQEATEELLSLEQklsvAQAAH 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 240 VEQERIAQ------EQAEAERAEQQRIAAEqaeaERLEQQRIAAEQAEAERleqeriaQEQGEAERAEQERIVAEAEAER 313
Cdd:PRK04863 473 SQFEQAYQlvrkiaGEVSRSEAWDVARELL----RRLREQRHLAEQLQQLR-------MRLSELEQRLRQQQRAERLLAE 541
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184249154 314 LEQQRIAAEQAEAErLEQEriaQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEK 377
Cdd:PRK04863 542 FCKRLGKNLDDEDE-LEQL---QEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAAR 601
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
174-381 |
2.24e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 47.28 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 174 KAEAERLEQERIAQEQAEAERAEQERIAAE----KAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQ 249
Cdd:PRK07735 36 KLEEENREKEKALPKNDDMTIEEAKRRAAAaakaKAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKREG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 250 AEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAERL 329
Cdd:PRK07735 116 TEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEV 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1184249154 330 EQERIAQEQAEAERAEQERIAAEAEADRLEQERITA-ELAKEEAKLAEKPKKE 381
Cdd:PRK07735 196 TEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGdEDAKAKAIAAAKAKAA 248
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
197-381 |
2.43e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 197 QERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRia 276
Cdd:COG4913 241 HEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL-- 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 277 aEQAEAERLE-QERIAQEQGEAEraeqerivaeaeaERLEQQrIAAEQAEAERLEQERIAQEQA----------EAERAE 345
Cdd:COG4913 319 -DALREELDElEAQIRGNGGDRL-------------EQLERE-IERLERELEERERRRARLEALlaalglplpaSAEEFA 383
|
170 180 190
....*....|....*....|....*....|....*.
gi 1184249154 346 QERIAAEAEADRLEQERITAELAKEEAKLAEKPKKE 381
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
188-286 |
2.98e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 47.64 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 188 EQAEAERAEQERIAAEKAEADRLEQERiAAEQAEAERVEQERIAAEQAEAERveQERIAQEQAEAERAEQQriaAEQAEA 267
Cdd:PRK11448 139 DPENLLHALQQEVLTLKQQLELQAREK-AQSQALAEAQQQELVALEGLAAEL--EEKQQELEAQLEQLQEK---AAETSQ 212
|
90
....*....|....*....
gi 1184249154 268 ERLEQQRIAAEQAeAERLE 286
Cdd:PRK11448 213 ERKQKRKEITDQA-AKRLE 230
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
137-375 |
3.21e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 137 LLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEKAEAERLEQERIAQEQAEAERAE-----QERIAAEKAEADRLE 211
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARriralEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 212 QERIAAEQAEAERVEQ--ERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQEr 289
Cdd:COG4942 90 KEIAELRAELEAQKEElaELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 290 IAQEQGEAERAEQERIVAEAEAERL--EQQRIAAEQAEAERLEQERIAQEQAEAERAEQERIAAEAEADRLEQERITAEL 367
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALkaERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
....*...
gi 1184249154 368 AKEEAKLA 375
Cdd:COG4942 249 AALKGKLP 256
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
160-285 |
3.56e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 47.25 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 160 EAQMRLEQERVAAEKAEAERLEQERiAQEQAEAERAEQERIAAEKaeadrLEQERIAAEQAEAERVEQERIAAEQAEAER 239
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREK-AQSQALAEAQQQELVALEG-----LAAELEEKQQELEAQLEQLQEKAAETSQER 214
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1184249154 240 VEQERIAQEQAEaeraeqQRIAAEQAEAERL--EQQRIAAEQAEAERL 285
Cdd:PRK11448 215 KQKRKEITDQAA------KRLELSEEETRILidQQLRKAGWEADSKTL 256
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
160-344 |
3.64e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.38 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 160 EAQMRLEQErvAAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQ------------ERIAAEQAEAERVEQ 227
Cdd:TIGR02794 68 ERQKKLEQQ--AEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQkqaeeakakqaaEAKAKAEAEAERKAK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 228 ERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVA 307
Cdd:TIGR02794 146 EEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEA 225
|
170 180 190
....*....|....*....|....*....|....*..
gi 1184249154 308 EAEAERLEQQRIAAEQAEAERLEQERIAQEQAEAERA 344
Cdd:TIGR02794 226 ERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVD 262
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
176-301 |
3.65e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 44.26 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 176 EAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEaERA 255
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAE-ERE 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1184249154 256 EQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQeQGEAERAE 301
Cdd:pfam05672 90 QREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQ-QEEQERLE 134
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
160-273 |
3.99e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.93 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 160 EAQMRLEQERVAaEKAEAErleQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAE----RVEQERIAAEqA 235
Cdd:PTZ00491 678 EARGRLERQKMH-DKAKAE---EQRTKLLELQAESAAVESSGQSRAEALAEAEARLIEAEAEVEqaelRAKALRIEAE-A 752
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1184249154 236 EAERVEQER---IAQEQAEAERAEQQRIAAEQAEAERLEQQ 273
Cdd:PTZ00491 753 ELEKLRKRQeleLEYEQAQNELEIAKAKELADIEATKFERI 793
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
95-328 |
4.04e-05 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 46.91 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 95 EAQMrlEQERMAAQRAEQqrlDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEK 174
Cdd:TIGR00927 682 EGEI--PAERKGEQEGEG---EIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVE 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 175 AEAERLEQERIAQEQAEAERAEQE-RIAAEKAEADRLEQERIAAEQAEAERVEQERIaaeqaEAERVEQERIAQEQAEAE 253
Cdd:TIGR00927 757 TEGDRKETEHEGETEAEGKEDEDEgEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKD-----EHEGQSETQADDTEVKDE 831
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184249154 254 RAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERivaEAEAERLEQQRIAAEQAEAER 328
Cdd:TIGR00927 832 TGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEE---EEEEEEENEEPLSLEWPETRQ 903
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
166-333 |
4.11e-05 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 46.96 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 166 EQERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAEK-AEADRLEQERIAAEQAEAERVEQERIAAEQAEAERV-EQE 243
Cdd:PRK10811 855 VEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEvVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQViTES 934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 244 RIAQEQAEAERAEQqrIAAEQAEAERLEQQRIAAEQAEAErleqeriaqeqGEAERAEQERIVAEAEAERLEQQRIAAEQ 323
Cdd:PRK10811 935 DVAVAQEVAEHAEP--VVEPQDETADIEEAAETAEVVVAE-----------PEVVAQPAAPVVAEVAAEVETVTAVEPEV 1001
|
170
....*....|
gi 1184249154 324 AEAERLEQER 333
Cdd:PRK10811 1002 APAQVPEATV 1011
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
262-359 |
4.64e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 46.87 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 262 AEQAEAERLEQQRIAAEQAEAERLEQERiAQEQGEAERAEQERIVAEAEAERLEQQRiaaeQAEAERLEQERIAQEQAEA 341
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREK-AQSQALAEAQQQELVALEGLAAELEEKQ----QELEAQLEQLQEKAAETSQ 212
|
90
....*....|....*...
gi 1184249154 342 ERAEQERIAAEAEADRLE 359
Cdd:PRK11448 213 ERKQKRKEITDQAAKRLE 230
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
190-381 |
4.71e-05 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 46.96 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 190 AEAERAEQERIAAEKAEADRLEQERIAAEQAEA-ERVEQERIAAEQAEAE----RVEQERIAQEQAEAERAEQQRIAAEQ 264
Cdd:PRK10811 582 GGEETKPQEQPAPKAEAKPERQQDRRKPRQNNRrDRNERRDTRDNRTRREgrenREENRRNRRQAQQQTAETRESQQAEV 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 265 AEAERLEQQRIAAEQAEAERLEQE--RIAQEQGEAERAEQERIVAEAEAERLEQ--QRIAAEQaeaerLEQE-RIAQEQA 339
Cdd:PRK10811 662 TEKARTQDEQQQAPRRERQRRRNDekRQAQQEAKALNVEEQSVQETEQEERVQQvqPRRKQRQ-----LNQKvRIEQSVA 736
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1184249154 340 EAE--RAEQERIAAEAEADRLEQERitAELAKEEAKLAEKPKKE 381
Cdd:PRK10811 737 EEAvaPVVEETVAAEPVVQEVPAPR--TELVKVPLPVVAQTAPE 778
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
256-374 |
5.60e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.81 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 256 EQQRIAAEQAEAeRLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAER--------------LEQQRIAA 321
Cdd:COG1566 79 TDLQAALAQAEA-QLAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERyqalykkgavsqqeLDEARAAL 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1184249154 322 EQAEAeRLEQERIAQEQAEAERAEQERI-AAEAEADRLEQERITAELAKEEAKL 374
Cdd:COG1566 158 DAAQA-QLEAAQAQLAQAQAGLREEEELaAAQAQVAQAEAALAQAELNLARTTI 210
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
20-368 |
6.87e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 46.39 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 20 QAEADKQQALAQQQEAERLAAEKAEAEREEQARIAAEKAQAERLAIEKANAELLAKEQAEAQAQQQAQAARLAEQEAQMR 99
Cdd:COG3899 763 EAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHW 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 100 LEQERMAAQRAEQ-----QRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEK 174
Cdd:COG3899 843 LGPLREALELLREaleagLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLA 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 175 AEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAER 254
Cdd:COG3899 923 AAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALL 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 255 AEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAERLEQERI 334
Cdd:COG3899 1003 AAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAA 1082
|
330 340 350
....*....|....*....|....*....|....
gi 1184249154 335 AQEQAEAERAEQERIAAEAEADRLEQERITAELA 368
Cdd:COG3899 1083 AAAAALAAALAAAALAAAAAAALALAAALAALAL 1116
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
248-341 |
7.05e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 46.10 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 248 EQAEAERAEQQRIAAEQAEAERLEQQRiAAEQAEAERLEQERIAQEQgEAERAEQERIVAEAEAERLEQQriaAEQAEAE 327
Cdd:PRK11448 139 DPENLLHALQQEVLTLKQQLELQAREK-AQSQALAEAQQQELVALEG-LAAELEEKQQELEAQLEQLQEK---AAETSQE 213
|
90
....*....|....
gi 1184249154 328 RLEQERIAQEQAEA 341
Cdd:PRK11448 214 RKQKRKEITDQAAK 227
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
100-361 |
7.28e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 7.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 100 LEQERMAAQR---AEQQRL-DTEREQAEQDEKLAIEKANAEL----LAKEQAEAQVQQQAQAARLAEQEAQMRLEqerva 171
Cdd:PRK04863 291 LRRELYTSRRqlaAEQYRLvEMARELAELNEAESDLEQDYQAasdhLNLVQTALRQQEKIERYQADLEELEERLE----- 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 172 aEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRleQERIAAEQAEAERVEQERIAAEQAE---------AERVEq 242
Cdd:PRK04863 366 -EQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADY--QQALDVQQTRAIQYQQAVQALERAKqlcglpdltADNAE- 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 243 ERIAQEQAEAERAEQQRIAAEQ------AEAERLEQ--QRIAAEQAEAERLEQERIAQEQgeAERAEQERIVAE----AE 310
Cdd:PRK04863 442 DWLEEFQAKEQEATEELLSLEQklsvaqAAHSQFEQayQLVRKIAGEVSRSEAWDVAREL--LRRLREQRHLAEqlqqLR 519
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1184249154 311 AERLEQQRIAAEQAEAERLEQE---RIAQEQAEAERAEQERIAAEAEADRLEQE 361
Cdd:PRK04863 520 MRLSELEQRLRQQQRAERLLAEfckRLGKNLDDEDELEQLQEELEARLESLSES 573
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
231-378 |
7.43e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 46.02 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 231 AAEQAEAERVEQERIAQEQAEAER-AEQQRIAAEQAEAErleqqrIAAEQAEAERLEQeriAQEQGEAERAEQERIVAEA 309
Cdd:PRK12472 181 KAEALAAAPARAETLAREAEDAARaADEAKTAAAAAARE------AAPLKASLRKLER---AKARADAELKRADKALAAA 251
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184249154 310 EAE----RLEQQRIAAEQAEAERLEQERIAQEQAEAERAEQEriAAEAEADRLEQERITAELAKEEAKLAEKP 378
Cdd:PRK12472 252 KTDeakaRAEERQQKAAQQAAEAATQLDTAKADAEAKRAAAA--ATKEAAKAAAAKKAETAKAATDAKLALEP 322
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
175-221 |
7.57e-05 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 46.02 E-value: 7.57e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1184249154 175 AEAERLEQERIAQEQAEAER--AEQERIAAEKA--EADRLEQERIAAEQAE 221
Cdd:PLN02316 251 LEEKRRELEKLAKEEAERERqaEEQRRREEEKAamEADRAQAKAEVEKRRE 301
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
179-315 |
8.11e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.42 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 179 RLEQERIAQEQAEAERAEQERIAAEKAEADRLEQEriaaeqaeaerVEQERIAAEQAEAERVEQERIAQEQAE-AERAEQ 257
Cdd:COG1566 84 ALAQAEAQLAAAEAQLARLEAELGAEAEIAAAEAQ-----------LAAAQAQLDLAQRELERYQALYKKGAVsQQELDE 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1184249154 258 QRIAAEQAEAeRLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLE 315
Cdd:COG1566 153 ARAALDAAQA-QLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
160-228 |
1.02e-04 |
|
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.
Pssm-ID: 464947 [Multi-domain] Cd Length: 201 Bit Score: 43.89 E-value: 1.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 160 EAQMRLEQERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEA-DRLEQERIAAEQAEAERVEQE 228
Cdd:pfam15927 1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELkHLLEERKEALEKLRAEAREEA 70
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
101-267 |
1.02e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.25 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 101 EQERMAAQ-RAEQQRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEqervaaekaEAER 179
Cdd:COG2268 218 QANREAEEaELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLE---------IAER 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 180 LEQERIAQEQAEAERAEQERIAAEKAEADRLEQEriAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQ- 258
Cdd:COG2268 289 EREIELQEKEAEREEAELEADVRKPAEAEKQAAE--AEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKl 366
|
170
....*....|
gi 1184249154 259 -RIAAEQAEA 267
Cdd:COG2268 367 pEIAEAAAKP 376
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
233-321 |
1.09e-04 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 44.59 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 233 EQAEAER------VEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQaEAERLEQE-----RIAQEQGEAErAE 301
Cdd:cd03406 169 EAMEAEKtklliaEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEK-EAEKKISEiedemHLAREKARAD-AE 246
|
90 100
....*....|....*....|....*..
gi 1184249154 302 QERIVAEAEAER-------LEQQRIAA 321
Cdd:cd03406 247 YYRALREAEANKlkltpeyLELKKYQA 273
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
263-365 |
1.35e-04 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 44.59 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 263 EQAEAER------LEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLeQQRIAAEQaeaerleqeRIAQ 336
Cdd:cd03406 169 EAMEAEKtklliaEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKK-ISEIEDEM---------HLAR 238
|
90 100 110
....*....|....*....|....*....|....*.
gi 1184249154 337 EQAEAErAEQERIAAEAEADR-------LEQERITA 365
Cdd:cd03406 239 EKARAD-AEYYRALREAEANKlkltpeyLELKKYQA 273
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
99-350 |
1.53e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 45.21 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 99 RLEQER---MAAQRAEQQRLDTEREQA----EQDEKLAIEKanaellakeqaeaqvqqqaqaarlaeqeaqmrlEQERVA 171
Cdd:NF012221 1573 RLEQEKqqqLAAISGSQSQLESTDQNAletnGQAQRDAILE---------------------------------ESRAVT 1619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 172 AEKAE-AERLEQERiAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVE--QERIAAEQAEAerveQERIAQE 248
Cdd:NF012221 1620 KELTTlAQGLDALD-SQATYAGESGDQWRNPFAGGLLDRVQEQLDDAKKISGKQLAdaKQRHVDNQQKV----KDAVAKS 1694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 249 QAEAERAEQQRIAAEqaeaerleqQRIAAEQAEAERLEQERIAQeQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAER 328
Cdd:NF012221 1695 EAGVAQGEQNQANAE---------QDIDDAKADAEKRKDDALAK-QNEAQQAESDANAAANDAQSRGEQDASAAENKANQ 1764
|
250 260
....*....|....*....|..
gi 1184249154 329 LEQERIAQEQAEAERAEQERIA 350
Cdd:NF012221 1765 AQADAKGAKQDESDKPNRQGAA 1786
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
247-381 |
1.94e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.55 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 247 QEQAEAERAEQQRIAAEQAEaERLE--QQRIAAEQAEAErleqERiAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQA 324
Cdd:PRK05035 433 QAKAEIRAIEQEKKKAEEAK-ARFEarQARLEREKAARE----AR-HKKAAEARAAKDKDAVAAALARVKAKKAAATQPI 506
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184249154 325 EAERLEQ----ERIAQEQAEAERAEQERIAAEA-EADRLEQERITAELAKEEAKLAEKPKKE 381
Cdd:PRK05035 507 VIKAGARpdnsAVIAAREARKAQARARQAEKQAaAAADPKKAAVAAAIARAKAKKAAQQAAN 568
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
181-303 |
1.98e-04 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 44.46 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 181 EQERIAQEQAEAERAEQERIAAEKAEADR-------LEQERIAAEQAEAERVEQERiaAEQAEAERVEQERIAQEQAEAE 253
Cdd:PRK00247 281 DEFKEHHAEQRAQYREKQKEKKAFLWTLRrnrlrmiITPWRAPELHAENAEIKKTR--TAEKNEAKARKKEIAQKRRAAE 358
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1184249154 254 R-AEQQRIAAEQAEAERLEQQRIAAEQA-----EAERLEQERIAQEQGEAERAEQE 303
Cdd:PRK00247 359 ReINREARQERAAAMARARARRAAVKAKkkgliDASPNEDTPSENEESKGSPPQVE 414
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
168-311 |
2.03e-04 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 44.58 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 168 ERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQ 247
Cdd:PRK13108 297 EREPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEREQP 376
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184249154 248 EQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAErlEQERIAQEQGEAERAEQERIVAEAEA 311
Cdd:PRK13108 377 GDLAGQAPAAHQVDAEAASAAPEEPAALASEAHDET--EPEVPEKAAPIPDPAKPDELAVAGPG 438
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
161-292 |
2.12e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.69 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 161 AQMRLEQERVAAEKAEAERleqeRIAQEQAEAERAEQERIAAEKAEADRLEQErIAAEQAEAERVEQEriaaEQAEAERV 240
Cdd:COG0542 400 ARVRMEIDSKPEELDELER----RLEQLEIEKEALKKEQDEASFERLAELRDE-LAELEEELEALKAR----WEAEKELI 470
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1184249154 241 EQERIAQEQAEaerAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQ 292
Cdd:COG0542 471 EEIQELKEELE---QRYGKIPELEKELAELEEELAELAPLLREEVTEEDIAE 519
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
99-377 |
2.19e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 99 RLEQERMAAQRAEQQRLDTEREQAEQDEKLA-IEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAA-EKAE 176
Cdd:PRK02224 224 RYEEQREQARETRDEADEVLEEHEERREELEtLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlAEAG 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 177 AERLEQERIAQEQAEAERAEQERiaaekaeADRLEQERIAA----EQAEAERVE----QERIAAEQAEAERVEQERIAQE 248
Cdd:PRK02224 304 LDDADAEAVEARREELEDRDEEL-------RDRLEECRVAAqahnEEAESLREDaddlEERAEELREEAAELESELEEAR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 249 QAEAERAEQQRIAAEQAEA--ERLEQQRIAAEQAE------AERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIA 320
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEElrERFGDAPVDLGNAEdfleelREERDELREREAELEATLRTARERVEEAEALLEAGKCPE 456
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1184249154 321 AEQAEAERLEQERIAQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEK 377
Cdd:PRK02224 457 CGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIER 513
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
299-377 |
3.00e-04 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 43.29 E-value: 3.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184249154 299 RAEQERIVAEAEAERLEQQRIAAEQAEAERLEQEriaqeqAEAERaEQERIAAEAEADRLEQerITAELAKEEAKLAEK 377
Cdd:COG0330 178 KAEREREAAILEAEGYREAAIIRAEGEAQRAIIE------AEAYR-EAQILRAEGEAEAFRI--VAEAYSAAPFVLFYR 247
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
72-302 |
3.25e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 72 LLAKEQAEAQAQQQaQAARLAEQEAQMRLEQERMAAQRAEQQRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQA 151
Cdd:COG4942 9 LLLALAAAAQADAA-AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 152 QAARLAEQEAQMRLEQERVAAEKAEAERLEQERIAQEQAEAERAEQ----ERIAAEKAEADRLEQERIAAEQAEAERVEQ 227
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDavrrLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184249154 228 ERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQ 302
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
92-297 |
3.59e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.30 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 92 AEQEAQM-RLEQERMAAQRAEQQRLDTEREQAEQDEKLAIEKANAELLAKeqAEAQVQQQAQAARLAEQEAQMRLEQERV 170
Cdd:TIGR02794 56 QQQKKPAaKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK--QAEQAAKQAEEKQKQAEEAKAKQAAEAK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 171 AAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQA 250
Cdd:TIGR02794 134 AKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKA 213
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1184249154 251 EAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEA 297
Cdd:TIGR02794 214 EAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
36-368 |
3.67e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 43.74 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 36 ERLAAEKAEAEREEQARIAAEKAQAERLAIEKANAELLAKEQAEAQAQQQAQAARLAEQEAQMRLEQERMAAQRAEQQRL 115
Cdd:COG5278 110 DELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 116 DTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEKAEAERLEQERIAQEQAEAERA 195
Cdd:COG5278 190 ELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLA 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 196 EQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRI 275
Cdd:COG5278 270 LAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 276 AAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAERLEQERIAQEQAEAERAEQERIAAEAEA 355
Cdd:COG5278 350 LLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALA 429
|
330
....*....|...
gi 1184249154 356 DRLEQERITAELA 368
Cdd:COG5278 430 EALALAEEEALAL 442
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
209-362 |
3.73e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 209 RLEQERIAAEQAEAERVEQERIAAEQAEAERVE-QERIAQEQAEAERAEQQRIAAEQAEAERLeQQRIAAEQAEAERLEQ 287
Cdd:PRK12705 24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEaKELLLRERNQQRQEARREREELQREEERL-VQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184249154 288 ERIAQEQGEAERAEQERIVAEAEaERLEQQRIAAEQAEAERLEQERIAQEQAEAERAEQERIAAEAEADRLEQER 362
Cdd:PRK12705 103 LENQLEEREKALSARELELEELE-KQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAER 176
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
193-344 |
3.87e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 193 ERAeQERIAAEKAEAD----RLEQERIAAEQAeaerveqeriaAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAE 268
Cdd:PRK00409 505 EEA-KKLIGEDKEKLNeliaSLEELERELEQK-----------AEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAE 572
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184249154 269 RLEQQRIAAEQAEAERLEQE-RIAQEQGEAERAEQERIvaeaeaERLEQQRIAAEQAEAERLEQERIAQEQAEAERA 344
Cdd:PRK00409 573 KEAQQAIKEAKKEADEIIKElRQLQKGGYASVKAHELI------EARKRLNKANEKKEKKKKKQKEKQEELKVGDEV 643
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
47-382 |
3.89e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 47 REEQARIAAEKAQAERlaiEKANAELLAKEQAEAQAQQQAQAARLAEQEAQMRLEQERMAAQRAEQQRLDTEREQAEQDE 126
Cdd:pfam02463 179 IEETENLAELIIDLEE---LKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 127 KLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQM--RLEQERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAEK 204
Cdd:pfam02463 256 SKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAkeEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 205 AEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAER 284
Cdd:pfam02463 336 EIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELAR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 285 LEQERIaqeqgEAERAEQERIVAEAEAERLEQQRIAAEQAEAERLEQERIAQEQAEAERAEQERIAAEAEADRLEQERIT 364
Cdd:pfam02463 416 QLEDLL-----KEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLL 490
|
330
....*....|....*...
gi 1184249154 365 AELAKEEAKLAEKPKKEG 382
Cdd:pfam02463 491 SRQKLEERSQKESKARSG 508
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
267-381 |
4.50e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.32 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 267 AERLEQQRIAaeQAEAERLEQERIAQeqgeaerAEQERIVAEAEAER-LEQQRIAAEQAEAERLEQEriAQEQAEAERAE 345
Cdd:COG2268 195 AEIIRDARIA--EAEAERETEIAIAQ-------ANREAEEAELEQEReIETARIAEAEAELAKKKAE--ERREAETARAE 263
|
90 100 110
....*....|....*....|....*....|....*...
gi 1184249154 346 QERIAAEAEADRLEQERITAELAKEEA--KLAEKPKKE 381
Cdd:COG2268 264 AEAAYEIAEANAEREVQRQLEIAEREReiELQEKEAER 301
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
99-315 |
5.01e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 99 RLEQERMAAQRAEQQRLDTEREQAEQdeklaiekanaellakeqaeaqvqqqAQAARLAEQEAQMRLEQERVAAEKAEAE 178
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEE--------------------------LQQKQAAEQERLKQLEKERLAAQEQKKQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 179 RLEQERIA---QEQAEAERAEQERIAAEKAEADRlEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERA 255
Cdd:PRK09510 120 AEEAAKQAalkQKQAEEAAAKAAAAAKAKAEAEA-KRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 256 EQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLE 315
Cdd:PRK09510 199 AKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
201-366 |
5.15e-04 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 43.04 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 201 AAEKAEADRLEQEriAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQA 280
Cdd:PRK13108 287 GSEYVVDEALERE--PAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 281 EAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQqriAAEQAEAERLEQERIAQEQAEAERA---EQERIAAEAEADR 357
Cdd:PRK13108 365 ETSEADIEREQPGDLAGQAPAAHQVDAEAASAAPEE---PAALASEAHDETEPEVPEKAAPIPDpakPDELAVAGPGDDP 441
|
....*....
gi 1184249154 358 LEQERITAE 366
Cdd:PRK13108 442 AEPDGIRRQ 450
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
99-351 |
5.17e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 99 RLEQERMAAQRAEQQRLDTEREQAEQ--DEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEKAE 176
Cdd:pfam12128 276 SRQEERQETSAELNQLLRTLDDQWKEkrDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 177 AERLEQERIAQE------QAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQE------- 243
Cdd:pfam12128 356 LENLEERLKALTgkhqdvTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLeagklef 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 244 RIAQEQAEAERAEQQ-RIAAEQAEAERLEQQRIAAEQAEAerleqeriAQEQGEAERAEQERivaeAEAERLEQQRIAAE 322
Cdd:pfam12128 436 NEEEYRLKSRLGELKlRLNQATATPELLLQLENFDERIER--------AREEQEAANAEVER----LQSELRQARKRRDQ 503
|
250 260
....*....|....*....|....*....
gi 1184249154 323 QAEAERLEQERIAQEQAEAERAEQERIAA 351
Cdd:pfam12128 504 ASEALRQASRRLEERQSALDELELQLFPQ 532
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
324-380 |
5.76e-04 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 43.32 E-value: 5.76e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1184249154 324 AEAERLEQERIAQEQAEAER--AEQERIAAEAEADRLEQERITAELAKEEAKLAEKPKK 380
Cdd:PLN02316 251 LEEKRRELEKLAKEEAERERqaEEQRRREEEKAAMEADRAQAKAEVEKRREKLQNLLKK 309
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
218-380 |
6.02e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 43.10 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 218 EQAEAERVEQERIAAEQAEAERVEQERIAQE-QAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGE 296
Cdd:PRK10811 857 EQREAEEVQVQPVVAEVPVAAAVEPVVSAPVvEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQVITESDV 936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 297 AERAEqeriVAEAEAERLEQQRIAAEQAEAERLEQERIAQEQAEAERAEQERIAAEAEadrlEQERITAELAKEEAKLAE 376
Cdd:PRK10811 937 AVAQE----VAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAE----VETVTAVEPEVAPAQVPE 1008
|
....
gi 1184249154 377 KPKK 380
Cdd:PRK10811 1009 ATVE 1012
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
166-370 |
6.13e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 166 EQERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERI 245
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 246 AQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQAE 325
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREEL 455
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1184249154 326 AERLEQERIAQEQAEAERAEQERIAAEAEADRLEQERITAELAKE 370
Cdd:COG4717 456 AELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALE 500
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
97-331 |
6.78e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 97 QMRLEQERMAAQRAEQQRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERvAAEKAE 176
Cdd:TIGR00618 264 QLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ-QSSIEE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 177 AERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQ-ERIAAEQAEAERVEQERIAQEQAEaERA 255
Cdd:TIGR00618 343 QRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQkLQSLCKELDILQREQATIDTRTSA-FRD 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184249154 256 EQQRIAAEQAEaERLEQQRIAAEQAEAERLEQERIAQE--QGEAERAEQERIVAEAEAERLEQQRIAAEQAEAERLEQ 331
Cdd:TIGR00618 422 LQGQLAHAKKQ-QELQQRYAELCAAAITCTAQCEKLEKihLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLE 498
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
178-293 |
6.81e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 178 ERLEQERIAQEQaEAERAEQERiaaEKAEADRLEQERIAAEQAEAERV---EQERIAAEQAEAERVEQERIAQEQAEAER 254
Cdd:PRK00409 523 ASLEELERELEQ-KAEEAEALL---KEAEKLKEELEEKKEKLQEEEDKlleEAEKEAQQAIKEAKKEADEIIKELRQLQK 598
|
90 100 110
....*....|....*....|....*....|....*....
gi 1184249154 255 AEQQRIAAEQAEaERLEQQRIAAEQAEAERLEQERIAQE 293
Cdd:PRK00409 599 GGYASVKAHELI-EARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
220-266 |
7.31e-04 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.94 E-value: 7.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1184249154 220 AEAERVEQERIAAEQAEAERV--EQERIAQEQA--EAERAEQQRIAAEQAE 266
Cdd:PLN02316 251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
235-281 |
7.31e-04 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.94 E-value: 7.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1184249154 235 AEAERVEQERIAQEQAEAER--AEQQRIAAEQA--EAERLEQQRIAAEQAE 281
Cdd:PLN02316 251 LEEKRRELEKLAKEEAERERqaEEQRRREEEKAamEADRAQAKAEVEKRRE 301
|
|
| RIB43A |
pfam05914 |
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar ... |
171-381 |
7.36e-04 |
|
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar microtubules contain a specialized set of protofilaments, termed ribbons, that are composed of tubulin and several associated proteins. RIB43A was first characterized in the unicellular biflagellate, Chlamydomonas reinhardtii although highly related sequences are present in several higher eukaryotes including humans. The function of this protein is unknown although the structure of RIB43A and its association with the specialized protofilament ribbons and with basal bodies is relevant to the proposed role of ribbons in forming and stabilising doublet and triplet microtubules and in organizing their three-dimensional structure. Human RIB43A homologs could represent a structural requirement in centriole replication in dividing cells.
Pssm-ID: 461780 [Multi-domain] Cd Length: 372 Bit Score: 42.58 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 171 AAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEAdrLEQERIAAEQAEAERVEQERIAAEQAEAErvEQERIAQEQA 250
Cdd:pfam05914 131 SMQKFEGEDLNREERKKLQQEQMREWLEQQIEEKKQA--EEEEKHAELLYDQKRLERDRRALELAKLE--EECRRAVNAA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 251 EAEraEQQRIAAEQAEAERLEQQRIAAE------------------QAEAERLEQERI--------AQEQGEAERAEQER 304
Cdd:pfam05914 207 TKN--FNQALAAEQAERRRLEKRQEQEDnlaeiynhltsdlltenpEVAQSSLGPHRVipdrwkgmSPEQLKEIRKEQEQ 284
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184249154 305 IVAEAEAERLEQQRIAAEQAeaerLEQERIAQEQAEAERAEQERIAAEaeadRLEQERITAELAKEEAKLAEKPKKE 381
Cdd:pfam05914 285 QREEKERRREEEKQRDAEWD----RQRLELARAALLLEREQQRLRREL----RRQLDEENLQLAQEQKARQEYLNKE 353
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
216-329 |
8.05e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 216 AAEQAEAERVEQERIAAEQAEAERveQERIAQEQAEAERAEQQRIAAEQAEAE---RLEQQRIAAEQAEAERLEQERIAQ 292
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQS--QALAEAQQQELVALEGLAAELEEKQQEleaQLEQLQEKAAETSQERKQKRKEIT 222
|
90 100 110
....*....|....*....|....*....|....*....
gi 1184249154 293 EQgeaerAEQERIVAEAEAERL--EQQRIAAEQAEAERL 329
Cdd:PRK11448 223 DQ-----AAKRLELSEEETRILidQQLRKAGWEADSKTL 256
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
171-486 |
8.23e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 171 AAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQA 250
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 251 EAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERleQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAerle 330
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAEL--QSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA---- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 331 QERIAQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKPKKEGFFSRLKKGLLKTRVNIGSGFASIFSGKK 410
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184249154 411 IDDDLFEDLETQLLTADLGVDTTMKLIDSLTDAANRKQLKDGDALYDLMKQEMAAMLKTAEQPLEIRADKKPFVIL 486
Cdd:COG4372 262 ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLA 337
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
199-359 |
8.47e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.03 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 199 RIAAEKAEADRLE-QERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAA 277
Cdd:pfam00529 50 QLDPTDYQAALDSaEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 278 EQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAERLEQERIAQEQAEAERAEQERIAAEAEADR 357
Cdd:pfam00529 130 RVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLER 209
|
..
gi 1184249154 358 LE 359
Cdd:pfam00529 210 TE 211
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
239-381 |
8.52e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.39 E-value: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 239 RVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQriaaEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQR 318
Cdd:PRK12705 24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAK----ELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEK 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 319 IAAEQAEAERLEQERIAQEQAEAERAEQ-----ERIA--AEAEADRLEQERITAELAKEEAKLAEKPKKE 381
Cdd:PRK12705 100 LDNLENQLEEREKALSARELELEELEKQldnelYRVAglTPEQARKLLLKLLDAELEEEKAQRVKKIEEE 169
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
188-357 |
8.71e-04 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 42.67 E-value: 8.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 188 EQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEA 267
Cdd:COG3914 1 AAAAALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 268 ERLEQQRIAA--EQAEAERLEQeRIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAERLEQERIAQEQAEAERAE 345
Cdd:COG3914 81 LELAALLLQAlgRYEEALALYR-RALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRL 159
|
170
....*....|..
gi 1184249154 346 QERIAAEAEADR 357
Cdd:COG3914 160 GRLEEAIAALRR 171
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
190-257 |
8.85e-04 |
|
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.
Pssm-ID: 464947 [Multi-domain] Cd Length: 201 Bit Score: 41.19 E-value: 8.85e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184249154 190 AEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERV-EQERIAQEQAEAERAEQ 257
Cdd:pfam15927 1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHLlEERKEALEKLRAEAREE 69
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
273-349 |
9.12e-04 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 41.75 E-value: 9.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184249154 273 QRIAAEQ-AEAERLEQERIAQEQGEAERAEQERIVAEAEAERleQQRIAAEQAEAERLEQerIAQEQAEAERAEQERI 349
Cdd:COG0330 175 DRMKAEReREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYR--EAQILRAEGEAEAFRI--VAEAYSAAPFVLFYRS 248
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
175-358 |
1.01e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 175 AEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQEriaaeqAEAERVEQERIAAEQAEAERVEQERIAQEQAEAER 254
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNE------FEKELRERRNELQKLEKRLLQKEENLDRKLELLEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 255 AEQQRIAAEQAEAER---LEQQRIAAEQAEAERLEQ-ERIAQEQGEAERAEQ-ERIVAEAEAERLEQQRIAAEQA--EAE 327
Cdd:PRK12704 108 REEELEKKEKELEQKqqeLEKKEEELEELIEEQLQElERISGLTAEEAKEILlEKVEEEARHEAAVLIKEIEEEAkeEAD 187
|
170 180 190
....*....|....*....|....*....|.
gi 1184249154 328 RLEQERIAQeqaeaerAEQeRIAAEAEADRL 358
Cdd:PRK12704 188 KKAKEILAQ-------AIQ-RCAADHVAETT 210
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
162-284 |
1.02e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 162 QMRLEQErvaAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVE 241
Cdd:PRK00409 529 ERELEQK---AEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVK 605
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1184249154 242 qeriAQEQAEAERaeQQRIAAEQAEAERLEQQRIAAEQAEAER 284
Cdd:PRK00409 606 ----AHELIEARK--RLNKANEKKEKKKKKQKEKQEELKVGDE 642
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
97-345 |
1.13e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.16 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 97 QMRLEQERMAAQRAEQQRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQ--MRLEQERVAAEK 174
Cdd:pfam02029 69 AKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEirEKEYQENKWSTE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 175 AEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQER------IAAEQAEAERVEQERIAAEQAEAERVEQERIAQE 248
Cdd:pfam02029 149 VRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKkvkyesKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQG 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 249 QAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAE------RAEQERIVAEAEAERLEQQRiaaE 322
Cdd:pfam02029 229 GLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAELEleelkkKREERRKLLEEEEQRRKQEE---A 305
|
250 260
....*....|....*....|...
gi 1184249154 323 QAEAERLEQERIAQEQAEAERAE 345
Cdd:pfam02029 306 ERKLREEEEKRRMKEEIERRRAE 328
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
99-277 |
1.50e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 99 RLEQERMAAQRAEQQRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLE--QERVAAEKAE 176
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAelPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 177 AERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERiaqEQAEAERAE 256
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL---EELEEELEQ 231
|
170 180
....*....|....*....|.
gi 1184249154 257 QQRIAAEQAEAERLEQQRIAA 277
Cdd:COG4717 232 LENELEAAALEERLKEARLLL 252
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
175-361 |
1.53e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.12 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 175 AEAERLEQERIAQEQAEAERAEQER-IAAEKAEADRLEQE--RIAAEQAEAERVEQERIAAE-QAEAERVEQERIAQEQA 250
Cdd:NF041483 154 AEQLRARTESQARRLLDESRAEAEQaLAAARAEAERLAEEarQRLGSEAESARAEAEAILRRaRKDAERLLNAASTQAQE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 251 EAERAEQQRiAAEQAEAERLEQQRIAAEQAEAERLEQeriAQEQGEAERAEQERIVAEAE---------AERLEQQRIAA 321
Cdd:NF041483 234 ATDHAEQLR-SSTAAESDQARRQAAELSRAAEQRMQE---AEEALREARAEAEKVVAEAKeaaakqlasAESANEQRTRT 309
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1184249154 322 EQAEAERLEQERIAQEQAEAERAEQERIAAEAEADRLEQE 361
Cdd:NF041483 310 AKEEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAE 349
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
56-300 |
1.53e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 56 EKAQAERLA-IEKANAELLAKEQAEAQAQQQAQAARLAEQEAQMRLEQERMAAQRAEQQRLDTEREQAEQDEKLAIEKAN 134
Cdd:COG4913 247 AREQIELLEpIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 135 AellakeqaeaqvqqqaqaarlaEQEAQMRLEQERVAAEKAEAERLEQERiaqEQAEAERAEQERIAAEKAEADRLEQER 214
Cdd:COG4913 327 E----------------------LEAQIRGNGGDRLEQLEREIERLEREL---EERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 215 IAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQqriaaeQAEAERLEQQR--IAAEQAEAerleQERIAQ 292
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL------EAEIASLERRKsnIPARLLAL----RDALAE 451
|
....*...
gi 1184249154 293 EQGEAERA 300
Cdd:COG4913 452 ALGLDEAE 459
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
53-349 |
1.84e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 53 IAAEKAQAERLAIEKANAE-LLAKEQAEAQAQQQAQAARLAEQEAQMRLEQERMAAQRAEQQRLDTEREQAEQdEKLAIE 131
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAErYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEK-RLEEIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 132 KANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEKAEAERLE-QERIAQEQAEAERAEQE----RIAAEKAE 206
Cdd:TIGR02169 272 QLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEeRLAKLEAEIDKLLAEIEelerEIEEERKR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 207 ADRLEQERIAAEQAEAE-RVEQERIAAEQAEA-ERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAER 284
Cdd:TIGR02169 352 RDKLTEEYAELKEELEDlRAELEEVDKEFAETrDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 285 LE-------------QERIAQEQGEAERAEQERIVAE-------AEAERLEqQRIAAEQAEAERLEQERIAQEQAEAERA 344
Cdd:TIGR02169 432 IEakineleeekedkALEIKKQEWKLEQLAADLSKYEqelydlkEEYDRVE-KELSKLQRELAEAEAQARASEERVRGGR 510
|
....*
gi 1184249154 345 EQERI 349
Cdd:TIGR02169 511 AVEEV 515
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
160-390 |
1.95e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 41.11 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 160 EAQMRLEQERVAAEkAEAERLEQERIAQEQAEAERAE--QERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEA 237
Cdd:PHA03169 57 QVRAVAEQGHRQTE-SDTETAEESRHGEKEERGQGGPsgSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 238 ERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQ 317
Cdd:PHA03169 136 PPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQ 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 318 RIAAEQAEAERLEQEriaqEQAEAERAEQERIAAEAEADRLEQERITAELAKEEA--------KLAEKPKKEgffSRLKK 389
Cdd:PHA03169 216 SPTPQQAPSPNTQQA----VEHEDEPTEPEREGPPFPGHRSHSYTVVGWKPSTRPggvpklclRCTSHPSHR---SRLPE 288
|
.
gi 1184249154 390 G 390
Cdd:PHA03169 289 G 289
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
250-316 |
2.08e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 41.39 E-value: 2.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184249154 250 AEAERAEQQRIAAEQAEAERleqqriaaEQAEAERLEQERIAQeqgEAERAEQERIVaEAEAERLEQ 316
Cdd:PLN02316 251 LEEKRRELEKLAKEEAERER--------QAEEQRRREEEKAAM---EADRAQAKAEV-EKRREKLQN 305
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
164-286 |
2.09e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 39.25 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 164 RLEQERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAE----AER 239
Cdd:pfam05672 14 RILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEereqREQ 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1184249154 240 VEQERIAQEQAEAERAEQqriaaEQAEAERLEQQRIaAEQAEAERLE 286
Cdd:pfam05672 94 EEQERLQKQKEEAEAKAR-----EEAERQRQEREKI-MQQEEQERLE 134
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
160-312 |
2.09e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 41.56 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 160 EAQMRLEQERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAER 239
Cdd:PRK10811 860 EAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQVITESDVAVA 939
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184249154 240 VE----QERIAQEQAEAERAEQQRIAAEQAEAErleqQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAE 312
Cdd:PRK10811 940 QEvaehAEPVVEPQDETADIEEAAETAEVVVAE----PEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATVE 1012
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
205-251 |
2.25e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 41.39 E-value: 2.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1184249154 205 AEADRLEQERIAAEQAEAERV--EQERIAAEQA--EAERVEQERIAQEQAE 251
Cdd:PLN02316 251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
230-548 |
2.25e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 41.11 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 230 IAAEQAEAERVEQERIAQEQAEAERAEQqriAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEA 309
Cdd:PRK06995 51 LAPPAAAAPAAAQPPPAAAPAAVSRPAA---PAAEPAPWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAAEN 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 310 EAERLEQQRIAAEQAEAERLEQERIAQE-QAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEkPKKegffSRLK 388
Cdd:PRK06995 128 AARRLARAAAAAPRPRVPADAAAAVADAvKARIERIVNDTVMQELRSLRGMLEEQLASLAWGERQRRD-PVR----AALL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 389 KGLLktrvniGSGFASIFSGKKIDDdlfedletqlLTADLGVDTTMKLIDSLTDAaNRKQLKDGDALYDlmkqemaamlk 468
Cdd:PRK06995 203 KHLL------AAGFSAQLVRMLVDN----------LPEGDDAEAALDWVQSALAK-NLPVLDSEDALLD----------- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 469 taeqpleiradkKPFVILMVGVNGVGKTTTIGKLAKQF-QNEGKS-VMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTG 546
Cdd:PRK06995 255 ------------RGGVFALMGPTGVGKTTTTAKLAARCvMRHGASkVALLTTDSYRIGGHEQLRIYGKILGVPVHAVKDA 322
|
..
gi 1184249154 547 AD 548
Cdd:PRK06995 323 AD 324
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
238-352 |
2.25e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 238 ERVEQERIAQEQaEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQ 317
Cdd:PRK00409 523 ASLEELERELEQ-KAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGY 601
|
90 100 110
....*....|....*....|....*....|....*
gi 1184249154 318 RIAAEQAEAERLEQERIAQEQAEAERAEQERIAAE 352
Cdd:PRK00409 602 ASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| flhF |
PRK14721 |
flagellar biosynthesis regulator FlhF; Provisional |
484-682 |
2.55e-03 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173184 [Multi-domain] Cd Length: 420 Bit Score: 40.70 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 484 VILMVGVNGVGKTTTIGKLAKQ--FQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPViaqHTGADSASVVFdAFQAAK 561
Cdd:PRK14721 193 VYALIGPTGVGKTTTTAKLAARavIRHGADKVALLTTDSYRIGGHEQLRIYGKLLGVSV---RSIKDIADLQL-MLHELR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 562 ARNVdVLIaDTAGRLQNKDNLMQELEKIARVMKKIdpdaphEVMLTIDAGTGQNAISQVNLFNQCVGLTGITLSKLDGTA 641
Cdd:PRK14721 269 GKHM-VLI-DTVGMSQRDQMLAEQIAMLSQCGTQV------KHLLLLNATSSGDTLDEVISAYQGHGIHGCIITKVDEAA 340
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1184249154 642 KGGVIFAVADKFNIPIRYIGVGEGI-DDLRAFKSDDFIDALF 682
Cdd:PRK14721 341 SLGIALDAVIRRKLVLHYVTNGQKVpEDLHEANSRYLLHRIF 382
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
186-348 |
2.71e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 40.73 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 186 AQEQAEAERAEQEriAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAERAEQQRIA---- 261
Cdd:PRK13108 287 GSEYVVDEALERE--PAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTpave 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 262 -AEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQErivaEAEAERLEQQRIAAEQAEAERLEQERIAQEQAE 340
Cdd:PRK13108 365 eTSEADIEREQPGDLAGQAPAAHQVDAEAASAAPEEPAALASE----AHDETEPEVPEKAAPIPDPAKPDELAVAGPGDD 440
|
....*...
gi 1184249154 341 AERAEQER 348
Cdd:PRK13108 441 PAEPDGIR 448
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
13-331 |
2.81e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 13 FGKSDKKQAEADKQQALAQQQEAERLAAEKAEAEREEQAriaaEKAQAERLAIEKANAELLAKEQAEAQAQQQAQAARLA 92
Cdd:PRK04863 347 QEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARA----EAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQA 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 93 EQEAQMRLE---------QERMAAQRAEQQRLDTEREQAEQdeKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQM 163
Cdd:PRK04863 423 LERAKQLCGlpdltadnaEDWLEEFQAKEQEATEELLSLEQ--KLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 164 RLEQERvaAEKAEAERLEQ--------ERIAQEQAEAERAEQE---RIAAEKAEADRLEQERIAAEQAEAERVEQERIAA 232
Cdd:PRK04863 501 LLRRLR--EQRHLAEQLQQlrmrlselEQRLRQQQRAERLLAEfckRLGKNLDDEDELEQLQEELEARLESLSESVSEAR 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 233 EQAEAERVEQERIAQEQAEAERAEQQRIAAeQAEAERLEQQrIAAEQAEAERLEQERiaQEQGEAER-AEQERIVAEAEA 311
Cdd:PRK04863 579 ERRMALRQQLEQLQARIQRLAARAPAWLAA-QDALARLREQ-SGEEFEDSQDVTEYM--QQLLEREReLTVERDELAARK 654
|
330 340
....*....|....*....|...
gi 1184249154 312 ERLEQQR---IAAEQAEAERLEQ 331
Cdd:PRK04863 655 QALDEEIerlSQPGGSEDPRLNA 677
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
175-258 |
2.85e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 38.45 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 175 AEAERLEQErIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAerveQERIAAEQAEAERVEQERIAQEQAEAER 254
Cdd:PRK07353 53 AEAEKLEAQ-YEQQLASARKQAQAVIAEAEAEADKLAAEALAEAQAEA----QASKEKARREIEQQKQAALAQLEQQVDA 127
|
....
gi 1184249154 255 AEQQ 258
Cdd:PRK07353 128 LSRQ 131
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
176-335 |
2.86e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 40.76 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 176 EAERLEQERIAQEQAEAERAEQERIAAEKAEADR----LEQERIAAEQAEAERVEQERIAAEQaeaERVEQERIAQEQA- 250
Cdd:pfam05262 205 ERESQEDAKRAQQLKEELDKKQIDADKAQQKADFaqdnADKQRDEVRQKQQEAKNLPKPADTS---SPKEDKQVAENQKr 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 251 EAERAEQQriaAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAeaerleQQRIAAEQAEAERLE 330
Cdd:pfam05262 282 EIEKAQIE---IKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDL------QKTKPQVEAQPTSLN 352
|
....*
gi 1184249154 331 QERIA 335
Cdd:pfam05262 353 EDAID 357
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
233-382 |
3.43e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 40.37 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 233 EQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAErLEQQRIAAEQAeaerLEQERIAQEQGEAERAEQERIVAEAEAE 312
Cdd:pfam05262 207 ESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDN-ADKQRDEVRQK----QQEAKNLPKPADTSSPKEDKQVAENQKR 281
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184249154 313 RLEQQRIAAEQAEAERLEQERIAQEQAEAERAEQERIAAEAEAD-RLEQERITAELAKEEAKLAEKPKKEG 382
Cdd:pfam05262 282 EIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEaQKKREPVAEDLQKTKPQVEAQPTSLN 352
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
190-380 |
3.53e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 40.62 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 190 AEAERAEQERIAAEKAEADRL-EQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAE---RAEQQRIAAEQA 265
Cdd:pfam02029 2 EDEEEAARERRRRAREERRRQkEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDrtaKREERRQKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 266 EAERlEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAERLEQERIAQ-EQAEAERA 344
Cdd:pfam02029 82 ALER-QKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQaEEEGEEEE 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1184249154 345 EQERIAAEAEADRLEQERITAELAKEEAKLAEKPKK 380
Cdd:pfam02029 161 DKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKV 196
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
160-327 |
3.69e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 40.38 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 160 EAQMRLEQervAAEKAEAERLEQER----IAQEQAEAERAEQErIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQA 235
Cdd:NF033838 308 EAEKKVEE---AKKKAKDQKEEDRRnyptNTYKTLELEIAESD-VKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKA 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 236 EAERVE----QERIAQEQAEAERAEQQRIA---AEQAEAERLEQQRIAAEQAE--AERLEQERIAQEQGEAERAEQeriv 306
Cdd:NF033838 384 EATRLEkiktDRKKAEEEAKRKAAEEDKVKekpAEQPQPAPAPQPEKPAPKPEkpAEQPKAEKPADQQAEEDYARR---- 459
|
170 180
....*....|....*....|.
gi 1184249154 307 AEAEAERLEQQRIAAEQAEAE 327
Cdd:NF033838 460 SEEEYNRLTQQQPPKTEKPAQ 480
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
164-206 |
3.72e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 40.62 E-value: 3.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1184249154 164 RLEQERVAAEKAEAERL--EQERIAQEQA--EAERAEQERIAAEKAE 206
Cdd:PLN02316 255 RRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
161-284 |
3.80e-03 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 40.22 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 161 AQMRLEQERVAAEKAEAERLEQERIA------------QEQAEAERAEQERIAAEKAEADRLEQERIAAE-QAEAERVEQ 227
Cdd:PRK00247 289 EQRAQYREKQKEKKAFLWTLRRNRLRmiitpwrapelhAENAEIKKTRTAEKNEAKARKKEIAQKRRAAErEINREARQE 368
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1184249154 228 ERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAER 284
Cdd:PRK00247 369 RAAAMARARARRAAVKAKKKGLIDASPNEDTPSENEESKGSPPQVEATTTAEPNREP 425
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
175-378 |
4.46e-03 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 40.36 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 175 AEAERLEQE--RIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQE----RIAAEQAEAERVEQERIAQE 248
Cdd:PRK14900 842 AETARVDKEigKVDQDLAVLERKLQNPSFVQNAPPAVVEKDRARAEELREKRGKLEahraMLSGSEANSARRDTMEIQNE 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 249 QAEAERAeqqriAAEQAEAErleQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIvaeaEAERLEQQRIAAEQAEAER 328
Cdd:PRK14900 922 QKPTQDG-----PAAEAQPA---QENTVVESAEKAVAAVSEAAQQAATAVASGIEKV----AEAVRKTVRRSVKKAAATR 989
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1184249154 329 leqerIAQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKP 378
Cdd:PRK14900 990 -----AAMKKKVAKKAPAKKAAAKKAAAKKAAAKKKVAKKAPAKKVARKP 1034
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
211-292 |
4.64e-03 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 39.44 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 211 EQERIAAEqAEAERVEQERIAAEQAEAERVEQEriaqeqAEAERAEQQRIAaeQAEAERLEQqrIAAEQAEAERLEQERI 290
Cdd:COG0330 180 EREREAAI-LEAEGYREAAIIRAEGEAQRAIIE------AEAYREAQILRA--EGEAEAFRI--VAEAYSAAPFVLFYRS 248
|
..
gi 1184249154 291 AQ 292
Cdd:COG0330 249 LE 250
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
231-330 |
4.77e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.32 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 231 AAEQAEAERVEQERiaQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAeraeqerivaeAE 310
Cdd:PRK11448 145 HALQQEVLTLKQQL--ELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAE-----------TS 211
|
90 100
....*....|....*....|
gi 1184249154 311 AERLEQQRIAAEQAeAERLE 330
Cdd:PRK11448 212 QERKQKRKEITDQA-AKRLE 230
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
277-377 |
4.81e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.32 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 277 AEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAERleQERIAQEQAEAERAEQEriAAEAEAD 356
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAEL--EEKQQELEAQLEQLQEK--AAETSQE 213
|
90 100
....*....|....*....|.
gi 1184249154 357 RLEQERITAELAKEEAKLAEK 377
Cdd:PRK11448 214 RKQKRKEITDQAAKRLELSEE 234
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
309-352 |
4.89e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 40.24 E-value: 4.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1184249154 309 AEAERLEQQRIAAEQAEAERL--EQERIAQEQA--EAERAEQERIAAE 352
Cdd:PLN02316 251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEK 298
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
247-348 |
4.91e-03 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 39.39 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 247 QEQAEAER----AEQQRIAAEQAEAERleqqRIAAEQAEAERLEQERIAQEQGEAERAEQERIVA--EAEAERLEQQRIA 320
Cdd:PRK06991 149 QAQADAARarhdARQARLRREREAAEA----RAAARAAASAAAAAAEASAAAAPAADDAEAKKRAiiAAALERARKKKEE 224
|
90 100
....*....|....*....|....*....
gi 1184249154 321 AEQAEAERLEQERIAQE-QAEAERAEQER 348
Cdd:PRK06991 225 LAAQGAGPKNTEGVSAAvQAQIDAAEARR 253
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
239-319 |
4.98e-03 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 39.44 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 239 RVEQERIAQEqAEAERAEQQRIAAEQAEAERLEqqriaaEQAEAERleQERIAQEQGEAERAeqeRIVAEA--EAERLEQ 316
Cdd:COG0330 178 KAEREREAAI-LEAEGYREAAIIRAEGEAQRAI------IEAEAYR--EAQILRAEGEAEAF---RIVAEAysAAPFVLF 245
|
...
gi 1184249154 317 QRI 319
Cdd:COG0330 246 YRS 248
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
53-306 |
5.01e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.34 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 53 IAAEKAQAERLAIEKANAELLAKEQAEAQAQQQAQAARLAEQEAQMRLEQERMAAQRAEQQRLDTEREQAEQDEKLAIEK 132
Cdd:pfam02463 766 KSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEE 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 133 ANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQ 212
Cdd:pfam02463 846 QKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKE 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 213 ERIAAEQAEAERVEQ--ERIAAEQAEAERVEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERI 290
Cdd:pfam02463 926 EAEILLKYEEEPEELllEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
250
....*....|....*.
gi 1184249154 291 AQEQGEAERAEQERIV 306
Cdd:pfam02463 1006 KLIRAIIEETCQRLKE 1021
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
263-379 |
5.14e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.11 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 263 EQAEAERLEQQRIaaEQAEAERLEQERiaqeQGEAERAEQERIVAEAE-AERLEQQRIAAEQAEAERL------EQERIA 335
Cdd:pfam17380 281 QKAVSERQQQEKF--EKMEQERLRQEK----EEKAREVERRRKLEEAEkARQAEMDRQAAIYAEQERMamererELERIR 354
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1184249154 336 QEQA--EAERAEQERIAAEA----EADRLEQERITA-ELAKEEAKLAEKPK 379
Cdd:pfam17380 355 QEERkrELERIRQEEIAMEIsrmrELERLQMERQQKnERVRQELEAARKVK 405
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
181-361 |
5.40e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 39.68 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 181 EQERIAQEQAEAERAEQERIAAEKAEADRLEQeriAAEQAEAERVEQERIAAEQAEA-----------------ERVEQE 243
Cdd:PRK11637 79 KQEEAISQASRKLRETQNTLNQLNKQIDELNA---SIAKLEQQQAAQERLLAAQLDAafrqgehtglqlilsgeESQRGE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 244 RIAQEQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAER---LEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIA 320
Cdd:PRK11637 156 RILAYFGYLNQARQETIAELKQTREELAAQKAELEEKQSQQktlLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQL 235
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1184249154 321 AEQAEAERLEQERIAQEQAEA-ERAEQEriAAEAEADRLEQE 361
Cdd:PRK11637 236 SELRANESRLRDSIARAEREAkARAERE--AREAARVRDKQK 275
|
|
| RqcH |
COG1293 |
Ribosome quality control (RQC) protein RqcH, Rqc2/NEMF/Tae2 family, contains fibronectin-(FbpA) ... |
177-289 |
5.48e-03 |
|
Ribosome quality control (RQC) protein RqcH, Rqc2/NEMF/Tae2 family, contains fibronectin-(FbpA) and RNA- (NFACT) binding domains [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440904 [Multi-domain] Cd Length: 578 Bit Score: 39.82 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 177 AERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQE----------RI- 245
Cdd:COG1293 292 SEKAERDRVKQLAEDLRKKVENELEKLERKLEKQEEELEEAEKAEKYREKGELLTANLYQVEKGMKEvtlpnyyeevTIp 371
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184249154 246 ------AQEQAE--------AERAE---QQRIAAEQAEAERLEQQRIAAEQAEAERLEQER 289
Cdd:COG1293 372 ldprlsPSENAQryykkykkLKRKKegaEEQLEETEEELEYLESVLAQLEQAEDEDLEEIR 432
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
480-592 |
5.48e-03 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350691 [Multi-domain] Cd Length: 155 Bit Score: 37.92 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 480 KKPFVILmVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAgDTFRAAAVeqLqvwGERNSIPV--IAQHTGADSASVVFDaF 557
Cdd:cd17933 11 RNRVSVL-TGGAGTGKTTTLKALLAALEAEGKRVVLAA-PTGKAAKR--L---SESTGIEAstIHRLLGINPGGGGFY-Y 82
|
90 100 110
....*....|....*....|....*....|....*....
gi 1184249154 558 QAAKARNVDVLIADTAG----RLQNKdnLMQELEKIARV 592
Cdd:cd17933 83 NEENPLDADLLIVDEASmvdtRLMAA--LLSAIPAGARL 119
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
190-236 |
5.94e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 39.85 E-value: 5.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1184249154 190 AEAERAEQERIAAEKAEADRL--EQERIAAEQA--EAERVEQERIAAEQAE 236
Cdd:PLN02316 251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
|
|
| HAMP |
COG2770 |
HAMP domain [Signal transduction mechanisms]; |
95-376 |
6.10e-03 |
|
HAMP domain [Signal transduction mechanisms];
Pssm-ID: 442051 [Multi-domain] Cd Length: 631 Bit Score: 39.71 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 95 EAQMRlEQERMAAQRAEQQRLDTEREQAEQDEKLAIEKANAELLAKEQAEAQVQQQAQAARLAEQEAQMRLEQERVAAEK 174
Cdd:COG2770 274 FNRMA-DSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAADLLL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 175 AEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQAEAER 254
Cdd:COG2770 353 ALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALALLALAAAAAAAE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 255 AEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAERLEQERI 334
Cdd:COG2770 433 AAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEEEEEAGAAAEELAEELLLL 512
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1184249154 335 AQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAE 376
Cdd:COG2770 513 EGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELAALLAL 554
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
168-299 |
6.47e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 39.58 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 168 ERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQ 247
Cdd:PRK13108 327 DDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEREQPGDLAGQAPAAHQVDAEAASAAPEEPAALAS 406
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1184249154 248 EQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAER 299
Cdd:PRK13108 407 EAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPAEPDGIRRQDDFSSRRR 458
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
224-351 |
6.57e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.68 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 224 RVEQERIAAEQAEAERveqeRIAQEQAEAERAEQQRIAAEQAEAERLEQQrIAAEQAEAERLEqeriaqEQGEAERAEQE 303
Cdd:COG0542 403 RMEIDSKPEELDELER----RLEQLEIEKEALKKEQDEASFERLAELRDE-LAELEEELEALK------ARWEAEKELIE 471
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1184249154 304 RIVAEAEAERLEQQRIAAEQAEAERLEQERIAQEQAEAERAEQERIAA 351
Cdd:COG0542 472 EIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDIAE 519
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
160-304 |
7.27e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 39.31 E-value: 7.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 160 EAQMRLEQervAAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAaEQAEAERVEQERIAAEQAEAER 239
Cdd:PRK12705 34 EAERILQE---AQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLV-QKEEQLDARAEKLDNLENQLEE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184249154 240 VEQERIAQEQAEAERAEQQRIAAEQAEAERLEQQR---IAAEQAEAERLEQERIAQEQGEAeRAEQER 304
Cdd:PRK12705 110 REKALSARELELEELEKQLDNELYRVAGLTPEQARkllLKLLDAELEEEKAQRVKKIEEEA-DLEAER 176
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
171-229 |
7.29e-03 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 39.09 E-value: 7.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184249154 171 AAEKAEAERLEQERI---AQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQER 229
Cdd:pfam07946 258 ALKKAKKTREEEIEKikkAAEEERAEEAQEKKEEAKKKEREEKLAKLSPEEQRKYEEKERKK 319
|
|
| PRK13709 |
PRK13709 |
conjugal transfer nickase/helicase TraI; Provisional |
233-333 |
8.06e-03 |
|
conjugal transfer nickase/helicase TraI; Provisional
Pssm-ID: 237478 [Multi-domain] Cd Length: 1747 Bit Score: 39.78 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 233 EQAEAERVEQERIAQEQAEAE-RAEQQRIAAEQA-EAERLEQQRIAAEQAEAER----LEQERIAQEQGEA--------E 298
Cdd:PRK13709 1632 GAGNGEPVTAEVLAQRQAEEAiRRETERRADEIVrKMAENKPDLPDGKTEQAVRdiagQERDRAAISEREAalpesvlrE 1711
|
90 100 110
....*....|....*....|....*....|....*.
gi 1184249154 299 RAEQERIVAEAEAERLEQQRIAAEQAEAER-LEQER 333
Cdd:PRK13709 1712 PQREREAVREVARENLLRERLQQMERDMVRdLQKEK 1747
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
168-304 |
8.10e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 39.19 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 168 ERVAAEKAEAERLEQERIAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQ 247
Cdd:PRK13108 312 ASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEREQPGDLAGQAPAAHQVDA 391
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1184249154 248 EQAEAERAEQQRIAAEQAEAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAEQER 304
Cdd:PRK13108 392 EAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPAEPDGIR 448
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
119-381 |
8.66e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 119 REQAEQDEKLAIEKANAELlakeqaeaqVQQQAQAARLAEQEAQMRLEQERVAAEKAEAERLEQERIAQEQAEAERAEQE 198
Cdd:PRK03918 443 RELTEEHRKELLEEYTAEL---------KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLK 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 199 RIAAEKAEADRLEQERIAAEQAEAERvEQERIAAEQAEAERVEQERIAQE----QAEAERAEQQRIAAEQA--------- 265
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLIKLKG-EIKSLKKELEKLEELKKKLAELEkkldELEEELAELLKELEELGfesveelee 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 266 ---EAERLEQQRIAAEQAEAE-RLEQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQA----EAERLEQE----- 332
Cdd:PRK03918 593 rlkELEPFYNEYLELKDAEKElEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeEYEELREEylels 672
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1184249154 333 -RIAQEQAEAERAEQERIAAEAEADRLEQERITAELAKEEAKLAEKPKKE 381
Cdd:PRK03918 673 rELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALER 722
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
287-375 |
8.68e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 37.63 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 287 QERIAQEQGEAEraeqERIVAEAEAERLEQQRIAAEQAEAERLEQEriAQEQAEAERAEQE--------RIAAEAEAD-R 357
Cdd:PRK07352 52 REAILQALKEAE----ERLRQAAQALAEAQQKLAQAQQEAERIRAD--AKARAEAIRAEIEkqaiedmaRLKQTAAADlS 125
|
90
....*....|....*...
gi 1184249154 358 LEQERITAELAKEEAKLA 375
Cdd:PRK07352 126 AEQERVIAQLRREAAELA 143
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
187-325 |
9.06e-03 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 38.62 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 187 QEQAEAERAEQERIAAekaeadrleqeRIAAEQAEAERveqeRIAAEQAEAERVEQERIAQEQAEAER-AEQQRIAAEQA 265
Cdd:PRK06991 149 QAQADAARARHDARQA-----------RLRREREAAEA----RAAARAAASAAAAAAEASAAAAPAADdAEAKKRAIIAA 213
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 266 EAERLEQQRIAAEQAEAERLEQERIAQEQGEAERAeqerivAEAEAERLEQQRIAAEQAE 325
Cdd:PRK06991 214 ALERARKKKEELAAQGAGPKNTEGVSAAVQAQIDA------AEARRKRLAEQRDAPDDAN 267
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
171-346 |
9.63e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 39.19 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 171 AAEKAEAERLEQEriAQEQAEAERAEQERIAAEKAEADRLEQERIAAEQAEAERVEQERIAAEQAEAERVEQERIAQEQA 250
Cdd:PRK13108 287 GSEYVVDEALERE--PAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 251 EAERAeqqriAAEQAEAERLEQQRIAAEQAEAErleQERIAQEQGEAERAEQERIVAEAEAERLEQQRIAAEQAEAERLE 330
Cdd:PRK13108 365 ETSEA-----DIEREQPGDLAGQAPAAHQVDAE---AASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAG 436
|
170
....*....|....*.
gi 1184249154 331 QERIAQEQAEAERAEQ 346
Cdd:PRK13108 437 PGDDPAEPDGIRRQDD 452
|
|
| HpsJ_fam |
NF038305 |
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the ... |
234-333 |
9.71e-03 |
|
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the biosynthesis or secretion of an extracellular polysaccharide shared by many Cyanobacteria.
Pssm-ID: 468465 [Multi-domain] Cd Length: 230 Bit Score: 38.33 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184249154 234 QAEAERVEQerIAQEQAEAERAEQQRIAAEQAEAERLE-QQRIAAEQAEAERLEQERIAQEQGEAERAEQERIVAEAEAE 312
Cdd:NF038305 104 RLSTQALQQ--INQQAGQQETQLQQQLNQLQAQTSPQQlNQLLKSEQKQGQALASGQLPEEQKEQLQQFKSNPQALDKFL 181
|
90 100
....*....|....*....|.
gi 1184249154 313 RLEQQRIAAEQAEAERLEQER 333
Cdd:NF038305 182 AQQLTQIRTQAEEAEKQARLE 202
|
|
| |
